PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22000507-2 2011 A recent study in Nature (Slade et al., 2011) reports the structure of PAR glycohydrolase (PARG), revealing unexpected similarity to the ubiquitous ADP-ribose-binding macrodomains. Ribose 152-158 poly(ADP-ribose) glycohydrolase Homo sapiens 71-89 25706250-3 2015 Here we describe the chemical synthesis of the ADP-ribose dimer, and we use this compound to obtain the first human PARG substrate-enzyme cocrystal structure. Ribose 51-57 poly(ADP-ribose) glycohydrolase Homo sapiens 116-120 23524370-3 2013 In this work, we present a computational study on the hydrolysis of glycosidic ribose-ribose bond catalyzed by PARG using hybrid density functional theory (DFT) methods. Ribose 79-85 poly(ADP-ribose) glycohydrolase Homo sapiens 111-115 23524370-3 2013 In this work, we present a computational study on the hydrolysis of glycosidic ribose-ribose bond catalyzed by PARG using hybrid density functional theory (DFT) methods. Ribose 86-92 poly(ADP-ribose) glycohydrolase Homo sapiens 111-115 23467693-2 2013 In order to investigate the biological effects of degradation of poly(ADP-ribose), knockdown of the poly(ADP-ribose) glycohydrolase (PARG) gene was performed by introducing a short interfering RNA (siRNA)-pool into HeLa S3 cells. Ribose 74-80 poly(ADP-ribose) glycohydrolase Homo sapiens 133-137 28687616-4 2017 HuR-dependent upregulation of PARG expression facilitated DNA repair via hydrolysis of polyADP-ribose on related repair proteins. Ribose 95-101 poly(ADP-ribose) glycohydrolase Homo sapiens 30-34 27406238-3 2016 Protein ADP-ribosylation can be reversed by the macrodomain-containing proteins PARG, TARG1, MacroD1 and MacroD2, which hydrolyse the ester bond known to link proteins to ADP-ribose as well as consecutive ADP-ribose subunits; targeting this bond can thus result in the complete removal of the protein modification or the conversion of poly(ADP-ribose) to mono(ADP-ribose). Ribose 175-181 poly(ADP-ribose) glycohydrolase Homo sapiens 80-84 27406238-3 2016 Protein ADP-ribosylation can be reversed by the macrodomain-containing proteins PARG, TARG1, MacroD1 and MacroD2, which hydrolyse the ester bond known to link proteins to ADP-ribose as well as consecutive ADP-ribose subunits; targeting this bond can thus result in the complete removal of the protein modification or the conversion of poly(ADP-ribose) to mono(ADP-ribose). Ribose 209-215 poly(ADP-ribose) glycohydrolase Homo sapiens 80-84 27406238-3 2016 Protein ADP-ribosylation can be reversed by the macrodomain-containing proteins PARG, TARG1, MacroD1 and MacroD2, which hydrolyse the ester bond known to link proteins to ADP-ribose as well as consecutive ADP-ribose subunits; targeting this bond can thus result in the complete removal of the protein modification or the conversion of poly(ADP-ribose) to mono(ADP-ribose). Ribose 209-215 poly(ADP-ribose) glycohydrolase Homo sapiens 80-84 22000507-2 2011 A recent study in Nature (Slade et al., 2011) reports the structure of PAR glycohydrolase (PARG), revealing unexpected similarity to the ubiquitous ADP-ribose-binding macrodomains. Ribose 152-158 poly(ADP-ribose) glycohydrolase Homo sapiens 91-95 21892188-3 2011 PAR glycohydrolase (PARG) is the only protein capable of specific hydrolysis of the ribose-ribose bonds present in PAR chains; its deficiency leads to cell death. Ribose 84-90 poly(ADP-ribose) glycohydrolase Homo sapiens 0-18 21892188-3 2011 PAR glycohydrolase (PARG) is the only protein capable of specific hydrolysis of the ribose-ribose bonds present in PAR chains; its deficiency leads to cell death. Ribose 84-90 poly(ADP-ribose) glycohydrolase Homo sapiens 20-24 21892188-3 2011 PAR glycohydrolase (PARG) is the only protein capable of specific hydrolysis of the ribose-ribose bonds present in PAR chains; its deficiency leads to cell death. Ribose 91-97 poly(ADP-ribose) glycohydrolase Homo sapiens 0-18 21892188-3 2011 PAR glycohydrolase (PARG) is the only protein capable of specific hydrolysis of the ribose-ribose bonds present in PAR chains; its deficiency leads to cell death. Ribose 91-97 poly(ADP-ribose) glycohydrolase Homo sapiens 20-24 21892188-5 2011 We present the first PARG crystal structure (derived from the bacterium Thermomonospora curvata), which reveals that the PARG catalytic