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(ADP-D-ribose)15 + H2O
(ADP-ribose)14 + ADP-D-ribose
2'-O-(ADP-ribosyl)-adenosine 5'-phosphate + H2O
?
-
-
-
?
2'-O-acetyl-ADP-ribose + H2O
ADP-ribose + acetate
-
rate of hydrolysis by isoform ARH3 is 250fold that observed with isoform ARH1, isoform ARH2 is inactive with this substrate
-
-
?
ADP-ribose dimer + H2O
2 ADP-ribose
the N-1 adenine group interacts with the amide nitrogen of the conserved Leu752 in human PARG, while the beta-phosphate forms H-bonds with the conserved Ala750, enzyme-substrate binding structure, crystal structure analysis, overview
-
-
?
histone-bound poly(ADP-ribose) + H2O
ADP-ribose + ADP-ribose oligomer + ?
-
C14-labelled poly(ADP-ribose) produced by PARP-1 (poly(ADP-ribose) polymerase) of labelled NAD+
-
-
?
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
poly(ADP-ribose) + H2O
ADP-ribose + ADP-ribose oligomer
poly(ADP-ribose) + H2O
ADP-ribose oligomer + ADP-ribose
poly(ADP-ribose)n + H2O
?
poly(ADP-ribose)n + H2O
ADP-ribose
poly(ADP-ribose)n-poly(ADP-ribose) polymerase + H2O
ADP-ribose + poly(ADP-ribose) polymerase
-
-
-
?
poly(ADP-ribosyl)ated-Hrp38 + H2O
?
-
-
-
-
?
propargyl ADP-ribose dimer + H2O
propargyl ADP-ribose + ADP-ribose
-
-
-
?
additional information
?
-
(ADP-D-ribose)15 + H2O
(ADP-ribose)14 + ADP-D-ribose
-
-
-
-
?
(ADP-D-ribose)15 + H2O
(ADP-ribose)14 + ADP-D-ribose
-
-
-
-
?
PARP1-XRCC1 + H2O
?
efficient disassembly of complexes of the DNA scaffold repair protein XRCC1 and the poly(ADP-ribose) polymerase 1 by poly(ADP-ribose) glycohydrolase (PARG)
-
-
?
PARP1-XRCC1 + H2O
?
PARG rapidly reverses the PARylation of PARP1 and efficiently disassembles the PARP1-XRCC1 complex
-
-
?
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
-
-
-
-
?
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
-
-
-
?
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
binding structure of ADP-ribose to wild-type and mutant enzymes, overview
-
-
?
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
the activity is dependent on the conserved glutamate residues
-
-
?
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
-
-
-
?
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
-
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
?
poly(ADP-ribose) + H2O
?
PARylated PARP1 substrate
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
?
poly(ADP-ribose) + H2O
?
PARylated PARP1 substrate
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
-
?
poly(ADP-ribose) + H2O
?
-
-
-
?
poly(ADP-ribose) + H2O
?
a commercial Bt-NAD ribosylated PARP1 substrate
-
-
?
poly(ADP-ribose) + H2O
?
commercial Bt-NAD ribosylated PARP1 substrate
-
-
?
poly(ADP-ribose) + H2O
?
enzyme-substrate binding complex structure analysis, overview
-
-
?
poly(ADP-ribose) + H2O
?
PAR
-
-
?
poly(ADP-ribose) + H2O
ADP-ribose + ADP-ribose oligomer
-
-
-
-
?
poly(ADP-ribose) + H2O
ADP-ribose + ADP-ribose oligomer
-
tritium-labelled poly(ADP-ribose) produced by PARP-1 (poly(ADP-ribose) polymerase) with tritium-labelled NAD + sonicated DNA containing histones, and bovine albumin
-
-
?
poly(ADP-ribose) + H2O
ADP-ribose + ADP-ribose oligomer
-
P32-labelled poly(ADP-ribose) produced by PARP-1 (poly(ADP-ribose) polymerase) of labelled NAD+
-
-
?
poly(ADP-ribose) + H2O
ADP-ribose oligomer + ADP-ribose
-
-
-
-
?
poly(ADP-ribose) + H2O
ADP-ribose oligomer + ADP-ribose
-
-
-
-
?
poly(ADP-ribose) + H2O
ADP-ribose oligomer + ADP-ribose
-
-
-
?
poly(ADP-ribose) + H2O
ADP-ribose oligomer + ADP-ribose
-
-
-
-
?
poly(ADP-ribose) + H2O
ADP-ribose oligomer + ADP-ribose
-
-
-
-
?
poly(ADP-ribose)n + H2O
?
-
-
-
?
poly(ADP-ribose)n + H2O
?
-
the enzyme may regulate functionally the chain length of poly(ADP-ribose) which plays a role in DNA synthesis or in the structure of chromatin
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-
?
poly(ADP-ribose)n + H2O
?
-
the enzyme is responsible for the catabolism of poly(ADP-ribose), the enzyme is a crucial determinant of polymer metabolism which is known to be implicated in DNA repair and other cellular processes
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-
?
poly(ADP-ribose)n + H2O
?
-
regulates differentially the levels of large and small poly(ADP-ribose) in the cell
-
-
?
poly(ADP-ribose)n + H2O
?
-
poly(ADP-ribose) glycohydrolase II may be involved in extranuclear de(ADP-ribosyl)n-ation, but not in membrane de-mono(ADP-ribosyl)ation
-
-
?
poly(ADP-ribose)n + H2O
ADP-ribose
-
-
-
-
?
poly(ADP-ribose)n + H2O
ADP-ribose
-
-
-
?
poly(ADP-ribose)n + H2O
ADP-ribose
-
n greater 20, degradation proceeds in a biphasic as well as bimodal manner
-
-
?
poly(ADP-ribose)n + H2O
ADP-ribose
-
-
-
-
?
poly(ADP-ribose)n + H2O
ADP-ribose
-
-
-
-
?
poly(ADP-ribose)n + H2O
ADP-ribose
-
and lower molecular weight poly(ADP-ribose)n fragment products, no product: phosphoribosyl-AMP
-
?
poly(ADP-ribose)n + H2O
ADP-ribose
-
and lower molecular weight poly(ADP-ribose)n fragment products, no product: phosphoribosyl-AMP
-
?
poly(ADP-ribose)n + H2O
ADP-ribose
-
-
-
-
?
poly(ADP-ribose)n + H2O
ADP-ribose
-
-
-
-
?
additional information
?
-
-
several isoforms, functions in embryonic development, genotixicity, cell cycle regulation, mitotic spindle assembly, development, differentiation, and cell death
-
-
?
additional information
?
-
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
-
-
?
additional information
?
-
-
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
-
-
?
additional information
?
-
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
-
-
?
additional information
?
-
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
-
-
?
additional information
?
-
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
-
-
?
additional information
?
-
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
-
-
?
additional information
?
-
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
-
-
?
additional information
?
-
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
-
-
?
additional information
?
-
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
-
-
?
additional information
?
-
enzyme DrPARG possesses endoglycohydrolase activity toward poly-ADP-ribose (PAR). DrPARG acts in both exo- and endo-glycohydrolase modes
-
-
?
additional information
?
-
-
poly(ADP-ribose) polymerase and poly(ADP-ribose) glycohydrolase promote chromatin silencing at least in part by regulating the localization and function of silencing protein SIR2 and possible other nuclear proteins
-
-
?
additional information
?
-
-
the enzyme is responsible for the cleavage of poly(ADP-D-ribose) into the single ADP-ribose unit by hydrolyzing the ribose-ribose bonds within the polymer chain
-
-
?
additional information
?
-
-
the enzyme cannot hydrolyze the bond between terminal ADP-ribose and glutamate residues of automodifed PARP1
-
-
?
additional information
?
-
-
shuttling of enzyme between nucleus and cytoplasm and proper control of poly(ADP-ribose) metabolism throughout cell cycle may be an important role in regulating cell cycle progression and centrosome duplication
-
-
?
additional information
?
-
transient decrease in nuclear enzyme activity is important for the onset of differentiation of HL-60 cells to macrophage-like cells
-
-
?
additional information
?
-
-
poly(ADP-ribose) glycohydrolase is a critical component of single-strand break repair and accelerates this process in concert with poly(ADP-ribose) polymerase
-
-
?
additional information
?
-
poly(ADP-ribose) glycohydrolase is the only enzyme known to catalyse hydrolysis of the O-glycosidic linkages of ADP-ribose polymers
-
-
?
additional information
?
-
-
poly(ADP-ribose) glycohydrolase is the only enzyme known to catalyse hydrolysis of the O-glycosidic linkages of ADP-ribose polymers
-
-
?
additional information
?
-
-
the enzyme can effectively process the added poly-/oligo(ADP-ribose) units from both GST-Smad3 and PARP-1, but fails to act as a mono(ADP-ribose) hydrolase, inability of the enzme to cleave the last ADP-ribose unit, which is coupled to the protein substrate
-
-
?
additional information
?
-
assay using the PARylated PARP1 substrates, poly(ADP-ribose)-linked N-terminal DNA-binding domain of PARP1, i.e. PAR polymerase 1, a nicked DNA. Poly(ADP-ribose) binding structures of wild-type and D314A mutant, overview
-
-
?
additional information
?
-
-
assay using the PARylated PARP1 substrates, poly(ADP-ribose)-linked N-terminal DNA-binding domain of PARP1, i.e. PAR polymerase 1, a nicked DNA. Poly(ADP-ribose) binding structures of wild-type and D314A mutant, overview
-
-
?
additional information
?
-
development of a high-throughput homogeneous time-resolved fluorescence (HTRF) assay method, 6His-TEV-PAR(32:1)PARP-1(2-1014) substrate, combinantion with the activity of poly(ADP-ribose) polymerase, PARP. Enzyme PARG binds to PARylated PARP-1 and cleaves off the PAR moiety, which activates PARP-1 preventing the production of a fluorescent signal. Inactive PARP-1 leads to the production of the measurable fluoresecnt signal, mechanism and evaluation, overview
-
-
?
additional information
?
-
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development of a high-throughput homogeneous time-resolved fluorescence (HTRF) assay method, 6His-TEV-PAR(32:1)PARP-1(2-1014) substrate, combinantion with the activity of poly(ADP-ribose) polymerase, PARP. Enzyme PARG binds to PARylated PARP-1 and cleaves off the PAR moiety, which activates PARP-1 preventing the production of a fluorescent signal. Inactive PARP-1 leads to the production of the measurable fluoresecnt signal, mechanism and evaluation, overview
-
-
?
additional information
?
-
structure of poly(ADP-ribose) glycohydrolase (PARG) in complex with the poly(ADP-ribose) (PAR) substrate reveals that PARG-PAR contacts are provided almost exclusively by the macrodomain. The accessory domain (which is part of the PARG catalytic region) has only limited interaction with PAR, but it structurally supports the PARG catalytic loop and may have an important role in regulation of PARG catalytic activity. The PARG-PAR structure also reveals that PARGs preferably bind PAR at the chain termini and primarily act as exo-glycohydrolases (whereby PARG sequentially degrades terminal ADP-ribose units). While binding along the PAR chain and endo-glycohydrolytic cleavage of PAR is structurally possible, it appears to be less efficient. Due to active site constraints and the conformation of bound PAR, canonical PARGs are unlikely to efficiently bind the aforementioned putative PAR branch sites
-
-
?
additional information
?
-
synthesis of derivatives of the ADP-ribose dimer and development of a PAR Binding assay, overview. Propargyl ADP-ribose dimer binds to E756N and E755N mutants of human PARG with KD values of 83 nM and 208 nM, respectively. Fluorescent propargyl ADP-ribose dimer does not bind proteins devoid of PAR binding activity such as bovine serum albumin even at high concentrations of protein. Wild-type PARG is unable to process the truncated substrates 2'-O-alpha-D-ribofuranosyladenosine and 2'-O-(5-O-phosphono-a-D-ribofuranosyl)adenosine 5'-phosphate)
-
-
?
additional information
?
-
-
synthesis of derivatives of the ADP-ribose dimer and development of a PAR Binding assay, overview. Propargyl ADP-ribose dimer binds to E756N and E755N mutants of human PARG with KD values of 83 nM and 208 nM, respectively. Fluorescent propargyl ADP-ribose dimer does not bind proteins devoid of PAR binding activity such as bovine serum albumin even at high concentrations of protein. Wild-type PARG is unable to process the truncated substrates 2'-O-alpha-D-ribofuranosyladenosine and 2'-O-(5-O-phosphono-a-D-ribofuranosyl)adenosine 5'-phosphate)
-
-
?
additional information
?
-
-
enzyme is a necessary component of the poly(ADP-ribose) polymerase 1 mediated cell death pathway
-
-
?
additional information
?
-
no substrate: mono-ADP-ribosylated proteins, ADP-ribose-arginine, ADP-ribose-cysteine, ADP-ribose-diphthaminde, ADP-ribose-asparagine
-
-
?
additional information
?
-
-
enzyme activity modulates the inflammatory response and tissue events associated with spinal cord trauma and participates in target organ damage under these conditions
-
-
?
additional information
?
-
-
function in cell death
-
-
?
additional information
?
-
-
modification of the adenine moiety of poly(ADP-ribose) abrogates the susceptibility to digestion by the enzyme
-
-
?
additional information
?
-
the enzyme functions as an endo-glycosidase to release oligo(ADP-ribose) and as an exo-glycosidase to release ADP-ribose. Long poly(ADP-ribose) polymers are efficiently hydrolyzed by a combination of endo- and exo-glycosidic activity, whereas smaller digestion products are poor substrates for the enzyme allowing release of oligo(ADP-ribose) chains that are ligands for histones and DNA repair and damage checkpoint proteins such as XRCC1 and p53
-
-
?
additional information
?
-
quantitative, real-time assay of PAR-dependent protein-protein interactions and PAR turnover by PARG. PARG degrades the PAR posttranslational modification by a combination of exo- and endo-glycohydrolase activity, leaving a single ADP-ribose moiety attached to PARP1 that is a substrate for the mono(ADP-ribose) (MAR) hydrolases
-
-
?
additional information
?
-
hydrolysis of glycosidic ribose-ribose bond
-
-
?
