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Volumn 23, Issue , 2014, Pages 4-16

Distribution of protein poly(ADP-ribosyl)ation systems across all domains of life

Author keywords

DNA damage response; Macrodomain; PARG; PARP; Poly(ADP ribose)

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLHYDROLASE 3; DOUBLE STRANDED DNA; HYDROLASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 12; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 13; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 14; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 15; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 7; POLY(ADENOSINE DIPHOSPHATE RIBOSE); POLY(ADENOSINE DIPHOSPHATE RIBOSE) GLYCOHYDROLASE; PROTEIN; TANKYRASE; TRIPELENNAMINE; UNCLASSIFIED DRUG; ARCHAEAL PROTEIN; DNA LIGASE; INSECT PROTEIN; MACROD2 PROTEIN, HUMAN; ONCOPROTEIN; PARP10 PROTEIN, HUMAN; PARP16 PROTEIN, HUMAN; VEGETABLE PROTEIN;

EID: 84916887602     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2014.05.003     Document Type: Article
Times cited : (135)

References (97)
  • 1
    • 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
  • 4
    • 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
  • 5
    • 70349935191 scopus 로고    scopus 로고
    • Identification of the ADP-ribosylation sites in the PARP-1 automodification domain: analysis and implications
    • Tao Z., Gao P., Liu H.W. Identification of the ADP-ribosylation sites in the PARP-1 automodification domain: analysis and implications. J. Am. Chem. Soc. 2009, 131:14258-14260.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 14258-14260
    • Tao, Z.1    Gao, P.2    Liu, H.W.3
  • 7
    • 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
  • 8
    • 25444463296 scopus 로고    scopus 로고
    • Poly(ADP-ribose). The most elaborate metabolite of NAD+
    • Burkle A. Poly(ADP-ribose). The most elaborate metabolite of NAD+. FEBS J. 2005, 272:4576-4589.
    • (2005) FEBS J. , vol.272 , pp. 4576-4589
    • Burkle, A.1
  • 9
    • 77957743077 scopus 로고    scopus 로고
    • Evolutionary history of the poly(ADP-ribose) polymerase gene family in eukaryotes
    • Citarelli M., Teotia S., Lamb R.S. Evolutionary history of the poly(ADP-ribose) polymerase gene family in eukaryotes. BMC Evol. Biol. 2010, 10:308.
    • (2010) BMC Evol. Biol. , vol.10 , pp. 308
    • Citarelli, M.1    Teotia, S.2    Lamb, R.S.3
  • 10
    • 77956526559 scopus 로고    scopus 로고
    • PARP-1 regulates chromatin structure and transcription through a KDM5B-dependent pathway
    • Krishnakumar R., Kraus W.L. PARP-1 regulates chromatin structure and transcription through a KDM5B-dependent pathway. Mol. Cell 2010, 39:736-749.
    • (2010) Mol. Cell , vol.39 , pp. 736-749
    • Krishnakumar, R.1    Kraus, W.L.2
  • 11
    • 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
  • 12
    • 84865731753 scopus 로고    scopus 로고
    • The role of PARP-1 and PARP-2 enzymes in metabolic regulation and disease
    • Bai P., Canto C. The role of PARP-1 and PARP-2 enzymes in metabolic regulation and disease. Cell Metab. 2012, 16:290-295.
    • (2012) Cell Metab. , vol.16 , pp. 290-295
    • Bai, P.1    Canto, C.2
  • 15
    • 33744494346 scopus 로고    scopus 로고
    • Functional characterization of the putative Aspergillus nidulans poly(ADP-ribose) polymerase homolog PrpA
    • Semighini C.P., Savoldi M., Goldman G.H., Harris S.D. Functional characterization of the putative Aspergillus nidulans poly(ADP-ribose) polymerase homolog PrpA. Genetics 2006, 173:87-98.
    • (2006) Genetics , vol.173 , pp. 87-98
    • Semighini, C.P.1    Savoldi, M.2    Goldman, G.H.3    Harris, S.D.4
  • 19
  • 20
    • 77749328925 scopus 로고    scopus 로고
    • The transcription factor interacting protein RCD1 contains a novel conserved domain
    • Jaspers P., Brosche M., Overmyer K., Kangasjarvi J. The transcription factor interacting protein RCD1 contains a novel conserved domain. Plant Signal. Behav. 2010, 5:78-80.