domain is a distant member of the ubiquitous ADP-ribose-binding macrodomain family. Ribose 185-191 poly(ADP-ribose) glycohydrolase Homo sapiens 21-25 21892188-5 2011 We present the first PARG crystal structure (derived from the bacterium Thermomonospora curvata), which reveals that the PARG catalytic domain is a distant member of the ubiquitous ADP-ribose-binding macrodomain family. Ribose 185-191 poly(ADP-ribose) glycohydrolase Homo sapiens 121-125 17188026-3 2007 ADP-ribose polymers are rapidly catabolized into free ADP-ribose units by poly(ADP-ribose) glycohydrolase (PARG). Ribose 4-10 poly(ADP-ribose) glycohydrolase Homo sapiens 107-111 20079708-2 2010 PARG hydrolyzes glycosidic linkages of poly(ADP-ribose) synthesized by PARP and liberates ADP-ribose residues. Ribose 48-54 poly(ADP-ribose) glycohydrolase Homo sapiens 0-4 20079708-5 2010 However, previous PARG assay systems are not appropriate for high-throughput screening because PARG activity is measured by radioactivities of ADP-ribose residues released from radioisotope (RI)-labeled poly(ADP-ribose). Ribose 147-153 poly(ADP-ribose) glycohydrolase Homo sapiens 95-99 17306228-7 2007 Furthermore, poly(epsilonADP-ribose) inhibited Parg activity to hydrolyse ribose-ribose bonds of poly(ADP-ribose). Ribose 29-35 poly(ADP-ribose) glycohydrolase Homo sapiens 47-51 17306228-7 2007 Furthermore, poly(epsilonADP-ribose) inhibited Parg activity to hydrolyse ribose-ribose bonds of poly(ADP-ribose). Ribose 74-80 poly(ADP-ribose) glycohydrolase Homo sapiens 47-51 17306228-8 2007 This study suggests the possibility that poly(epsilonADP-ribose) might be a useful tool for studying the poly(ADP-ribose) dynamics and function of Parg. Ribose 56-63 poly(ADP-ribose) glycohydrolase Homo sapiens 147-151 16278211-5 2006 We report here the identification of an ARH1-like protein, termed poly(ADP-ribose) hydrolase or ARH3, which exhibited PARG activity, generating ADP-ribose from poly-(ADP-ribose), but did not hydrolyze ADP-ribose-arginine, -cysteine, -diphthamide, or -asparagine bonds. Ribose 75-81 poly(ADP-ribose) glycohydrolase Homo sapiens 118-122 15450800-1 2004 The enzyme poly(ADP-ribose) glycohydrolase (PARG) catalyzes the hydrolysis of glycosidic bonds of ADP-ribose polymers, producing monomeric ADP-ribose units. Ribose 20-26 poly(ADP-ribose) glycohydrolase Homo sapiens 44-48 15450800-1 2004 The enzyme poly(ADP-ribose) glycohydrolase (PARG) catalyzes the hydrolysis of glycosidic bonds of ADP-ribose polymers, producing monomeric ADP-ribose units. Ribose 102-108 poly(ADP-ribose) glycohydrolase Homo sapiens 11-42 15450800-1 2004 The enzyme poly(ADP-ribose) glycohydrolase (PARG) catalyzes the hydrolysis of glycosidic bonds of ADP-ribose polymers, producing monomeric ADP-ribose units. Ribose 102-108 poly(ADP-ribose) glycohydrolase Homo sapiens 44-48 15450800-6 2004 This article describes a method whereby the ADP-ribose product of the PARG-catalyzed reaction is converted into a fluorescent dye. Ribose 48-54 poly(ADP-ribose) glycohydrolase Homo sapiens 70-74 14987257-9 2004 Therefore, PARG is likely to contribute to maintaining the active state of PARP-1 by continuously removing inhibitory ADP-ribose residues from PARP-1. Ribose 122-128 poly(ADP-ribose) glycohydrolase Homo sapiens 11-15 14685157-5 2004 The hydrolysis of poly(ADP-ribose) by poly(ADP-ribose) glycohydrolase (PARG) was also required, since specific PARG inhibitors, which limit the production of ADP-ribose molecules, restored the function of ABC transporters. Ribose 27-33 poly(ADP-ribose) glycohydrolase Homo sapiens 38-69 14685157-5 2004 The hydrolysis of poly(ADP-ribose) by poly(ADP-ribose) glycohydrolase (PARG) was also required, since specific PARG inhibitors, which limit the production of ADP-ribose molecules, restored the function of ABC transporters. Ribose 27-33 poly(ADP-ribose) glycohydrolase Homo sapiens 71-75 14685157-5 2004 The hydrolysis of poly(ADP-ribose) by poly(ADP-ribose) glycohydrolase (PARG) was also required, since specific PARG inhibitors, which limit the production of ADP-ribose molecules, restored the function of ABC transporters. Ribose 27-33 poly(ADP-ribose) glycohydrolase Homo sapiens 111-115 3718700-1 1986 Hydrolysis of protein-bound 32P-labelled poly(ADP-ribose) by poly(ADP-ribose) glycohydrolase shows that there is differential