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PARP1-XRCC1 + H2O
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efficient disassembly of complexes of the DNA scaffold repair protein XRCC1 and the poly(ADP-ribose) polymerase 1 by poly(ADP-ribose) glycohydrolase (PARG)
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poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
poly(ADP-ribose)n + H2O
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poly(ADP-ribosyl)ated-Hrp38 + H2O
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additional information
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poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
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poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
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poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
the activity is dependent on the conserved glutamate residues
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poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
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poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
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poly(ADP-ribose) + H2O
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poly(ADP-ribose) + H2O
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poly(ADP-ribose) + H2O
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poly(ADP-ribose) + H2O
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poly(ADP-ribose) + H2O
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poly(ADP-ribose) + H2O
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poly(ADP-ribose) + H2O
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poly(ADP-ribose) + H2O
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poly(ADP-ribose) + H2O
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poly(ADP-ribose) + H2O
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poly(ADP-ribose) + H2O
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poly(ADP-ribose) + H2O
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poly(ADP-ribose) + H2O
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poly(ADP-ribose) + H2O
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poly(ADP-ribose) + H2O
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poly(ADP-ribose) + H2O
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poly(ADP-ribose) + H2O
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poly(ADP-ribose)n + H2O
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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
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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
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regulates differentially the levels of large and small poly(ADP-ribose) in the cell
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poly(ADP-ribose)n + H2O
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poly(ADP-ribose) glycohydrolase II may be involved in extranuclear de(ADP-ribosyl)n-ation, but not in membrane de-mono(ADP-ribosyl)ation
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additional information
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several isoforms, functions in embryonic development, genotixicity, cell cycle regulation, mitotic spindle assembly, development, differentiation, and cell death
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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transient decrease in nuclear enzyme activity is important for the onset of differentiation of HL-60 cells to macrophage-like cells
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additional information
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poly(ADP-ribose) glycohydrolase is a critical component of single-strand break repair and accelerates this process in concert with poly(ADP-ribose) polymerase
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additional information
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poly(ADP-ribose) glycohydrolase is the only enzyme known to catalyse hydrolysis of the O-glycosidic linkages of ADP-ribose polymers
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additional information
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poly(ADP-ribose) glycohydrolase is the only enzyme known to catalyse hydrolysis of the O-glycosidic linkages of ADP-ribose polymers
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additional information
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enzyme is a necessary component of the poly(ADP-ribose) polymerase 1 mediated cell death pathway
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additional information
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enzyme activity modulates the inflammatory response and tissue events associated with spinal cord trauma and participates in target organ damage under these conditions
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additional information
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function in cell death
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additional information
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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
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