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Volumn 23, Issue , 2014, Pages 88-94

Structure and function of the ARH family of ADP-ribosyl-acceptor hydrolases

Author keywords

ADP ribose acceptor hydrolase; ADP ribosylation; ARH; Cholera toxin; Parthanatos; Tumorigenesis

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; ADP RIBOSYL ACCEPTOR HYDROLASE 1; ADP RIBOSYL ACCEPTOR HYDROLASE 3; ARGININE; BACTERIAL TOXIN; GLYCOSIDASE; HYDROLASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; POLY(ADP RIBOSE)GLYCOHYDROLASES; UNCLASSIFIED DRUG; ADPRHL2 PROTEIN, HUMAN; ARH1 PROTEIN, MOUSE; CHOLERA TOXIN; LDLRAP1 PROTEIN, HUMAN; POLY ADP-RIBOSE GLYCOHYDROLASE; POLY(ADENOSINE DIPHOSPHATE RIBOSE); SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 84917680186     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2014.03.005     Document Type: Article
Times cited : (64)

References (102)
  • 2
    • 33749260519 scopus 로고    scopus 로고
    • Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?
    • Hassa P.O., Haenni S.S., Elser M., Hottiger M.O. Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?. Microbiol. Mol. Biol. Rev. 2006, 70:789-829.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 789-829
    • Hassa, P.O.1    Haenni, S.S.2    Elser, M.3    Hottiger, M.O.4
  • 3
    • 0019760719 scopus 로고
    • Mono (ADP-ribosyl)transferases and their effects on cellular metabolism
    • Vaughan M., Moss J. Mono (ADP-ribosyl)transferases and their effects on cellular metabolism. Curr. Top. Cell Regul. 1981, 20:205-246.
    • (1981) Curr. Top. Cell Regul. , vol.20 , pp. 205-246
    • Vaughan, M.1    Moss, J.2
  • 4
    • 0000838807 scopus 로고
    • NAD-dependent inhibition of protein synthesis by Pseudomonas aeruginosa toxin
    • Iglewski B.H., Kabat D. NAD-dependent inhibition of protein synthesis by Pseudomonas aeruginosa toxin. Proc. Natl. Acad. Sci. U. S. A. 1975, 72:2284-2288.
    • (1975) Proc. Natl. Acad. Sci. U. S. A. , vol.72 , pp. 2284-2288
    • Iglewski, B.H.1    Kabat, D.2
  • 6
    • 0347349553 scopus 로고
    • Mechanism of cholera toxin action: covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase system
    • Cassel D., Pfeuffer T. Mechanism of cholera toxin action: covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase system. Proc. Natl. Acad. Sci. U. S. A. 1978, 75:2669-2673.
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 2669-2673
    • Cassel, D.1    Pfeuffer, T.2
  • 7
    • 0020362248 scopus 로고
    • Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model
    • Tamura M., Nogimori K., Murai S., Yajima M., Ito K., Katada T., Ui M., Ishii S. Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model. Biochemistry 1982, 21:5516-5522.
    • (1982) Biochemistry , vol.21 , pp. 5516-5522
    • Tamura, M.1    Nogimori, K.2    Murai, S.3    Yajima, M.4    Ito, K.5    Katada, T.6    Ui, M.7    Ishii, S.8
  • 8
    • 0019332669 scopus 로고
    • Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes
    • Moss J., Stanley S.J., Watkins P.A. Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes. J. Biol. Chem. 1980, 255:5838-5840.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5838-5840
    • Moss, J.1    Stanley, S.J.2    Watkins, P.A.3
  • 9
    • 0021120015 scopus 로고
    • NAD:arginine mono-ADP-ribosyltransferases from animal cells
    • Moss J., Vaughan M. NAD:arginine mono-ADP-ribosyltransferases from animal cells. Methods Enzymol. 1984, 106:430-437.
    • (1984) Methods Enzymol. , vol.106 , pp. 430-437
    • Moss, J.1    Vaughan, M.2
  • 10
    • 0018801346 scopus 로고
    • Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes
    • Moss J., Stanley S.J., Oppenheimer N.J. Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes. J. Biol. Chem. 1979, 254:8891-8894.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8891-8894
    • Moss, J.1    Stanley, S.J.2    Oppenheimer, N.J.3
  • 11
    • 0032797983 scopus 로고    scopus 로고
    • Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases
    • Okazaki I.J., Moss J. Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases. Annu. Rev. Nutr. 1999, 19:485-509.
