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Information on EC 3.2.1.143 - poly(ADP-ribose) glycohydrolase and Organism(s) Homo sapiens

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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
poly(adp-ribose) glycohydrolase, parg1, par glycohydrolase, poly (adp-ribose) glycohydrolase, adprhl2, poly(adp-ribose)glycohydrolase, parg110, adp-ribose glycohydrolase, adp-ribosyl-acceptor hydrolase 3, drparg, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ADP-ribose glycohydrolase
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ADP-ribosyl-acceptor hydrolase 3
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Genbank AB019366-derived protein GI 6518480
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Genbank U78975-derived protein GI 2062407
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glycohydrolase, poly(adenosine diphosphoribose)
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glycohydrolase, poly(adenosine diphosphoribose) (cattle clone 4/5)
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glycohydrolase, poly(adenosine diphosphoribose) (Rattus norvegicus strain BUF gene Parg)
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PAR glycohydrolase
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PAR glyco­hydrolase
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PARG111
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full-length enzyme
PARG59
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poly (ADP-ribose) glycohydrolase
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poly(adenosine diphosphoribose) glycohydrolase
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poly(adenosine diphosphoribose) glycosidase
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poly(ADP-ribose) glycohydrolase
poly(ADP-ribose) glycohydrolase (Arabidopsis thaliana gene At2g31860)
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poly(ADP-ribose) glycohydrolase (Arabidopsis thaliana gene At2g31870)
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poly(ADP-ribose) glycohydrolase (cattly clone 4/5)
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poly(ADP-ribosyl) glycohydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(ADP-ribose)n + H2O = (ADP-ribose)n-1 + ADP-ribose
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
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hydrolysis of O-glycosyl bonds
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CAS REGISTRY NUMBER
COMMENTARY hide
190209-88-2
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253766-41-5
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253766-42-6
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253767-74-7
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9068-16-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(ADP-D-ribose)15 + H2O
(ADP-ribose)14 + ADP-D-ribose
show the reaction diagram
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-
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?
2'-O-(ADP-ribosyl)-adenosine 5'-phosphate + H2O
?
show the reaction diagram
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-
-
?
2'-O-acetyl-ADP-ribose + H2O
ADP-ribose + acetate
show the reaction diagram
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rate of hydrolysis by isoform ARH3 is 250fold that observed with isoform ARH1, isoform ARH2 is inactive with this substrate
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-
?
ADP-ribose dimer + H2O
2 ADP-ribose
show the reaction diagram
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
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?
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
show the reaction diagram
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?
poly(ADP-ribose) + H2O
?
show the reaction diagram
poly(ADP-ribose) + H2O
ADP-ribose + ADP-ribose oligomer
show the reaction diagram
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P32-labelled poly(ADP-ribose) produced by PARP-1 (poly(ADP-ribose) polymerase) of labelled NAD+
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?
poly(ADP-ribose) + H2O
ADP-ribose oligomer + ADP-ribose
show the reaction diagram
poly(ADP-ribose)n + H2O
?
show the reaction diagram
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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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?
poly(ADP-ribose)n + H2O
ADP-ribose
show the reaction diagram
poly(ADP-ribose)n-poly(ADP-ribose) polymerase + H2O
ADP-ribose + poly(ADP-ribose) polymerase
show the reaction diagram
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?
propargyl ADP-ribose dimer + H2O
propargyl ADP-ribose + ADP-ribose
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
poly(ADP-D-ribose)n + H2O
poly(ADP-D-ribose)n-1 + ADP-ribose
show the reaction diagram
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?
poly(ADP-ribose) + H2O
?
show the reaction diagram
poly(ADP-ribose)n + H2O
?
