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integrin alpha7 + NAD+
(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
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the extracellular domain of integrin alpha7 is ADP-ribosylated by an arginine-specific ecto-ADP-ribosyltransferase after adding exogenous NAD+ to intact C2C12 muscle cells, integrin alpha7 N-terminal ADP-ribosylation inhibits the binding of integrin alpha7beta1 to laminin activation status of integrin alpha7beta1 in intact myotubes, overview
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
NAD+ + (ADP-D-ribosyl)n-aryl hydrocarbon receptor
nicotinamide + (ADP-D-ribosyl)n+1-aryl hydrocarbon receptor + H+
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NAD+ + (ADP-D-ribosyl)n-beta-transducin repeat-containing protein
nicotinamide + (ADP-D-ribosyl)n+1-beta-transducin repeat-containing protein + H+
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NAD+ + (ADP-D-ribosyl)n-NEMO protein
nicotinamide + (ADP-D-ribosyl)n+1-NEMO protein + H+
the enzyme prevents poly-ubiquitination of NEMO protein
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NAD+ + (ADP-D-ribosyl)n-p21ras
nicotinamide + (ADP-D-ribosyl)n+1-p21ras
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ADP-ribosylation of p21ras does not alter interactions with guanidine nucleotides. Possible function of the enzyme in pathogenesis
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NAD+ + (ADP-D-ribosyl)n-P2X7 ion channel
nicotinamide + (ADP-D-ribosyl)n+1-P2X7 ion channel + H+
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NAD+ + (ADP-D-ribosyl)n-rab4
nicotinamide + (ADP-D-ribosyl)n+1-rab4
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ADP-ribosylation affects Rab4 function in membrane recycling
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NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5
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ADP-ribosylation of Rab5 by ExoS affects endocytosis. Interaction of Rab5 with endosome antigen 1 is markedly diminished after Rab5 ADP-ribosylation by ExoS
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NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5 + H+
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the enzyme ADP-ribosylates Rab5 at Gln79
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NAD+ + (ADP-D-ribosyl)n-RalA
nicotinamide + (ADP-D-ribosyl)n+1-RalA
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ADP-ribosylation of RalA by ExoS interferes with RalA activation and binding to its downstream effector in J774A.1 macrophages and suggests the potential of ExoS ADPRT activity to interfere with filiopodium formation through the inactivation of RalA and downstream effects mediated through the exocyst complex
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NAD+ + (ADP-D-ribosyl)n-Ras
nicotinamide + (ADP-D-ribosyl)n+1-Ras
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ADP-ribosylation of Ras at Arg41 disrupts Ras-Cdc25 interactions, which inhibits the rate-limiting step in Ras signal transduction, the activation of Ras by its guanine nucleotide exchange factor
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NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Btk
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Btk + H+
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NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Csk
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Csk + H+
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NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Hck
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Hck + H+
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NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Lyn
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Lyn + H+
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NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Src
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Src + H+
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NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Syk
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Syk + H+
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NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Tec
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Tec + H+
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NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Yes1
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Yes1 + H+
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NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
NAD+ + Galphai
nicotinamide + (ADP-D-ribosyl)-Galphai + H+
NAD+ + histone H2A
nicotinamide + (ADP-D-ribosyl)-histone H2A
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the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
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NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
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the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
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NAD+ + moesin
nicotinamide + (ADP-D-ribosyl)-moesin
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ADP-ribosylated-moesin is a poor target for phosphorylation by protein kinase C and Rho kinase, which shows that ADP-ribosylation directly inhibits ERM phosphorylation
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NAD+ + p53
nicotinamide + (ADP-D-ribosyl)-p53
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NAD+ + Rab31
nicotinamide + (ADP-D-ribosyl)-Rab31 + H+
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the enzyme ADP-ribosylates Rab31 at Gln64
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NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
NAD+ + Ras
nicotinamide + (ADP-D-ribosyl)-Ras
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interaction requires residue Leu428
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NAD+ + Ras GTPase
nicotinamide + (ADP-D-ribosyl)-Ras GTPase
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NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
NAD+ + topoisomerase I
nicotinamide + (ADP-D-ribosyl)-topoisomerase I
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NAD+ + vimentin
nicotinamide + (ADP-D-ribosyl)-vimentin
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additional information
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
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the enzyme is a DNA repair enzyme
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
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poly(ADP-ribosyl)ation, i.e. PARylation, plays diverse roles in many molecular and cellular processes, including DNA damage detection and repair, chromatin modification, transcription, cell death pathways, insulator function, and mitotic apparatus function, connections between nuclear NAD+ metabolism and nuclear signaling through PARP-1, physiologic functions, detailed overview, synthesis and degradation of PAR on an acceptor protein, pathway overview, the enzyme is involved in regulation of the steady-state levels of PAR
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