    • (2010) Plant Signal. Behav. , vol.5 , pp. 78-80
    • Jaspers, P.1    Brosche, M.2    Overmyer, K.3    Kangasjarvi, J.4
  • 22
    • 84873694897 scopus 로고    scopus 로고
    • 2,3,7,8-Tetrachlorodibenzo-p-dioxin poly(ADP-ribose) polymerase (TiPARP, ARTD14) is a mono-ADP-ribosyltransferase and repressor of aryl hydrocarbon receptor transactivation
    • MacPherson L., Tamblyn L., Rajendra S., Bralha F., McPherson J.P., Matthews J. 2,3,7,8-Tetrachlorodibenzo-p-dioxin poly(ADP-ribose) polymerase (TiPARP, ARTD14) is a mono-ADP-ribosyltransferase and repressor of aryl hydrocarbon receptor transactivation. Nucleic Acids Res. 2013, 41:1604-1621.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 1604-1621
    • MacPherson, L.1    Tamblyn, L.2    Rajendra, S.3    Bralha, F.4    McPherson, J.P.5    Matthews, J.6
  • 24
    • 0035338814 scopus 로고    scopus 로고
    • The WWE domain: a common interaction module in protein ubiquitination and ADP ribosylation
    • Aravind L. The WWE domain: a common interaction module in protein ubiquitination and ADP ribosylation. Trends Biochem. Sci. 2001, 26:273-275.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 273-275
    • Aravind, L.1
  • 25
    • 8644267555 scopus 로고    scopus 로고
    • The zinc finger antiviral protein directly binds to specific viral mRNAs through the CCCH zinc finger motifs
    • Guo X.M., Carroll J.W.N., MacDonald M.R., Goff S.P., Gao G.X. The zinc finger antiviral protein directly binds to specific viral mRNAs through the CCCH zinc finger motifs. J. Virol. 2004, 78:12781-12787.
    • (2004) J. Virol. , vol.78 , pp. 12781-12787
    • Guo, X.M.1    Carroll, J.W.N.2    MacDonald, M.R.3    Goff, S.P.4    Gao, G.X.5
  • 28
    • 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
  • 29
    • 85016372152 scopus 로고    scopus 로고
    • Molecular insights into poly(ADP-ribose) recognition and processing
    • Zaja R., Mikoc A., Barkauskaite E., Ahel I. Molecular insights into poly(ADP-ribose) recognition and processing. Biomolecules 2013, 3:1-17.
    • (2013) Biomolecules , vol.3 , pp. 1-17
    • Zaja, R.1    Mikoc, A.2    Barkauskaite, E.3    Ahel, I.4
  • 30
    • 84880330905 scopus 로고    scopus 로고
    • Tankyrases as drug targets
    • Lehtio L., Chi N.W., Krauss S. Tankyrases as drug targets. FEBS J. 2013, 280:3576-3593.
    • (2013) FEBS J. , vol.280 , pp. 3576-3593
    • Lehtio, L.1    Chi, N.W.2    Krauss, S.3
  • 31
    • 36749045682 scopus 로고    scopus 로고
    • Tankyrase function at telomeres, spindle poles, and beyond
    • Hsiao S.J., Smith S. Tankyrase function at telomeres, spindle poles, and beyond. Biochimie 2008, 90:83-92.
    • (2008) Biochimie , vol.90 , pp. 83-92
    • Hsiao, S.J.1    Smith, S.2
  • 32
    • 84876935501 scopus 로고    scopus 로고
    • Proteasome regulation by ADP-ribosylation
    • Cho-Park P.F., Steller H. Proteasome regulation by ADP-ribosylation. Cell 2013, 153:614-627.
    • (2013) Cell , vol.153 , pp. 614-627
    • Cho-Park, P.F.1    Steller, H.2
  • 33
    • 85047693635 scopus 로고    scopus 로고
    • Tankyrase-1 polymerization of poly(ADP-ribose) is required for spindle structure and function
    • Chang P., Coughlin M., Mitchison T.J. Tankyrase-1 polymerization of poly(ADP-ribose) is required for spindle structure and function. Nat. Cell Biol. 2005, 7:1133-1139.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1133-1139
    • Chang, P.1    Coughlin, M.2    Mitchison, T.J.3
  • 35
    • 0031046294 scopus 로고    scopus 로고
    • A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins
    • Bork P., Hofmann K., Bucher P., Neuwald A.F., Altschul S.F., Koonin E.V. A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins. FASEB J. 1997, 11:68-76.