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(17-chloro-3b-hydroxy-androsta-5,16-diene)-succinyl-glutathione
-
-
(3Z)-5-bromo-1-(2,6-dichlorobenzyl)-3-[4-oxo-3-[2-(1H-tetrazol-5-yl)ethyl]-2-thioxo-1,3-thiazolidin-5-ylidene]-1,3-dihydro-2H-indol-2-one
-
specific detergent-insensitive inhibition
(3Z)-5-chloro-1-(2,6-dichlorobenzyl)-3-[4-oxo-3-[2-(1H-tetrazol-5-yl)ethyl]-2-thioxo-1,3-thiazolidin-5-ylidene]-1,3-dihydro-2H-indol-2-one
-
specific detergent-insensitive inhibition
1,2,3,4,6-pentakis-O-galloyl-beta-D-glucoside
-
about 25% inhibition at 10 microM in vitro
1,3,6-tris-O-galloyl-beta-D-glucoside
-
about 25% inhibition at 10 microM in vitro
1,3-diethyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
1,3-dimethyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
1-(cyclopropylmethyl)-N-(1-methylcyclopropyl)-3-[(1-methylpyrazol-4-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-(cyclopropylmethyl)-N-(1-methylcyclopropyl)-3-[(2-methylthiazol-5-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-(cyclopropylmethyl)-N-(1-methylcyclopropyl)-3-[(3-methylisoxazol-5-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-ethyl-N-(1-methylcyclopropyl)-3-[(1-methylpyrazol-4-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-ethyl-N-(1-methylcyclopropyl)-3-[(3-methylisoxazol-5-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-ethyl-N-(1-methylcyclopropyl)-3-[(5-methyl-1,3,4-thiadiazol-2-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyc lopropyl)-2,4-dioxo-3-(3-thienylmethyl)quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-1,2,3,4-tetrahydroquinazoline-6-sulfonamide
-
-
1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-(1H-pyrazol-4-ylmethyl)quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-(2-pyridylmethyl)quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-(3-pyridylmethyl)quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-(4-pyridylmethyl)quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-(thiadiazol-4-ylmethyl)quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-(thiazol-2-ylmethyl)quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-(thiazol-5-ylmethyl)quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-phenacyl-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-phenyl-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-prop-2-ynyl-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-[2-oxo-2-(4-pyridyl)ethyl]quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-(oxazol-4-ylmethyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-(oxetan-3-ylmethyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(1-methylpyrazol-3-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(1-methylpyrazol-4-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(1-methyltetrazol-5-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(2-methyl-4-phenyl-thiazol-5-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(2-methylpyrazol-3-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(2-methylthiazol-4-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(2-methylthiazol-5-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(3-methyl-1,2,4-oxadiazol-5-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(3-methyl-1H-pyrazol-5-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(3-methylimidazol-4-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(3-methylisoxazol-5-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(4-methyl-1,2,4-triazol-3-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(4-methylthiadiazol-5-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(5-methyl-1,3,4-oxadiazol-2-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(5-methyl-1,3,4-thiadiazol-2-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(5-methylisoxazol-3-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-methyl-N-(1-methylcyclopropyl)-3-[(5-methylisoxazol-4-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-Naphthylamine
-
1 mM, 45% inhibition
1-[(1,3-dimethyl-1H-pyrazol-5-yl)methyl]-N-(1-methylcyclopropyl)-3-[(2-methyl-1,3-thiazol-5-yl)methyl]-2,4-dioxo-1,2,3,4-tetrahydroquinazoline-6-sulfonamide
-
1-[(2,4-dimethyl-1,3-thiazol-5-yl)methyl]-N-(1-methylcyclopropyl)-2-oxo-3-(1,2,4-thiadiazol-5-yl)-2,3-dihydro-1H-benzimidazole-5-sulfonamide
-
1-[(2,4-dimethylthiazol-5-yl)methyl]-3-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
1-[(2,4-dimethylthiazol-5-yl)methyl]-N-(1-methylcyclopropyl)-3-[(1-methylpyrazol-4-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-[(2,4-dimethylthiazol-5-yl)methyl]-N-(1-methylcyclopropyl)-3-[(2-methylthiazol-5-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-[(2,5-dimethylpyrazol-3-yl)methyl]-3-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
1-[(2,5-dimethylpyrazol-3-yl)methyl]-N-(1-methylcyclopropyl)-3-[(1-methylpyrazol-4-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-[(2,5-dimethylpyrazol-3-yl)methyl]-N-(1-methylcyclopropyl)-3-[(2-methylthiazol-5-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-[(2,5-dimethylpyrazol-3-yl)methyl]-N-(1-methylcyclopropyl)-3-[(3-methylisoxazol-5-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-[(2,5-dimethylpyrazol-3-yl)methyl]-N-(1-methylcyclopropyl)-3-[(5-methyl-1,3,4-thiadiazol-2-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
1-[(2-fluorophenyl)methyl]-3-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
1-[(2-methoxyphenyl)methyl]-3-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
1-[(3-fluorophenyl)methyl]-3-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
1-[(3-methoxyphenyl)methyl]-3-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
1-[(4-fluorophenyl)methyl]-3-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
1-[(4-methoxyphenyl)methyl]-3-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
12-O-tetradecanoyl-phorbol-13-acetate
reduction of nuclear enzyme activity to 30-40% of control, cytosolic activity remains unchanged. Reduction is suppressed by protein kinase C inhibitor H7. Enzyme expression is reduced in presence of 12-O-tetradecanoyl-phorbol-13-acetate
2-(3-chloro-4-(naphthalen-2-yloxy)phenylcarbamoyl)benzoic acid
-
-
2-N3-adenosine diphosphate (hydroxymethyl)pyrrolidinediol
-
50% inhibition at 0.290 mM, native protein and 50% inhibition at 0.148 mM, recombinant catalytic fragment
2-naphthalene sulfonic acid
-
5 mM, 26% inhibition
2-Naphthylamine
-
1 mM, 50% inhibition
2-[(9,10-dioxo-2-anthryl)sulfonylamino]acetamide
-
-
3,5-dichloro-2-hydroxy-N-(3-methyl-4-(naphthalen-2-yloxy)phenyl)benzamide
-
-
3,5-dichloro-2-hydroxy-N-(4-(naphthalen-2-yloxy)-3-(trifluoromethyl)phenyl)benzamide
-
-
3,5-dichloro-2-hydroxy-N-(4-(naphthalen-2-yloxy)phenyl)benzamide
-
-
3,5-dichloro-2-hydroxy-N-m-tolylbenzamide
-
between 10% and 30% inhibition at 0.5 mM
3,5-dichloro-2-hydroxy-N-o-tolylbenzamide
-
between 10% and 30% inhibition at 0.5 mM
3,5-dichloro-2-hydroxy-N-p-tolylbenzamide
-
between 10% and 30% inhibition at 0.5 mM
3,5-dichloro-N-(2-chlorophenyl)-2-hydroxybenzamide
-
between 10% and 30% inhibition at 0.5 mM
3,5-dichloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxy-N-methylbenzamide
-
-
3,5-dichloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
-
-
3,5-dichloro-N-(3-chloro-4-(p-tolyloxy)phenyl)-2-hydroxybenzamide
-
-
3,5-dichloro-N-(3-chloro-4-phenoxyphenyl)-2-hydroxybenzamide
-
-
3,5-dichloro-N-(3-chlorophenyl)-2-hydroxybenzamide
-
-
3,5-dichloro-N-(3-fluoro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
-
-
3,5-dichloro-N-(4-chlorophenyl)-2-hydroxybenzamide
-
-
3,5-dichloro-N-[3-chloro-4-(naphthalen-2-yloxy)cyclohexa-1,5-dien-1-yl]-2-hydroxybenzamide
-
3,5-dichloro-N-[3-chloro-4-(naphthalen-2-yloxy)phenyl]-2-hydroxybenzamide
-
-
3-(1H-imidazol-4-ylmethyl)-1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
3-(3-furylmethyl)-1-methyl-N-(1-methylcyclopropyl)-2,4-dioxoquinazoline-6-sulfonamide
-
3-(cyanomethyl)-1-(cyclopropylmethyl)-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
3-(cyanomethyl)-1-methyl-N-(1-methylcyclopropyl)-2,4-dioxoquinazoline-6-sulfonamide
-
3-(cyanomethyl)-1-[(2,5-dimethylpyrazol-3-yl)methyl]-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
3-(cyanomethyl)-N-(1-methylcyclopropyl)-2,4-dioxo-1-prop-2-ynyl-quinazoline-6-sulfonamide
-
3-(cyclohexylmethyl)-1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
3-(cyclopropylmethyl)-1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
3-(isothiazol-5-ylmethyl)-1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
3-(isoxazol-5-ylmethyl)-1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
3-benzyl-1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
3-bromo-5-chloro-N-[5-chloro-2-[(1-chloronaphthalen-2-yl)oxy]phenyl]-2-hydroxybenzamide
-
-
3-bromo-N-[2-[2-bromo-6-methyl-3-(propan-2-yl)phenoxy]-5-chlorophenyl]-5-chloro-2-hydroxybenzamide
-
-
3-chloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
-
-
3-ethyl-1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
3-galloyl-D-glucose
-
about 50% inhibition at 1 microM, 65% inhibition at 10 microM, about 85% at 100 microM in vitro, no inhibitory effect in HeLa cell death at 10 microM, induced by methylating agent 1-methyl-3-nitro-1-nitrosoguanidine (100 microM), because cell-permeability is probably hindered
3-methyl-N-(1-methylcyclopropyl)-1-[(2-methylpyrazol-3-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
-
3-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-1-(2-pyridylmethyl)quinazoline-6-sulfonamide
-
3-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-1-(3-pyridylmethyl)quinazoline-6-sulfonamide
-
3-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-1-(4-pyridylmethyl)quinazoline-6-sulfonamide
-
3-O-galloyl-beta-D-glucose
-
3-[(1-ethylpyrazol-4-yl)methyl]-1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
3-[(2,4-dimethylthiazol-5-yl)methyl]-1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
3-[(2-aminothiazol-5-yl)methyl]-1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
3-[(3,5-dimethylisoxazol-4-yl)methyl]-1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
3-[(5Z)-5-[1-(2-chlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
specific detergent-insensitive inhibition
3-[(5Z)-5-[5-bromo-1-(2,6-dichlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
specific detergent-insensitive inhibition
3-[(5Z)-5-[5-bromo-1-(2-chloro-6-fluorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
specific detergent-insensitive inhibition
3-[(5Z)-5-[5-chloro-1-(2,6-dichlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
3-[(9,10-dioxo-2-anthryl)sulfonylamino]propanamide
-
3-[[1-(cyanomethyl)pyrazol-4-yl]methyl]-1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
4-amino-3-hydroxynaphthalene 1-sulfonic acid
-
5 m, 79% inhibition
5-chloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
-
-
6,9-diamino-2-ethoxyacridine lactate
-
8-bromoadenosine 3',5'-monophosphate
-
5 mM, 13% inhibition
8-chlorophenylthioadenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
-
50% inhibition at 0.12 mM, recombinant catalytic fragment
8-methylaminoadenosine 3',5'-monophosphate
-
5 mM, 14% inhibition
8-n-octyl-amino-adenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
binding structure with mutant enzyme K616A/Q617A/K618A/E688A/K689A/K690A
8-N3-adenosine diphosphate (hydroxymethyl)pyrrolidinediol
-
50% inhibition at 390 nM, native protein and 50% inhibition at 0.0014 mM, recombinant catalytic fragment
acetone
-
20%, 95% inhibition
adenine(5'-9)ribofuranoside
-
5 mM, 24% inhibition
adenosine 3':5'-cyclic monophosphate
adenosine 5'-carboxylic acid
-
5 mM, 26% inhibition
adenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
ADP-HPD, binding structure with mutant enzyme K616A/Q617A/K618A/E688A/K689A/K690A
adenosine 5'-diphosphate-(hydroxymethyl)-pyrrolidinediol
ADP-HPD, an analogue of ADP-ribose
adenosine cyclic 2':3'-monophosphate
adenosine diphosphate (hydroxymethyl) pyrrolidinediol
adenosine diphosphate (hydroxymethyl)-pyrrolidinediol
adenosine diphosphate (hydroxymethyl)pyrrolidine
-
50% inhibition at 0.019 mM, native protein and 50% inhibition at 0.063 mM, recombinant catalytic fragment
adenosine diphosphate (hydroxymethyl)pyrrolidine-monoalcohol
-
50% inhibition at 330nM, native protein and 50% inhibition at 440 nM, recombinant catalytic fragment
adenosine diphosphate (hydroxymethyl)pyrrolidinediol
adenosine diphosphate(hydroxymethyl)pyrrolidine 3,4-diol
-
ADP-(hydroxymethyl)pyrrolidinediol
-
-
Ahx
-
50% inhibition at 0.001 mM, recombinant catalytic fragment
Congo red
-
detergent-sensitive inhibition with complete loss of inhibition in the presence of detergent
cyclic dAMP
-
5 mM, 34% inhibition
ethacridine lactate
PARG inhibitor, synergized with ibrutinib in TEX and OCI-AML2 leukemia cell lines. The combination of ibrutinib and ethacridine induces a synergistic increase in reactive oxygen species that is functionally important to explain the observed cell death, synergistic cytotoxicity of ibrutinib and ethacridine. The ibrutinib-ethacridine combination is preferentially cytotoxic to a subset of primary AML cells compared to normal hematopoietic cells
ethanol
-
20%, 91% inhibition
F3Ahx
-
50% inhibition at 0.57 mM, recombinant catalytic fragment
gallic acid
-
0.1 mg/ml, 9% inhibition
galloylgallic acid
-
0.1 mg/ml, 11% inhibition
glucuronic acid
-
0.1 mg/ml, 14% inhibition
GPI 16552
-
pharmacological inhibitor, treatment of wild-type mice shows a protective effect in dinitrobenzene sulfonic acid-induced colitis
GPI 18214
-
pharmacological inhibitor, treatment of wild-type mice shows a protective effect in dinitrobenzene sulfonic acid-induced colitis
-
guanosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
-
50% inhibition above 1 mM, native protein and 50% inhibition at 0.970 mM,+ recombinant catalytic fragment
guanosine cyclic 3':5'-monophosphate
methyl 2-O-galloyl-beta-D-glucoside
-
about 25% inhibition at 1 microM, 65% inhibition at 10 microM, about 85% inhibition at 100 microM in vitro
methyl 3-O-galloyl-beta-D-glucoside
-
about 25% inhibition at 1 microM, 65% inhibition at 10 microM, about 85% inhibition at 100 microM in vitro
MgCl2
-
10 mM, 18% inhibition
N'',N'''-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]carbonohydrazide
-
-
N'',N'''-bis[(E)-(3,4,5-trihydroxyphenyl)methylidene]carbonohydrazide
-
-
N'1,N'3-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]propanedihydrazide
-
-
N'1,N'3-bis[(E)-(3,4,5-trihydroxyphenyl)methylidene]propanedihydrazide
-
-
N'1,N'4-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
N'1,N'4-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]butanedihydrazide
-
-
N'1,N'4-bis[(E)-(3,4,5-trihydroxyphenyl)methylidene]butanedihydrazide
-
-
N'1,N'4-bis[(E)-(3,4-dihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
slight inhibition
N'1,N'5-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]pentanedihydrazide
-
-
N'1,N'5-bis[(E)-(3,4,5-trihydroxyphenyl)methylidene]pentanedihydrazide
-
-
N'1-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-N'3-[(Z)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
-
-
N'1-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-N'4-[(Z)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
-
N'1-[(E)-(2,3-dihydroxyphenyl)methylidene]-N'3-[(Z)-(2,3-dihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
-
-
N'1-[(E)-(2,4,6-trihydroxyphenyl)methylidene]-N'3-[(Z)-(2,4,6-trihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
-
-
N'1-[(E)-(2,4,6-trihydroxyphenyl)methylidene]-N'4-[(Z)-(2,4,6-trihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
-
N'1-[(E)-(2,4-dihydroxyphenyl)methylidene]-N'3-[(Z)-(2,4-dihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
-
-
N'1-[(E)-(3,4,5-trihydroxyphenyl)methylidene]-N'3-[(Z)-(3,4,5-trihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
-
-
N'1-[(E)-(3,4,5-trihydroxyphenyl)methylidene]-N'4-[(Z)-(3,4,5-trihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
-
N'1-[(E)-(3,4-dihydroxyphenyl)methylidene]-N'3-[(Z)-(3,4-dihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
-
-
N'1-[(E)-(4,6-dihydroxycyclohexa-1,3-dien-1-yl)methylidene]-N'4-[(E)-(2,4-dihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
slight inhibition
N'1-[(E)-(5,6-dihydroxycyclohexa-1,3-dien-1-yl)methylidene]-N'4-[(E)-(2,3-dihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
slight inhibition
N,1,3-triethyl-2,4-dioxo-1,2,3,4-tetrahydroquinazoline-6-sulfonamide
-
N-(1,1-dimethylpropyl)-9,10-dioxo-anthracene-2-sulfonamide
-
N-(1-cyanocyclopropyl)-1,3-diethyl-2,4-dioxo-quinazoline-6-sulfonamide
-
N-(1-cyanocyclopropyl)-1,3-dimethyl-2,4-dioxo-quinazoline-6-sulfonamide
-
N-(1-cyanocyclopropyl)-9,10-dioxo-anthracene-2-sulfonamide
-
N-(1-methylcyclopropyl)-3-[(1-methylpyrazol-4-yl)methyl]-1-(oxetan-3-ylmethyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
N-(1-methylcyclopropyl)-3-[(1-methylpyrazol-4-yl)methyl]-2,4-dioxo-1-prop-2-ynyl-quinazoline-6-sulfonamide
-
N-(1-methylcyclopropyl)-3-[(2-methylthiazol-5-yl)methyl]-2,4-dioxo-1-prop-2-ynyl-quinazoline-6-sulfonamide
-
N-(1-methylcyclopropyl)-3-[(3-methylisoxazol-5-yl)methyl]-1-(oxetan-3-ylmethyl)-2,4-dioxo-quinazoline-6-sulfonamide
-
N-(1-methylcyclopropyl)-3-[(3-methylisoxazol-5-yl)methyl]-2,4-dioxo-1-prop-2-ynyl-quinazoline-6-sulfonamide
-
N-(1-methylcyclopropyl)-9,10-dioxo-anthracene-2-sulfonamide
-
N-(1-methylcyclopropyl)naphthalene-2-sulfonamide
-
N-(2-cyanoethyl)-9,10-dioxo-anthracene-2-sulfonamide
-
N-(2-hydroxyethyl)-9,10-dioxo-anthracene-2-sulfonamide
-
N-(2-methoxy-1,1-dimethyl-ethyl)-9,10-dioxo-anthracene-2-sulfonamide
-
N-(2-methoxyethyl)-9,10-dioxo-anthracene-2-sulfonamide
-
N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
-
-
N-(cyclopropylmethyl)-9,10-dioxo-anthracene-2-sulfonamide
-
N-bis-(3-phenyl-propyl)9-oxo-fluorene-2,7-diamide
-
i.e. GPI 16552, pharmacological inhibitor. Enzyme inhibition results in significant reduction of spinal cord inflammation and tissue injury, neutrophil infiltration, cytokine production, and apoptosis upon spinal cord injury. Additionally, inhibition significantly ameliorates the recovery of limb function
N-bis-(3-phenylpropyl)-9-oxofluorene-2,7-diamide
-
GPI 16552
N-cyclobutyl-9,10-dioxo-anthracene-2-sulfonamide
-
N-cyclopropyl-1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydroquinazoline-6-sulfonamide
-
N-cyclopropyl-6-oxo-5,6-dihydrophenanthridine-2-sulfonamide
