메뉴 건너뛰기




Volumn 19, Issue 7, 2014, Pages 1041-1056

Identification of ADP-ribosylated peptides and ADP-ribose acceptor sites

Author keywords

Acceptor Side; Activity; ADP ribosylation; ARTD; Mass Spectrometry; PARP; Post Translational Modification; Review

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; ADP-RIBOSYLARGININE HYDROLASE; AMINO ACID; GLYCOSIDASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PEPTIDE; PROTEIN;

EID: 84904660397     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/4266     Document Type: Article
Times cited : (24)

References (143)
  • 1
    • 33745800293 scopus 로고    scopus 로고
    • Interpreting the protein language using proteomics
    • DOI 10.1038/nrm1939, PII NRM1939
    • O. N. Jensen: Interpreting the protein language using proteomics. Nat Rev Mol Cell Biol, 7(6), 391-403 (2006). (Pubitemid 44050093)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.6 , pp. 391-403
    • Jensen, O.N.1
  • 2
    • 84910679144 scopus 로고    scopus 로고
    • Proteome-wide post-translational modification statistics: Frequency analysis and curation of the swiss-prot database
    • G. A. Khoury, R. C. Baliban and C. A. Floudas: Proteome-wide post-translational modification statistics: frequency analysis and curation of the swiss-prot database. Sci Rep, 1 (2011).
    • (2011) Sci Rep , vol.1
    • Khoury, G.A.1    Baliban, R.C.2    Floudas, C.A.3
  • 3
    • 35848970747 scopus 로고    scopus 로고
    • Mapping protein post-translational modifications with mass spectrometry
    • DOI 10.1038/nmeth1100, PII NMETH1100
    • E. S. Witze, W. M. Old, K. A. Resing and N. G. Ahn: Mapping protein post-translational modifications with mass spectrometry. Nat Methods, 4(10), 798-806 (2007). (Pubitemid 350055576)
    • (2007) Nature Methods , vol.4 , Issue.10 , pp. 798-806
    • Witze, E.S.1    Old, W.M.2    Resing, K.A.3    Ahn, N.G.4
  • 4
    • 84886719040 scopus 로고    scopus 로고
    • PARP-1 and gene regulation: Progress and puzzles
    • W. L. Kraus and M. O. Hottiger: PARP-1 and gene regulation: Progress and puzzles. Mol Aspects Med (2013).
    • (2013) Mol Aspects Med
    • Kraus, W.L.1    Hottiger, M.O.2
  • 5
    • 0002160618 scopus 로고
    • Nicotinamide mononucleotide activation of new DNA-dependent polyadenylic acid synthesizing nuclear enzyme
    • P. Chambon, J. D. Weill and P. Mandel: Nicotinamide mononucleotide activation of new DNA-dependent polyadenylic acid synthesizing nuclear enzyme. Biochem Biophys Res Commun, 11, 39-43 (1963).
    • (1963) Biochem Biophys Res Commun , vol.11 , pp. 39-43
    • Chambon, P.1    Weill, J.D.2    Mandel, P.3
  • 7
    • 0018107954 scopus 로고
    • Two different types of bonds linking single ADP-ribose residues covalently to proteins. Quantification in eukaryotic cells
    • R. Bredehorst, K. Wielckens, A. Gartemann, H. Lengyel, K. Klapproth and H. Hilz: Two different types of bonds linking single ADP-ribose residues covalently to proteins. Quantification in eukaryotic cells. Eur J Biochem, 92(1), 129-35 (1978).
    • (1978) Eur J Biochem , vol.92 , Issue.1 , pp. 129-135
    • Bredehorst, R.1    Wielckens, K.2    Gartemann, A.3    Lengyel, H.4    Klapproth, K.5    Hilz, H.6
  • 8
    • 55549139051 scopus 로고    scopus 로고
    • The expanding field of poly(adp-ribosyl)ation reactions. 'Protein modifications: Beyond the usual suspects' Review series
    • A. Hakme, H. K. Wong, F. Dantzer and V. Schreiber: The expanding field of poly(ADP-ribosyl)ation reactions. 'Protein Modifications: Beyond the Usual Suspects' Review Series. EMBO Rep, 9(11), 1094-100 (2008).
    • (2008) EMBO Rep , vol.9 , Issue.11 , pp. 1094-1100
    • Hakme, A.1    Wong, H.K.2    Dantzer, F.3    Schreiber, V.4
  • 9
    • 0029162298 scopus 로고
    • Dissection of ADP-ribose polymer synthesis into individual steps of initiation, elongation, and branching
    • R. Alvarez-Gonzalez and H. Mendoza-Alvarez: Dissection of ADP-ribose polymer synthesis into individual steps of initiation, elongation, and branching. Biochimie, 77(6), 403-7 (1995).
    • (1995) Biochimie , vol.77 , Issue.6 , pp. 403-407
    • Alvarez-Gonzalez, R.1    Mendoza-Alvarez, H.2
  • 10
    • 0020479802 scopus 로고
    • DNA fragmentation and NAD depletion. Their relation to the turnover of endogenous mono(ADP-ribosyl) and poly(ADP-ribosyl) proteins
    • K. Wielckens, A. Schmidt, E. George, R. Bredehorst and H. Hilz: DNA fragmentation and NAD depletion. Their relation to the turnover of endogenous mono(ADP-ribosyl) and poly(ADP-ribosyl) proteins. J Biol Chem, 257(21), 12872-12877 (1982).
    • (1982) J Biol Chem , vol.257 , Issue.21 , pp. 12872-12877
    • Wielckens, K.1    Schmidt, A.2    George, E.3    Bredehorst, R.4    Hilz, H.5
  • 11
    • 84880324619 scopus 로고    scopus 로고
    • Expanding functions of intracellular resident mono-ADP-ribosylation in cell physiology
    • K. L. Feijs, P. Verheugd and B. Luscher: Expanding functions of intracellular resident mono-ADP-ribosylation in cell physiology. FEBS J, 280(15), 3519-3529 (2013).
    • (2013) FEBS J , vol.280 , Issue.15 , pp. 3519-3529
    • Feijs, K.L.1    Verheugd, P.2    Luscher, B.3
  • 12
    • 79955957616 scopus 로고    scopus 로고
    • Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm
    • A. K. Leung, S. Vyas, J. E. Rood, A. Bhutkar, P. A. Sharp and P. Chang: Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm. Mol Cell, 42(4), 489-499 (2011).