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poly(ADP-ribosyl)ation, i.e. PARylation, plays diverse roles in many molecular and cellular processes, including DNA damage detection and repair, chromatin modification, transcription, cell death pathways, insulator function, and mitotic apparatus function, connections between nuclear NAD+ metabolism and nuclear signaling through PARP-1, physiologic functions, detailed overview, synthesis and degradation of PAR on an acceptor protein, pathway overview, the enzyme is involved in regulation of the steady-state levels of PAR
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
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ADPRT domain of ExoT is active in vivo and contributes to the pathogenesis of Pseudomonas aeruginosa infections
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
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exoenzyme S is an ADP-ribosyltransferase produced and directly translocated into eukaryotic cells by the opportunistic pathogen Pseudomonas aeruginosa. Factors expressed by growing epithelial cells are required for the bacterial contact-dependent translocation of ExoS. As normal epithelial cells differentiate into polarized confluent monolayers, expression of these factors is altered, and cells in turn become more resistant to the effects of ExoS
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
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ExoS can modify multiple GTPases of the Ras superfamily in vivo. ExoS modulates the activity of several of GTP-binding proteins, such as Ras, Rap1, Rap2, Ral, Rac1, RhoA and Cdc42. It is suggested that ExoS is the major ADP-ribosyltransferase protein modulating small GTPase function encoded by Pseudomonas aeruginosa
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
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ExoT modifies and inactivates host cell proteins involved in maintaining the actin cytoskeleton in vivo by two independent mechanisms. ADP-ribosylation activity of ExoT induces an irreversible disruption of actin microfilaments of infected Hela cells
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
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intracellular expression of the amino terminus of ExoS in eukaryotic cells stimulates actin reorganization without cytotoxicity, which involves small-molecular-weight GTPases of the Rho subfamily
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
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intracellular Ras is modified by bacterially translocated ExoS, inhibition of target cell proliferation correlates with the efficiency of Ras modification
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the emzyme protects homologous DNA against thermal denaturation by lowering the amount of melted DNA and increasing melting temperature. The archaeal protein induces structural changes of the nucleic acid by modifying the dichroic spectra towards a shape typical of condensing DNA
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the emzyme protects homologous DNA against thermal denaturation by lowering the amount of melted DNA and increasing melting temperature. The archaeal protein induces structural changes of the nucleic acid by modifying the dichroic spectra towards a shape typical of condensing DNA
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
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NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
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NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
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NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
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NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
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cytosolic protein of several human epithelial cells, modification at Arg55 and Arg69 of cyclophilin A, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, overview
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NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
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cytosolic protein of several human epithelial cells, modification at Arg55 and Arg69 of cyclophilin A, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, overview
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NAD+ + Galphai
nicotinamide + (ADP-D-ribosyl)-Galphai + H+
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NAD+ + Galphai
nicotinamide + (ADP-D-ribosyl)-Galphai + H+
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NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
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Rab5 mediates entry of the EGFR into early endosomes
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NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
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Rab5 mediates entry of the EGFR into early endosomes
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NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
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NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
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NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4
three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
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NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4 ModA
three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
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NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4 ModB
three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
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additional information
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cuts produced in vivo on DNA during DNA repair activate the enzyme, which then synthesiszes poly(ADP-ribose) on histone H1, in particular, and contributes to the opening of the 25 nm chromatin fiber, resulting in the increased accessibility of DNA to excision repair enzymes
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additional information
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the enzyme modifies eukaryotic 21000-24000 Da GTP-binding proteins
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additional information
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transcriptional regulation mechanism, overview
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additional information
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ADP-ribosylation seems to be involved in regulation of differentiation, the enzyme may be centrally involved in tumorigenic cell transformation, the enzyme appears to be a central controller of cell processes: higher activities shift the cell towards proliferation, low activities shift the cell towards differentiation, role of the enzyme in DNA repair
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additional information
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role of the enzyme in DNA repair, the unmodified polymerase molecules bind tightly to DNA strand breaks: auto-poly(ADP-ribosyl)ation of the protein then effects its release and allows access to lesions for DNA repair enzymes
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additional information