-
N-cyclopropyl-9,10-dioxo-anthracene-2-sulfonamide
-
N-ethyl-1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydroquinazoline-6-sulfonamide
-
N-ethyl-9,10-dioxo-9,10-dihydroanthracene-2-sulfonamide
-
N-methyl-9,10-dioxo-9,10-dihydroanthracene-2-sulfonamide
-
N-tert-butyl-1,3-dimethyl-2,4-dioxo-quinazoline-6-sulfonamide
-
N-tert-butyl-1,4-dimethyl-2-oxo-1,2-dihydroquinoline-6-sulfonamide
-
N-tert-butyl-2-oxo-1,2-dihydroquinoline-6-sulfonamide
-
N-tert-butyl-9,10-dioxo-9,10-dihydroanthracene-2-sulfonamide
N-[4-[(3-bromonaphthalen-2-yl)oxy]-3-chlorophenyl]-3,5-dichloro-2-hydroxybenzamide
-
-
N1-naphthylethanenediamine
-
5 mM, 70% inhibition
N6,O2'-dibutyryl adenosine cyclic 3':5'-monophosphate
-
10 mM, 11% inhibition
N6-benzyladenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
-
50% inhibition above 1 mM, recombinant catalytic fragment
N6-hexyladenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
-
50% inhibition at 0.51 mM, recombinant catalytic fragment
N6-monobutyryl adenosine cyclic 3':5'-monophosphate
-
10 mM, 50% inhibition
nobotanin B
-
inhibition of enzyme activity. In presence of inhibitor, reduction of cell death after exposure to hydrogen peroxide, N-methyl-D-aspartate, or N-methyl-N-nitro-N-nitrosoguanidine
nuclear matrix proteins
-
due to non-covalent interactions of the protein with free ADP-ribose polymers
-
p-chloromercuribenzenesulfonate
phosphorodiamidate morpholino oligonucleotide
-
antisense phosphorodiamidate morpholino oligonucleotide blocks exon 1 of the full length nuclear PARG 111 kDa isoform, slowing down the rate of nuclear poly(ADP-ribose) degradation, attenuating poly(ADP-ribose) polymerase-1 mediated cell death, reducing PARG expression as shown by immunostaining, upon incubation with 50 microM alcylating agent N-methyl-N'-nitro-N'-nitrosoguanidine to induce cell death blocking of nuclear PARG reduced cell condensation and cell death, no inhibitory influence on cytosol PARG
-
poly(etheno ADP-ribose)
-
inhibits hydrolysis of ribose-ribose bonds by the enzyme, highly resistant to digestion by the enzyme
Poly(G)
-
inhibitory effect is eliminated when 250 mM KCl is present in the reaction mixture
RBPI-3
a rhodanine-containing mammalian PARG inhibitor, enzyme-inhibitor structure analysis, overview. RBPI-3 binds predominantly via a pi-pi stacking interaction with Tyr296 and the conserved Phe398. To accommodate the binding of RBPI-3, Phe398 moves into the adenosine binding pocket. The RBPI-3 carboxyl moiety occupies a region corresponding to the ADP-ribose alpha-phosphate group and H-bonds to main chain atoms of Lys365 and Gln254. The RBPI-3 di-chlorobenzyl moiety extends into the solvent and is disordered
sanguinin H-6
-
about 50% inhibition at 10 microM in vitro
SDS
-
0.01%, 96% inhibition
siRNA
-
small interfering RNA, down regulation of PARG to 50% 24 h after siRNA transfection, maximum of 84% inhibition after 72 compared to negative control with ineffective scrambled siRNA, siRNA produced in vitro from cDNA with 21-nucleotide sequence target in human coding region of the enzyme
-
Tannic acid
continous decrease in activity of nuclear enzyme activity, reduction in enzyme expression
tannin
-
0.01 mg/ml, 89% inhibition, competitive with respect to poly(ADP-ribose)
-
3-[(5Z)-5-[5-chloro-1-(2,6-dichlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
specific detergent-insensitive inhibition
3-[(5Z)-5-[5-chloro-1-(2,6-dichlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
adenosine 3':5'-cyclic monophosphate
-
-
adenosine 3':5'-cyclic monophosphate
-
0.3 mM, 50% inhibition
adenosine 3':5'-cyclic monophosphate
-
-
adenosine 3':5'-cyclic monophosphate
-
-
adenosine cyclic 2':3'-monophosphate
-
-
adenosine cyclic 2':3'-monophosphate
-
10 mM, 23% inhibition
adenosine diphosphate (hydroxymethyl) pyrrolidinediol
-
adenosine diphosphate (hydroxymethyl) pyrrolidinediol
-
39% inhibition at 0.025 mM
adenosine diphosphate (hydroxymethyl) pyrrolidinediol
-
ADP-HPD
adenosine diphosphate (hydroxymethyl) pyrrolidinediol
ADP-HPD, tight binding inhibitor, binding structure, overview
adenosine diphosphate (hydroxymethyl) pyrrolidinediol
-
adenosine diphosphate (hydroxymethyl)-pyrrolidinediol
-
adenosine diphosphate (hydroxymethyl)-pyrrolidinediol
ADP-HPD
adenosine diphosphate (hydroxymethyl)pyrrolidinediol
-
partial noncompetitive inhibition
adenosine diphosphate (hydroxymethyl)pyrrolidinediol
-
i.e. APD-HPD, 50% inhibition at 0.0031 mM, native protein and 50% inhibition at 0.0042 mM, recombinant catalytic fragment
adenosine diphosphate (hydroxymethyl)pyrrolidinediol
-
-
ADP
-
-
ADP
-
10 mM, 39% inhibition
ADP-HPD
-
about 40% inhibition at 1 microM, about 70% inhibition at 10 microM, about 85% inhibition at 100 microM in vitro
ADP-ribose
-
-
ADP-ribose
-
1.1 mM, 50% inhibition
ADP-ribose
-
5 mM, 55% inhibition
ADP-ribose
-
inhibits poly(ADP-ribose) glycohydrolase II more strongly than poly(ADP-ribose) glycohydrolase I
ADP-ribose
binding structure with mutant enzyme K616A/Q617A/K618A/E688A/K689A/K690A
AMP
-
-
AMP
-
10 mM, 64% inhibition
ATP
-
-
ATP
-
10 mM, 23% inhibition
CaCl2
-
1.5 mM, 50% inhibition. 96% inhibition at 10 mM
CaCl2
-
5 mM 86% inhibition
cAMP
-
inhibits poly(ADP-ribose) glycohydrolase II more strongly than poly(ADP-ribose) glycohydrolase I
DNA
-
denatured; no inhibition by native DNA
DNA
-
denatured; no inhibition by native DNA
DNA
-
single-stranded DNA, no inhibition by double-stranded DNA
gallotannin
-
25% inhibition at 10 micorM in vitro, reduced cell death in HeLa cells at 3 and 6 h exposure
-
gallotannin
-
inhibition of enzyme activity. In presence of inhibitor, reduction of cell death after exposure to hydrogen peroxide, N-methyl-D-aspartate, or N-methyl-N-nitro-N-nitrosoguanidine
-
guanosine cyclic 3':5'-monophosphate
-
-
guanosine cyclic 3':5'-monophosphate
-
10 mM, 42% inhibition
histone
-
lysine-rich histone of calf thymus
histone
-
histone f2a, f2b and f3. Inhibition by histone f2a is reversed by DNA
histone
-
histone H1, H2A, H2B, H3 and H4
histone
-
due to noncovalent interactions of the protein with free ADP-ribose polymers
histone
-
histone H1, H2A, H2B and H3
KCl
-
100 mM, 50% inhibition, poly(ADP-ribose) glycohydrolase II
N-tert-butyl-9,10-dioxo-9,10-dihydroanthracene-2-sulfonamide
PDD00013907, inhibition of enzyme PARG with the small molecule leads to poly(ADP-ribose) (PAR) chain persistence in intact cells, overview. It shows cellular activity and cytotoxicity in HeLa cells
N-tert-butyl-9,10-dioxo-9,10-dihydroanthracene-2-sulfonamide
-
NaCl
-
50-100 mM, poly(ADP-ribose) glycohydrolase II
NaCl
-
400 mM, 75% inhibition
NAD+
-
-
NAD+
-
10 mM, 40% inhibition
p-chloromercuribenzenesulfonate
-
-
p-chloromercuribenzenesulfonate
-
0.01 mM
phloxine B
-
-
Poly(A)
-
-
Poly(A)
-
inhibitory effect is eliminated when 250 mM KCl is present in the reaction mixture, inhibition is markedly diminished after hybridization with polyT
poly(I)
-
inhibitory effect is eliminated when 250 mM KCl is present in the reaction mixture, inhibition is markedly diminished after hybridization with polyC
poly(L-Lys)
-
-
protamine
-
-
additional information
-
not inhibitory: ADP, pyrrolidine
-
additional information
-
gallotannin is a complex mixture of hydrolysable tannins, gallic acid and various galloyl glucose derivatives with up to 12 galloyl residues, from oak gall, that inhibits PARG; no inhibitory effect of 100 microM gallic acid, of 10 microM methyl gallate, of 10 microM 2,3-digalloyl-D-glucose, of 10 microM 2,3-digalloyl-O-methyl-D-glucose, of 10 microM 2,3-hexahydroxydiphenoyl-D-glucose, of 10 microM 2,3-di(3-galloyl,4,5-dihydroxy-benzoyl)-D-glucose, of 10 microM epigallocatechin gallate, and of 10 and 100 microM 3-galloyl-1,2-O-isopropylidene-alpha-D-glucose in vitro, the latter can act in vivo as cell-permeable precursor of 3-D-galloyl-D-glucose preventing poly(ADP-ribose) degradation, reduced cell death in HeLa cells at 3 and 6 h exposure (10 or 100 microM), cell death induction by methylating agent 1-methyl-3-nitro-1-nitrosoguanidine (100 microM), increased intracellular NAD content without 1-methyl-3-nitro-1-nitrosoguanidine, no effect in the presence of this agent
-
additional information
-
inhibition of PARG in HeLa cells treated with 50 microM cell death inducing alkylating agent N-methyl-N'-nitro-N'-nitrosoguanidine leads (MNNG) increases poly(ADP-ribose) levels beyond control, untreated and MNNG-treated PARG-silenced cells show a tendency to larger amounts of long (more than 20 ADP-ribose units) polymers, and a slight increase in short and medium long polymers, however PARG-silencing has no effect on cell death, no effect on translocation of apoptosis-inducing factor (AIF) into nucleus
-
additional information
-
not inhibited by benzamide, 3,5-dichloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)benzamide, 3,5-dichloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-methoxybenzamide, 2,4-dichloro-6-((3-chloro-4-(naphthalen-2-yloxy)phenylimino)methyl)phenol, 2,4-dichloro-6-((3-chloro-4-(naphthalen-2-yloxy)phenylamino)methyl)phenol, 3,5-dichloro-2-hydroxybenzamide, 3,5-dichloro-N-(3-chloro-4-hydroxyphenyl)-2-hydroxybenzamide, and 3,5-dichloro-2-hydroxy-N-benzamide
-
additional information
-
small molecule inhibitor screening, detection of rhodamine-based enzyme inhibitors (RBPIs), 3-[(5Z)-5-[1-(2-fluorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid and (3Z)-1-(2-fluorobenzyl)-3-[4-oxo-3-[2-(1H-tetrazol-5-yl)ethyl]-2-thioxo-1,3-thiazolidin-5-ylidene]-1,3-dihydro-2H-indol-2-one are inactive, RBPIs do not inhibit beta-lactamase, ADP-ribosylhydrolase 3, or poly(ADP-ribose) polymerase 1. No inhibiiton by DMO
-
additional information
structure-activity relationship analysis of the enzyme inhibitors by isothermal titration calorimetry and surface plasmon resonance, molecular modelling, overview
-
additional information
-
structure-activity relationship analysis of the enzyme inhibitors by isothermal titration calorimetry and surface plasmon resonance, molecular modelling, overview
-
additional information
first-in-class chemical probes against poly(ADP-ribose) glycohydrolase (PARG) inhibit DNA repair with differential pharmacology to poly(ADP-ribose) polymerase (PARP) inhibitor olaparib. No inhibition of PARG by 1-[(1,3-dimethyl-1H-pyrazol-5-yl)methyl]-N-methyl-N-(1-methylcyclopropyl)-3-[(2-methyl-1,3-thiazol-5-yl)methyl]-2,4-dioxo-1,2,3,4-tetrahydroquinazoline-6-sulfonamide and 1-[(2,4-dimethyl-1,3-thiazol-5-yl)methyl]-N-methyl-N-(1-methylcyclopropyl)-2-oxo-3-(1,2,4-thiadiazol-5-yl)-2,3-dihydro-1H-benzimidazole-5-sulfonamide. Cytotoxicity measurements of inhibitors with different cell lines
-
additional information
development of a high-throughput homogeneous time-resolved fluorescence (HTRF) assay method allows high-throughput screening for the identification and advancement of multiple validated series of tool compounds for PARG inhibition
-
additional information
-
development of a high-throughput homogeneous time-resolved fluorescence (HTRF) assay method allows high-throughput screening for the identification and advancement of multiple validated series of tool compounds for PARG inhibition
-
additional information
specific killing of DNA damage-response deficient cells with inhibitors of poly(ADP-ribose) glycohydrolase. Single treatment therapy with PARG inhibitors can be used for treatment of certain homologous recombination-deficient tumours and provide insight into the relationship between poly(ADP-ribose) polymerase (PARP), PARG and the processes of DNA repair
-
additional information
discovery and optimization of orally bioavailable quinazolinedione sulfonamides as cell-active small molecule inhibitors of DNA-damage repair enzyme poly(ADP-ribose) glycohydrolase (PARG), structure-based virtual screening and library design, overview. Physicochemical properties of 8a and 12b. Structure-activity relationships, cytotoxicity in HeLa cells, selectivity, and EC50 values, overview
-
additional information
-
discovery and optimization of orally bioavailable quinazolinedione sulfonamides as cell-active small molecule inhibitors of DNA-damage repair enzyme poly(ADP-ribose) glycohydrolase (PARG), structure-based virtual screening and library design, overview. Physicochemical properties of 8a and 12b. Structure-activity relationships, cytotoxicity in HeLa cells, selectivity, and EC50 values, overview
-
additional information
ibrutinib synergizes with poly(ADP-ribose) glycohydrolase inhibitors to induce cell death in AML cells via a Bruton's tyrosine kinase (BTK)-independent mechanism, synergistic cytotoxicity of ibrutinib and ethacridine. The ibrutinib-ethacridine combination is preferentially cytotoxic to a subset of primary AML cells compared to normal hematopoietic cells. The inhibitory effect of ibrutinib against BTK, as knockdown of BTK does not sensitize TEX and OCI-AML2 cells to ethacridine treatment
-
additional information
the N-terminal regulatory fragment can activate in trans the inactive enzyme fragment depleted with this segment. This suggests that, whereas the enzyme activity can be inhibited by disrupting the docking of this segment to its enzyme binding groove (via posttranslational modification or protein-proteins interactions), the enzyme can be reversibly activated once the disruptive factor is removed
-
additional information
-
the N-terminal regulatory fragment can activate in trans the inactive enzyme fragment depleted with this segment. This suggests that, whereas the enzyme activity can be inhibited by disrupting the docking of this segment to its enzyme binding groove (via posttranslational modification or protein-proteins interactions), the enzyme can be reversibly activated once the disruptive factor is removed
-
additional information
-
design and synthesis of phenolic hydrazide hydrazones as potent poly(ADP-ribose) glycohydrolase inhibitors, molecular docking analyses, overview
-
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Adenocarcinoma
Combined Targeting of PARG and Wee1 Causes Decreased Cell Survival and DNA Damage in an S-Phase-Dependent Manner.
Adenomatous Polyps
Aberration of poly(adenosine diphosphate-ribose) metabolism in human colon adenomatous polyps and cancers.
Ataxia
Bi-allelic ADPRHL2 Mutations Cause Neurodegeneration with Developmental Delay, Ataxia, and Axonal Neuropathy.
Ataxia
Biallelic Mutations in ADPRHL2, Encoding ADP-Ribosylhydrolase 3, Lead to a Degenerative Pediatric Stress-Induced Epileptic Ataxia Syndrome.
Ataxia
Episodic psychosis, ataxia, motor neuropathy with pyramidal signs (PAMP syndrome) caused by a novel mutation in ADPRHL2 (AHR3).
Ataxia
[Pediatric stress-induced epileptic ataxia syndrome caused by ADPRHL2 gene variation].
Breast Neoplasms
Global analysis of transcriptional regulation by poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase in MCF-7 human breast cancer cells.
Breast Neoplasms
Silencing of Apoptosis-Inducing factor and poly(ADP-ribose) glycohydrolase reveals novel roles in breast cancer cell death after chemotherapy.
Breast Neoplasms
Variations in the mRNA expression of poly(ADP-ribose) polymerases, poly(ADP-ribose) glycohydrolase and ADP-ribosylhydrolase 3 in breast tumors and impact on clinical outcome.
Carcinogenesis
Non-NAD-like PARP-1 inhibitors in prostate cancer treatment.
Carcinogenesis
Poly (ADP-ribose) glycohydrolase silencing-mediated maintenance of H2A and downregulation of H2AK9me protect human bronchial epithelial cells from benzo(a)pyrene-induced carcinogenesis.
Carcinogenesis
Poly(ADP-ribose) glycohydrolase silencing down-regulates TCTP and Cofilin-1 associated with metastasis in benzo(a)pyrene carcinogenesis.
Carcinogenesis
Poly(ADP-ribose) glycohydrolase silencing-mediated H2B expression inhibits benzo(a)pyrene-induced carcinogenesis.
Carcinogenesis
Poly(ADP-ribosyl)ation in relation to cancer and autoimmune disease.
Carcinogenesis
Regulation of Wnt Singaling Pathway by Poly (ADP-Ribose) Glycohydrolase (PARG) Silencing Suppresses Lung Cancer in Mice Induced by Benzo(a)pyrene Inhalation Exposure.
Carcinoma
Progression of Human Renal Cell Carcinoma via Inhibition of RhoA-ROCK Axis by PARG1.
Carcinoma
Silencing PARG decreases invasion in CT26 cells.
Carcinoma
Tannic acid, an inhibitor of poly(ADP-ribose) glycohydrolase, sensitizes ovarian carcinoma cells to cisplatin.
Carcinoma, Renal Cell
Progression of Human Renal Cell Carcinoma via Inhibition of RhoA-ROCK Axis by PARG1.
Chagas Disease
Host cell poly(ADP-ribose) glycohydrolase is crucial for Trypanosoma cruzi infection cycle.
Colonic Neoplasms
Silencing Poly (ADP-Ribose) Glycohydrolase (PARG) Expression Inhibits Growth of Human Colon Cancer Cells In Vitro via PI3K/Akt/NF?-B Pathway.
Colorectal Neoplasms
Combined Targeting of PARG and Wee1 Causes Decreased Cell Survival and DNA Damage in an S-Phase-Dependent Manner.
Glioma
Expression and activity of poly(ADP-ribose) glycohydrolase in cultured astrocytes, neurons, and C6 glioma cells.
Herpes Simplex
Herpes simplex virus 1 infection activates poly(ADP-ribose) polymerase and triggers the degradation of poly(ADP-ribose) glycohydrolase.
Hypersensitivity
Hypersensitivity to DNA double-strand breaks associated with PARG deficiency is suppressed by exo-1 and polq-1 mutations in Caenorhabditis elegans.
Infections
Herpes simplex virus 1 infection activates poly(ADP-ribose) polymerase and triggers the degradation of poly(ADP-ribose) glycohydrolase.
Infections
Host cell poly(ADP-ribose) glycohydrolase is crucial for Trypanosoma cruzi infection cycle.
Inflammatory Bowel Diseases
Role of poly(ADP-ribose) glycohydrolase in the development of inflammatory bowel disease in mice.
Leukemia
Ibrutinib synergizes with poly(ADP-ribose) glycohydrolase inhibitors to induce cell death in AML cells via a BTK-independent mechanism.
Leukemia, Myeloid, Acute
Erlotinib synergizes with the poly(ADP-ribose) glycohydrolase inhibitor ethacridine in acute myeloid leukemia cells.
Leukemia, T-Cell
Inhibitory effect of tannic acid on human immunodeficiency virus promoter activity induced by 12-O-tetra decanoylphorbol-13-acetate in Jurkat T-cells.
Lung Neoplasms
Dysfunction of Poly (ADP-Ribose) Glycohydrolase Induces a Synthetic Lethal Effect in Dual Specificity Phosphatase 22-Deficient Lung Cancer Cells.