    • (2011) Mol Cell , vol.42 , Issue.4 , pp. 489-499
    • Leung, A.K.1    Vyas, S.2    Rood, J.E.3    Bhutkar, A.4    Sharp, P.A.5    Chang, P.6
  • 13
    • 84857891632 scopus 로고    scopus 로고
    • On PAR with PARP: Cellular stress signaling through poly(ADP-ribose) and PARP-1
    • X. Luo and W. L. Kraus: On PAR with PARP: cellular stress signaling through poly(ADP-ribose) and PARP-1. Genes Dev, 26(5), 417-432 (2012).
    • (2012) Genes Dev , vol.26 , Issue.5 , pp. 417-432
    • Luo, X.1    Kraus, W.L.2
  • 14
    • 33749260519 scopus 로고    scopus 로고
    • Nuclear ADP-ribosylation reactions in mammalian cells: Where are we today and where are we going?
    • DOI 10.1128/MMBR.00040-05
    • P. O. Hassa, S. Haenni, M. Elser and M. O. Hottiger: Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going? Microbiol Mol Biol Rev, 70(3), 789-829 (2006). (Pubitemid 44484693)
    • (2006) Microbiology and Molecular Biology Reviews , vol.70 , Issue.3 , pp. 789-829
    • Hassa, P.O.1    Haenni, S.S.2    Elser, M.3    Hottiger, M.O.4
  • 16
    • 79957572693 scopus 로고    scopus 로고
    • ADP-ribosylation of histones by ARTD1: An additional module of the histone code?
    • M. O. Hottiger: ADP-ribosylation of histones by ARTD1: An additional module of the histone code? FEBS Lett, 585, 1595-1599 (2011).
    • (2011) FEBS Lett , vol.585 , pp. 1595-1599
    • Hottiger, M.O.1
  • 17
    • 84870855799 scopus 로고    scopus 로고
    • Tankyrase-targeted therapeutics: Expanding opportunities in the PARP family
    • J. L. Riffell, C. J. Lord and A. Ashworth: Tankyrase-targeted therapeutics: expanding opportunities in the PARP family. Nat Rev Drug Discovery, 11(12), 923-36 (2012).
    • (2012) Nat Rev Drug Discovery , vol.11 , Issue.12 , pp. 923-936
    • Riffell, J.L.1    Lord, C.J.2    Ashworth, A.3
  • 18
    • 84880330797 scopus 로고    scopus 로고
    • The expanding role of PARPs in the establishment and maintenance of heterochromatin
    • F. Dantzer and R. Santoro: The expanding role of PARPs in the establishment and maintenance of heterochromatin. FEBS J (2013).
    • (2013) FEBS J
    • Dantzer, F.1    Santoro, R.2
  • 20
    • 84884840336 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation regulates insulator function and intrachromosomal interactions in Drosophila
    • C. T. Ong, K. Van Bortle, E. Ramos and V. G. Corces: Poly(ADP-ribosyl) ation regulates insulator function and intrachromosomal interactions in Drosophila. Cell, 155(1), 148-159 (2013).
    • (2013) Cell , vol.155 , Issue.1 , pp. 148-159
    • Ong, C.T.1    Van Bortle, K.2    Ramos, E.3    Corces, V.G.4
  • 21
    • 84876935501 scopus 로고    scopus 로고
    • Proteasome regulation by ADP-ribosylation
    • P. F. Cho-Park and H. Steller: Proteasome regulation by ADP-ribosylation. Cell, 153(3), 614-627 (2013).
    • (2013) Cell , vol.153 , Issue.3 , pp. 614-627
    • Cho-Park, P.F.1    Steller, H.2
  • 22
    • 84860662327 scopus 로고    scopus 로고
    • Complex roles of members of the ADP-ribosyl transferase super family in immune defences: Looking beyond PARP1
    • I. Welsby, D. Hutin and O. Leo: Complex roles of members of the ADP-ribosyl transferase super family in immune defences: looking beyond PARP1. Biochem Pharmacol, 84(1), 11-20 (2012).
    • (2012) Biochem Pharmacol , vol.84 , Issue.1 , pp. 11-20
    • Welsby, I.1    Hutin, D.2    Leo, O.3
  • 23
    • 84862758175 scopus 로고    scopus 로고
    • New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
    • B. A. Gibson and W. L. Kraus: New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs. Nat Rev Mol Cell Biol, 13(7), 411-424 (2012).
    • (2012) Nat Rev Mol Cell Biol , vol.13 , Issue.7 , pp. 411-424
    • Gibson, B.A.1    Kraus, W.L.2
  • 24
    • 77956526559 scopus 로고    scopus 로고
    • PARP-1 regulates chromatin structure and transcription through a KDM5B-dependent pathway
    • R. Krishnakumar and W. L. Kraus: PARP-1 regulates chromatin structure and transcription through a KDM5B-dependent pathway. Mol Cell, 39(5), 736-49 (2010).
    • (2010) Mol Cell , vol.39 , Issue.5 , pp. 736-749
    • Krishnakumar, R.1    Kraus, W.L.2
  • 25
    • 77956627087 scopus 로고    scopus 로고
    • Poly(ADPribose) polymerase 1 participates in the phase entrainment of circadian clocks to feeding
    • G. Asher, H. Reinke, M. Altmeyer, M. Gutierrez- Arcelus, M. O. Hottiger and U. Schibler: Poly(ADPribose) polymerase 1 participates in the phase entrainment of circadian clocks to feeding. Cell, 142(6), 943-953 (2010).
    • (2010) Cell , vol.142 , Issue.6 , pp. 943-953
    • Asher, G.1    Reinke, H.2    Altmeyer, M.3    Gutierrez-Arcelus, M.4    Hottiger, M.O.5    Schibler, U.6
  • 26
    • 54249118102 scopus 로고    scopus 로고
    • Needle in the haystack: Structure-based toxin discovery
    • R. J. Fieldhouse and A. R. Merrill: Needle in the haystack: structure-based toxin discovery. Trends Biochem Sci, 33(11), 546-56 (2008).
    • (2008) Trends Biochem Sci , vol.33 , Issue.11 , pp. 546-556
    • Fieldhouse, R.J.1    Merrill, A.R.2
  • 27
    • 53849133471 scopus 로고    scopus 로고
    • Molecular mechanisms of the cytotoxicity of ADP-ribosylating toxins
    • Q. Deng and J. T. Barbieri: Molecular mechanisms of the cytotoxicity of ADP-ribosylating toxins. Annu Rev Microbiol, 62, 271-288 (2008).