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mechanistic basis for the physiological function of PARP-1 in the dynamics of the local modulation of chromatin structure. PARP-1 activation upon binding to base-unpaired regions and stem-loops structures in DNA leads to a local PAR modification of histones and non-histone proteins at genomic sites where such DNA structures are formed. Subsequent PARP-1 automodification results in its dissociation from DNA leading to an enzymatic self-inactivation thus ensuring a transient character of chromatin ADP-ribosylation. In combination with the PAR-glycohydrolase degradation of ADP-ribose polymers on acceptor proteins, PARP-1 interaction with DNA secondary structures provides a mechanism for local and transient chromatin modification by PAR during physiological nuclear processes
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additional information
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PARP-1 inhibits the transcription factor tonicity-responsive enhancer/osmotic response element-binding protein, TonEBP/OREBP. Inhibition of TonEBP/OREBP transcriptional activity by PARP-1 does not require PARP-1 catalytic activity, functional interaction anaylsis, overview
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additional information
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the enzyme is involved in pathogenesis of Parkinson's disease, analysis of polymorphisms, overview
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additional information
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the enzyme has the ability to ADP-ribosylate itself
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additional information
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raft association focuses ART2.2 on specific targets that constitutively or inducibly assoiate with lipid rafts
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additional information
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PARP-1 is involved in modulation of NO-derived injury and response to genotoxic damage
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additional information
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PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
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additional information
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PARP-1 plays fundamental roles in the recruitment and modulation of enzymatic and regulatory factors involved in transcription, DNA replication, repair and recombination, the enzyme antagonizes topoisomerase I-dependent recombination stimulation by P53
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additional information
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PARP-1 responds to DNA damage by transferring 50 to 200 molecules of ADP-ribose to various nuclear proteins, including transcription factors, histones and PARP-1 itself, interaction between ATM and PARP-1 in response to DNA damage and sensitization of ATM deficient cells through PARP inhibition, ATM and PARP-1 are two of the most important players in the cell's response to DNA damage, PARP-1 is needed for optimal activation of ATM, overview
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additional information
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role for PARP-1 in DNA double-strand break repair, the enzyme is not required for homologous recombination itself, it regulates the process through its involvement in the repair of DNA single-strand breaks, PARP-1 binds to DNA breaks to facilitate DNA repair, but the role of PARP-1 in DNA repair appears to not be critical since PARP-1 knockout mice are viable, fertile and do not develop early onset tumors, DNA binding and auto-modification of PARP-1 attracts the DNA repair proteins
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additional information
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the enzyme is involved in endothelial cell dysfunction
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additional information
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transcriptional regulation mechanism, overview
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additional information
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the enzyme itself is a target for P2X7-triggered ectodomain shedding at F239/S240
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additional information
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the enzyme is involved in endothelial cell dysfunction
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additional information
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PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
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additional information
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exoenzyme S and 14-3-3 interact in a direct fashion, interaction involves the conserved amphiphatic groove of 14-3-3
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additional information
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exoenzyme S is an important adhesin
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additional information
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ExoS is a virulence factor of the pathogen
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additional information
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Pseudomonas aeruginosa inhibits mammalian cytokinesis in a type III secretion system and exotoxin T-dependent manner, the ADP-ribosyl transferase domain inhibits late steps of cytokinesis by blocking syntaxin-2 localization to the midbody, an event essential for completion of cytokinesis, e.g. in Madin-Darby canine kidney cells, mechanism, overview
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additional information
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the bacterial enzyme shows the ability to mediate cell death in the host and is a toxin, residues 426-428 are required for this activity
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additional information
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ExoS is a toxin playing a pivotal role during Pseudomonas aeruginosa infections, it is a virulence factor causing growth inhibition in Saccharomyces cerevisiae. Exoenzyme S ADP-ribosylates identical targets in both human and yeast
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additional information
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ExoS is a type III cytotoxin, that ADP-ribosylates Rab GTPases to inhibit host cell vesicle trafficking pathways by modulating HeLa host cell endocytosis, wild-type ExoS uncouples Rab5-early endosome antigen 1 interaction and inhibits fluid phase uptake, as well as Pseudomonas aeruginosa internalization, RhoGAP, but not ADPr, the ADPr domain is dispensable for anti-internalization function, but is required for inhibition of EGF-activated EGFR degradation in HeLa cells, mechanism, overview
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additional information
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ExoS is a type III cytotoxin, that ADP-ribosylates Rab GTPases to inhibit host cell vesicle trafficking pathways by modulating HeLa host cell endocytosis, wild-type ExoS uncouples Rab5-early endosome antigen 1 interaction and inhibits fluid phase uptake, as well as Pseudomonas aeruginosa internalization, RhoGAP, but not ADPr, the ADPr domain is dispensable for anti-internalization function, but is required for inhibition of EGF-activated EGFR degradation in HeLa cells, mechanism, overview
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