show the reaction diagram
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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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MgCl2
10 mM, activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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
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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
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specific detergent-insensitive inhibition
1,3-diethyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
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1,3-dimethyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
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1-(cyclopropylmethyl)-N-(1-methylcyclopropyl)-3-[(1-methylpyrazol-4-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-(cyclopropylmethyl)-N-(1-methylcyclopropyl)-3-[(2-methylthiazol-5-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-(cyclopropylmethyl)-N-(1-methylcyclopropyl)-3-[(3-methylisoxazol-5-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-ethyl-N-(1-methylcyclopropyl)-3-[(1-methylpyrazol-4-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-ethyl-N-(1-methylcyclopropyl)-3-[(3-methylisoxazol-5-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-ethyl-N-(1-methylcyclopropyl)-3-[(5-methyl-1,3,4-thiadiazol-2-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyc lopropyl)-2,4-dioxo-3-(3-thienylmethyl)quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-1,2,3,4-tetrahydroquinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-(1H-pyrazol-4-ylmethyl)quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-(2-pyridylmethyl)quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-(3-pyridylmethyl)quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-(4-pyridylmethyl)quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-(thiadiazol-4-ylmethyl)quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-(thiazol-2-ylmethyl)quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-(thiazol-5-ylmethyl)quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-phenacyl-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-phenyl-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-prop-2-ynyl-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-3-[2-oxo-2-(4-pyridyl)ethyl]quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-(oxazol-4-ylmethyl)-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-(oxetan-3-ylmethyl)-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(1-methylpyrazol-3-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(1-methylpyrazol-4-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(1-methyltetrazol-5-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(2-methyl-4-phenyl-thiazol-5-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(2-methylpyrazol-3-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(2-methylthiazol-4-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(2-methylthiazol-5-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(3-methyl-1,2,4-oxadiazol-5-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(3-methyl-1H-pyrazol-5-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(3-methylimidazol-4-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(3-methylisoxazol-5-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(4-methyl-1,2,4-triazol-3-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(4-methylthiadiazol-5-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(5-methyl-1,3,4-oxadiazol-2-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(5-methyl-1,3,4-thiadiazol-2-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(5-methylisoxazol-3-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-methyl-N-(1-methylcyclopropyl)-3-[(5-methylisoxazol-4-yl)-methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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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
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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
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1-[(2,4-dimethylthiazol-5-yl)methyl]-N-(1-methylcyclopropyl)-3-[(1-methylpyrazol-4-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-[(2,4-dimethylthiazol-5-yl)methyl]-N-(1-methylcyclopropyl)-3-[(2-methylthiazol-5-yl)methyl]-2,4-dioxo-quinazoline-6-sulfonamide
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1-[(2,5-dimethylpyrazol-3-yl)methyl]-3-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
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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
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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
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1-[(2-fluorophenyl)methyl]-3-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