accessibility of poly(ADP-ribosyl)ated proteins in chromatin to poly(ADP-ribose) glycohydrolase. Ribose 50-56 poly(ADP-ribose) glycohydrolase Homo sapiens 61-92 14527731-3 2003 At present, only a single enzyme, poly (ADP-ribose) glycohydrolase (PARG), has been identified to catalyze ADP-ribose polymer hydrolysis in the cell causing a rapid turnover of the biopolymer which may ultimately result in lethal depletion of cellular NAD(+) pools. Ribose 44-50 poly(ADP-ribose) glycohydrolase Homo sapiens 68-72 12628300-5 2002 The inhibition of PARG or ADP-ribose-degrading enzymes allowed the demonstration that in vitro synthesized 32P-poly(ADP-ribose) is first digested to ADP-ribose monomers by a typical PARG reaction, and that ADP-ribose is further rapidly converted into AMP by an Mg(2+)-dependent activity. Ribose 30-36 poly(ADP-ribose) glycohydrolase Homo sapiens 182-186 12628300-5 2002 The inhibition of PARG or ADP-ribose-degrading enzymes allowed the demonstration that in vitro synthesized 32P-poly(ADP-ribose) is first digested to ADP-ribose monomers by a typical PARG reaction, and that ADP-ribose is further rapidly converted into AMP by an Mg(2+)-dependent activity. Ribose 120-126 poly(ADP-ribose) glycohydrolase Homo sapiens 18-22 12628300-5 2002 The inhibition of PARG or ADP-ribose-degrading enzymes allowed the demonstration that in vitro synthesized 32P-poly(ADP-ribose) is first digested to ADP-ribose monomers by a typical PARG reaction, and that ADP-ribose is further rapidly converted into AMP by an Mg(2+)-dependent activity. Ribose 120-126 poly(ADP-ribose) glycohydrolase Homo sapiens 182-186 12628300-5 2002 The inhibition of PARG or ADP-ribose-degrading enzymes allowed the demonstration that in vitro synthesized 32P-poly(ADP-ribose) is first digested to ADP-ribose monomers by a typical PARG reaction, and that ADP-ribose is further rapidly converted into AMP by an Mg(2+)-dependent activity. Ribose 120-126 poly(ADP-ribose) glycohydrolase Homo sapiens 18-22 12628300-5 2002 The inhibition of PARG or ADP-ribose-degrading enzymes allowed the demonstration that in vitro synthesized 32P-poly(ADP-ribose) is first digested to ADP-ribose monomers by a typical PARG reaction, and that ADP-ribose is further rapidly converted into AMP by an Mg(2+)-dependent activity. Ribose 120-126 poly(ADP-ribose) glycohydrolase Homo sapiens 182-186 7578425-4 1995 Finally, we have evidence that very short oligomers and even monomers of ADP-ribose covalently bound to proteins can be removed by poly(ADP-ribose) glycohydrolase. Ribose 77-83 poly(ADP-ribose) glycohydrolase Homo sapiens 131-162 3718700-1 1986 Hydrolysis of protein-bound 32P-labelled poly(ADP-ribose) by poly(ADP-ribose) glycohydrolase shows that there is differential accessibility of poly(ADP-ribosyl)ated proteins in chromatin to poly(ADP-ribose) glycohydrolase. Ribose 50-56 poly(ADP-ribose) glycohydrolase Homo sapiens 190-221 6782097-4 1981 Poly(ADP-ribose) glycohydrolase, which specifically hydrolyzes the ribose-ribose bonds of poly(ADP-ribose), also cleaves the ribose-ribose-ribose bonds at the site of branching. Ribose 67-73 poly(ADP-ribose) glycohydrolase Homo sapiens 0-31 6782097-4 1981 Poly(ADP-ribose) glycohydrolase, which specifically hydrolyzes the ribose-ribose bonds of poly(ADP-ribose), also cleaves the ribose-ribose-ribose bonds at the site of branching. Ribose 67-73 poly(ADP-ribose) glycohydrolase Homo sapiens 0-31 6782097-4 1981 Poly(ADP-ribose) glycohydrolase, which specifically hydrolyzes the ribose-ribose bonds of poly(ADP-ribose), also cleaves the ribose-ribose-ribose bonds at the site of branching. Ribose 67-73 poly(ADP-ribose) glycohydrolase Homo sapiens 0-31 33005627-6 2020 Poly(ADP-ribose) glycohydrolase (PARG) reverses the action of PARP enzymes, hydrolysing the ribose-ribose bonds present in poly(ADP-ribose). Ribose 9-15 poly(ADP-ribose) glycohydrolase Homo sapiens 33-37 33005627-6 2020 Poly(ADP-ribose) glycohydrolase (PARG) reverses the action of PARP enzymes, hydrolysing the ribose-ribose bonds present in poly(ADP-ribose). Ribose 92-98 poly(ADP-ribose) glycohydrolase Homo sapiens 0-31 33005627-6 2020 Poly(ADP-ribose) glycohydrolase (PARG) reverses the action of PARP enzymes, hydrolysing the ribose-ribose bonds present in poly(ADP-ribose). Ribose 92-98 poly(ADP-ribose) glycohydrolase Homo sapiens 33-37