    • (1999) Annu. Rev. Nutr. , vol.19 , pp. 485-509
    • Okazaki, I.J.1    Moss, J.2
  • 12
    • 1842430537 scopus 로고    scopus 로고
    • Ecto-ADP-ribosyltransferases (ARTs): emerging actors in cell communication and signaling
    • Seman M., Adriouch S., Haag F., Koch-Nolte F. Ecto-ADP-ribosyltransferases (ARTs): emerging actors in cell communication and signaling. Curr. Med. Chem. 2004, 11:857-872.
    • (2004) Curr. Med. Chem. , vol.11 , pp. 857-872
    • Seman, M.1    Adriouch, S.2    Haag, F.3    Koch-Nolte, F.4
  • 13
    • 0032508689 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored and secretory isoforms of mono-ADP-ribosyltransferases
    • Okazaki I.J., Moss J. Glycosylphosphatidylinositol-anchored and secretory isoforms of mono-ADP-ribosyltransferases. J. Biol. Chem. 1998, 273:23617-23620.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23617-23620
    • Okazaki, I.J.1    Moss, J.2
  • 14
    • 0026445547 scopus 로고
    • Molecular characterization of NAD:arginine ADP-ribosyltransferase from rabbit skeletal muscle
    • Zolkiewska A., Nightingale M.S., Moss J. Molecular characterization of NAD:arginine ADP-ribosyltransferase from rabbit skeletal muscle. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:11352-11356.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 11352-11356
    • Zolkiewska, A.1    Nightingale, M.S.2    Moss, J.3
  • 15
    • 0029834653 scopus 로고    scopus 로고
    • Cloning and characterization of a novel membrane-associated lymphocyte NAD:arginine ADP-ribosyltransferase
    • Okazaki I.J., Kim H.J., Moss J. Cloning and characterization of a novel membrane-associated lymphocyte NAD:arginine ADP-ribosyltransferase. J. Biol. Chem. 1996, 271:22052-22057.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22052-22057
    • Okazaki, I.J.1    Kim, H.J.2    Moss, J.3
  • 18
    • 0030908945 scopus 로고    scopus 로고
    • Cell-surface ADP-ribosylation of fibroblast growth factor-2 by an arginine-specific ADP-ribosyltransferase
    • Jones E.M., Baird A. Cell-surface ADP-ribosylation of fibroblast growth factor-2 by an arginine-specific ADP-ribosyltransferase. Biochem. J. 1997, 323(Pt 1):173-177.
    • (1997) Biochem. J. , vol.323 , pp. 173-177
    • Jones, E.M.1    Baird, A.2
  • 19
    • 0034874385 scopus 로고    scopus 로고
    • Inactivation of platelet-derived growth factor-BB following modification by ADP-ribosyltransferase
    • Saxty B.A., Yadollahi-Farsani M., Upton P.D., Johnstone S.R., MacDermot J. Inactivation of platelet-derived growth factor-BB following modification by ADP-ribosyltransferase. Br. J. Pharmacol. 2001, 133:1219-1226.
    • (2001) Br. J. Pharmacol. , vol.133 , pp. 1219-1226
    • Saxty, B.A.1    Yadollahi-Farsani, M.2    Upton, P.D.3    Johnstone, S.R.4    MacDermot, J.5
  • 21
    • 0027331555 scopus 로고
    • Integrin alpha 7 as substrate for a glycosylphosphatidylinositol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells
    • Zolkiewska A., Moss J. Integrin alpha 7 as substrate for a glycosylphosphatidylinositol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells. J. Biol. Chem. 1993, 268:25273-25276.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25273-25276
    • Zolkiewska, A.1    Moss, J.2
  • 23
    • 0033600176 scopus 로고    scopus 로고
    • Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity
    • Frye R.A. Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem. Biophys. Res. Commun. 1999, 260:273-279.
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 273-279
    • Frye, R.A.1
  • 24
    • 70450225307 scopus 로고    scopus 로고
    • Structure-based mechanism of ADP-ribosylation by sirtuins
    • Hawse W.F., Wolberger C. Structure-based mechanism of ADP-ribosylation by sirtuins. J. Biol. Chem. 2009, 284:33654-33661.