Lung Neoplasms
Regulation of Wnt Singaling Pathway by Poly (ADP-Ribose) Glycohydrolase (PARG) Silencing Suppresses Lung Cancer in Mice Induced by Benzo(a)pyrene Inhalation Exposure.
Lung Neoplasms
Silencing of poly(ADP-ribose) glycohydrolase sensitizes lung cancer cells to radiation through the abrogation of DNA damage checkpoint.
Lymphoma, Mantle-Cell
Promoter methylation of PARG1, a novel candidate tumor suppressor gene in mantle-cell lymphomas.
Melanoma
Poly(ADP-ribose) glycohydrolase inhibitor as chemosensitiser of malignant melanoma for temozolomide.
Neoplasm Metastasis
Poly(ADP-ribose) glycohydrolase silencing down-regulates TCTP and Cofilin-1 associated with metastasis in benzo(a)pyrene carcinogenesis.
Neoplasms
A macrocircular ellagitannin, oenothein B, suppresses mouse mammary tumor gene expression via inhibition of poly(ADP-ribose) glycohydrolase.
Neoplasms
Aberration of poly(adenosine diphosphate-ribose) metabolism in human colon adenomatous polyps and cancers.
Neoplasms
Decreasing P-selectin and ICAM-1 via activating Akt: a possible mechanism by which PARG inhibits adhesion of mouse colorectal carcinoma CT26 cells to platelets.
Neoplasms
Enhanced DNA accessibility and increased DNA damage induced by the absence of poly(ADP-ribose) hydrolysis.
Neoplasms
Identification of Mitochondrial-Related Prognostic Biomarkers Associated With Primary Bile Acid Biosynthesis and Tumor Microenvironment of Hepatocellular Carcinoma.
Neoplasms
Inhibition of poly(ADP-ribose) glycohydrolase (PARG) specifically kills BRCA2-deficient tumor cells.
Neoplasms
Mouse mammary tumor virus gene expression is suppressed by oligomeric ellagitannins, novel inhibitors of poly(ADP-ribose) glycohydrolase.
Neoplasms
PARP and PARG inhibitors in cancer treatment.
Neoplasms
PARP and PARG Inhibitors-New Therapeutic Targets in Cancer Treatment.
Neoplasms
Poly(ADP-ribose) glycohydrolase inhibition sequesters NAD+ to potentiate the metabolic lethality of alkylating chemotherapy in IDH mutant tumor cells.
Neoplasms
Progression of Human Renal Cell Carcinoma via Inhibition of RhoA-ROCK Axis by PARG1.
Neoplasms
Promoter methylation of PARG1, a novel candidate tumor suppressor gene in mantle-cell lymphomas.
Neoplasms
Selective Loss of PARG Restores PARylation and Counteracts PARP Inhibitor-Mediated Synthetic Lethality.
Neoplasms
Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death.
Neoplasms
Silencing Poly (ADP-Ribose) Glycohydrolase (PARG) Expression Inhibits Growth of Human Colon Cancer Cells In Vitro via PI3K/Akt/NF?-B Pathway.
Neoplasms
Targeting poly(ADP-ribose) glycohydrolase to draw apoptosis codes in cancer.
Neoplasms
Variations in the mRNA expression of poly(ADP-ribose) polymerases, poly(ADP-ribose) glycohydrolase and ADP-ribosylhydrolase 3 in breast tumors and impact on clinical outcome.
Neurodegenerative Diseases
Bi-allelic ADPRHL2 Mutations Cause Neurodegeneration with Developmental Delay, Ataxia, and Axonal Neuropathy.
Osteosarcoma
Hydrogen peroxide-induced poly(ADP-ribosyl)ation regulates osteogenic differentiation-associated cell death.
Ovarian Neoplasms
DNA Replication Vulnerabilities Render Ovarian Cancer Cells Sensitive to Poly(ADP-Ribose) Glycohydrolase Inhibitors.
Placenta, Retained
Poly(ADP-ribose) glycohydrolase in bovine retained and not retained placenta.
poly(adp-ribose) glycohydrolase deficiency
Poly(ADP-ribose) Glycohydrolase deficiency sensitizes mouse ES cells to DNA damaging agents.
Prostatic Neoplasms
Androgen Receptor and Poly(ADP-ribose) Glycohydrolase Inhibition Increases Efficiency of Androgen Ablation in Prostate Cancer Cells.
Retinitis
Parthanatos-associated proteins are stimulated intraocularly during development of experimental murine cytomegalovirus retinitis in mice with retrovirus-induced immunosuppression.
Seizures
Bi-allelic ADPRHL2 Mutations Cause Neurodegeneration with Developmental Delay, Ataxia, and Axonal Neuropathy.
Seizures
Episodic psychosis, ataxia, motor neuropathy with pyramidal signs (PAMP syndrome) caused by a novel mutation in ADPRHL2 (AHR3).
Spinal Cord Injuries
Poly(ADP-Ribose) Glycohydrolase Activity Mediates Post-Traumatic Inflammatory Reaction after Experimental Spinal Cord Trauma.
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0.0045
(3Z)-5-bromo-1-(2,6-dichlorobenzyl)-3-[4-oxo-3-[2-(1H-tetrazol-5-yl)ethyl]-2-thioxo-1,3-thiazolidin-5-ylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH not specified in the publication, 37°C
0.0123
(3Z)-5-chloro-1-(2,6-dichlorobenzyl)-3-[4-oxo-3-[2-(1H-tetrazol-5-yl)ethyl]-2-thioxo-1,3-thiazolidin-5-ylidene]-1,3-dihydro-2H-indol-2-one
Homo sapiens
-
pH not specified in the publication, 37°C
0.000026
1-[(1,3-dimethyl-1H-pyrazol-5-yl)methyl]-N-(1-methylcyclopropyl)-3-[(2-methyl-1,3-thiazol-5-yl)methyl]-2,4-dioxo-1,2,3,4-tetrahydroquinazoline-6-sulfonamide
Homo sapiens
pH 7.4, 22°C
0.00004
1-[(2,4-dimethyl-1,3-thiazol-5-yl)methyl]-N-(1-methylcyclopropyl)-2-oxo-3-(1,2,4-thiadiazol-5-yl)-2,3-dihydro-1H-benzimidazole-5-sulfonamide
Homo sapiens
pH 7.4, 22°C
0.072
2-(3-chloro-4-(naphthalen-2-yloxy)phenylcarbamoyl)benzoic acid
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.025
3,5-dichloro-2-hydroxy-N-(3-methyl-4-(naphthalen-2-yloxy)phenyl)benzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.021
3,5-dichloro-2-hydroxy-N-(4-(naphthalen-2-yloxy)-3-(trifluoromethyl)phenyl)benzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.042
3,5-dichloro-2-hydroxy-N-(4-(naphthalen-2-yloxy)phenyl)benzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.14
3,5-dichloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxy-N-methylbenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.012
3,5-dichloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.026
3,5-dichloro-N-(3-chloro-4-(p-tolyloxy)phenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.061
3,5-dichloro-N-(3-chloro-4-phenoxyphenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.261
3,5-dichloro-N-(3-chlorophenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.027
3,5-dichloro-N-(3-fluoro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.5
3,5-dichloro-N-(4-chlorophenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.012
3,5-dichloro-N-[3-chloro-4-(naphthalen-2-yloxy)phenyl]-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.022
3-bromo-5-chloro-N-[5-chloro-2-[(1-chloronaphthalen-2-yl)oxy]phenyl]-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.026
3-bromo-N-[2-[2-bromo-6-methyl-3-(propan-2-yl)phenoxy]-5-chlorophenyl]-5-chloro-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.061
3-chloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.95
3-galloyl-D-glucose
Bos taurus
-
enzyme for 240 min at 37°C
0.0465
3-[(5Z)-5-[1-(2-chlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH not specified in the publication, 37°C
0.0029
3-[(5Z)-5-[5-bromo-1-(2,6-dichlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH not specified in the publication, 37°C
0.003
3-[(5Z)-5-[5-bromo-1-(2-chloro-6-fluorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH not specified in the publication, 37°C
0.0058
3-[(5Z)-5-[5-chloro-1-(2,6-dichlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
pH not specified in the publication, 37°C
0.117
5-chloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.0163
8-n-octyl-amino-adenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
Homo sapiens
with wild-type enzyme, pH 7.0, 25°C
0.0011 - 0.0031
adenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
0.00012
adenosine 5'-diphosphate-(hydroxymethyl)-pyrrolidinediol
Mus musculus
pH and temperature not specified in the publication
0.0001
adenosine diphosphate (hydroxymethyl) pyrrolidinediol
Rattus norvegicus
-
pH 7.5, 37°C
0.00066
adenosine diphosphate (hydroxymethyl)pyrrolidinediol
Bos taurus
-
37°C
0.00012
ADP-(hydroxymethyl)pyrrolidinediol
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
3.2
ADP-HPD
Bos taurus
-
enzyme for 240 min at 37°C
0.0019
eosine Y
Bos taurus
-
37°C
7.2
methyl 2-O-galloyl-beta-D-glucoside
Bos taurus
-
enzyme for 240 min at 37°C
7.1
methyl 3-O-galloyl-beta-D-glucoside
Bos taurus
-
enzyme for 240 min at 37°C
0.0031
N'',N'''-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]carbonohydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.0028
N'',N'''-bis[(E)-(3,4,5-trihydroxyphenyl)methylidene]carbonohydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.0016
N'1,N'3-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]propanedihydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.0154
N'1,N'3-bis[(E)-(3,4,5-trihydroxyphenyl)methylidene]propanedihydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.0098
N'1,N'4-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]butanedihydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.0082
N'1,N'4-bis[(E)-(3,4,5-trihydroxyphenyl)methylidene]butanedihydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.0139
N'1,N'5-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]pentanedihydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.0274
N'1,N'5-bis[(E)-(3,4,5-trihydroxyphenyl)methylidene]pentanedihydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.0031
N'1-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-N'3-[(Z)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.001
N'1-[(E)-(2,3,4-trihydroxyphenyl)methylidene]-N'4-[(Z)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.0148
N'1-[(E)-(2,3-dihydroxyphenyl)methylidene]-N'3-[(Z)-(2,3-dihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.0188
N'1-[(E)-(2,4,6-trihydroxyphenyl)methylidene]-N'3-[(Z)-(2,4,6-trihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.0099
N'1-[(E)-(2,4,6-trihydroxyphenyl)methylidene]-N'4-[(Z)-(2,4,6-trihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.0401
N'1-[(E)-(2,4-dihydroxyphenyl)methylidene]-N'3-[(Z)-(2,4-dihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.0032
N'1-[(E)-(3,4,5-trihydroxyphenyl)methylidene]-N'3-[(Z)-(3,4,5-trihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.0021
N'1-[(E)-(3,4,5-trihydroxyphenyl)methylidene]-N'4-[(Z)-(3,4,5-trihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.0192
N'1-[(E)-(3,4-dihydroxyphenyl)methylidene]-N'3-[(Z)-(3,4-dihydroxyphenyl)methylidene]benzene-1,3-dicarbohydrazide
Rattus norvegicus
-
pH 7.5, 37°C
0.5
N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.06
N-tert-butyl-9,10-dioxo-9,10-dihydroanthracene-2-sulfonamide
Homo sapiens
pH 7.4, 22°C
0.08
N-[4-[(3-bromonaphthalen-2-yl)oxy]-3-chlorophenyl]-3,5-dichloro-2-hydroxybenzamide
Homo sapiens
-
in 150 mM potassium phosphate buffer, pH 7.5, 150 mM KCl, 0.3 mg/ml bovine serum albumin, and 30 mM 2-mercaptoethanol, at 37°C
0.0000026
PDD00017273
Homo sapiens
pH and temperature not specified in the publication
0.005
phloxine B
Bos taurus
-
37°C
0.0011
adenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
Homo sapiens
with mutant enzyme K616A/Q617A/K618A/E688A/K689A/K690A, pH 7.0, 25°C
0.0031
adenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
Homo sapiens
with wild-type enzyme, pH 7.0, 25°C
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evolution
canonical poly(ADP-ribose) glycohydrolase is a highly conserved protein found in organisms ranging from protozoa to humans, phylogenetic analysis. The full-length enzyme from Tetrahymena thermophila is highly similar to the minimal catalytic region of thhe human enzyme, but it lacks the obvious RS/MTS motif
evolution
conservation of key residues involved in the catalytic process
evolution
conservation of overall fold amongst mammalian enzyme glycohydrolase domains, additional flexible regions in the catalytic site, overview
evolution
full-length ARH3 (ARH3FL) adopts a compact all-alpha-helical fold with a central deep ADPR-binding cleft, a signature of the ARH3 superfamily
evolution
function and domain architecture of human ADP-ribosylation removing enzymes, overview. The key poly(ADP-ribose) (PAR) processing enzyme, PARG, emerged only recently
malfunction
-
osmotic (mannitol treatment) or oxidative (methyl viologen treatment) stress reduces germination rates of the mutant parg1-3 seeds compared with wild type seeds. The parg1-3 plants show reduced tolerance to drought (withholding water), osmotic, and oxidative stress, as well as increased levels of cell damage under osmotic and oxidative stress and reduced survival under drought stress when compared with the wild type plants. Stomata of the parg1-3 plants fail to close under drought stress conditions
malfunction
benzo(a)pyrene induces the cell cycle in enzyme-suppressed shPARG cells, phenotype, overview
malfunction
enzyme deficiency leads to cell death whilst enzyme depletion causes sensitisation to certain DNA damaging agents
malfunction
-
genetic disruption of the enzyme leads to increased level of cell death by accumulation of poly(ADP-ribose)
malfunction
-
knockout mutants of isozyme PARG110 show resistance to photoreceptor degeneration, the mutant retina is morphologically and functionally undistinguishable from wild-type. Absence of PARG110 disrupts the poly-ADP-ribose polymerase activation
malfunction
lack of poly(ADPribose) glycohydrolase activity in Vero and A549 host cells, achieved by chemical inhibition or iRNA, produces the reduction of the percentage of infected cells as well as the number of amastigotes per cell and trypomastigotes released, leading to a nearly complete abrogation of the infection process
malfunction
-
poly(ADP-ribose) glycohydrolase loss-of-function causes increased Hrp38 poly(ADP-ribosyl)ation and also results in the rough-eye phenotype with disrupted ommatidial lattice and and bristles and reduced number of photoreceptor cells. Hrp38 is essential for fly eye development. Parg mutant eye clones have decreased expression level of DE-cadherin with orientation defects, which is reminiscent of DE-cadherin mutant eye phenotype. The Parg mutant eye accumulates a large amount of poly(ADP-ribose)
malfunction
-
RNAi knockdown of PARG or pretreatment with 2-((R)-2-methylpyrrolidin-2-yl)-1H-benzimidazole-4-carboxamide (ABT-888), meaning an increase in poly(ADP-ribose) level, lead to increased HeLa cell death in N-methyl-N'-nitro-N-nitrosoguanidine-treated HeLa cells. The effect can be reduced by PARP-1 inhibitors. Combination of poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase inhibition in chemotherapy does not produce increased HeLa cell death
malfunction
-
silencing of endogenous enzyme expression causes inhibition of TGFbeta-mediated transcription. This can be relieved after simultaneous depletion of poly(ADP-ribose) polymerase 1
malfunction
a deficiency in PARG glycohydrolase activity prolongs DNA damage foci, containing PAR, and similarly delays DNA repair, causing hypersensitivity to DNA damaging agents and selective killing of repair-deficient tumors such as BRCA mutated breast cancers-deficient cancer cells in a manner similar to PARP inhibition
malfunction
disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. Endogenous PAR levels in Deinococcus radiodurans are elevated after UV irradiation, indicating that the prokaryotic PARylation may be involved in resistance to genotoxic stresses
malfunction
mutation of PARG1 results in increased DNA damage level and enhanced cell death in plants after bleomycin treatment. Inhibition or silencing of PARPs improves abiotic stress tolerance, enhancing resistance to drought, high light, heat and oxidative stresses, and perturbs innate immune responses to microbe-associated molecular patterns such as flg22 and elf18, resulting in a compromised basal defense response. Phenotypic comparison of the loss-of-function mutants of all PARP and PARG genes in Arabidopsis thaliana, overview. Loss-of-PARG1 leads to the transcriptional up-regulation of DNA repair genes and increase of cellular DNA damage level. The parg1 mutants show only yellow instead of green seedlings with reduced fresh weight compared to wild-type. The parg1-4 mutant root is more sensitive to bleomycin than that of wild-type Col-0
malfunction
PARG inhibition increases endogenous DNA damage, stalls replication forks and increases homologous recombination, and the lack of homologous recombination (HR) proteins at PARG inhibitor-induced stalled replication forks induces cell death. siRNA screen for increased DNA damage with PARG depletion. Model whereby inhibition or depletion of PARG leads to fork stalling and fork aberrations, resulting in signalling and recruitment of HRR proteins for repair. Therefore in the absence of these homologous recombination repair (HRR) proteins, PARG depleted or inhibited cells cannot survive
malfunction
poly(ADP-ribose) glycohydrolase (PARG) silencing suppresses benzo(a)pyrene induced cell transformation. Benzo(a)pyrene (BaP) is a ubiquitously distributed environmental pollutant and known carcinogen, which can induce malignant transformation in cells. PARG silencing dramatically reduces DNA damages, chromosome abnormalities, and micronuclei formations in the PARG-deficient human bronchial epithelial cells compared to the control 16HBE cells. PARG silencing down-regulates cell colony formation induced by BaP, reduces BaP-induced genomic instability, and protects cells from BaP-induced DNA damage
malfunction
poly(ADP-ribosyl) glycohydrolase (PARG) depletion affects cell proliferation and DNA synthesis, leading to replication-coupled H2AX phosphorylation. PARG depletion or inhibition per se slows down individual replication forks similarly to mild chemotherapeutic treatment. Electron microscopic analysis of replication intermediates reveals marked accumulation of reversed forks and single-stranded DNA (ssDNA) gaps in unperturbed PARG-defective cells. PARG-defective cells display both ataxia-telangiectasia-mutated (ATM) and ataxia-Rad3-related (ATR) activation, as well as chromatin recruitment of standard double-strand-break-repair factors, such as 53BP1 and RAD51, but no physical evidence for chromosomal breakage. PARG-deficient cell phenotype, detailed overview. PARG depletion results in slow replication fork progression even in the absence of genotoxic treatments. PARG downregulation and inhibition lead to similar phenotypic consequences
malfunction
the wild-type strain with or without H2O2 shows no evident changes in the randomly amplified polymorphic DNA, RAPD, pattern. The mutant DELTAparg strain, in the presence of H2O2, exhibits a reduced pattern, suggesting that DNA is damaged in this strain and repair is impaired. No morphological differences in color, growth rate or morphology are observed for the mutant strain on solid medium as compared with the wild-type strain
malfunction
-
the wild-type strain with or without H2O2 shows no evident changes in the randomly amplified polymorphic DNA, RAPD, pattern. The mutant DELTAparg strain, in the presence of H2O2, exhibits a reduced pattern, suggesting that DNA is damaged in this strain and repair is impaired. No morphological differences in color, growth rate or morphology are observed for the mutant strain on solid medium as compared with the wild-type strain
-
malfunction
-
disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. Endogenous PAR levels in Deinococcus radiodurans are elevated after UV irradiation, indicating that the prokaryotic PARylation may be involved in resistance to genotoxic stresses
-
malfunction
-
the wild-type strain with or without H2O2 shows no evident changes in the randomly amplified polymorphic DNA, RAPD, pattern. The mutant DELTAparg strain, in the presence of H2O2, exhibits a reduced pattern, suggesting that DNA is damaged in this strain and repair is impaired. No morphological differences in color, growth rate or morphology are observed for the mutant strain on solid medium as compared with the wild-type strain
-
malfunction
-
the wild-type strain with or without H2O2 shows no evident changes in the randomly amplified polymorphic DNA, RAPD, pattern. The mutant DELTAparg strain, in the presence of H2O2, exhibits a reduced pattern, suggesting that DNA is damaged in this strain and repair is impaired. No morphological differences in color, growth rate or morphology are observed for the mutant strain on solid medium as compared with the wild-type strain
-
malfunction
-
the wild-type strain with or without H2O2 shows no evident changes in the randomly amplified polymorphic DNA, RAPD, pattern. The mutant DELTAparg strain, in the presence of H2O2, exhibits a reduced pattern, suggesting that DNA is damaged in this strain and repair is impaired. No morphological differences in color, growth rate or morphology are observed for the mutant strain on solid medium as compared with the wild-type strain
-
malfunction
-
mutation of PARG1 results in increased DNA damage level and enhanced cell death in plants after bleomycin treatment. Inhibition or silencing of PARPs improves abiotic stress tolerance, enhancing resistance to drought, high light, heat and oxidative stresses, and perturbs innate immune responses to microbe-associated molecular patterns such as flg22 and elf18, resulting in a compromised basal defense response. Phenotypic comparison of the loss-of-function mutants of all PARP and PARG genes in Arabidopsis thaliana, overview. Loss-of-PARG1 leads to the transcriptional up-regulation of DNA repair genes and increase of cellular DNA damage level. The parg1 mutants show only yellow instead of green seedlings with reduced fresh weight compared to wild-type. The parg1-4 mutant root is more sensitive to bleomycin than that of wild-type Col-0