    • (1997) FASEB J. , vol.11 , pp. 68-76
    • Bork, P.1    Hofmann, K.2    Bucher, P.3    Neuwald, A.F.4    Altschul, S.F.5    Koonin, E.V.6
  • 37
    • 84863804147 scopus 로고    scopus 로고
    • Crystal structure of human ADP-ribose transferase ARTD15/PARP16 reveals a novel putative regulatory domain
    • Karlberg T., Thorsell A.G., Kallas A., Schuler H. Crystal structure of human ADP-ribose transferase ARTD15/PARP16 reveals a novel putative regulatory domain. J. Biol. Chem. 2012, 287:24077-24081.
    • (2012) J. Biol. Chem. , vol.287 , pp. 24077-24081
    • Karlberg, T.1    Thorsell, A.G.2    Kallas, A.3    Schuler, H.4
  • 38
    • 27644577665 scopus 로고    scopus 로고
    • In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs)
    • Otto H., Reche P.A., Bazan F., Dittmar K., Haag F., Koch-Nolte F. In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs). BMC Genomics 2005, 6:139.
    • (2005) BMC Genomics , vol.6 , pp. 139
    • Otto, H.1    Reche, P.A.2    Bazan, F.3    Dittmar, K.4    Haag, F.5    Koch-Nolte, F.6
  • 39
    • 0032532020 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a poly(ADP-ribose) polymerase-like enzyme from the thermophilic archaeon Sulfolobus solfataricus
    • Faraone-Mennella M.R., Gambacorta A., Nicolaus B., Farina B. Purification and biochemical characterization of a poly(ADP-ribose) polymerase-like enzyme from the thermophilic archaeon Sulfolobus solfataricus. Biochem. J. 1998, 335(Pt 2):441-447.
    • (1998) Biochem. J. , vol.335 , pp. 441-447
    • Faraone-Mennella, M.R.1    Gambacorta, A.2    Nicolaus, B.3    Farina, B.4
  • 43
    • 0031010494 scopus 로고    scopus 로고
    • Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase
    • Lin W., Ame J.C., Aboul-Ela N., Jacobson E.L., Jacobson M.K. Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase. J. Biol. Chem. 1997, 272:11895-11901.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11895-11901
    • Lin, W.1    Ame, J.C.2    Aboul-Ela, N.3    Jacobson, E.L.4    Jacobson, M.K.5
  • 45
    • 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
  • 48
    • 63849128257 scopus 로고    scopus 로고
    • Sensing NAD metabolites through macro domains
    • Till S., Ladurner A.G. Sensing NAD metabolites through macro domains. Front Biosci. (Landmark Ed.) 2009, 14:3246-3258.
    • (2009) Front Biosci. (Landmark Ed.) , vol.14 , pp. 3246-3258
    • Till, S.1    Ladurner, A.G.2
  • 51
    • 84863010981 scopus 로고    scopus 로고
    • Recognition of the iso-ADP-ribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl)ation-dependent ubiquitination
    • Wang Z., Michaud G.A., Cheng Z., Zhang Y., Hinds T.R., Fan E., Cong F., Xu W. Recognition of the iso-ADP-ribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl)ation-dependent ubiquitination. Genes Dev. 2012, 26:235-240.
    • (2012) Genes Dev. , vol.26 , pp. 235-240
    • Wang, Z.1    Michaud, G.A.2    Cheng, Z.3    Zhang, Y.4    Hinds, T.R.5    Fan, E.6    Cong, F.7    Xu, W.8
  • 53
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar R.C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 2004, 32:1792-1797.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 54
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K., Peterson D., Peterson N., Stecher G., Nei M., Kumar S. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol. Biol. Evol. 2011, 28:2731-2739.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 55
    • 18744382506 scopus 로고    scopus 로고
    • ProtTest: selection of best-fit models of protein evolution
    • Abascal F., Zardoya R., Posada D. ProtTest: selection of best-fit models of protein evolution. Bioinformatics 2005, 21:2104-2105.
    • (2005) Bioinformatics , vol.21 , pp. 2104-2105
    • Abascal, F.1    Zardoya, R.2    Posada, D.3
  • 56
    • 0031773680 scopus 로고    scopus 로고
    • MODELTEST: testing the model of DNA substitution
    • Posada D., Crandall K.A. MODELTEST: testing the model of DNA substitution. Bioinformatics 1998, 14:817-818.