    • (2009) J. Biol. Chem. , vol.284 , pp. 33654-33661
    • Hawse, W.F.1    Wolberger, C.2
  • 25
    • 20444409132 scopus 로고    scopus 로고
    • Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase
    • Liszt G., Ford E., Kurtev M., Guarente L. Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase. J. Biol. Chem. 2005, 280:21313-21320.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21313-21320
    • Liszt, G.1    Ford, E.2    Kurtev, M.3    Guarente, L.4
  • 27
    • 0033610894 scopus 로고    scopus 로고
    • CobB, a new member of the SIR2 family of eucaryotic regulatory proteins, is required to compensate for the lack of nicotinate mononucleotide: 5,6-dimethylbenzimidazole phosphoribosyltransferase activity in cobT mutants during cobalamin biosynthesis in Salmonella typhimurium LT2
    • Tsang A.W., Escalante-Semerena J.C. CobB, a new member of the SIR2 family of eucaryotic regulatory proteins, is required to compensate for the lack of nicotinate mononucleotide: 5,6-dimethylbenzimidazole phosphoribosyltransferase activity in cobT mutants during cobalamin biosynthesis in Salmonella typhimurium LT2. J. Biol. Chem. 1998, 273:31788-31794.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31788-31794
    • Tsang, A.W.1    Escalante-Semerena, J.C.2
  • 28
    • 22544439038 scopus 로고    scopus 로고
    • Identification of ADP-ribosylation site in human glutamate dehydrogenase isozymes
    • Choi M.M., Huh J.W., Yang S.J., Cho E.H., Choi S.Y., Cho S.W. Identification of ADP-ribosylation site in human glutamate dehydrogenase isozymes. FEBS Lett. 2005, 579:4125-4130.
    • (2005) FEBS Lett. , vol.579 , pp. 4125-4130
    • Choi, M.M.1    Huh, J.W.2    Yang, S.J.3    Cho, E.H.4    Choi, S.Y.5    Cho, S.W.6
  • 30
    • 84862233980 scopus 로고    scopus 로고
    • PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-ss1
    • Di Paola S., Micaroni M., Di Tullio G., Buccione R., Di Girolamo M. PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-ss1. PLoS One 2012, 7:e37352.
    • (2012) PLoS One , vol.7 , pp. e37352
    • Di Paola, S.1    Micaroni, M.2    Di Tullio, G.3    Buccione, R.4    Di Girolamo, M.5
  • 31
    • 84862758175 scopus 로고    scopus 로고
    • New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
    • Gibson B.A., Kraus W.L. New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs. Nat. Rev. Mol. Cell Biol. 2012, 13:411-424.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 411-424
    • Gibson, B.A.1    Kraus, W.L.2
  • 37
    • 79955957616 scopus 로고    scopus 로고
    • Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm
    • Leung A.K., Vyas S., Rood J.E., Bhutkar A., Sharp P.A., Chang P. Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm. Mol. Cell 2011, 42:489-499.
    • (2011) Mol. Cell , vol.42 , pp. 489-499
    • Leung, A.K.1    Vyas, S.2    Rood, J.E.3    Bhutkar, A.4    Sharp, P.A.5    Chang, P.6
  • 40
    • 84860806404 scopus 로고    scopus 로고
    • Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1
    • Langelier M.F., Planck J.L., Roy S., Pascal J.M. Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1. Science 2012, 336:728-732.
    • (2012) Science , vol.336 , pp. 728-732
    • Langelier, M.F.1    Planck, J.L.2    Roy, S.3    Pascal, J.M.4
  • 41
    • 0019888393 scopus 로고
    • Multiple autopoly(ADP-ribosyl)ation of rat liver poly(ADP-ribose) synthetase. Mode of modification and properties of automodified synthetase
    • Kawaichi M., Ueda K., Hayaishi O. Multiple autopoly(ADP-ribosyl)ation of rat liver poly(ADP-ribose) synthetase. Mode of modification and properties of automodified synthetase. J. Biol. Chem. 1981, 256:9483-9489.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9483-9489
    • Kawaichi, M.1    Ueda, K.2    Hayaishi, O.3
  • 43
    • 67649888368 scopus 로고    scopus 로고
    • Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites
    • Altmeyer M., Messner S., Hassa P.O., Fey M., Hottiger M.O. Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites. Nucl. Acids Res. 2009, 37:3723-3738.