-
malfunction
-
disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. Endogenous PAR levels in Deinococcus radiodurans are elevated after UV irradiation, indicating that the prokaryotic PARylation may be involved in resistance to genotoxic stresses
-
malfunction
-
disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. Endogenous PAR levels in Deinococcus radiodurans are elevated after UV irradiation, indicating that the prokaryotic PARylation may be involved in resistance to genotoxic stresses
-
malfunction
-
disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. Endogenous PAR levels in Deinococcus radiodurans are elevated after UV irradiation, indicating that the prokaryotic PARylation may be involved in resistance to genotoxic stresses
-
malfunction
-
disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. Endogenous PAR levels in Deinococcus radiodurans are elevated after UV irradiation, indicating that the prokaryotic PARylation may be involved in resistance to genotoxic stresses
-
malfunction
-
disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. Endogenous PAR levels in Deinococcus radiodurans are elevated after UV irradiation, indicating that the prokaryotic PARylation may be involved in resistance to genotoxic stresses
-
malfunction
-
disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. Endogenous PAR levels in Deinococcus radiodurans are elevated after UV irradiation, indicating that the prokaryotic PARylation may be involved in resistance to genotoxic stresses
-
malfunction
-
disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. Endogenous PAR levels in Deinococcus radiodurans are elevated after UV irradiation, indicating that the prokaryotic PARylation may be involved in resistance to genotoxic stresses
-
metabolism
-
isozyme PARG110 and poly-ADP-ribose polymerase-1 act in a positive feedback loop, which is especially active under pathologic conditions
metabolism
-
molecular mechanism(s) connecting poly(ADP-ribosyl)ation with DNA methylation, giving a possible explanation as to how DNA methylation modulates by poly(ADP-ribosyl)ation as the posttranslational modification. DNA methyltransferases also interact with poly(ADP-D-ribose)
metabolism
-
poly(ADP-ribose) glycohydrolase partly controls the turnover of dynamic protein ADP-ribosylation mediated by poly(ADP-ribose) polymerase 1, PARP-1. Poly(ADP-ribose) glycohydrolase (PARG) can remove poly(ADP-ribose) chains from target proteins of PARP-1. Endogenous PARP-1 and the enzyme have opposing roles on TGFbeta-induced gene expression, overview
metabolism
PARP-dependent ADP-ribosylation cycle involving enzyme PARG
metabolism
poly(ADP-ribosyl)ation is a reversible post-translational modification of proteins, characterized by the addition of poly(ADP-ribose) (PAR) to proteins by poly(ADP-ribose) polymerase (PARP), and removal of PAR by poly(ADP-ribose) glycohydrolase (PARG). Three PARPs and two PARGs have been found in Arabidopsis thaliana. PARG1 and PARG2 play an essential and a minor role, respectively under the same conditions
metabolism
-
poly(ADP-ribosyl)ation is a reversible post-translational modification of proteins, characterized by the addition of poly(ADP-ribose) (PAR) to proteins by poly(ADP-ribose) polymerase (PARP), and removal of PAR by poly(ADP-ribose) glycohydrolase (PARG). Three PARPs and two PARGs have been found in Arabidopsis thaliana. PARG1 and PARG2 play an essential and a minor role, respectively under the same conditions
-
physiological function
-
generation of A549 lung adenocarcinoma cell lines with stably suppressed PARG and poly(ADP-ribose) polymerase PARP-1 expression, i.e. shPARG and shPARP1 cell lines, respectively. shPARG cells accumulate large amounts of poly-(ADP-ribosyl)ated proteins and exhibit reduced PARP activation. Hydrogen peroxide-induced cell death is regulated by PARG in a dual fashion. Whereas the shPARG cell line is resistant to the necrotic effect of high concentrations of hydrogen peroxide, these cells exhibit stronger apoptotic response. Both shPARP1 and especially shPARG cells display a delayed repair of DNA breaks and exhibit reduced clonogenic survival following hydrogen peroxide treatment. Translocation of apoptosis-inducing factor cannot be observed, but cells can be saved by methyl pyruvate and alpha-ketoglutarate
physiological function
-
homozygous T-DNA knockout line parg1 seedlings exhibit exaggerated seedling growth inhibition and pigment accumulation in response to elf18 and are hypersensitive to the DNA-damaging agent mitomycin C. Both parg1 and parg2 knockout plants show accelerated onset of disease symptoms when infected with Botrytis cinerea. Cellular levels of ADP-ribose polymer increase after infection with avirulent Pseudomonas syringae pv tomato DC3000 avrRpt2+, and pathogen-dependent changes in the poly(ADP-ribosyl)ation of discrete proteins are also observed
physiological function
-
stable knock-down of poly(ADP-ribose) polymerase PARP-1 and PARG. The majority of genes affected by the knockdown of one factor are similarly affected by the knockdown of the other factor. The most robustly regulated common genes are enriched for stress-response and metabolic functions. PARP-1 and PARG localize to the promoters of positively and negatively regulated target genes. The levels of chromatin-bound PARG at a given promoter generally correlate with the levels of PARP-1 across the subset of promoters tested. For about half of the genes tested, the binding of PARP-1 at the promoter is dependent on the binding of PARG. PARP-1 and PARG enzymatic activities are required for some, but not all, target genes
physiological function
-
Arabidopsis poly(ADP-ribose) glycohydrolase 1 is required for drought, osmotic and oxidative stress responses
physiological function
-
at higher levels of DNA damage, the coordinate activities of PARPs-1/2 and PARG can rapidly deplete the pool of cellular NAD(H), facilitating the release of mitochondrial proteins through signaling pathways that promote cell death
physiological function
-
coordinate regulation of PARP-1 and -2 and PARG is required for cellular responses to genotoxic stress
physiological function
-
poly(ADP-ribose)glycohydrolase is an upstream regulator of Ca2+ fluxes in oxidative cell death. Transient receptor potential 2 is the primary Ca2+ channel for cell death signaling under poly(ADP-ribose)glycohydrolase control
physiological function
-
by regulating the hydrolytic arm of poly(ADP-ribosyl)ation, the enzyme participates in a number of biological processes, including the repair of DNA damage, chromatin dynamics, transcriptional regulation, and cell death. Role of silencing of the enzyme in DNA methylation pattern changed by benzo(a)pyrene, a carcinogen cytotoxic which can trigger extensive cellular responses
physiological function
-
causal involvement of wild-type isozyme PARG110 in the process of photoreceptor degeneration. Contrasting its anticipated role as a functional antagonist, absence of PARG110 correlated with low PARP activity, suggesting that PARG110 and PARP1 act in a positive feedback loop, which is especially active under pathologic conditions
physiological function
poly(ADP-ribose) glycohydrolase (PARG) represents the main poly(ADP-D-ribose) hydrolyzing activity in the cell to ADP-ribose units. The enzyme is crucial for Trypanosoma cruzi infection cycle in the human host cell. Both, Trypanosoma cruzi and the human host, poly(ADP-ribose) glycohydrolase activities are important players in the life cycle of Trypanosoma cruzi
physiological function
poly(ADP-ribose) glycohydrolase catalyzes the removal of poly(ADP-ribose) chains from posttranslationally modified proteins by hydrolysis of alpha(122-22) O-glycosidic linkages, functioning as an endo-glycosidase to release oligo(ADP-ribose) and as an exo-glycosidase to release ADP-ribose
physiological function
poly(ADP-ribosyl)ation is a crucial regulator of cell fate in response to genotoxic stress, poly(ADP-ribose) degradation is carried out mainly by poly(ADP-ribose) glycohydrolase, role of poly(ADP-ribose) glycohydrolase in the regulation of cell fate in response to benzo(a)pyrene, overview
physiological function
protein poly(ADP-ribosyl)ation regulates a number of important cellular processes. Poly(ADP-ribose) glycohydrolase is the primary enzyme responsible for hydrolyzing the poly(ADP-ribose) polymer in vivo
physiological function
-
the enzyme activity regulates cellular poly(ADP-ribose) level. Since the enzyme cannot cleave the terminal ADP-ribose unit at the protein bound to glutamate residues, the residual activities of MacroD2 and TARG1 may contribute to the accumulation of poly(ADP-D-ribose)in the Parg knockout animals
physiological function
-
the enzyme is responsible for the degradation of poly(ADP-ribose) (PAR) polymers
physiological function
the reversion of poly(ADP-ribosyl)ation is catalysed by poly(ADP-ribose) glycohydrolase, which specifically targets the unique PAR (1''-2') ribose-ribose bonds
physiological function
a single poly(ADP-ribosyl) glycohydrolase (PARG) mediates PAR degradation. PARG prevents the accumulation of unusual replication structures during unperturbed S phase. Role of PARG in the replication of human chromosomes. PAR degradation is essential to promote resumption of replication at endogenous and e-exogenous lesions, preventing idle recruitment of repair factors to remodeled replication forks
physiological function
degradation of poly(ADP-ribose), PAR, is catalyzed by poly(ADP-ribose) glycohydrolase (PARG) by endo- and exoglycosidase reactions that release products of variable length and ADPribose monomers. The poly(ADP-ribosyl) glycohydrolase, PARG, protein of Fusarium oxysporum f. sp. lycopersici is involved in DNA repair and does not act in pathogenicity as an effector. The organism encodes for only one PARG enzyme, and this is responsible for the total cellular PARG activity
physiological function
enzyme ARH3 is a multifunctional enzyme that also hydrolyzes poly(ADP-ribose) (ADPR). Enzyme ARH3 plays a role in DNA damage repair. The recruitment of ARH3 to DNA lesions is mediated by ADPR recognition. The catalytic mechanism of protein ADP-ribose hydrolases can be classified into two different groups, namely metal-dependent and metal-independent catalysis. ARHs, such as ARH3, belong to metal-dependent catalysis, utilizing two Mg2+ ions and acidic residues to complete the catalytic reaction, which might be highly conserved. In contrast, the catalytic mechanism is not conserved in the macrodomain ADP-ribose hydrolases, For example, Glu756 and a water molecule act together to catalyze the reaction in PARG, whereas the key catalytic factor in MacroD2 is an activated water. The charge characteristic of the binding pocket in ARH3 is remarkably distinguished from that in PARG. The binding pocket of PARG, accommodating the ADPR dimer, is mostly composed of the basic region
physiological function
enzyme ARH3 is a multifunctional enzyme that also hydrolyzes poly(ADP-ribose) (PAR). ARH3 can specifically hydrolyze PAR, mono-ADP-ribose post-translational modifications (MARPTMs), and O-acetyl-ADP-ribose. For all these substrates, ARH3 preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADPR. In mammals, two enzymes, ADP-ribosyl-acceptor hydrolase 3 (ARH3 or ADPRHL2) and PAR glycohydrolase (PARG), function in tandem to reverse PARylation. These hydrolytic enzymes commonly cleave the alpha(1''-2') O-glycosidic linkages in PAR chains. ARH3 appears to catalyze primarily exocytic cleavage of PAR, generating free ADPR. It is reported that ARH3 protects cells from oxidative stress-induced parthanatos by lowering the cytoplasmic PAR level. ARH3 is a distinctive, multitasking enzyme that controls two biologically important NAD+-dependent cellular signaling pathways
physiological function
PARG1 has poly(ADP-ribose) (PAR)-degrading activity and regulates poly(ADP-ribose) level in vivo. PARG1 and PARG2 play an essential and a minor role, respectively under the same conditions. PARG1 expression is induced primarily in root and shoot meristems by bleomycin and induction of PARG1 is dependent on ATM and ATR kinases. PARG1 antagonistically modulates the DNA repair process by preventing the over-induction of DNA repair genes. PARG1 plays a critical role in this process. Roles of PARP1 and PARP2 in DNA damage signaling. Induction of PARG1 gene is ATM- and ATR-dependent and PARG1 represses the transcriptional upregulation of ATM, ATR and SOG1. ATM and ATR are two critical kinases which transduce double and single strand break signals to DNA repair machinery, respectively. They phosphorylate the transcription factor SOG1, which then induces the expression of DNA repair genes
physiological function
poly(ADP-ribosyl)ation (PARylation) is a transient posttranslational modification that generates a signaling mechanism with diverse roles within molecular and cellular processes. PAR chains remaining from DNA repair are broken down by the enzyme poly(ADP-ribose) glycohydrolase (PARG). PARG catalyzes the hydrolysis of endo- and exoglycosidic bonds within the poly(ADP-ribose) (PAR) polymers
physiological function
poly(ADP-ribosyl)ation is a common post-translational modification that mediates a wide variety of cellular processes including DNA damage repair, chromatin regulation, transcription, and apoptosis, involving interactions of PAR with poly(ADP-ribose) glycohydrolase (PARG) and other binding proteins
physiological function
poly(ADP-ribosylation) of proteins follows DNA damage. Like addition of poly(ADP-ribose) (PAR) by poly(ADP-ribose) polymerase (PARP), removal of PAR by PARG is also thought to be required for repair of DNA strand breaks and for con-tinued replication at perturbed forks. Poly(ADP-ribose) glycohydrolase (PARG) has endo- and exoglycosidase activities which can cleaveglycosidic bonds, rapidly reversing the action of PARP enzymes. The functions of PARP and PARG may not be completely identical
physiological function
poly(ADPribose) glycohydrolase (PARG) is the primary enzyme that catalyzes the degradation of poly (ADP-ribose) (PAR), it plays an important role in regulating DNA damage repair and maintaining genomic stability
physiological function
the enzyme poly(ADP-ribose) glycohydrolase (PARG) performs a critical role in the repair of DNA single strand breaks (SSBs). Critical to this repair process is the orderly degradation of PAR chains. The roles of PARG and poly(ADP-ribose) polymerase (PARP) are closely intertwined
physiological function
the PAR posttranslational modification by itself is a high affinity ligand for XRCC1, requiring a minimum chain length of 7 ADP-ribose units in the oligo(ADP-ribose) ligand for a stable interaction with XRCC1. This discrete binding interface enables the poly(ADP-ribose) (PAR) glycohydrolase (PARG) to completely disassemble the PARP1-XRCC1 complex without assistance from a mono(ADP-ribose) glycohydrolase. XRCC1 and other PAR-binding proteins mediate many of the downstream responses to PARP1 activation in the face of DNA damage. PARG rapidly reverses the PARylation of PARP1 and efficiently disassembles the PARP1-XRCC1 complex, thereby uncoupling the DNA repair scaffolding activities of XRCC1 from PARP1, which is targeted for proteasomal degradation after recruiting XRCC1 to sites of DNA damage. Ability of PARG to regulate the PARP1-XRCC1 interaction by converting PARylated PARP1 into MARylated PARP1, which retains a terminal ADP-ribose modification but does not bind to XRCC1
physiological function
the poly(ADP-ribose) glycohydrolase (PARG) endo-glycohydrolase activity may become significant in vivo at high PAR/PARG ratios (for example, in the case of an extreme cellular insult), thus releasing free PAR fragments to mediate apoptotic signaling
physiological function
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degradation of poly(ADP-ribose), PAR, is catalyzed by poly(ADP-ribose) glycohydrolase (PARG) by endo- and exoglycosidase reactions that release products of variable length and ADPribose monomers. The poly(ADP-ribosyl) glycohydrolase, PARG, protein of Fusarium oxysporum f. sp. lycopersici is involved in DNA repair and does not act in pathogenicity as an effector. The organism encodes for only one PARG enzyme, and this is responsible for the total cellular PARG activity
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physiological function
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degradation of poly(ADP-ribose), PAR, is catalyzed by poly(ADP-ribose) glycohydrolase (PARG) by endo- and exoglycosidase reactions that release products of variable length and ADPribose monomers. The poly(ADP-ribosyl) glycohydrolase, PARG, protein of Fusarium oxysporum f. sp. lycopersici is involved in DNA repair and does not act in pathogenicity as an effector. The organism encodes for only one PARG enzyme, and this is responsible for the total cellular PARG activity
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physiological function
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degradation of poly(ADP-ribose), PAR, is catalyzed by poly(ADP-ribose) glycohydrolase (PARG) by endo- and exoglycosidase reactions that release products of variable length and ADPribose monomers. The poly(ADP-ribosyl) glycohydrolase, PARG, protein of Fusarium oxysporum f. sp. lycopersici is involved in DNA repair and does not act in pathogenicity as an effector. The organism encodes for only one PARG enzyme, and this is responsible for the total cellular PARG activity
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physiological function
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degradation of poly(ADP-ribose), PAR, is catalyzed by poly(ADP-ribose) glycohydrolase (PARG) by endo- and exoglycosidase reactions that release products of variable length and ADPribose monomers. The poly(ADP-ribosyl) glycohydrolase, PARG, protein of Fusarium oxysporum f. sp. lycopersici is involved in DNA repair and does not act in pathogenicity as an effector. The organism encodes for only one PARG enzyme, and this is responsible for the total cellular PARG activity
-
physiological function
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PARG1 has poly(ADP-ribose) (PAR)-degrading activity and regulates poly(ADP-ribose) level in vivo. PARG1 and PARG2 play an essential and a minor role, respectively under the same conditions. PARG1 expression is induced primarily in root and shoot meristems by bleomycin and induction of PARG1 is dependent on ATM and ATR kinases. PARG1 antagonistically modulates the DNA repair process by preventing the over-induction of DNA repair genes. PARG1 plays a critical role in this process. Roles of PARP1 and PARP2 in DNA damage signaling. Induction of PARG1 gene is ATM- and ATR-dependent and PARG1 represses the transcriptional upregulation of ATM, ATR and SOG1. ATM and ATR are two critical kinases which transduce double and single strand break signals to DNA repair machinery, respectively. They phosphorylate the transcription factor SOG1, which then induces the expression of DNA repair genes
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additional information
E748 and E749 are the key catalytic residues in the signature loop, N733 directly recognizes the 3'-OH on the proximal ribose, catalytic domain structure in apo- and liganded-states, overview. The N-terminal flexible peptide preceding the enzyme's catalytic domain may regulate the enzymatic activity, catalytic and regulatory mechanisms, overview. A binding site outside of the catalytic cleft for iso-ADP-ribose, which is probably the smallest enzyme subtrate containing the alpha(1->2) ribose-ribose glycosidic bond, may explain the processivity of the enzyme activity
additional information
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E748 and E749 are the key catalytic residues in the signature loop, N733 directly recognizes the 3'-OH on the proximal ribose, catalytic domain structure in apo- and liganded-states, overview. The N-terminal flexible peptide preceding the enzyme's catalytic domain may regulate the enzymatic activity, catalytic and regulatory mechanisms, overview. A binding site outside of the catalytic cleft for iso-ADP-ribose, which is probably the smallest enzyme subtrate containing the alpha(1->2) ribose-ribose glycosidic bond, may explain the processivity of the enzyme activity
additional information
enzyme structure overview
additional information
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enzyme structure overview
additional information
enzyme structure-function relationship, computational analysis based on the crystal structure, PDB ID 3SIG, modelling of active site structure and SN2 mechanism catalytic mechanism, overview. The oxocarbenium expected by Dea Slade is a possible transition state but not an intermediate.