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1-[(2-methoxyphenyl)methyl]-3-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
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1-[(3-fluorophenyl)methyl]-3-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
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1-[(3-methoxyphenyl)methyl]-3-methyl-N-(1-methylcyclopropyl)-2,4-dioxo-quinazoline-6-sulfonamide
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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
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2-[(9,10-dioxo-2-anthryl)sulfonylamino]acetamide
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3,5-dichloro-2-hydroxy-N-(3-methyl-4-(naphthalen-2-yloxy)phenyl)benzamide
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3,5-dichloro-2-hydroxy-N-(4-(naphthalen-2-yloxy)-3-(trifluoromethyl)phenyl)benzamide
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3,5-dichloro-2-hydroxy-N-(4-(naphthalen-2-yloxy)phenyl)benzamide
-
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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
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3,5-dichloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
-
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3,5-dichloro-N-(3-chloro-4-(p-tolyloxy)phenyl)-2-hydroxybenzamide
-
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3,5-dichloro-N-(3-chloro-4-phenoxyphenyl)-2-hydroxybenzamide
-
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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-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
-
5-chloro-N-(3-chloro-4-(naphthalen-2-yloxy)phenyl)-2-hydroxybenzamide
-
-
8-n-octyl-amino-adenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
binding structure with mutant enzyme K616A/Q617A/K618A/E688A/K689A/K690A
adenosine 5'-diphosphate (hydroxymethyl)pyrrolidinediol
ADP-HPD, binding structure with mutant enzyme K616A/Q617A/K618A/E688A/K689A/K690A
adenosine diphosphate (hydroxymethyl) pyrrolidinediol
adenosine diphosphate(hydroxymethyl)pyrrolidine 3,4-diol
-
ADP-(hydroxymethyl)pyrrolidinediol
-
-
ADP-ribose
cAMP
-
-
Congo red
-
detergent-sensitive inhibition with complete loss of inhibition in the presence of detergent
ethacridine
-
-
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
gallic acid
-
0.1 mg/ml, 9% inhibition
galloylgallic acid
-
0.1 mg/ml, 11% inhibition
glucuronic acid
-
0.1 mg/ml, 14% inhibition
N'1,N'4-bis[(E)-(2,3,4-trihydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
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-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
-
-
PDD00017273
-
phloxine B
-
salicylanilides
-
-
-
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)
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0058
(ADP-D-ribose)15
-
-
-
0.009
Poly(ADP-ribose)
purified recombinant catalytic enzyme domain, in 50 mM KPO4 (pH 7.2), at 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.0465
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
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
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00102
-
full length enzyme PARG111, pH and temperature not specified in the publication
35.6
purified recombinant catalytic enzyme domain, at pH 7.2, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
7.8
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
26
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
during mitosis
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADPRS_HUMAN
363
0
38947
Swiss-Prot
Mitochondrion (Reliability: 2)
PARG_HUMAN
976
0
111110
Swiss-Prot
other Location (Reliability: 5)
B4DX76_HUMAN
516
0
59585
TrEMBL
Mitochondrion (Reliability: 2)
Q0MQR4_HUMAN
976
0
110970
TrEMBL
other Location (Reliability: 5)
B7Z2K8_HUMAN
136
0
14737
TrEMBL
Mitochondrion (Reliability: 3)
B4DHS4_HUMAN
244
0
27773
TrEMBL
other Location (Reliability: 2)
B4DF23_HUMAN
153
0
17589
TrEMBL
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
x * 100000, SDS-PAGE
39000
x * 39000, SDS-PAGE
56000
-
gel filtration
59000
-
1 * 59000, SDS-PAGE
90000
x * 90000, purified recombinant catalytic enzyme domain, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 59000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
PARG59 expression constructs with amino acids encoded by exon 4 at the N-terminus 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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified ARH3-ADPR substrate complex, sitting drop vapour diffusion method, ARH3 and ADPR are mixed in the molar ratio of 1:3, mixing of equal volumes of 11 mg/ml protein complex in 10 mM Tris-HCl, pH 8.0, and 100 mM NaCl with reservoir solution consisting of 0.1 M MES, pH 6.0, and 20% w/v PEG MME 2000, addition of 0.2 M non-detergent sulfobetaine NDSB-201, 20°C, X-ray diffraction structure determination and analysis at 1.58 A resolution, molecular replacement using the structure of apo-ARH3 (PDB ID 2FOZ) as the search model, modeling