    • (2009) Nucl. Acids Res. , vol.37 , pp. 3723-3738
    • Altmeyer, M.1    Messner, S.2    Hassa, P.O.3    Fey, M.4    Hottiger, M.O.5
  • 44
    • 0019332813 scopus 로고
    • ADP-ribosylation of histone H1. Identification of glutamic acid residues 2, 14, and the COOH-terminal lysine residue as modification sites
    • Ogata N., Ueda K., Kagamiyama H., Hayaishi O. ADP-ribosylation of histone H1. Identification of glutamic acid residues 2, 14, and the COOH-terminal lysine residue as modification sites. J. Biol. Chem. 1980, 255:7616-7620.
    • (1980) J. Biol. Chem. , vol.255 , pp. 7616-7620
    • Ogata, N.1    Ueda, K.2    Kagamiyama, H.3    Hayaishi, O.4
  • 45
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • D'Amours D., Desnoyers S., D'Silva I., Poirier G.G. Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochem. J. 1999, 342(Pt 2):249-268.
    • (1999) Biochem. J. , vol.342 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 46
    • 84886246082 scopus 로고    scopus 로고
    • Proteome-wide identification of poly(ADP-ribosyl)ation targets in different genotoxic stress responses
    • Jungmichel S., Rosenthal F., Altmeyer M., Lukas J., Hottiger M.O., Nielsen M.L. Proteome-wide identification of poly(ADP-ribosyl)ation targets in different genotoxic stress responses. Mol. Cell 2013, 52:272-285.
    • (2013) Mol. Cell , vol.52 , pp. 272-285
    • Jungmichel, S.1    Rosenthal, F.2    Altmeyer, M.3    Lukas, J.4    Hottiger, M.O.5    Nielsen, M.L.6
  • 48
    • 0024571820 scopus 로고
    • ADP-ribosylation of ADPR-transferase and topoisomerase I in intact mouse epidermal cells JB6
    • Krupitza G., Cerutti P. ADP-ribosylation of ADPR-transferase and topoisomerase I in intact mouse epidermal cells JB6. Biochemistry 1989, 28:2034-2040.
    • (1989) Biochemistry , vol.28 , pp. 2034-2040
    • Krupitza, G.1    Cerutti, P.2
  • 49
    • 0019876860 scopus 로고
    • Poly(ADP-ribose) synthetase, a main acceptor of poly(ADP-ribose) in isolated nuclei
    • Ogata N., Ueda K., Kawaichi M., Hayaishi O. Poly(ADP-ribose) synthetase, a main acceptor of poly(ADP-ribose) in isolated nuclei. J. Biol. Chem. 1981, 256:4135-4137.
    • (1981) J. Biol. Chem. , vol.256 , pp. 4135-4137
    • Ogata, N.1    Ueda, K.2    Kawaichi, M.3    Hayaishi, O.4
  • 50
    • 84875939839 scopus 로고    scopus 로고
    • Mapping PARP-1 auto-ADP-ribosylation sites by liquid chromatography-tandem mass spectrometry
    • Chapman J.D., Gagne J.P., Poirier G.G., Goodlett D.R. Mapping PARP-1 auto-ADP-ribosylation sites by liquid chromatography-tandem mass spectrometry. J. Proteome Res. 2013, 12:1868-1880.
    • (2013) J. Proteome Res. , vol.12 , pp. 1868-1880
    • Chapman, J.D.1    Gagne, J.P.2    Poirier, G.G.3    Goodlett, D.R.4
  • 51
    • 0031844311 scopus 로고    scopus 로고
    • XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage
    • Masson M., Niedergang C., Schreiber V., Muller S., Menissier-de Murcia J., de Murcia G. XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage. Mol. Cell Biol. 1998, 18:3563-3571.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 3563-3571
    • Masson, M.1    Niedergang, C.2    Schreiber, V.3    Muller, S.4    Menissier-de Murcia, J.5    de Murcia, G.6
  • 52
    • 35148896262 scopus 로고    scopus 로고
    • Role of poly(ADP-ribose) polymerase 1 (PARP-1) in cardiovascular diseases: the therapeutic potential of PARP inhibitors
    • Pacher P., Szabo C. Role of poly(ADP-ribose) polymerase 1 (PARP-1) in cardiovascular diseases: the therapeutic potential of PARP inhibitors. Cardiovasc. Drug Rev. 2007, 25:235-260.