additional information
structure analysis and comparisons, overview. The poorly structured A-domain does not contribute to PARG activity in vitro. The rPARG385 catalytic domain adopts a beanshaped structure with a deep central cleft containing the conserved PARG-signature motif (GGG-X6-8-QEE)10 and Tyr791 that contributes strongly to PARG catalytic efficiency and inhibitor binding. The active site cleft lies on one edge of the beta-sheet and an extended N-terminal segment containing the MTS wraps around the other edge of the beta-sheet, contributing to the PARG catalytic domain
additional information
structure-based mechanism for the reported endo- and exo-glycohydrolase activities in human enzyme, overview
additional information
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structure-based mechanism for the reported endo- and exo-glycohydrolase activities in human enzyme, overview
additional information
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the Glu752 residue plays an important role in the enzyme's catalytic activity by functioning as a general acid or base to protonate the 2'-OH of the ribose of the leaving group, and subsequently activating a water molecule for nucleophilic attack
additional information
analysis of the catalytic site structure of ARH3, overview
additional information
CD spectra of enzyme DrPARG in the absence and presence of ADP-ribose exhibit increased proportion of alpha-helices and beta-strands from 11.78% and 30.37% to 15.10% and 33.52%, respectively, which suggests that conformational changes occur during the binding of ADP-ribose. The intrinsically disordered N-terminal region of DrPARG might be highly flexible. ADP-ribose binding pocket and complex structure, and conformational effects, detailed overview
additional information
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CD spectra of enzyme DrPARG in the absence and presence of ADP-ribose exhibit increased proportion of alpha-helices and beta-strands from 11.78% and 30.37% to 15.10% and 33.52%, respectively, which suggests that conformational changes occur during the binding of ADP-ribose. The intrinsically disordered N-terminal region of DrPARG might be highly flexible. ADP-ribose binding pocket and complex structure, and conformational effects, detailed overview
additional information
proposed catalytic role of residue Asp314. Asp314 is located proximal to the 1''-O-linkage in substrates. Asp314 might protonate the leaving group (general acid), forming an oxocarbenium ion intermediate, and then activate the water (general base) for back-side attack. The W1 ligand of MgB can serve as the nucleophile attacking the anomeric C1'' of the ribose''. This is consistent with the observed O18 incorporation during hydrolysis of O-acetyl-ADP-ribose, reaction mechanism, overview. Asp314 is essential for the formation of the binuclear metal center. A conformational switch of ARH3 enables specific substrate recognition. ARH3 specifically exposes the scissile 1''-O-linkage in substrates for cleavage
additional information
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proposed catalytic role of residue Asp314. Asp314 is located proximal to the 1''-O-linkage in substrates. Asp314 might protonate the leaving group (general acid), forming an oxocarbenium ion intermediate, and then activate the water (general base) for back-side attack. The W1 ligand of MgB can serve as the nucleophile attacking the anomeric C1'' of the ribose''. This is consistent with the observed O18 incorporation during hydrolysis of O-acetyl-ADP-ribose, reaction mechanism, overview. Asp314 is essential for the formation of the binuclear metal center. A conformational switch of ARH3 enables specific substrate recognition. ARH3 specifically exposes the scissile 1''-O-linkage in substrates for cleavage
additional information
quantitative, real-time assay of PAR-dependent protein-protein interactions and PAR turnover by PARG is an excellent tool for high-throughput screening to identify pharmacological modulators of PAR metabolism that
additional information
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CD spectra of enzyme DrPARG in the absence and presence of ADP-ribose exhibit increased proportion of alpha-helices and beta-strands from 11.78% and 30.37% to 15.10% and 33.52%, respectively, which suggests that conformational changes occur during the binding of ADP-ribose. The intrinsically disordered N-terminal region of DrPARG might be highly flexible. ADP-ribose binding pocket and complex structure, and conformational effects, detailed overview
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additional information
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CD spectra of enzyme DrPARG in the absence and presence of ADP-ribose exhibit increased proportion of alpha-helices and beta-strands from 11.78% and 30.37% to 15.10% and 33.52%, respectively, which suggests that conformational changes occur during the binding of ADP-ribose. The intrinsically disordered N-terminal region of DrPARG might be highly flexible. ADP-ribose binding pocket and complex structure, and conformational effects, detailed overview
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additional information
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CD spectra of enzyme DrPARG in the absence and presence of ADP-ribose exhibit increased proportion of alpha-helices and beta-strands from 11.78% and 30.37% to 15.10% and 33.52%, respectively, which suggests that conformational changes occur during the binding of ADP-ribose. The intrinsically disordered N-terminal region of DrPARG might be highly flexible. ADP-ribose binding pocket and complex structure, and conformational effects, detailed overview
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additional information
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CD spectra of enzyme DrPARG in the absence and presence of ADP-ribose exhibit increased proportion of alpha-helices and beta-strands from 11.78% and 30.37% to 15.10% and 33.52%, respectively, which suggests that conformational changes occur during the binding of ADP-ribose. The intrinsically disordered N-terminal region of DrPARG might be highly flexible. ADP-ribose binding pocket and complex structure, and conformational effects, detailed overview
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additional information
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CD spectra of enzyme DrPARG in the absence and presence of ADP-ribose exhibit increased proportion of alpha-helices and beta-strands from 11.78% and 30.37% to 15.10% and 33.52%, respectively, which suggests that conformational changes occur during the binding of ADP-ribose. The intrinsically disordered N-terminal region of DrPARG might be highly flexible. ADP-ribose binding pocket and complex structure, and conformational effects, detailed overview
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additional information
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CD spectra of enzyme DrPARG in the absence and presence of ADP-ribose exhibit increased proportion of alpha-helices and beta-strands from 11.78% and 30.37% to 15.10% and 33.52%, respectively, which suggests that conformational changes occur during the binding of ADP-ribose. The intrinsically disordered N-terminal region of DrPARG might be highly flexible. ADP-ribose binding pocket and complex structure, and conformational effects, detailed overview
-
additional information
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CD spectra of enzyme DrPARG in the absence and presence of ADP-ribose exhibit increased proportion of alpha-helices and beta-strands from 11.78% and 30.37% to 15.10% and 33.52%, respectively, which suggests that conformational changes occur during the binding of ADP-ribose. The intrinsically disordered N-terminal region of DrPARG might be highly flexible. ADP-ribose binding pocket and complex structure, and conformational effects, detailed overview
-
additional information
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CD spectra of enzyme DrPARG in the absence and presence of ADP-ribose exhibit increased proportion of alpha-helices and beta-strands from 11.78% and 30.37% to 15.10% and 33.52%, respectively, which suggests that conformational changes occur during the binding of ADP-ribose. The intrinsically disordered N-terminal region of DrPARG might be highly flexible. ADP-ribose binding pocket and complex structure, and conformational effects, detailed overview
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D738N
no enzymic activity, no structural effect of mutation
E708N
119% of wild-type activity, no structural effect of mutation
E728N
18% of wild-type activity, no structural effect of mutation
E756N/E757N |
no enzymic activity
E757N
no enzymic activity, no structural effect of mutation
E774N
61% of wild-type activity
E780N
57% of wild-type activity
E788N
100% of wild-type activity
D253N
decrease in catalytic activity
D536N
loss of catalytic activity
E271N
complete loss of catalytic activity
E272N
complete loss of catalytic activity
E554N
decrease in catalytic activity
E555N
loss of catalytic activity
Y311A
almost complete loss of catalytic activity
Y594A
decrease in catalytic activity
E112A
site-directed mutagenesis, inactive mutant
T267K
site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
T267R
site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
E112A
-
site-directed mutagenesis, inactive mutant
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T267K
-
site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
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T267R
-
site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
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E112A
-
site-directed mutagenesis, inactive mutant
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T267K
-
site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
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T267R
-
site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
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E112A
-
site-directed mutagenesis, inactive mutant
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T267K
-
site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
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T267R
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site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
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E112A
-
site-directed mutagenesis, inactive mutant
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T267K
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site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
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T267R
-
site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
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E112A
-
site-directed mutagenesis, inactive mutant
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T267K
-
site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
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T267R
-
site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
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E112A
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site-directed mutagenesis, inactive mutant
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T267K
-
site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
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T267R
-
site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
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E112A
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site-directed mutagenesis, inactive mutant
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T267K
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site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
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T267R
-
site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
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E112A
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site-directed mutagenesis, inactive mutant
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T267K
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site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
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T267R
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site-directed mutagenesis, the mutant loses its endoglycohydrolase activity but retains the exo activity on poly(ADP-ribose), PAR
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A874W
-
the mutant shows about 45% activity compared to the wild type enzyme
D314A
site-directed mutagenesis, the mutation impairs ARH3-dependent DNA damage repair
D314E
site-directed mutagenesis, poly(ADP-ribose) binding structures of wild-type and D314A mutant, overview
D77N
site-directed mutagenesis, the mutation impairs ARH3-dependent DNA damage repair
D77N/D78N
-
mutation abolishes the hydrolytic activity on O-acetyl-ADP-ribose
E41Q
site-directed mutagenesis, the mutation impairs ARH3-dependent DNA damage repair
E688A
site-directed mutagenesis, a surface entropy reduction mutation
E755N
site-directed mutagenesis, inactive mutant
E756N
site-directed mutagenesis, inactive mutant
F875A
-
the mutant shows about 1% activity compared to the wild type enzyme
H182A
site-directed mutagenesis, the mutation impairs ARH3-dependent DNA damage repair
K616A
site-directed mutagenesis, a surface entropy reduction mutation
K616A/Q617A/K618A/E688A/K689A/K690A
site-directed mutagenesis, six surface entropy reduction mutations
K618A
site-directed mutagenesis, a surface entropy reduction mutation
K689A
site-directed mutagenesis, a surface entropy reduction mutation
K690A
site-directed mutagenesis, a surface entropy reduction mutation
L11D
-
the mutation increases enzyme activity to 148%
L11D/L13D
-
the mutant almost entirely abolishes enzyme activity (4% activity)
L11D/L13D/L14D
-
the mutant results in no detectable activity (less than 0.1% activity)
N740A
-
the mutant shows about 30% activity compared to the wild type enzyme
Q617A
site-directed mutagenesis, a surface entropy reduction mutation
R10A
-
the mutation results in a significant increase in activity (144%)
R2A/R3A/R6A/R10A
-
the mutant shows 113% enzyme activity
R3A
-
the mutant shows 105% enzyme activity
R6A
-
the mutation results in a significant increase in activity (248%)
S148A
site-directed mutagenesis, the mutation impairs ARH3-dependent DNA damage repair
T317A
site-directed mutagenesis, the mutation impairs ARH3-dependent DNA damage repair
Y149A
site-directed mutagenesis, the mutation impairs ARH3-dependent DNA damage repair
D77N/D78N
no enzymic activity, binding of ADP-ribose is similar to wild-type
E238Q/E239Q
catalytic activity similar to wild-type
E261Q/E262Q
catalytic activity similar to wild-type
E748N
site-directed mutagenesis, the mutant is inactive, activity is disrupted due to significant conformational changes
E748Q
site-directed mutagenesis, the mutant activity is highly reduced compared to the wild-type enzyme
E749N
site-directed mutagenesis, the mutant is inactive, activity is disrupted due to significant conformational changes
E749Q
site-directed mutagenesis, the mutant activity is highly reduced compared to the wild-type enzyme
F868A
site-directed mutagenesis, the mutant activity is reduced compared to the wild-type enzyme
G737A/G738A
site-directed mutagenesis, the mutant activity is reduced compared to the wild-type enzyme
G866A
site-directed mutagenesis, the mutant activity is reduced compared to the wild-type enzyme
E752N
site-directed mutagenesis, catalytically inactive mutant
E114A
-
the mutant shows about 2% activity compared to the wild type enzyme
S298K
-
the mutant shows about 2% activity compared to the wild type enzyme
V226W
-
the mutant shows about 5% activity compared to the wild type enzyme
E273N
site-directed mutagenesis
E273N
-
site-directed mutagenesis
-
E756N
29% of wild-type activity
E756N
no enzymic activity, no structural effect of mutation
additional information
enzyme knock-down by RNAi results in increased radiation sensitivity of worms
additional information
enzyme knock-down by RNAi results in increased radiation sensitivity of worms
additional information
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enzyme knock-down by RNAi results in increased radiation sensitivity of worms
additional information
disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. A substitution of Arg268 for the smaller and uncharged side chain of Thr267 than that of arginine disrupts the interaction matrix of Thr267, Asp260, and n ribose' and allows for accommodating the n+1 ADP-ribose
additional information
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disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. A substitution of Arg268 for the smaller and uncharged side chain of Thr267 than that of arginine disrupts the interaction matrix of Thr267, Asp260, and n ribose' and allows for accommodating the n+1 ADP-ribose
additional information
-
disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. A substitution of Arg268 for the smaller and uncharged side chain of Thr267 than that of arginine disrupts the interaction matrix of Thr267, Asp260, and n ribose' and allows for accommodating the n+1 ADP-ribose
-
additional information
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disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. A substitution of Arg268 for the smaller and uncharged side chain of Thr267 than that of arginine disrupts the interaction matrix of Thr267, Asp260, and n ribose' and allows for accommodating the n+1 ADP-ribose
-
additional information
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disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. A substitution of Arg268 for the smaller and uncharged side chain of Thr267 than that of arginine disrupts the interaction matrix of Thr267, Asp260, and n ribose' and allows for accommodating the n+1 ADP-ribose
-
additional information