    • (2008) Annu Rev Microbiol , vol.62 , pp. 271-288
    • Deng, Q.1    Barbieri, J.T.2
  • 29
    • 38449088040 scopus 로고    scopus 로고
    • The diverse biological roles of mammalian PARPs, a small but powerful family of poly-ADP-ribose polymerases
    • DOI 10.2741/2909
    • P. O. Hassa and M. O. Hottiger: The diverse biological roles of mammalian PARPs, a small but powerful family of poly-ADP-ribose polymerases. Front Biosci, 13, 3046-3082 (2008). (Pubitemid 351589219)
    • (2008) Frontiers in Bioscience , vol.13 , Issue.8 , pp. 3046-3082
    • Hassa, P.O.1    Hottiger, M.O.2
  • 34
    • 0036407637 scopus 로고    scopus 로고
    • Functional characterization of the poly(ADP-ribose) polymerase activity of tankyrase 1, a potential regulator of telomere length
    • DOI 10.1016/S0022-2836(02)00946-4
    • J. F. Rippmann, K. Damm and A. Schnapp: Functional characterization of the poly(ADP-ribose) polymerase activity of tankyrase 1, a potential regulator of telomere length. J Mol Biol, 323(2), 217-24 (2002). (Pubitemid 35283687)
    • (2002) Journal of Molecular Biology , vol.323 , Issue.2 , pp. 217-224
    • Rippmann, J.F.1    Damm, K.2    Schnapp, A.3
  • 35
    • 0036132673 scopus 로고    scopus 로고
    • Role for the related poly(ADP-ribose) polymerases tankyrase 1 and 2 at human telomeres
    • DOI 10.1128/MCB.22.1.332-342.2002
    • B. D. Cook, J. N. Dynek, W. Chang, G. Shostak and S. Smith: Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres. Mol Cell Biol, 22(1), 332-42 (2002). (Pubitemid 33144279)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.1 , pp. 332-342
    • Cook, B.D.1    Dynek, J.N.2    Chang, W.3    Shostak, G.4    Smith, S.5
  • 37
    • 26644446700 scopus 로고    scopus 로고
    • B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity
    • DOI 10.1074/jbc.M505408200
    • R. C. Aguiar, K. Takeyama, C. He, K. Kreinbrink and M. A. Shipp: B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity. J Biol Chem, 280(40), 33756-33765 (2005). (Pubitemid 41443094)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.40 , pp. 33756-33765
    • Aguiar, R.C.T.1    Takeyama, K.2    He, C.3    Kreinbrink, K.4    Shipp, M.A.5
  • 38
    • 84882437564 scopus 로고    scopus 로고
    • A systematic analysis of the PARP protein family identifies new functions critical for cell physiology
    • S. Vyas, M. Chesarone-Cataldo, T. Todorova, Y. H. Huang and P. Chang: A systematic analysis of the PARP protein family identifies new functions critical for cell physiology. Nat Commun, 4, 2240 (2013).
    • Nat Commun , vol.4 , Issue.2240 , pp. 2013
    • Vyas, S.1    Chesarone-Cataldo, M.2    Todorova, T.3    Huang, Y.H.4    Chang, P.5
  • 39
    • 84861231399 scopus 로고    scopus 로고
    • The diverse roles and clinical relevance of PARPs in DNA damage repair: Current state of the art
    • M. De Vos, V. Schreiber and F. Dantzer: The diverse roles and clinical relevance of PARPs in DNA damage repair: Current state of the art. Biochem Pharmacol, 84(2), 137-46 (2012).
    • (2012) Biochem Pharmacol , vol.84 , Issue.2 , pp. 137-146
    • De Vos, M.1    Schreiber, V.2    Dantzer, F.3
  • 41
    • 84880333185 scopus 로고    scopus 로고
    • The recognition and removal of cellular poly(ADP-ribose) signals
    • E. Barkauskaite, G. Jankevicius, A. G. Ladurner, I. Ahel and G. Timinszky: The recognition and removal of cellular poly(ADP-ribose) signals. FEBS J, 280(15), 3491- 3507 (2013).
    • (2013) FEBS J , vol.280 , Issue.15 , pp. 3491-3507
    • Barkauskaite, E.1    Jankevicius, G.2    Ladurner, A.G.3    Ahel, I.4    Timinszky, G.5
  • 42
    • 0034731455 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins
    • DOI 10.1074/jbc.M006520200
    • J. M. Pleschke, H. E. Kleczkowska, M. Strohm and F. R. Althaus: Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins. J Biol Chem, 275(52), 40974-80 (2000). (Pubitemid 32054922)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.52 , pp. 40974-40980
    • Pleschke, J.M.1    Kleczkowska, H.E.2    Strohm, M.3    Althaus, F.R.4
  • 43
    • 58749112769 scopus 로고    scopus 로고
    • Proteome-wide identification of poly(ADP-ribose) binding proteins and poly(ADP-ribose)-associated protein complexes
    • J. P. Gagne, M. Isabelle, K. S. Lo, S. Bourassa, M. J. Hendzel, V. L. Dawson, T. M. Dawson and G. G. Poirier: Proteome-wide identification of poly(ADP-ribose) binding proteins and poly(ADP-ribose)-associated protein complexes. Nucleic Acids Res, 36(22), 6959-76 (2008).
    • (2008) Nucleic Acids Res , vol.36 , Issue.22 , pp. 6959-6976
    • Gagne, J.P.1    Isabelle, M.2    Lo, K.S.3    Bourassa, S.4    Hendzel, M.J.5    Dawson, V.L.6    Dawson, T.M.7    Poirier, G.G.8
  • 44
    • 0038047136 scopus 로고    scopus 로고
    • The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A
    • DOI 10.1016/S0022-2836(03)00473-X
    • M. D. Allen, A. M. Buckle, S. C. Cordell, J. Lowe and M. Bycroft: The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A. J Mol Biol, 330(3), 503-11 (2003). (Pubitemid 36808684)
    • (2003) Journal of Molecular Biology , vol.330 , Issue.3 , pp. 503-511
    • Allen, M.D.1    Buckle, A.M.2    Cordell, S.C.3    Lowe, J.4    Bycroft, M.5
  • 45
    • 0026737922 scopus 로고
    • MacroH2A, a core histone containing a large nonhistone region
    • J. R. Pehrson and V. A. Fried: MacroH2A, a core histone containing a large nonhistone region. Science, 257(5075), 1398-400 (1992).