    • (1998) Bioinformatics , vol.14 , pp. 817-818
    • Posada, D.1    Crandall, K.A.2
  • 57
    • 0036017382 scopus 로고    scopus 로고
    • RtREV: an amino acid substitution matrix for inference of retrovirus and reverse transcriptase phylogeny
    • Dimmic M.W., Rest J.S., Mindell D.P., Goldstein R.A. rtREV: an amino acid substitution matrix for inference of retrovirus and reverse transcriptase phylogeny. J. Mol. Evol. 2002, 55:65-73.
    • (2002) J. Mol. Evol. , vol.55 , pp. 65-73
    • Dimmic, M.W.1    Rest, J.S.2    Mindell, D.P.3    Goldstein, R.A.4
  • 59
    • 0037102454 scopus 로고    scopus 로고
    • The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development
    • Tulin A., Stewart D., Spradling A.C. The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development. Genes Dev. 2002, 16:2108-2119.
    • (2002) Genes Dev. , vol.16 , pp. 2108-2119
    • Tulin, A.1    Stewart, D.2    Spradling, A.C.3
  • 61
    • 0347990464 scopus 로고    scopus 로고
    • The C. elegans gene pme-5: molecular cloning and role in the DNA-damage response of a tankyrase orthologue
    • Gravel C., Stergiou L., Gagnon S.N., Desnoyers S. The C. elegans gene pme-5: molecular cloning and role in the DNA-damage response of a tankyrase orthologue. DNA Repair (Amst.) 2004, 3:171-182.
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 171-182
    • Gravel, C.1    Stergiou, L.2    Gagnon, S.N.3    Desnoyers, S.4
  • 62
    • 2942539327 scopus 로고    scopus 로고
    • Vault poly(ADP-ribose) polymerase is associated with mammalian telomerase and is dispensable for telomerase function and vault structure in vivo
    • Liu Y., Snow B.E., Kickhoefer V.A., Erdmann N., Zhou W., Wakeham A., Gomez M., Rome L.H., Harrington L. Vault poly(ADP-ribose) polymerase is associated with mammalian telomerase and is dispensable for telomerase function and vault structure in vivo. Mol. Cell Biol. 2004, 24:5314-5323.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 5314-5323
    • Liu, Y.1    Snow, B.E.2    Kickhoefer, V.A.3    Erdmann, N.4    Zhou, W.5    Wakeham, A.6    Gomez, M.7    Rome, L.H.8    Harrington, L.9
  • 64
    • 34848847210 scopus 로고    scopus 로고
    • PARP-1-induced cell death through inhibition of the MEK/ERK pathway in MNNG-treated HeLa cells
    • Ethier C., Labelle Y., Poirier G.G. PARP-1-induced cell death through inhibition of the MEK/ERK pathway in MNNG-treated HeLa cells. Apoptosis 2007, 12:2037-2049.
    • (2007) Apoptosis , vol.12 , pp. 2037-2049
    • Ethier, C.1    Labelle, Y.2    Poirier, G.G.3
  • 65
    • 0037155285 scopus 로고    scopus 로고
    • Overexpression of poly(ADP-ribose) polymerase disrupts organization of cytoskeletal F-actin and tissue polarity in Drosophila
    • Uchida M., Hanai S., Uematsu N., Sawamoto K., Okano H., Miwa M., Uchida K. Overexpression of poly(ADP-ribose) polymerase disrupts organization of cytoskeletal F-actin and tissue polarity in Drosophila. J. Biol. Chem. 2002, 277:6696-6702.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6696-6702
    • Uchida, M.1    Hanai, S.2    Uematsu, N.3    Sawamoto, K.4    Okano, H.5    Miwa, M.6    Uchida, K.7
  • 67
    • 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.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 789
    • Hassa, P.O.1    Haenni, S.S.2    Elser, M.3    Hottiger, M.O.4
  • 68
  • 69
    • 85047669941 scopus 로고    scopus 로고
    • The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway
    • Hofmann K., Bucher P. The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Trends Biochem. Sci. 1996, 21:172-173.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 172-173
    • Hofmann, K.1    Bucher, P.2
  • 71
    • 84869094697 scopus 로고    scopus 로고
    • PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1alpha-mediated unfolded protein response
    • Jwa M., Chang P. PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1alpha-mediated unfolded protein response. Nat. Cell Biol. 2012, 14:1223-1230.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 1223-1230
    • Jwa, M.1    Chang, P.2
  • 72
    • 84882437564 scopus 로고    scopus 로고
    • A systematic analysis of the PARP protein family identifies new functions critical for cell physiology
    • Vyas S., Chesarone-Cataldo M., Todorova T., Huang Y.H., Chang P. A systematic analysis of the PARP protein family identifies new functions critical for cell physiology. Nat. Commun. 2013, 4:2240.