    • (2007) Cardiovasc. Drug Rev. , vol.25 , pp. 235-260
    • Pacher, P.1    Szabo, C.2
  • 53
    • 18044388712 scopus 로고    scopus 로고
    • Poly (adp-ribose) polymerase inhibitors as potential therapeutic agents in stroke and neurotrauma
    • Komjati K., Besson V.C., Szabo C. Poly (adp-ribose) polymerase inhibitors as potential therapeutic agents in stroke and neurotrauma. Curr. Drug Targets CNS Neurol. Disord. 2005, 4:179-194.
    • (2005) Curr. Drug Targets CNS Neurol. Disord. , vol.4 , pp. 179-194
    • Komjati, K.1    Besson, V.C.2    Szabo, C.3
  • 59
    • 0030000690 scopus 로고    scopus 로고
    • DNA strand breakage, activation of poly (ADP-ribose) synthetase, and cellular energy depletion are involved in the cytotoxicity of macrophages and smooth muscle cells exposed to peroxynitrite
    • Szabo C., Zingarelli B., O'Connor M., Salzman A.L. DNA strand breakage, activation of poly (ADP-ribose) synthetase, and cellular energy depletion are involved in the cytotoxicity of macrophages and smooth muscle cells exposed to peroxynitrite. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:1753-1758.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 1753-1758
    • Szabo, C.1    Zingarelli, B.2    O'Connor, M.3    Salzman, A.L.4
  • 60
    • 0033598713 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion
    • Ha H.C., Snyder S.H. Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:13978-13982.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13978-13982
    • Ha, H.C.1    Snyder, S.H.2
  • 63
    • 0023020120 scopus 로고
    • Purification and characterization of poly(ADP-ribose) glycohydrolase. Different modes of action on large and small poly(ADP-ribose)
    • Hatakeyama K., Nemoto Y., Ueda K., Hayaishi O. Purification and characterization of poly(ADP-ribose) glycohydrolase. Different modes of action on large and small poly(ADP-ribose). J. Biol. Chem. 1986, 261:14902-14911.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14902-14911
    • Hatakeyama, K.1    Nemoto, Y.2    Ueda, K.3    Hayaishi, O.4
  • 64
    • 0015240269 scopus 로고
    • Splitting of the ribose-ribose linkage of poly(adenosine diphosphate-robose) by a calf thymus extract
    • Miwa M., Sugimura T. Splitting of the ribose-ribose linkage of poly(adenosine diphosphate-robose) by a calf thymus extract. J. Biol. Chem. 1971, 246:6362-6364.
    • (1971) J. Biol. Chem. , vol.246 , pp. 6362-6364
    • Miwa, M.1    Sugimura, T.2
  • 65
    • 84860844237 scopus 로고    scopus 로고
    • ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose)
    • Niere M., Mashimo M., Agledal L., Dolle C., Kasamatsu A., Kato J., Moss J., Ziegler M. ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose). J. Biol. Chem. 2012, 287:16088-16102.
    • (2012) J. Biol. Chem. , vol.287 , pp. 16088-16102
    • Niere, M.1    Mashimo, M.2    Agledal, L.3    Dolle, C.4    Kasamatsu, A.5    Kato, J.6    Moss, J.7    Ziegler, M.8
  • 66
    • 2942707644 scopus 로고    scopus 로고
    • Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments
    • 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. 2004, 297:521-532.
    • (2004) Exp. Cell Res. , vol.297 , pp. 521-532
    • Meyer-Ficca, M.L.1    Meyer, R.G.2    Coyle, D.L.3    Jacobson, E.L.4    Jacobson, M.K.5
  • 67
    • 0033080520 scopus 로고    scopus 로고
    • Poly(ADP-ribose) glycohydrolase is present and active in mammalian cells as a 110-kDa protein
    • Winstall E., Affar E.B., Shah R., Bourassa S., Scovassi A.I., Poirier G.G. Poly(ADP-ribose) glycohydrolase is present and active in mammalian cells as a 110-kDa protein. Exp. Cell Res. 1999, 246:395-398.