    • (1992) Science , vol.257 , Issue.5075 , pp. 1398-1400
    • Pehrson, J.R.1    Fried, V.A.2
  • 46
    • 84865426155 scopus 로고    scopus 로고
    • New readers and interpretations of poly(ADP-ribosyl)ation
    • T. Kalisch, J. C. Ame, F. Dantzer and V. Schreiber: New readers and interpretations of poly(ADP-ribosyl)ation. Trends Biochem Sci, 37(9), 381-90 (2012).
    • (2012) Trends Biochem Sci , vol.37 , Issue.9 , pp. 381-390
    • Kalisch, T.1    Ame, J.C.2    Dantzer, F.3    Schreiber, V.4
  • 47
    • 84876195523 scopus 로고    scopus 로고
    • Expanding the functional repertoire of macrodomains
    • M. J. Gamble: Expanding the functional repertoire of macrodomains. Nat Struct Mol Biol, 20(4), 407-8 (2013).
    • (2013) Nat Struct Mol Biol , vol.20 , Issue.4 , pp. 407-408
    • Gamble, M.J.1
  • 50
    • 57749190795 scopus 로고    scopus 로고
    • Differential activities of cellular and viral macro domain proteins in binding of ADP-ribose metabolites
    • M. Neuvonen and T. Ahola: Differential activities of cellular and viral macro domain proteins in binding of ADP-ribose metabolites. J Mol Biol, 385(1), 212-225 (2009).
    • (2009) J Mol Biol , vol.385 , Issue.1 , pp. 212-225
    • Neuvonen, M.1    Ahola, T.2
  • 52
    • 63849128257 scopus 로고    scopus 로고
    • Sensing NAD metabolites through macro domains
    • S. Till and A. G. Ladurner: Sensing NAD metabolites through macro domains. Front Biosci, 14, 3246-58 (2009).
    • (2009) Front Biosci , vol.14 , pp. 3246-3258
    • Till, S.1    Ladurner, A.G.2
  • 53
    • 0035338814 scopus 로고    scopus 로고
    • The WWE domain: A common interaction module in protein ubiquitination and ADP ribosylation
    • DOI 10.1016/S0968-0004(01)01787-X, PII S096800040101787X
    • L. Aravind: The WWE domain: a common interaction module in protein ubiquitination and ADP ribosylation. Trends Biochem Sci, 26(5), 273-5 (2001). (Pubitemid 32436369)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.5 , pp. 273-275
    • Aravind, L.1
  • 54
    • 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)ationdependent ubiquitination
    • Z. Wang, G. A. Michaud, Z. Cheng, Y. Zhang, T. R. Hinds, E. Fan, F. Cong and W. Xu: Recognition of the iso- ADP-ribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl)ationdependent ubiquitination. Genes Dev, 26(3), 235-240 (2012).
    • (2012) Genes Dev , vol.26 , Issue.3 , 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
  • 56
    • 78649874455 scopus 로고    scopus 로고
    • Structural basis of poly(ADP-ribose) recognition by the multizinc binding domain of checkpoint with forkhead-associated and RING Domains (CHFR)
    • J. Oberoi, M. W. Richards, S. Crumpler, N. Brown, J. Blagg and R. Bayliss: Structural basis of poly(ADP-ribose) recognition by the multizinc binding domain of checkpoint with forkhead-associated and RING Domains (CHFR). J Biol Chem, 285(50), 39348-58 (2010).
    • (2010) J Biol Chem , vol.285 , Issue.50 , pp. 39348-39358
    • Oberoi, J.1    Richards, M.W.2    Crumpler, S.3    Brown, N.4    Blagg, J.5    Bayliss, R.6
  • 58
    • 38049064044 scopus 로고    scopus 로고
    • Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins
    • I. Ahel, D. Ahel, T. Matsusaka, A. J. Clark, J. Pines, S. J. Boulton and S. C. West: Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins. Nature, 451(7174), 81-5 (2008).
    • (2008) Nature , vol.451 , Issue.7174 , pp. 81-85
    • Ahel, I.1    Ahel, D.2    Matsusaka, T.3    Clark, A.J.4    Pines, J.5    Boulton, S.J.6    West, S.C.7
  • 60
    • 0022347238 scopus 로고
    • Pertussis toxin-catalyzed ADP-ribosylation of transducin
    • R. E. West, Jr., J. Moss, M. Vaughan, T. Liu and T. Y. Liu: Pertussis toxin-catalyzed ADP-ribosylation of transducin. Cysteine 347 is the ADP-ribose acceptor site. J Biol Chem, 260(27), 14428-30 (1985). (Pubitemid 16210959)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.27 , pp. 14428-14430
    • West Jr., R.E.1    Moss, J.2    Vaughan, M.3
  • 63
    • 0019332813 scopus 로고
    • ADP-ribosylation of histone H1. Identification of glutamic acid residues 2, 14, and the COOH-terminal lysine residue as modification sites
    • N. Ogata, K. Ueda, H. Kagamiyama and O. Hayaishi: ADP-ribosylation of histone H1. Identification of glutamic acid residues 2, 14, and the COOH-terminal lysine residue as modification sites. J Biol Chem, 255(16), 7616-20 (1980).
    • (1980) J Biol Chem , vol.255 , Issue.16 , pp. 7616-7620
    • Ogata, N.1    Ueda, K.2    Kagamiyama, H.3    Hayaishi, O.4
  • 64
    • 0019888393 scopus 로고
    • Multiple autopoly(ADP-ribosyl)ation of rat liver poly(ADP-ribose) synthetase. Mode of modification and properties of automodified synthetase
    • M. Kawaichi, K. Ueda and O. Hayaishi: Multiple autopoly(ADP-ribosyl)ation of rat liver poly(ADP-ribose) synthetase. Mode of modification and properties of automodified synthetase. J Biol Chem, 256(18), 9483-9 (1981).
    • (1981) J Biol Chem , vol.256 , Issue.18 , pp. 9483-9489
    • Kawaichi, M.1    Ueda, K.2    Hayaishi, O.3
  • 66
    • 1842417452 scopus 로고
    • Isolation of an avian erythrocyte protein possessing ADP ribosyltransferase activity and capable of activating adenylate cyclase
    • J. Moss and M. Vaughan: Isolation of an avian erythrocyte protein possessing ADP-ribosyltransferase activity and capable of activating adenylate cyclase. Proc Natl Acad Sci USA, 75(8), 3621-4 (1978). (Pubitemid 8399898)
    • (1978) Proceedings of the National Academy of Sciences of the United States of America , vol.75 , Issue.8 , pp. 3621-3624
    • Moss, J.1    Vaughan, M.2
  • 67
    • 0021111894 scopus 로고
    • Amino acid-specific ADPribosylation. Evidence for two distinct NAD: Arginine ADPribosyltransferases in turkey erythrocytes
    • D. A. Yost and J. Moss: Amino acid-specific ADPribosylation. Evidence for two distinct NAD:arginine ADPribosyltransferases in turkey erythrocytes. J Biol Chem, 258(8), 4926-9 (1983).
