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(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
1,3-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-[(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-[(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-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
-
-
Congo red
-
detergent-sensitive inhibition with complete loss of inhibition in the presence of detergent
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
-
-
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 diphosphate (hydroxymethyl) pyrrolidinediol
-
adenosine diphosphate (hydroxymethyl) pyrrolidinediol
-
39% inhibition at 0.025 mM
ADP-ribose
-
-
ADP-ribose
binding structure with mutant enzyme K616A/Q617A/K618A/E688A/K689A/K690A
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
-
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
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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
0.0465
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
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
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
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
-
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
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
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
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
-
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
-
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
-
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
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
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
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
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 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
additional information
structure-based mechanism for the reported endo- and exo-glycohydrolase activities in human enzyme, overview
additional information
-
structure-based mechanism for the reported endo- and exo-glycohydrolase activities in human enzyme, overview
additional information
analysis of the catalytic site structure of ARH3, 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
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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
additional information
-
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
-
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
-
deletion of the regulatory segment/MTS from full-length human PARG111 results in a complete loss of activity
additional information
-
constitutive expression shRNA directed against the catalytic domain of all enzyme isoforms in the 16HBE cell line
additional information
-
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
-
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
-
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
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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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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