purified enzyme in complex with ADP-ribose dimer, X-ray diffraction structure determination and analysis at 1.9 A resolution
purified recombinant full-length ARH3 wild-type enzyme and D314E mutant in complex with ADP-ribose and Mg2+, hanging drop vapor diffusion method, 10 mg/ml protein in 25 mM Tris-HCl, pH 7.5, 150 mM NaCl, 1 mM DTT, and 5% glycerol, is mixed with reservoir solution containing 22% PEG 4000, 0.1 M sodium acetate, pH 4.5, and 0.1 M MgSO4, at 22°C, crystals are briefly equilibrated in a harvesting solution containing 26% PEG 4000, 0.1 M sodium acetate, pH 4.5, 0.1 M MgSO4, and 5 mM ADP-ribose, transferred to a cryoprotectant solution (26% PEG 4000, 0.1 M sodium acetate, pH 4.5, 0.1 M MgSO4, 5 mM ADPR, and 15% glycerol), and then flash-cooled in liquid nitrogen for data collection, X-ray diffraction structure determination and analysis at 1.6-1.7 A resolution, molecular replacement using the apo-ARH3DELTAN16 structure as a search model
purified recombinant mutant K616A/Q617A/K618A/E688A/K689A/K690A, also in selenomethionine-labeld form, in complex with inhibitors, sitting drop vapour diffusion, mixing protein in SEC buffer at 7.5 mg/mL with a precipitant consisting of 28% PEG 3350, 0.2 M magnesium chloride, 0.1 M PCTP (0.04 M sodium propionate, 0.02 M sodium cacodylate, 0.04 M Bis-Tris propane), pH 7.5, in a 1:1 ratio to give a 0.004 ml drop, 20°C, X-ray diffraction structure determination and analysis at 1.75-1.83 A resolution, molecular replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
E755A
-
inactive
E755N
site-directed mutagenesis, inactive mutant
E756A
-
inactive
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
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
-
poly(ADP-ribose) glycohydrolase II
-
recombinant C-terminally His-tagged hPARG from Escherichia coli BL21(DE3) Gold by nickel affinity chromatography and gel filtration
recombinant His-tagged wild-type enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage through rhinovirus 3C (HRV 3C) protease, anion exchange chromatography, gel filtration, and ultrafiltration, recombinant GST-tagged mutant enzymes by glutathione affinity chromatography
recombinant human PARG catalytic domain (residues 448-976) from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography, heparin chromatography, and gel filtration, recombinant His-tagged full-length wild-type and mutant D314E enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage through PreScission protease, and gel filtration, followed by ultrafiltration
recombinant N-terminally, TEV protease-cleavable His6-tagged wild-type and mutant enzymes, and selenomethionine-labeled enzyme from Escherichia coli strains BL21 (DE3) GOLD and B834 (DE3) by nickel affinity chromatography and gel filtration
Talon immobilized metal affinity resin column chromatography and glutathione-Sepharose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli K12 TB1 and Rosetta ells
-
expression in HeLa cell
expression of His-tagged wild-type and mutant enzymes and selenomethionine-labeled enzyme in Escherichia coli strain BL21 (DE3) GOLD
expression of isoform PARG59 in HeLa cell
-
gene ADPRHL2, recombinant expression of His-tagged human PARG catalytic domain (residues 448-976) from Escherichia coli strain Rosetta (DE3), recombinant expression of His-tagged full-length wild-type and mutant D314E enzymes in Escherichia coli strain BL21(DE3)
gene ADPRHL2, sequence comparisons, recombinant expression of N-terminally His-tagged wild-type enzyme and GST-tagged mutant enzymes in Escherichia coli strain BL21(DE3)
gene PARG, real-time PCR expression analysis
gene PARG, single gene, recombinant expression of C-terminally His-tagged hPARG in Escherichia coli BL21(DE3) Gold
the catalytic domain is expressed in Escherichia coli Rosetta2 (DE3) cells as a fusion protein with a glutathione S-transferase tag at the N-terminus and a hexahistidine tag at the C-terminus
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
medicine
molecular biology
specific killing of DNA damage-response deficient cells with inhibitors of poly(ADP-ribose) glycohydrolase
pharmacology
PARG is a potential interventional target to improve the efficacy of cancer chemotherapy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tanuma, S.i.; Sakagami, H.; Endo, H.
Inhibitory effect of tannin on poly(ADP-rinbose) glycohydrolase
Biochem. Int.
18
701-708
1989
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Botta, D.; Jacobson, M.K.
Identification of a regulatory segment of poly(ADP-ribose) glycohydrolase
Biochemistry
49
7674-7682
2010
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
-
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team