    • (1983) J Biol Chem , vol.258 , Issue.8 , pp. 4926-4929
    • Yost, D.A.1    Moss, J.2
  • 69
    • 67649888368 scopus 로고    scopus 로고
    • Molecular mechanism of poly(ADPribosyl) ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites
    • M. Altmeyer, S. Messner, P. O. Hassa, M. Fey and M. O. Hottiger: Molecular mechanism of poly(ADPribosyl) ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites. Nucleic Acids Res, 37(11), 3723-3738 (2009).
    • (2009) Nucleic Acids Res , vol.37 , Issue.11 , pp. 3723-3738
    • Altmeyer, M.1    Messner, S.2    Hassa, P.O.3    Fey, M.4    Hottiger, M.O.5
  • 70
    • 0017858196 scopus 로고
    • + with guanidines
    • N. J. Oppenheimer: Structural determination and stereospecificity of the choleragen-catalyzed reaction of NAD+ with guanidines. J Biol Chem, 253(14), 4907-10 (1978). (Pubitemid 8382156)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.14 , pp. 4907-4910
    • Oppenheimer, N.J.1
  • 74
    • 0027499102 scopus 로고
    • Protein glycation by ADP-ribose: Studies of model conjugates
    • D. Cervantes-Laurean, D. E. Minter, E. L. Jacobson and M. K. Jacobson: Protein glycation by ADP-ribose: studies of model conjugates. Biochemistry, 32(6), 1528-34 (1993). (Pubitemid 23077560)
    • (1993) Biochemistry , vol.32 , Issue.6 , pp. 1528-1534
    • Cervantes-Laurean, D.1    Minter, D.E.2    Jacobson, E.L.3    Jacobson, M.K.4
  • 75
    • 0024428970 scopus 로고
    • Poly(ADP-ribose) catabolism in mammalian cells exposed to DNA-damaging agents
    • R. Alvarez-Gonzalez and F. R. Althaus: Poly(ADP-ribose) catabolism in mammalian cells exposed to DNA-damaging agents. Mutat Res, 218(2), 67-74 (1989). (Pubitemid 19227629)
    • (1989) Mutation Research , vol.218 , Issue.2 , pp. 67-74
    • Alvarez-Gonzalez, R.1    Althaus, F.R.2
  • 76
    • 0028208678 scopus 로고
    • Purification of poly(ADP-ribose) glycohydrolase and detection of its isoforms by a zymogram following one- or two-dimensional electrophoresis
    • DOI 10.1006/abio.1994.1177
    • G. Brochu, G. M. Shah and G. G. Poirier: Purification of poly(ADP-ribose) glycohydrolase and detection of its isoforms by a zymogram following one- or two-dimensional electrophoresis. Anal Biochem, 218(2), 265-72 (1994). (Pubitemid 24141622)
    • (1994) Analytical Biochemistry , vol.218 , Issue.2 , pp. 265-272
    • Brochu, G.1    Shah, G.M.2    Poirier, G.G.3
  • 77
    • 2942707644 scopus 로고    scopus 로고
    • Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments
    • DOI 10.1016/j.yexcr.2004.03.050, PII S0014482704001843
    • M. L. Meyer-Ficca, R. G. Meyer, D. L. Coyle, E. L. Jacobson and M. K. Jacobson: Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments. Exp Cell Res, 297(2), 521-32 (2004). (Pubitemid 38798412)
    • (2004) Experimental Cell Research , vol.297 , Issue.2 , pp. 521-532
    • Meyer-Ficca, M.L.1    Meyer, R.G.2    Coyle, D.L.3    Jacobson, E.L.4    Jacobson, M.K.5
  • 78
    • 63849177643 scopus 로고    scopus 로고
    • Poly (ADP-ribose) glycohydrolase (PARG) and its therapeutic potential
    • W. Min and Z. Q. Wang: Poly (ADP-ribose) glycohydrolase (PARG) and its therapeutic potential. Front Biosci (Landmark Ed), 14, 1619-26 (2009).
    • (2009) Front Biosci (Landmark Ed) , vol.14 , pp. 1619-1626
    • Min, W.1    Wang, Z.Q.2
  • 80
    • 20544475918 scopus 로고    scopus 로고
    • Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: Determining the PARG catalytic domain
    • DOI 10.1042/BJ20040942
    • C. N. Patel, D. W. Koh, M. K. Jacobson and M. A. Oliveira: Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: determining the PARG catalytic domain. Biochem J, 388(Pt 2), 493-500 (2005). (Pubitemid 40839926)
    • (2005) Biochemical Journal , vol.388 , Issue.2 , pp. 493-500
    • Patel, C.N.1    Koh, D.W.2    Jacobson, M.K.3    Oliveira, M.A.4
  • 83
    • 0028280995 scopus 로고
    • Endoglycosidic cleavage of branched polymers by poly(ADP-ribose) glycohydrolase
    • S. A. Braun, P. L. Panzeter, M. A. Collinge and F. R. Althaus: Endoglycosidic cleavage of branched polymers by poly(ADP-ribose) glycohydrolase. Eur J Biochem, 220(2), 369-375 (1994). (Pubitemid 24092801)
    • (1994) European Journal of Biochemistry , vol.220 , Issue.2 , pp. 369-375
    • Braun, S.A.1    Panzeter, P.L.2    Collinge, M.A.3    Althaus, F.R.4
  • 84
    • 33644849513 scopus 로고    scopus 로고
    • Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase
    • S. Oka, J. Kato and J. Moss: Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase. J Biol Chem, 281(2), 705-13 (2006).