    • (2013) Nat. Commun. , vol.4 , pp. 2240
    • Vyas, S.1    Chesarone-Cataldo, M.2    Todorova, T.3    Huang, Y.H.4    Chang, P.5
  • 73
    • 38949096858 scopus 로고    scopus 로고
    • Positive selection and increased antiviral activity associated with the PARP-containing isoform of human zinc-finger antiviral protein
    • Kerns J.A., Emerman M., Malik H.S. Positive selection and increased antiviral activity associated with the PARP-containing isoform of human zinc-finger antiviral protein. PLoS Genet. 2008, 4:e21.
    • (2008) PLoS Genet. , vol.4 , pp. e21
    • Kerns, J.A.1    Emerman, M.2    Malik, H.S.3
  • 74
    • 80053144075 scopus 로고    scopus 로고
    • Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation
    • Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T., Gao G. Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:15834-15839.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 15834-15839
    • Zhu, Y.1    Chen, G.2    Lv, F.3    Wang, X.4    Ji, X.5    Xu, Y.6    Sun, J.7    Wu, L.8    Zheng, Y.T.9    Gao, G.10
  • 75
    • 84862196500 scopus 로고    scopus 로고
    • Poly(ADP-ribose) regulates post-transcriptional gene regulation in the cytoplasm
    • Leung A., Todorova T., Ando Y., Chang P. Poly(ADP-ribose) regulates post-transcriptional gene regulation in the cytoplasm. RNA Biol. 2012, 9:542-548.
    • (2012) RNA Biol. , vol.9 , pp. 542-548
    • Leung, A.1    Todorova, T.2    Ando, Y.3    Chang, P.4
  • 77
    • 84916930091 scopus 로고    scopus 로고
    • Interferon-stimulated PARPs are potent inhibitors of cellular translation and virus replication
    • Atasheva S., Frolova E.I., Frolov I. Interferon-stimulated PARPs are potent inhibitors of cellular translation and virus replication. J. Virol. 2013.
    • (2013) J. Virol.
    • Atasheva, S.1    Frolova, E.I.2    Frolov, I.3
  • 80
    • 0034708216 scopus 로고    scopus 로고
    • The U box is a modified RING finger - a common domain in ubiquitination
    • Aravind L., Koonin E.V. The U box is a modified RING finger - a common domain in ubiquitination. Curr. Biol. 2000, 10:R132-R134.
    • (2000) Curr. Biol. , vol.10 , pp. R132-R134
    • Aravind, L.1    Koonin, E.V.2
  • 81
    • 26644446700 scopus 로고    scopus 로고
    • B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity
    • Aguiar R.C., Takeyama K., He C., Kreinbrink K., Shipp M.A. B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity. J. Biol. Chem. 2005, 280:33756-33765.
    • (2005) J. Biol. Chem. , vol.280 , pp. 33756-33765
    • Aguiar, R.C.1    Takeyama, K.2    He, C.3    Kreinbrink, K.4    Shipp, M.A.5
  • 82
    • 84856232767 scopus 로고    scopus 로고
    • Functions of the poly(ADP-ribose) polymerase superfamily in plants
    • Lamb R.S., Citarelli M., Teotia S. Functions of the poly(ADP-ribose) polymerase superfamily in plants. Cell. Mol. Life Sci. 2012, 69:175-189.
    • (2012) Cell. Mol. Life Sci. , vol.69 , pp. 175-189
    • Lamb, R.S.1    Citarelli, M.2    Teotia, S.3
  • 83
    • 73249148114 scopus 로고    scopus 로고
    • Disruption of poly(ADP-ribosyl)ation mechanisms alters responses of Arabidopsis to biotic stress
    • Adams-Phillips L., Briggs A.G., Bent A.F. Disruption of poly(ADP-ribosyl)ation mechanisms alters responses of Arabidopsis to biotic stress. Plant Physiol. 2010, 152:267-280.
    • (2010) Plant Physiol. , vol.152 , pp. 267-280
    • Adams-Phillips, L.1    Briggs, A.G.2    Bent, A.F.3
  • 84
    • 33847313804 scopus 로고    scopus 로고
    • Altered DNA damage response in Caenorhabditis elegans with impaired poly(ADP-ribose) glycohydrolases genes expression
    • St-Laurent J.F., Gagnon S.N., Dequen F., Hardy I., Desnoyers S. Altered DNA damage response in Caenorhabditis elegans with impaired poly(ADP-ribose) glycohydrolases genes expression. DNA Repair (Amst.) 2007, 6:329-343.