    • (1999) Exp. Cell Res. , vol.246 , pp. 395-398
    • Winstall, E.1    Affar, E.B.2    Shah, R.3    Bourassa, S.4    Scovassi, A.I.5    Poirier, G.G.6
  • 68
    • 34547153717 scopus 로고    scopus 로고
    • Two small enzyme isoforms mediate mammalian mitochondrial poly(ADP-ribose) glycohydrolase (PARG) activity
    • 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. 2007, 313:2920-2936.
    • (2007) Exp. Cell Res. , vol.313 , pp. 2920-2936
    • Meyer, R.G.1    Meyer-Ficca, M.L.2    Whatcott, C.J.3    Jacobson, E.L.4    Jacobson, M.K.5
  • 73
    • 84879415959 scopus 로고    scopus 로고
    • Macrodomain-containing proteins: regulating new intracellular functions of mono(ADP-ribosyl)ation
    • Feijs K.L., Forst A.H., Verheugd P., Luscher B. Macrodomain-containing proteins: regulating new intracellular functions of mono(ADP-ribosyl)ation. Nat. Rev. Mol. Cell Biol. 2013, 14:443-451.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 443-451
    • Feijs, K.L.1    Forst, A.H.2    Verheugd, P.3    Luscher, B.4
  • 76
    • 33644849513 scopus 로고    scopus 로고
    • Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase
    • Oka S., Kato J., Moss J. Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase. J. Biol. Chem. 2006, 281:705-713.
    • (2006) J. Biol. Chem. , vol.281 , pp. 705-713
    • Oka, S.1    Kato, J.2    Moss, J.3
  • 79
    • 0022366651 scopus 로고
    • Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-l-arginine cleavage enzyme
    • Moss J., Jacobson M.K., Stanley S.J. Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-l-arginine cleavage enzyme. Proc. Natl. Acad. Sci. U. S. A. 1985, 82:5603-5607.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 5603-5607
    • Moss, J.1    Jacobson, M.K.2    Stanley, S.J.3
  • 80
    • 0023055764 scopus 로고
    • Amino acid specific ADP-ribosylation: substrate specificity of an ADP-ribosylarginine hydrolase from turkey erythrocytes
    • Moss J., Oppenheimer N.J., West R.E., Stanley S.J. Amino acid specific ADP-ribosylation: substrate specificity of an ADP-ribosylarginine hydrolase from turkey erythrocytes. Biochemistry 1986, 25:5408-5414.
    • (1986) Biochemistry , vol.25 , pp. 5408-5414
    • Moss, J.1    Oppenheimer, N.J.2    West, R.E.3    Stanley, S.J.4
  • 81
    • 33750940806 scopus 로고    scopus 로고
    • The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases
    • 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. U. S. A. 2006, 103:16687-16691.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 16687-16691
    • Ono, T.1    Kasamatsu, A.2    Oka, S.3    Moss, J.4
  • 83
    • 19344377042 scopus 로고    scopus 로고
    • Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation
    • Liou G.G., Tanny J.C., Kruger R.G., Walz T., Moazed D. Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation. Cell 2005, 121:515-527.
    • (2005) Cell , vol.121 , pp. 515-527
    • Liou, G.G.1    Tanny, J.C.2    Kruger, R.G.3    Walz, T.4    Moazed, D.5
  • 86
    • 66449123334 scopus 로고    scopus 로고
    • + metabolites and modulates cellular redox
    • + metabolites and modulates cellular redox. J. Biol. Chem. 2009, 284:11256-11266.