    • (2006) J Biol Chem , vol.281 , Issue.2 , pp. 705-713
    • Oka, S.1    Kato, J.2    Moss, J.3
  • 87
    • 30744470374 scopus 로고    scopus 로고
    • The Nudix hydrolase superfamily
    • DOI 10.1007/s00018-005-5386-7
    • A. G. McLennan: The Nudix hydrolase superfamily. Cell Mol Life Sci, 63(2), 123-43 (2006). (Pubitemid 43100287)
    • (2006) Cellular and Molecular Life Sciences , vol.63 , Issue.2 , pp. 123-143
    • McLennan, A.G.1
  • 88
    • 58149526914 scopus 로고    scopus 로고
    • The plant Nudix hydrolase family
    • E. Kraszewska: The plant Nudix hydrolase family. Acta Biochim Pol, 55(4), 663-71 (2008).
    • (2008) Acta Biochim Pol , vol.55 , Issue.4 , pp. 663-671
    • Kraszewska, E.1
  • 89
    • 0033452851 scopus 로고    scopus 로고
    • Cloning, expression and characterization of YSA1H, a human adenosine 5'-diphosphosugar pyrophosphatase possessing a MutT motif
    • DOI 10.1042/0264-6021:3440331
    • L. Gasmi, J. L. Cartwright and A. G. McLennan: Cloning, expression and characterization of YSA1H, a human adenosine 5'-diphosphosugar pyrophosphatase possessing a MutT motif. Biochem J, 344 Pt 2, 331-7 (1999). (Pubitemid 30011587)
    • (1999) Biochemical Journal , vol.344 , Issue.2 , pp. 331-337
    • Gasmi, L.1    Cartwright, J.L.2    McLennan, A.G.3
  • 91
    • 33748904083 scopus 로고    scopus 로고
    • 2
    • DOI 10.1016/j.bbagen.2006.06.003, PII S0304416506001656
    • A. Carloto, M. J. Costas, J. C. Cameselle, A. G. McLennan and J. M. Ribeiro: The specific, submicromolar-Km ADPribose pyrophosphatase purified from human placenta is enzymically indistinguishable from recombinant NUDT9 protein, including a selectivity for Mn2+ as activating cation and increase in Km for ADP-ribose, both elicited by H2O2. Biochim Biophys Acta, 1760(10), 1545-1551 (2006). (Pubitemid 44428027)
    • (2006) Biochimica et Biophysica Acta - General Subjects , vol.1760 , Issue.10 , pp. 1545-1551
    • Carloto, A.1    Costas, M.J.2    Cameselle, J.C.3    McLennan, A.G.4    Ribeiro, J.M.5
  • 93
    • 0027992925 scopus 로고
    • Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositol-linked ADP-ribosyltransferases
    • DOI 10.1021/bi00209a014
    • I. J. Okazaki, A. Zolkiewska, M. S. Nightingale and J. Moss: Immunological and structural conservation of mammalian skeletal muscle glycosylphosphatidylinositollinked ADP-ribosyltransferases. Biochemistry, 33(43), 12828-36 (1994). (Pubitemid 24352873)
    • (1994) Biochemistry , vol.33 , Issue.43 , pp. 12828-12836
    • Okazaki, I.J.1    Zolkiewska, A.2    Nightingale, M.S.3    Moss, J.4
  • 94
    • 0032535340 scopus 로고    scopus 로고
    • +:arginine ecto-mono(ADP-ribosyl)transferase, Art1
    • R. Braren, G. Glowacki, M. Nissen, F. Haag and F. Koch- Nolte: Molecular characterization and expression of the gene for mouse NAD+:arginine ecto-mono(ADPribosyl) transferase, Art1. Biochem J, 336 ( Pt 3), 561-8 (1998). (Pubitemid 29008013)
    • (1998) Biochemical Journal , vol.336 , Issue.3 , pp. 561-568
    • Braren, R.1    Glowacki, G.2    Nissen, M.3    Haag, F.4    Koch-Nolte, F.5
  • 96
    • 80053928939 scopus 로고    scopus 로고
    • Orphan macrodomain protein (human C6orf130) is an O-acyl ADP-ribose deacylase: Solution structure and catalytic properties
    • F. C. Peterson, D. Chen, B. L. Lytle, M. N. Rossi, I. Ahel, J. M. Denu and B. F. Volkman: Orphan macrodomain protein (human C6orf130) is an O-acyl ADP-ribose deacylase: solution structure and catalytic properties. J Biol Chem, 286(41), 35955-35965 (2011).
    • (2011) J Biol Chem , vol.286 , Issue.41 , pp. 35955-35965
    • Peterson, F.C.1    Chen, D.2    Lytle, B.L.3    Rossi, M.N.4    Ahel, I.5    Denu, J.M.6    Volkman, B.F.7
  • 100
    • 84879415959 scopus 로고    scopus 로고
    • Macrodomain-containing proteins: Regulating new intracellular functions of mono(ADP-ribosyl)ation
    • K. L. Feijs, A. H. Forst, P. Verheugd and B. Luscher: Macrodomain-containing proteins: regulating new intracellular functions of mono(ADP-ribosyl)ation. Nat Rev Mol Cell Biol, 14(7), 443-451 (2013).
    • (2013) Nat Rev Mol Cell Biol , vol.14 , Issue.7 , pp. 443-451
    • Feijs, K.L.1    Forst, A.H.2    Verheugd, P.3    Luscher, B.4
  • 104
    • 80052961045 scopus 로고    scopus 로고
    • Identification of candidate substrates for poly(ADP-ribose) polymerase-2 (PARP2) in the absence of DNA damage using highdensity protein microarrays
    • S. Troiani, R. Lupi, R. Perego, S. R. Depaolini, S. Thieffine, R. Bosotti and L. Rusconi: Identification of candidate substrates for poly(ADP-ribose) polymerase-2 (PARP2) in the absence of DNA damage using highdensity protein microarrays. FEBS J, 278(19), 3676-3687 (2011).
    • (2011) FEBS J , vol.278 , Issue.19 , pp. 3676-3687
    • Troiani, S.1    Lupi, R.2    Perego, R.3    Depaolini, S.R.4    Thieffine, S.5    Bosotti, R.6    Rusconi, L.7
  • 105
    • 84867036962 scopus 로고    scopus 로고
    • Enrichment techniques employed in phosphoproteomics
    • J. Fila and D. Honys: Enrichment techniques employed in phosphoproteomics. Amino Acids, 43(3), 1025-47 (2012).
    • (2012) Amino Acids , vol.43 , Issue.3 , pp. 1025-1047
    • Fila, J.1    Honys, D.2
  • 106
    • 77956028057 scopus 로고    scopus 로고
    • Quantitative analysis of protein phosphorylation on a system-wide scale by mass spectrometry-based proteomics
    • B. Bodenmiller and R. Aebersold: Quantitative analysis of protein phosphorylation on a system-wide scale by mass spectrometry-based proteomics. Methods Enzymol, 470, 317-34 (2010).