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 329-343
    • St-Laurent, J.F.1    Gagnon, S.N.2    Dequen, F.3    Hardy, I.4    Desnoyers, S.5
  • 85
    • 84891796785 scopus 로고    scopus 로고
    • Structural basis for the molecular recognition of polyadenosine RNA by Nab2 Zn fingers
    • Kuhlmann S.I., Valkov E., Stewart M. Structural basis for the molecular recognition of polyadenosine RNA by Nab2 Zn fingers. Nucleic Acids Res. 2014, 42:672-680.
    • (2014) Nucleic Acids Res. , vol.42 , pp. 672-680
    • Kuhlmann, S.I.1    Valkov, E.2    Stewart, M.3
  • 89
    • 63149143191 scopus 로고    scopus 로고
    • The ADP-ribosylation of Sulfolobus solfataricus Sso7 modulates protein/DNA interactions in vitro
    • Castellano S., Farina B., Faraone-Mennella M.R. The ADP-ribosylation of Sulfolobus solfataricus Sso7 modulates protein/DNA interactions in vitro. FEBS Lett. 2009, 583:1154-1158.
    • (2009) FEBS Lett. , vol.583 , pp. 1154-1158
    • Castellano, S.1    Farina, B.2    Faraone-Mennella, M.R.3
  • 90
    • 0038047136 scopus 로고    scopus 로고
    • The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A
    • Allen M.D., Buckle A.M., Cordell S.C., Lowe J., Bycroft M. The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A. J. Mol. Biol. 2003, 330:503-511.
    • (2003) J. Mol. Biol. , vol.330 , pp. 503-511
    • Allen, M.D.1    Buckle, A.M.2    Cordell, S.C.3    Lowe, J.4    Bycroft, M.5
  • 91
    • 84862910351 scopus 로고    scopus 로고
    • Herpes simplex virus requires poly(ADP-ribose) polymerase activity for efficient replication and induces extracellular signal-related kinase-dependent phosphorylation and ICP0-dependent nuclear localization of tankyrase 1
    • Li Z., Yamauchi Y., Kamakura M., Murayama T., Goshima F., Kimura H., Nishiyama Y. Herpes simplex virus requires poly(ADP-ribose) polymerase activity for efficient replication and induces extracellular signal-related kinase-dependent phosphorylation and ICP0-dependent nuclear localization of tankyrase 1. J. Virol. 2012, 86:492-503.
    • (2012) J. Virol. , vol.86 , pp. 492-503
    • Li, Z.1    Yamauchi, Y.2    Kamakura, M.3    Murayama, T.4    Goshima, F.5    Kimura, H.6    Nishiyama, Y.7
  • 95
    • 67349175974 scopus 로고    scopus 로고
    • The nsP3 macro domain is important for Sindbis virus replication in neurons and neurovirulence in mice
    • Park E., Griffin D.E. The nsP3 macro domain is important for Sindbis virus replication in neurons and neurovirulence in mice. Virology 2009, 388:305-314.
    • (2009) Virology , vol.388 , pp. 305-314
    • Park, E.1    Griffin, D.E.2
  • 96
    • 70349319686 scopus 로고    scopus 로고
    • Interaction of Sindbis virus non-structural protein 3 with poly(ADP-ribose) polymerase 1 in neuronal cells
    • Park E., Griffin D.E. Interaction of Sindbis virus non-structural protein 3 with poly(ADP-ribose) polymerase 1 in neuronal cells. J. Gen. Virol. 2009, 90:2073-2080.
    • (2009) J. Gen. Virol. , vol.90 , pp. 2073-2080
    • Park, E.1    Griffin, D.E.2
  • 97
    • 84864381495 scopus 로고    scopus 로고
    • Herpes simplex virus 1 infection activates poly(ADP-ribose) polymerase and triggers the degradation of poly(ADP-ribose) glycohydrolase
    • Grady S.L., Hwang J., Vastag L., Rabinowitz J.D., Shenk T. Herpes simplex virus 1 infection activates poly(ADP-ribose) polymerase and triggers the degradation of poly(ADP-ribose) glycohydrolase. J. Virol. 2012, 86:8259-8268.
    • (2012) J. Virol. , vol.86 , pp. 8259-8268
    • Grady, S.L.1    Hwang, J.2    Vastag, L.3    Rabinowitz, J.D.4    Shenk, T.5


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