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disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. A substitution of Arg268 for the smaller and uncharged side chain of Thr267 than that of arginine disrupts the interaction matrix of Thr267, Asp260, and n ribose' and allows for accommodating the n+1 ADP-ribose
-
additional information
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disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. A substitution of Arg268 for the smaller and uncharged side chain of Thr267 than that of arginine disrupts the interaction matrix of Thr267, Asp260, and n ribose' and allows for accommodating the n+1 ADP-ribose
-
additional information
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disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. A substitution of Arg268 for the smaller and uncharged side chain of Thr267 than that of arginine disrupts the interaction matrix of Thr267, Asp260, and n ribose' and allows for accommodating the n+1 ADP-ribose
-
additional information
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disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. A substitution of Arg268 for the smaller and uncharged side chain of Thr267 than that of arginine disrupts the interaction matrix of Thr267, Asp260, and n ribose' and allows for accommodating the n+1 ADP-ribose
-
additional information
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disruption of DrPARG expression causes accumulation of endogenous poly-ADP-ribose (PAR) and compromises recovery from UV radiation damage. A substitution of Arg268 for the smaller and uncharged side chain of Thr267 than that of arginine disrupts the interaction matrix of Thr267, Asp260, and n ribose' and allows for accommodating the n+1 ADP-ribose
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additional information
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decrease or loss of enzyme expression by partial gene deletion or RNA results in mislocalization and hypermodification of silencing protein SIR2
additional information
construction of a DELTAparg deletion mutant. The mutant DELTAparg strain, in the presence of H2O2, exhibits a reduced randomly amplified polymorphic DNA (RAPD) pattern, suggesting that DNA is damaged in this strain and repair is impaired
additional information
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construction of a DELTAparg deletion mutant. The mutant DELTAparg strain, in the presence of H2O2, exhibits a reduced randomly amplified polymorphic DNA (RAPD) pattern, suggesting that DNA is damaged in this strain and repair is impaired
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additional information
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construction of a DELTAparg deletion mutant. The mutant DELTAparg strain, in the presence of H2O2, exhibits a reduced randomly amplified polymorphic DNA (RAPD) pattern, suggesting that DNA is damaged in this strain and repair is impaired
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additional information
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construction of a DELTAparg deletion mutant. The mutant DELTAparg strain, in the presence of H2O2, exhibits a reduced randomly amplified polymorphic DNA (RAPD) pattern, suggesting that DNA is damaged in this strain and repair is impaired
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additional information
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construction of a DELTAparg deletion mutant. The mutant DELTAparg strain, in the presence of H2O2, exhibits a reduced randomly amplified polymorphic DNA (RAPD) pattern, suggesting that DNA is damaged in this strain and repair is impaired
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additional information
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quantification of single-strand break repair rates in A-549 cells depleted of poly(ADP-ribose) glycohydrolase, poly(ADP-ribose) polymerase 1 and poly(ADP-ribose) polymerase 2, both separately and in combination. Poly(ADP-ribose) glycohydrolase is a critical component of single-strand break repair and accelerates this process in concert with poly(ADP-ribose) polymerase
additional information
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transient transfection of HeLa cells with PARG expression constructs with amino acids encoded by exon 4 at the N-terminus. Proteins are targeted to the mitochondria. Deletion and missense mutants allow identification of a canonical N-terminal mitochondrial targeting sequence consisting of the first 16 amino acids encoded by PARG exon 4. Sub-mitochondrial localization experiments indicate that this mitochondrial PARG isoform is targeted to the mitochondrial matrix
additional information
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deletion of the regulatory segment/MTS from full-length human PARG111 results in a complete loss of activity
additional information
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constitutive expression shRNA directed against the catalytic domain of all enzyme isoforms in the 16HBE cell line
additional information
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enzyme knockdown using siRNA
additional information
lentiviral gene silencing is used to generate 16HBE cell lines with stably suppressed enzyme, and determination of parameters of cell death and cell cycle following benz[a]pyrene exposure, overview
additional information
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lentiviral gene silencing is used to generate 16HBE cell lines with stably suppressed enzyme, and determination of parameters of cell death and cell cycle following benz[a]pyrene exposure, overview
additional information
enzyme knockout by expression of ARH3 siRNA in U2OS cells
additional information
poly(ADP-ribose) glycohydrolase (PARG) silencing and generation of PARG-deficient human bronchial epithelial cells. Silencing of PARG significantly reduces the volume and weight of tumors in Balb/c nude mice injected with benzo(a)pyrene (BaP)-induced transformed human bronchial epithelial cells. PARG-silenced shPARG cells show less chromosomal damage than wild-type 16HBE cells. PARG silencing inhibits BaP-induced micronuclei formation. PARG silencing protects cells against BaP-induced cytotoxicity and cytogenetic damage, and inhibits BaP-induced cell transformation by reducing genomic instability in cells. PARG-deficient phenotype, overview
additional information
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poly(ADP-ribose) glycohydrolase (PARG) silencing and generation of PARG-deficient human bronchial epithelial cells. Silencing of PARG significantly reduces the volume and weight of tumors in Balb/c nude mice injected with benzo(a)pyrene (BaP)-induced transformed human bronchial epithelial cells. PARG-silenced shPARG cells show less chromosomal damage than wild-type 16HBE cells. PARG silencing inhibits BaP-induced micronuclei formation. PARG silencing protects cells against BaP-induced cytotoxicity and cytogenetic damage, and inhibits BaP-induced cell transformation by reducing genomic instability in cells. PARG-deficient phenotype, overview
additional information
siRNA screen for synthetic lethality with PARG depletion, lethal with depletion of BRCA2. Reduction of expression of PARG protein by 80-90% without significant change in poly(ADP-ribose) polymerase PARP1 protein levels. Disruption of BRCA1, BRCA2, PALB2, RAD51D, BRIP1, BARD1, MRE11, NBN, RAD50, TP53, and FAM175A can be considered synthetically lethal with PARG depletion
additional information
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deletion of enzyme gene by gene targeting in embryonic stem cells and mice, severe compromisation of automodification of poly(ADP-ribose) polymerase 1. Enzyme deficient mice are viable and fertile, but hypersensitive to alkylating agents and ionizing radiation, and susceptible to streptozotocin-induced diabetes and endotoxic shock
additional information
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enzyme knockout mutation is lethal. Silencing by RNA interference results in 10% of enzyme protein that are sufficient to ensure normal proliferation through several subculturing rounds and cells that are able to repair DNA damage induced by sublethal doses of H2O2. Silenced cells are more resistant than wild-type to oxidant-induced apoptosis while exhibiting delayed poly(ADP-ribose) degradation and transient accumulation of ADP-ribose polymers
additional information
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disruption of poly(ADP-ribose) glycohydrolase gene results in significant reduction of spinal cord inflammation and tissue injury, neutrophil infiltration, cytokine production, and apoptosis upon spinal cord injury
additional information
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hypomorphic mouse model in which exons 2 and 3 of PARG gene have been deleted. Mutants exhibits nuclear localization of the enzyme which contains a catalytic domain but lacks the N-terminal region. Following DNA damage induced by N-methyl-N'-nitro-N-nitrosoguanidine, activity of both poly(ADP-ribose) glycohydrolase and poly(ADP-ribose) polymerase in mutant cell increases. Increase in poly(ADP-ribose) glycohydrolase activity leads to decrease in poly(ADP-ribose) polymerase-1 automodification resulting in increased activity. Mutant cells also show reduced formation of XCRR1 foci, delayed H2AX phosphorylation, decreased DNA break intermediates during repair, and increased cell death
additional information
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mice lacking the functional 110 kDa isoform of enzyme are resistant to colon injury by dinitrobenzene sulfonic acid. Mucosa of mutant mice colon tissue shows reduction of myeloperoxidase activity and attenuated staining for intercellular adhesion molecule 1 and vascular cell adhesion molecule 1. Overproduction of proinflammatory factors tumor necrosis factor alpha and interleukin 1beta and activation of cell death signaling pathway are inhibited in these mice
additional information
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the catalytic activity of poly(ADP-ribose) glucohydrolase strongly depends on the two Glu residues in the GGG-X6-8-QEE motif (E114 and E115)
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Lin, W.; Ame, J.C.; Aboul-Ela, N.; Jacobson, E.L.; Jacobson, M.K.
Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase
J. Biol. Chem.
272
11895-11901
1997
Bos taurus (O02776), Bos taurus
brenda
Maruta, H.; Inageda, K.; Aoki, T.; Nishina, H.; Tanuma, S.I.
Characterization of two forms of poly(ADP-ribose) glycohydrolase in guniea pig liver
Biochemistry
30
5907-5912
1991
Cavia porcellus
brenda
Brochu, G.; Shah, G.M.; Poirier, G.G.
Purification of poly(ADP-ribose) glycohydrolase detection of its isoforms by a zymogram following one- or two-dimensional electrophoresis
Anal. Biochem.
218
265-272
1994
Bos taurus
brenda
Sugimura, T.; Yamada, M.; Miwa, M.; Matsushima, T.; Hidaka, T.; Nagao, M.; Inui, N.; Takayama, S.
Properties of poly(adenosine diphosphate ribose) polymerase, poly(adenosine diphosphate ribose) glycohydrolase and poly(adenosine diphosphate ribose)
Biochem. Soc. Trans.
1
642-644
1973
Bos taurus
-
brenda
Pacheco-Rodriguez, G.; Alvarez-Gonzalez, R.
Measurement of poly(ADP-ribose) glycohydrolase activity by high resolution polyacrylamide gel electrophoresis: specific inhibition by histones and nuclear matrix proteins
Mol. Cell. Biochem.
193
13-18
1999
Rattus norvegicus
brenda
Concha, I.I.; Koide, S.S.; Burzio, L.O.
Characteristics of the inhibition of poly(ADP-ribose) glycohydrolase by homopolypurines
Biochem. Int.
16
397-403
1988
Rattus norvegicus
brenda
Tanuma, S.i.; Sakagami, H.; Endo, H.
Inhibitory effect of tannin on poly(ADP-rinbose) glycohydrolase
Biochem. Int.
18
701-708
1989
Homo sapiens
brenda
Miwa, M.; Sugimura, T.
Splitting of the ribose-ribose linkage of poly(adenosine diphosphate-ribose) by a calf thymus extract
J. Biol. Chem.
246
6362-6364
1971
Bos taurus
brenda
Miwa, M.; Tanaka, M.; Matsushima, T.; Sugimura, T.
Purification and properties of a glycohydrolase from calf thymus splitting ribose-ribose linkages of poly(adenosine diphosphate ribose)
J. Biol. Chem.
249
3475-3482
1974
Bos taurus
brenda
Hatakeyama, K.; Nemoto, Y.; Ueda, K.; Hayaishi, O.
Purification and characterization of poly(ADP-ribose) glycohydrolase. Different modes of action on large and small poly(ADP-ribose)
J. Biol. Chem.
261
14902-14911
1986
Bos taurus
brenda
Tanuma, S.i.; Kawashima, K.; Endo, H.
Purification and properties of an (ADP-ribose)n glycohydrolase from guinea pig liver nuclei
J. Biol. Chem.
261
965-969
1986
Cavia porcellus
brenda
Tanuma, S.i.; Endo, H.
Purification and characterization of an (ADP-ribose)n glycohydrolase from human erythrocytes
Eur. J. Biochem.
191
57-63
1990
Homo sapiens
brenda
Tavassoli, M.; Tavassoli, M.H.; Shall, S.
Isolation and purification of poly(ADP-ribose) glycohydrolase from pig thymus
Eur. J. Biochem.
135
449-455
1983
Sus scrofa
brenda
Slama, J.T.; Aboul-Ela, N.; Jacobson, M.K.
Mechanism of inhibition of poly(ADP-ribose) glycohydrolase by adenosine diphosphate (hydroxymethyl)pyrrolidinediol
J. Med. Chem.
38
4332-4336
1995
Bos taurus
brenda
Abe, H.; Tanuma, S.
Properties of poly(ADP-ribose) glycohydrolase purified from pig testis nuclei
Arch. Biochem. Biophys.
336
139-146
1996
Sus scrofa
brenda
Ohashi, S.; Kanai, M.; Hanai, S.; Uchiumi, F.; Maruta, H.; Tanuma, S.; Miwa, M.
Subcellular localization of poly(ADP-ribose) glycohydrolase in mammalian cells
Biochem. Biophys. Res. Commun.
307
915-921
2003
Homo sapiens
brenda
Patel, C.N.; Koh, D.W.; Jacobson, M.K.; Oliveira, M.A.
Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: determining the PARG catalytic domain
Biochem. J.
388
493-500
2005
Bos taurus (O02776), Bos taurus
brenda
Gagne, J.P.; Bonicalzi, M.E.; Gagne, P.; Ouellet, M.E.; Hendzel, M.J.; Poirier, G.G.
Poly(ADP-ribose) glycohydrolase is a component of the FMRP-associated messenger ribonucleoparticles
Biochem. J.
392
499-509
2005
Homo sapiens
brenda
Blenn, C.; Althaus, F.R.; Malanga, M.
Poly(ADP-ribose) glycohydrolase silencing protects against H2O2-induced cell death
Biochem. J.
396
419-429
2006
Mus musculus
brenda
Uchiumi, F.; Ikeda, D.; Tanuma, S.
Changes in the activities and gene expressions of poly(ADP-ribose) glycohydrolases during the differentiation of human promyelocytic leukemia cell line HL-60
Biochim. Biophys. Acta
1676
1-11
2004
Homo sapiens (Q86W56)
brenda
Haince, J.F.; Ouellet, M.E.; McDonald, D.; Hendzel, M.J.; Poirier, G.G.
Dynamic relocation of poly(ADP-ribose) glycohydrolase isoforms during radiation-induced DNA damage
Biochim. Biophys. Acta
1763
226-237
2006
Bos taurus, Homo sapiens
brenda
Bonicalzi, M.E.; Vodenicharov, M.; Coulombe, M.; Gagne, J.P.; Poirier, G.G.
Alteration of poly(ADP-ribose) glycohydrolase nucleocytoplasmic shuttling characteristics upon cleavage by apoptotic proteases
Biol. Cell.
95
635-644
2003
Bos taurus
brenda
Sevigny, M.B.; Silva, J.M.; Lan, W.C.; Alano, C.C.; Swanson, R.A.
Expression and activity of poly(ADP-ribose) glycohydrolase in cultured astrocytes, neurons, and C6 glioma cells
Brain Res. Mol. Brain Res.
117
213-220
2003
Mus musculus
brenda
Meyer-Ficca, M.L.; Meyer, R.G.; Coyle, D.L.; Jacobson, E.L.; Jacobson, M.K.
Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments
Exp. Cell Res.
297
521-532
2004
Homo sapiens (Q86W56), Homo sapiens
brenda
Oka, S.; Kato, J.; Moss, J.
Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase
J. Biol. Chem.
281
705-713
2006
Mus musculus (Q8CG72), Homo sapiens (Q9NX46), Homo sapiens
brenda
Koh, D.W.; Coyle, D.L.; Mehta, N.; Ramsinghani, S.; Kim, H.; Slama, J.T.; Jacobson, M.K.
SAR analysis of adenosine diphosphate (hydroxymethyl)pyrrolidinediol inhibition of poly(ADP-ribose) glycohydrolase
J. Med. Chem.
46
4322-4332
2003
Bos taurus
brenda
Di Meglio, S.; Denegri, M.; Vallefuoco, S.; Tramontano, F.; Scovassi, A.I.; Quesada, P.
Poly(ADPR) polymerase-1 and poly(ADPR) glycohydrolase level and distribution in differentiating rat germinal cells
Mol. Cell. Biochem.
248
85-91
2003
Rattus norvegicus
brenda
Cortes, U.; Tong, W.M.; Coyle, D.L.; Meyer-Ficca, M.L.; Meyer, R.G.; Petrilli, V.; Herceg, Z.; Jacobson, E.L.; Jacobson, M.K.; Wang, Z.Q.
Depletion of the 110-kilodalton isoform of poly(ADP-ribose) glycohydrolase increases sensitivity to genotoxic and endotoxic stress in mice
Mol. Cell. Biol.
24
7163-7178
2004
Mus musculus
brenda
Ying, W.; Sevigny, M.B.; Chen, Y.; Swanson, R.A.
Poly(ADP-ribose) glycohydrolase mediates oxidative and excitotoxic neuronal death
Proc. Natl. Acad. Sci. USA
98
12227-12232
2001
Mus musculus
brenda
Shirato, M.; Tozawa, S.; Maeda, D.; Watanabe, M.; Nakagama, H.; Masutani, M.
Poly(etheno ADP-ribose) blocks poly(ADP-ribose) glycohydrolase activity
Biochem. Biophys. Res. Commun.
355
451-456
2007
Rattus norvegicus
brenda
St-Laurent, J.F.; Gagnon, S.N.; Dequen, F.; Hardy, I.; Desnoyers, S.
Altered DNA damage response in Caenorhabditis elegans with impaired poly(ADP-ribose) glycohydrolases genes expression
DNA Repair
6
329-343
2007
Caenorhabditis elegans (Q867X0), Caenorhabditis elegans (Q9N5L4), Caenorhabditis elegans
brenda
Meyer, R.G.; Meyer-Ficca, M.L.; Whatcott, C.J.; Jacobson, E.L.; Jacobson, M.K.
Two small enzyme isoforms mediate mammalian mitochondrial poly(ADP-ribose) glycohydrolase (PARG) activity
Exp. Cell Res.
313
2920-2936
2007
Homo sapiens
brenda
Gao, H.; Coyle, D.L.; Meyer-Ficca, M.L.; Meyer, R.G.; Jacobson, E.L.; Wang, Z.Q.; Jacobson, M.K.
Altered poly(ADP-ribose) metabolism impairs cellular responses to genotoxic stress in a hypomorphic mutant of poly(ADP-ribose) glycohydrolase
Exp. Cell Res.
313
984-996
2007
Mus musculus
brenda
Cuzzocrea, S.; Mazzon, E.; Genovese, T.; Crisafulli, C.; Min, W.K.; Di Paola, R.; Muia, C.; Li, J.H.; Malleo, G.; Xu, W.; Massuda, E.; Esposito, E.; Zhang, J.; Wang, Z.Q.
Role of poly(ADP-ribose) glycohydrolase in the development of inflammatory bowel disease in mice
Free Radic. Biol. Med.
42
90-105
2007
Mus musculus
brenda
Tulin, A.; Naumova, N.M.; Menon, A.K.; Spradling, A.C.
Drosophila poly(ADP-ribose) glycohydrolase mediates chromatin structure and SIR2-dependent silencing
Genetics
172
363-371
2006
Drosophila melanogaster
brenda
Keil, C.; Groebe, T.; Oei, S.L.