    • (2010) Methods Enzymol , vol.470 , pp. 317-334
    • Bodenmiller, B.1    Aebersold, R.2
  • 107
    • 77955810108 scopus 로고    scopus 로고
    • Clickable NAD analogues for labeling substrate proteins of poly(ADP-ribose) polymerases
    • H. Jiang, J. H. Kim, K. M. Frizzell, W. L. Kraus and H. Lin: Clickable NAD analogues for labeling substrate proteins of poly(ADP-ribose) polymerases. J Am Chem Soc, 132(27), 9363-72 (2010).
    • (2010) J Am Chem Soc , vol.132 , Issue.27 , pp. 9363-9372
    • Jiang, H.1    Kim, J.H.2    Frizzell, K.M.3    Kraus, W.L.4    Lin, H.5
  • 108
    • 0017802365 scopus 로고
    • Purification of ADP-ribosylated nuclear proteins by covalent chromatography on dihydroxyboryl polyacrylamide beads and their characterization
    • DOI 10.1073/pnas.75.3.1111
    • H. Okayama, K. Ueda and O. Hayaishi: Purification of ADP-ribosylated nuclear proteins by covalent chromatography on dihydroxyboryl polyacrylamide beads and their characterization. Proc Natl Acad Sci USA, 75(3), 1111-5 (1978). (Pubitemid 8305217)
    • (1978) Proceedings of the National Academy of Sciences of the United States of America , vol.75 , Issue.3 , pp. 1111-1115
    • Okayama, H.1    Ueda, K.2    Hayaishi, O.3
  • 109
    • 0018599238 scopus 로고
    • Isolation and partial characterization of the ADP-ribosylated nuclear proteins from Ehrlich ascites tumor cells
    • P. Adamietz, K. Klapproth and H. Hilz: Isolation and partial characterization of the ADP-ribosylated nuclear proteins from Ehrlich ascites tumor cells. Biochem Biophys Res Commun, 91(4), 1232-1238 (1979). (Pubitemid 10143625)
    • (1979) Biochemical and Biophysical Research Communications , vol.91 , Issue.4 , pp. 1232-1238
    • Adamietz, P.1    Klapproth, K.2    Hilz, H.3
  • 110
    • 0014965042 scopus 로고
    • Synthesis of cellulose derivatives containing the dihydroxyboryl group and a study of their capacity to form specific complexes with sugars and nucleic acid components
    • H. L. Weith, J. L. Wiebers and P. T. Gilham: Synthesis of cellulose derivatives containing the dihydroxyboryl group and a study of their capacity to form specific complexes with sugars and nucleic acid components. Biochemistry, 9(22), 4396-4401 (1970).
    • (1970) Biochemistry , vol.9 , Issue.22 , pp. 4396-4401
    • Weith, H.L.1    Wiebers, J.L.2    Gilham, P.T.3
  • 111
    • 0015230826 scopus 로고
    • Hemoglobin components in patients with diabetes mellitus
    • L. A. Trivelli, H. M. Ranney and H. T. Lai: Hemoglobin components in patients with diabetes mellitus. N Engl J Med, 284(7), 353-357 (1971).
    • (1971) N Engl J Med , vol.284 , Issue.7 , pp. 353-357
    • Trivelli, L.A.1    Ranney, H.M.2    Lai, H.T.3
  • 114
    • 0035975870 scopus 로고    scopus 로고
    • Affinity chromatography as a method for sample preparation in gas chromatography/mass spectrometry
    • DOI 10.1016/S0165-022X(01)00230-5, PII S0165022X01002305
    • D. Tsikas: Affinity chromatography as a method for sample preparation in gas chromatography/mass spectrometry. J Biochem Biophys Methods, 49(1-3), 705-731 (2001). (Pubitemid 33022582)
    • (2001) Journal of Biochemical and Biophysical Methods , vol.49 , Issue.1-3 , pp. 705-731
    • Tsikas, D.1
  • 115
    • 70349900938 scopus 로고    scopus 로고
    • Ringopening polymerization with synergistic co-monomers: Access to a boronate-functionalized polymeric monolith for the specific capture of cis-diol-containing biomolecules under neutral conditions
    • L. Ren, Z. Liu, Y. Liu, P. Dou and H. Y. Chen: Ringopening polymerization with synergistic co-monomers: access to a boronate-functionalized polymeric monolith for the specific capture of cis-diol-containing biomolecules under neutral conditions. Angew Chem Int Ed Engl, 48(36), 6704-6707 (2009).
    • (2009) Angew Chem Int Ed Engl , vol.48 , Issue.36 , pp. 6704-6707
    • Ren, L.1    Liu, Z.2    Liu, Y.3    Dou, P.4    Chen, H.Y.5
  • 116
    • 79954449434 scopus 로고    scopus 로고
    • A unique boronic acid functionalized monolithic capillary for specific capture, separation and immobilization of cis-diol biomolecules
    • Y. Liu, L. Ren and Z. Liu: A unique boronic acid functionalized monolithic capillary for specific capture, separation and immobilization of cis-diol biomolecules. Chem Commun (Camb), 47(17), 5067-5069 (2011).
    • (2011) Chem Commun (Camb) , vol.47 , Issue.17 , pp. 5067-5069
    • Liu, Y.1    Ren, L.2    Liu, Z.3
  • 117
    • 0021774471 scopus 로고
    • Monoclonal antibodies to poly(adenosine diphosphate ribose) recognize different structures
    • H. Kawamitsu, H. Hoshino, H. Okada, M. Miwa, H. Momoi and T. Sugimura: Monoclonal antibodies to poly(adenosine diphosphate ribose) recognize different structures. Biochemistry, 23(16), 3771-7 (1984).
    • (1984) Biochemistry , vol.23 , Issue.16 , pp. 3771-3777
    • Kawamitsu, H.1    Hoshino, H.2    Okada, H.3    Miwa, M.4    Momoi, H.5    Sugimura, T.6
  • 118
    • 63149116496 scopus 로고    scopus 로고
    • Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome
    • N. Dani, A. Stilla, A. Marchegiani, A. Tamburro, S. Till, A. Ladurner, D. Corda and M. Di Girolamo: Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome. Proc Natl Acad Sci USA, 106(11), 4243-8 (2009).