    • (2009) J. Biol. Chem. , vol.284 , pp. 11256-11266
    • Tong, L.1    Lee, S.2    Denu, J.M.3
  • 87
    • 0033546332 scopus 로고    scopus 로고
    • Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases
    • Konczalik P., Moss J. Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases. J. Biol. Chem. 1999, 274:16736-16740.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16736-16740
    • Konczalik, P.1    Moss, J.2
  • 88
    • 0027198328 scopus 로고
    • Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase
    • Takada T., Iida K., Moss J. Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase. J. Biol. Chem. 1993, 268:17837-17843.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17837-17843
    • Takada, T.1    Iida, K.2    Moss, J.3
  • 89
    • 34547207148 scopus 로고    scopus 로고
    • Enhanced sensitivity to cholera toxin in ADP-ribosylarginine hydrolase-deficient mice
    • Kato J., Zhu J., Liu C., Moss J. Enhanced sensitivity to cholera toxin in ADP-ribosylarginine hydrolase-deficient mice. Mol. Cell Biol. 2007, 27:5534-5543.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 5534-5543
    • Kato, J.1    Zhu, J.2    Liu, C.3    Moss, J.4
  • 92
    • 37849013404 scopus 로고    scopus 로고
    • Functional localization of two poly(ADP-ribose)-degrading enzymes to the mitochondrial matrix
    • Niere M., Kernstock S., Koch-Nolte F., Ziegler M. Functional localization of two poly(ADP-ribose)-degrading enzymes to the mitochondrial matrix. Mol. Cell Biol. 2008, 28:814-824.
    • (2008) Mol. Cell Biol. , vol.28 , pp. 814-824
    • Niere, M.1    Kernstock, S.2    Koch-Nolte, F.3    Ziegler, M.4
  • 93
    • 84888110477 scopus 로고    scopus 로고
    • ADP-ribosyl-acceptor hydrolase 3 regulates poly (ADP-ribose) degradation and cell death during oxidative stress
    • Mashimo M., Kato J., Moss J. ADP-ribosyl-acceptor hydrolase 3 regulates poly (ADP-ribose) degradation and cell death during oxidative stress. Proc. Natl. Acad. Sci. U. S. A. 2013, 110:18964-18969.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 18964-18969
    • Mashimo, M.1    Kato, J.2    Moss, J.3
  • 94
    • 5044232010 scopus 로고    scopus 로고
    • Mitochondrial poly(ADP-ribosylation): from old data to new perspectives
    • Scovassi A.I. Mitochondrial poly(ADP-ribosylation): from old data to new perspectives. FASEB J. 2004, 18:1487-1488.
    • (2004) FASEB J. , vol.18 , pp. 1487-1488
    • Scovassi, A.I.1
  • 95
    • 33751113602 scopus 로고    scopus 로고
    • Mammalian sirtuins - emerging roles in physiology, aging, and calorie restriction
    • Haigis M.C., Guarente L.P. Mammalian sirtuins - emerging roles in physiology, aging, and calorie restriction. Genes Dev. 2006, 20:2913-2921.
    • (2006) Genes Dev. , vol.20 , pp. 2913-2921
    • Haigis, M.C.1    Guarente, L.P.2
  • 96
    • 76049093446 scopus 로고    scopus 로고
    • Outer mitochondrial membrane localization of apoptosis-inducing factor: mechanistic implications for release
    • Yu S.W., Wang Y., Frydenlund D.S., Ottersen O.P., Dawson V.L., Dawson T.M. Outer mitochondrial membrane localization of apoptosis-inducing factor: mechanistic implications for release. ASN Neuro 2009, 1:275-281.
    • (2009) ASN Neuro , vol.1 , pp. 275-281
    • Yu, S.W.1    Wang, Y.2    Frydenlund, D.S.3    Ottersen, O.P.4    Dawson, V.L.5    Dawson, T.M.6
  • 100
    • 0028280995 scopus 로고
    • Endoglycosidic cleavage of branched polymers by poly(ADP-ribose) glycohydrolase
    • Braun S.A., Panzeter P.L., Collinge M.A., Althaus F.R. Endoglycosidic cleavage of branched polymers by poly(ADP-ribose) glycohydrolase. Eur. J. Biochem. 1994, 220:369-375.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 369-375
    • Braun, S.A.1    Panzeter, P.L.2    Collinge, M.A.3    Althaus, F.R.4
  • 102
    • 0027528960 scopus 로고
    • Preferential degradation of protein-bound (ADP-ribose)n by nuclear poly(ADP-ribose) glycohydrolase from human placenta
    • Uchida K., Suzuki H., Maruta H., Abe H., Aoki K., Miwa M., Tanuma S. Preferential degradation of protein-bound (ADP-ribose)n by nuclear poly(ADP-ribose) glycohydrolase from human placenta. J. Biol. Chem. 1993, 268:3194-3200.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3194-3200
    • Uchida, K.1    Suzuki, H.2    Maruta, H.3    Abe, H.4    Aoki, K.5    Miwa, M.6    Tanuma, S.7


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