MNNG-induced cell death is controlled by interactions between PARP-1, poly(ADP-ribose) glycohydrolase, and XRCC1
J. Biol. Chem.
281
34394-34405
2006
Homo sapiens (Q0MQR4)
brenda
Cuzzocrea, S.; Genovese, T.; Mazzon, E.; Crisafulli, C.; Min, W.; Di Paola, R.; Muia, C.; Li, J.H.; Esposito, E.; Bramanti, P.; Xu, W.; Massuda, E.; Zhang, J.; Wang, Z.Q.
Poly(ADP-ribose) glycohydrolase activity mediates post-traumatic inflammatory reaction after experimental spinal cord trauma
J. Pharmacol. Exp. Ther.
319
127-138
2006
Mus musculus
brenda
Fisher, A.E.; Hochegger, H.; Takeda, S.; Caldecott, K.W.
Poly(ADP-ribose) polymerase 1 accelerates single-strand break repair in concert with poly(ADP-ribose) glycohydrolase
Mol. Cell. Biol.
27
5597-5605
2007
Homo sapiens
brenda
Ono, T.; Kasamatsu, A.; Oka, S.; Moss, J.
The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases
Proc. Natl. Acad. Sci. USA
103
16687-16691
2006
Homo sapiens
brenda
Formentini, L.; Arapistas, P.; Pittelli, M.; Jacomelli, M.; Pitozzi, V.; Menichetti, S.; Romani, A.; Giovannelli, L.; Moroni, F.; Chiarugi, A.
Mono-galloyl glucose derivatives are potent poly(ADP-ribose) glycohydrolase (PARG) inhibitors and partially reduce PARP-1-dependent cell death
Br. J. Pharmacol.
155
1235-1249
2008
Bos taurus
brenda
Cohausz, O.; Blenn, C.; Malanga, M.; Althaus, F.R.
The roles of poly(ADP-ribose)-metabolizing enzymes in alkylation-induced cell death
Cell. Mol. Life Sci.
65
644-655
2008
Homo sapiens
brenda
Burns, D.M.; Ying, W.; Kauppinen, T.M.; Zhu, K.; Swanson, R.A.
Selective down-regulation of nuclear poly(ADP-ribose) glycohydrolase
PLoS ONE
4
e4896
2009
Mus musculus
brenda
Adams-Phillips, L.; Briggs, A.G.; Bent, A.F.
Disruption of poly(ADP-ribosyl)ation mechanisms alters responses of Arabidopsis to biotic stress
Plant Physiol.
152
267-280
2010
Arabidopsis thaliana
brenda
Okita, N.; Ashizawa, D.; Ohta, R.; Abe, H.; Tanuma, S.
Discovery of novel poly(ADP-ribose) glycohydrolase inhibitors by a quantitative assay system using dot-blot with anti-poly(ADP-ribose)
Biochem. Biophys. Res. Commun.
392
485-489
2010
Bos taurus
brenda
Whatcott, C.J.; Meyer-Ficca, M.L.; Meyer, R.G.; Jacobson, M.K.
A specific isoform of poly(ADP-ribose) glycohydrolase is targeted to the mitochondrial matrix by a N-terminal mitochondrial targeting sequence
Exp. Cell Res.
315
3477-3485
2009
Homo sapiens
brenda
Erdelyi, K.; Bai, P.; Kovacs, I.; Szabo, E.; Mocsar, G.; Kakuk, A.; Szabo, C.; Gergely, P.; Virag, L.
Dual role of poly(ADP-ribose) glycohydrolase in the regulation of cell death in oxidatively stressed A549 cells
FASEB J.
23
3553-3563
2009
Homo sapiens
brenda
Frizzell, K.M.; Gamble, M.J.; Berrocal, J.G.; Zhang, T.; Krishnakumar, R.; Cen, Y.; Sauve, A.A.; Kraus, W.L.
Global analysis of transcriptional regulation by poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase in MCF-7 human breast cancer cells
J. Biol. Chem.
284
33926-33938
2009
Homo sapiens
brenda
Botta, D.; Jacobson, M.K.
Identification of a regulatory segment of poly(ADP-ribose) glycohydrolase
Biochemistry
49
7674-7682
2010
Homo sapiens
brenda
Blenn, C.; Wyrsch, P.; Bader, J.; Bollhalder, M.; Althaus, F.R.
Poly(ADP-ribose)glycohydrolase is an upstream regulator of Ca2+ fluxes in oxidative cell death
Cell. Mol. Life Sci.
68
1455-1466
2011
Mus musculus
brenda
Steffen, J.D.; Coyle, D.L.; Damodaran, K.; Beroza, P.; Jacobson, M.K.
Discovery and structure-activity relationships of modified salicylanilides as cell permeable inhibitors of poly(ADP-ribose) glycohydrolase (PARG)
J. Med. Chem.
54
5403-5413
2011
Homo sapiens
brenda
Slade, D.; Dunstan, M.; Barkauskaite, E.; Weston, R.; Lafite, P.; Dixon, N.; Ahel, M.; Leys, D.; Ahel, I.
The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase
Nature
477
616-622
2011
Homo sapiens, Thermomonospora curvata
brenda
Li, G.; Nasar, V.; Yang, Y.; Li, W.; Liu, B.; Sun, L.; Li, D.; Song, F.
Arabidopsis poly(ADP-ribose) glycohydrolase 1 is required for drought, osmotic and oxidative stress responses
Plant Sci.
180
283-291
2011
Arabidopsis thaliana
brenda
Okita, N.; Ohta, R.; Ashizawa, D.; Yamada, Y.; Abe, H.; Abe, T.; Tanuma, S.
Bacterial production of recombinant human poly(ADP-ribose) glycohydrolase
Protein Expr. Purif.
75
230-235
2011
Homo sapiens (Q86W56), Homo sapiens
brenda
Hassler, M.; Jankevicius, G.; Ladurner, A.G.
PARG: A macrodomain in disguise
Structure
19
1351-1353
2011
Thermomonospora curvata
brenda
Finch, K.E.; Knezevic, C.E.; Nottbohm, A.C.; Partlow, K.C.; Hergenrother, P.J.
Selective small molecule inhibition of poly(ADP-ribose) glycohydrolase (PARG)
ACS Chem. Biol.
7
563-570
2012
Homo sapiens
brenda
Huang, H.; Hu, G.; Cai, J.; Xia, B.; Liu, J.; Li, X.; Gao, W.; Zhang, J.; Liu, Y.; Zhuang, Z.
Role of poly(ADP-ribose) glycohydrolase silencing in DNA hypomethylation induced by benzo(a)pyrene
Biochem. Biophys. Res. Commun.
452
708-714
2014
Homo sapiens
brenda
Islam, R.; Koizumi, F.; Kodera, Y.; Inoue, K.; Okawara, T.; Masutani, M.
Design and synthesis of phenolic hydrazide hydrazones as potent poly(ADP-ribose) glycohydrolase (PARG) inhibitors
Bioorg. Med. Chem. Lett.
24
3802-3806
2014
Rattus norvegicus
brenda
Sahaboglu, A.; Tanimoto, N.; Bolz, S.; Garrido, M.G.; Ueffing, M.; Seeliger, M.W.; Loewenheim, H.; Ekstroem, P.; Paquet-Durand, F.
Knockout of PARG110 confers resistance to cGMP-induced toxicity in mammalian photoreceptors
Cell Death Dis.
5
e1234
2014
Mus musculus
brenda
Huang, H.Y.; Cai, J.F.; Liu, Q.C.; Hu, G.H.; Xia, B.; Mao, J.Y.; Wu, D.S.; Liu, J.J.; Zhuang, Z.X.
Role of poly(ADP-ribose) glycohydrolase in the regulation of cell fate in response to benzo(a)pyrene
Exp. Cell Res.
318
682-690
2012
Homo sapiens (Q86W56), Homo sapiens
brenda
Ji, Y.; Jarnik, M.; Tulin, A.V.
Poly(ADP-ribose) glycohydrolase and poly(ADP-ribose)-interacting protein Hrp38 regulate pattern formation during Drosophila eye development
Gene
526
187-194
2013
Drosophila melanogaster
brenda
Feng, X.; Koh, D.W.
Inhibition of poly(ADP-ribose) polymerase-1 or poly(ADP-ribose) glycohydrolase individually, but not in combination, leads to improved chemotherapeutic efficacy in HeLa cells
Int. J. Oncol.
42
749-756
2013
Homo sapiens
brenda
Hou, Q.; Hu, X.; Sheng, X.; Liu, Y.; Liu, C.
Theoretical study on the degradation of ADP-ribose polymer catalyzed by poly(ADP-ribose) glycohydrolase
J. Mol. Graph. Model.
42
26-31
2013
Thermomonospora curvata (D1AC29)
brenda
Kim, I.K.; Kiefer, J.R.; Ho, C.M.; Stegeman, R.A.; Classen, S.; Tainer, J.A.; Ellenberger, T.
Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element
Nat. Struct. Mol. Biol.
19
653-656
2012
Rattus norvegicus (Q9QYM2)
brenda
Dunstan, M.S.; Barkauskaite, E.; Lafite, P.; Knezevic, C.E.; Brassington, A.; Ahel, M.; Hergenrother, P.J.; Leys, D.; Ahel, I.
Structure and mechanism of a canonical poly(ADP-ribose) glycohydrolase
Nat. Commun.
3
878
2012
Tetrahymena thermophila (I6L8L8), Tetrahymena thermophila
brenda
Tucker, J.A.; Bennett, N.; Brassington, C.; Durant, S.T.; Hassall, G.; Holdgate, G.; McAlister, M.; Nissink, J.W.; Truman, C.; Watson, M.
Structures of the human poly (ADP-ribose) glycohydrolase catalytic domain confirm catalytic mechanism and explain inhibition by ADP-HPD derivatives
PLoS ONE
7
e50889
2012
Homo sapiens (Q86W56), Homo sapiens
brenda
Vilchez Larrea, S.C.; Schlesinger, M.; Kevorkian, M.L.; Flawia, M.M.; Alonso, G.D.; Fernandez Villamil, S.H.
Host cell poly(ADP-ribose) glycohydrolase is crucial for Trypanosoma cruzi infection cycle
PLoS ONE
8
e67356
2013
Trypanosoma cruzi (Q0PW90), Trypanosoma cruzi
brenda
Dahl, M.; Maturi, V.; Loenn, P.; Papoutsoglou, P.; Zieba, A.; Vanlandewijck, M.; van der Heide, L.P.; Watanabe, Y.; Soederberg, O.; Hottiger, M.O.; Heldin, C.H.; Moustakas, A.
Fine-tuning of Smad protein function by poly(ADP-ribose) polymerases and poly(ADP-ribose) glycohydrolase during transforming growth factor beta signaling
PLoS ONE
9
e103651
2014
Homo sapiens
brenda
Wang, Z.; Gagne, J.P.; Poirier, G.G.; Xu, W.
Crystallographic and biochemical analysis of the mouse poly(ADP-ribose) glycohydrolase
PLoS ONE
9
e86010
2014
Mus musculus (O88622), Mus musculus
brenda
James, D.I.; Smith, K.M.; Jordan, A.M.; Fairweather, E.E.; Griffiths, L.A.; Hamilton, N.S.; Hitchin, J.R.; Hutton, C.P.; Jones, S.; Kelly, P.; McGonagle, A.E.; Small, H.; Stowell, A.I.; Tucker, J.; Waddell, I.D.; Waszkowycz, B.; Ogilvie, D.J.
First-in-class chemical probes against poly(ADP-ribose) glycohydrolase (PARG) inhibit DNA repair with differential pharmacology to Olaparib
ACS Chem. Biol.
11
3179-3190
2016
Homo sapiens (Q86W56)
brenda
Stowell, A.I.; James, D.I.; Waddell, I.D.; Bennett, N.; Truman, C.; Hardern, I.M.; Ogilvie, D.J.
A high-throughput screening-compatible homogeneous time-resolved fluorescence assay measuring the glycohydrolase activity of human poly(ADP-ribose) glycohydrolase
Anal. Biochem.
503
58-64
2016
Homo sapiens (Q86W56), Homo sapiens
brenda
Araiza-Cervantes, C.; Meza-Carmen, V.; Martinez-Cadena, G.; Roncero, M.; Reyna-Lopez, G.; Franco, B.
Biochemical and genetic analysis of a unique poly(ADP-ribosyl) glycohydrolase (PARG) of the pathogenic fungus Fusarium oxysporum f. sp. lycopersici
Antonie Van Leeuwenhoek
111
285-295
2018
Fusarium oxysporum f. sp. lycopersici (A0A0D2XPQ9), Fusarium oxysporum f. sp. lycopersici 4287 (A0A0D2XPQ9), Fusarium oxysporum f. sp. lycopersici FGSC 9935 (A0A0D2XPQ9), Fusarium oxysporum f. sp. lycopersici CBS 123668 (A0A0D2XPQ9), Fusarium oxysporum f. sp. lycopersici NRRL 34936 (A0A0D2XPQ9)
-
brenda
Gravells, P.; Grant, E.; Smith, K.M.; James, D.I.; Bryant, H.E.
Specific killing of DNA damage-response deficient cells with inhibitors of poly(ADP-ribose) glycohydrolase
DNA Repair
52
81-91
2017
Homo sapiens (Q86W56)
brenda
Lambrecht, M.J.; Brichacek, M.; Barkauskaite, E.; Ariza, A.; Ahel, I.; Hergenrother, P.J.
Synthesis of dimeric ADP-ribose and its structure with human poly(ADP-ribose) glycohydrolase
J. Am. Chem. Soc.
137
3558-3564
2015
Homo sapiens (Q86W56), Homo sapiens
brenda
Kim, I.; Stegeman, R.; Brosey, C.; Ellenberger, T.
A quantitative assay reveals ligand specificity of the DNA scaffold repair protein XRCC1 and efficient disassembly of complexes of XRCC1 and the poly(ADP-ribose) polymerase 1 by poly(ADP-ribose) glycohydrolase
J. Biol. Chem.
290
3775-3783
2015
Rattus norvegicus (Q9QYM2)
-
brenda
Pourfarjam, Y.; Ventura, J.; Kurinov, I.; Cho, A.; Moss, J.; Kim, I.K.
Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition
J. Biol. Chem.
293
12350-12359
2018
Homo sapiens (Q9NX46), Homo sapiens
brenda
Wang, M.; Yuan, Z.; Xie, R.; Ma, Y.; Liu, X.; Yu, X.
Structure-function analyses reveal the mechanism of the ARH3-dependent hydrolysis of ADP-ribosylation
J. Biol. Chem.
293
14470-14480
2018
Homo sapiens (Q9NX46)
brenda
Waszkowycz, B.; Smith, K.M.; McGonagle, A.E.; Jordan, A.M.; Acton, B.; Fairweather, E.E.; Griffiths, L.A.; Hamilton, N.M.; Hamilton, N.S.; Hitchin, J.R.; Hutton, C.P.; James, D.I.; Jones, C.D.; Jones, S.; Mould, D.P.; Small, H.F.; Stowell, A.I.J.; Tucker, J.A.; Waddell, I.D.; Ogilvie, D.J.
Cell-active small molecule inhibitors of the DNA-damage repair enzyme poly(ADP-ribose) glycohydrolase (PARG) discovery and optimization of orally bioavailable quinazolinedione sulfonamides
J. Med. Chem.
61
10767-10792
2018
Homo sapiens (Q86W56), Homo sapiens
brenda
Barkauskaite, E.; Jankevicius, G.; Ahel, I.
Structures and mechanisms of enzymes employed in the synthesis and degradation of PARP-dependent protein ADP-ribosylation
Mol. Cell
58
935-946
2015
Homo sapiens (Q86W56)
brenda
Chaudhuri, A.; Ahuja, A.; Herrador, R.; Lopes, M.
Poly(ADP-ribosyl) glycohydrolase prevents the accumulation of unusual replication structures during unperturbed S phase
Mol. Cell. Biol.
35
856-865
2015
Homo sapiens (Q86W56)
-
brenda
Cho, C.C.; Chien, C.Y.; Chiu, Y.C.; Lin, M.H.; Hsu, C.H.
Structural and biochemical evidence supporting poly ADP-ribosylation in the bacterium Deinococcus radiodurans
Nat. Commun.
10
1491
2019
Deinococcus radiodurans (Q9RZM4), Deinococcus radiodurans, Deinococcus radiodurans R1 (Q9RZM4), Deinococcus radiodurans DSM 20539 (Q9RZM4), Deinococcus radiodurans VKM B-1422 (Q9RZM4), Deinococcus radiodurans NCIMB 9279 (Q9RZM4), Deinococcus radiodurans JCM 16871 (Q9RZM4), Deinococcus radiodurans LMG 4051 (Q9RZM4), Deinococcus radiodurans ATCC 13939 (Q9RZM4), Deinococcus radiodurans NBRC 15346 (Q9RZM4)
brenda
Rotin, L.E.; Gronda, M.; MacLean, N.; Hurren, R.; Wang, X.; Lin, F.H.; Wrana, J.; Datti, A.; Barber, D.L.; Minden, M.D.; Slassi, M.; Schimmer, A.D.
Ibrutinib synergizes with poly(ADP-ribose) glycohydrolase inhibitors to induce cell death in AML cells via a BTK-independent mechanism
Oncotarget
7
2765-2779
2016
Homo sapiens (Q86W56)
brenda
Li, X.; Li, X.; Zhu, Z.; Huang, P.; Zhuang, Z.; Liu, J.; Gao, W.; Liu, Y.; Huang, H.
Poly(ADP-Ribose) glycohydrolase (PARG) silencing suppresses benzo(a)pyrene induced cell transformation
PLoS ONE
11
e0151172
2016
Homo sapiens (Q86W56), Homo sapiens
brenda
Zhang, H.; Gu, Z.; Wu, Q.; Yang, L.; Liu, C.; Ma, H.; Xia, Y.; Ge, X.
Arabidopsis PARG1 is the key factor promoting cell survival among the enzymes regulating post-translational poly(ADP-ribosyl)ation
Sci. Rep.
5
15892
2015
Arabidopsis thaliana (Q9SKB3), Arabidopsis thaliana Col-0 (Q9SKB3)
brenda