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.11 , pp. 4243-4248
    • Dani, N.1    Stilla, A.2    Marchegiani, A.3    Tamburro, A.4    Till, S.5    Ladurner, A.6    Corda, D.7    Di Girolamo, M.8
  • 119
    • 84886246082 scopus 로고    scopus 로고
    • Proteome-wide identification of poly(ADP-ribosyl)ation targets in different genotoxic stress responses
    • S. Jungmichel, F. Rosenthal, M. Altmeyer, J. Lukas, M. O. Hottiger and M. L. Nielsen: Proteome-wide identification of poly(ADP-ribosyl)ation targets in different genotoxic stress responses. Mol Cell, 52(2), 272-85 (2013).
    • (2013) Mol Cell , vol.52 , Issue.2 , pp. 272-285
    • Jungmichel, S.1    Rosenthal, F.2    Altmeyer, M.3    Lukas, J.4    Hottiger, M.O.5    Nielsen, M.L.6
  • 120
    • 63149116496 scopus 로고    scopus 로고
    • Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome
    • N. Dani, A. Stilla, A. Marchegiani, A. Tamburro, S. Till, A. G. Ladurner, D. Corda and M. Di Girolamo: Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome. Proc Natl Acad Sci USA, 106(11), 4243-8 (2009).
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.11 , pp. 4243-4248
    • Dani, N.1    Stilla, A.2    Marchegiani, A.3    Tamburro, A.4    Till, S.5    Ladurner, A.G.6    Corda, D.7    Di Girolamo, M.8
  • 121
    • 77951634725 scopus 로고    scopus 로고
    • Systems-wide proteomic characterization of combinatorial post-translational modification patterns
    • N. L. Young, M. D. Plazas-Mayorca and B. A. Garcia: Systems-wide proteomic characterization of combinatorial post-translational modification patterns. Expert Rev Proteomics, 7(1), 79-92 (2010).
    • (2010) Expert Rev Proteomics , vol.7 , Issue.1 , pp. 79-92
    • Young, N.L.1    Plazas-Mayorca, M.D.2    Garcia, B.A.3
  • 122
    • 84861897793 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics and network biology
    • A. Bensimon, A. J. Heck and R. Aebersold: Mass spectrometry-based proteomics and network biology. Annu Rev Biochem, 81, 379-405 (2012).
    • (2012) Annu Rev Biochem , vol.81 , pp. 379-405
    • Bensimon, A.1    Heck, A.J.2    Aebersold, R.3
  • 123
    • 84874964821 scopus 로고    scopus 로고
    • Technologies and challenges in large-scale phosphoproteomics
    • K. Engholm-Keller and M. R. Larsen: Technologies and challenges in large-scale phosphoproteomics. Proteomics, 13(6), 910-931 (2013).
    • (2013) Proteomics , vol.13 , Issue.6 , pp. 910-931
    • Engholm-Keller, K.1    Larsen, M.R.2
  • 124
    • 84875252687 scopus 로고    scopus 로고
    • Advances in characterizing ubiquitylation sites by mass spectrometry
    • K. B. Sylvestersen, C. Young and M. L. Nielsen: Advances in characterizing ubiquitylation sites by mass spectrometry. Curr Opin Chem Biol, 17(1), 49-58 (2013).
    • (2013) Curr Opin Chem Biol , vol.17 , Issue.1 , pp. 49-58
    • Sylvestersen, K.B.1    Young, C.2    Nielsen, M.L.3
  • 125
    • 84875987561 scopus 로고    scopus 로고
    • Glycopeptide analysis, recent developments and applications
    • H. Desaire: Glycopeptide analysis, recent developments and applications. Mol Cell Proteomics, 12(4), 893-901 (2013).
    • (2013) Mol Cell Proteomics , vol.12 , Issue.4 , pp. 893-901
    • Desaire, H.1
  • 126
    • 33746855102 scopus 로고    scopus 로고
    • A Steric Antagonism of Actin Polymerization by a Salmonella Virulence Protein
    • DOI 10.1016/j.str.2006.05.022, PII S0969212606002887
    • S. M. Margarit, W. Davidson, L. Frego and C. E. Stebbins: A steric antagonism of actin polymerization by a salmonella virulence protein. Structure, 14(8), 1219-29 (2006). (Pubitemid 44176367)
    • (2006) Structure , vol.14 , Issue.8 , pp. 1219-1229
    • Margarit, S.M.1    Davidson, W.2    Frego, L.3    Stebbins, C.E.4
  • 127
    • 60649085333 scopus 로고    scopus 로고
    • Tandem mass spectrometry investigation of ADP-ribosylated kemptide
    • S. M. Hengel, S. A. Shaffer, B. L. Nunn and D. R. Goodlett: Tandem mass spectrometry investigation of ADP-ribosylated kemptide. J Am Soc Mass Spectrom, 20(3), 477-483 (2009).
    • (2009) J Am Soc Mass Spectrom , vol.20 , Issue.3 , pp. 477-483
    • Hengel, S.M.1    Shaffer, S.A.2    Nunn, B.L.3    Goodlett, D.R.4
  • 128
    • 33745684811 scopus 로고    scopus 로고
    • Electron capture dissociation mass spectrometry in characterization of peptides and proteins
    • R. Bakhtiar and Z. Guan: Electron capture dissociation mass spectrometry in characterization of peptides and proteins. Biotechnol Lett, 28(14), 1047-59 (2006).
    • (2006) Biotechnol Lett , vol.28 , Issue.14 , pp. 1047-1059
    • Bakhtiar, R.1    Guan, Z.2
  • 131
    • 75749098927 scopus 로고    scopus 로고
    • Electron transfer dissociation facilitates sequencing of adenosine diphosphate-ribosylated peptides
    • B. M. Zee and B. A. Garcia: Electron transfer dissociation facilitates sequencing of adenosine diphosphate-ribosylated peptides. Anal Chem, 82(1), 28- 31 (2010).
    • (2010) Anal Chem , vol.82 , Issue.1 , pp. 28-31
    • Zee, B.M.1    Garcia, B.A.2
  • 132
    • 77953155470 scopus 로고    scopus 로고
    • Fragmentation behavior of Amadori-peptides obtained by non-enzymatic glycosylation of lysine residues with ADPribose in tandem mass spectrometry
    • M. Fedorova, A. Frolov and R. Hoffmann: Fragmentation behavior of Amadori-peptides obtained by non-enzymatic glycosylation of lysine residues with ADPribose in tandem mass spectrometry. J Mass Spectrom, 45(6), 664-9 (2010).
    • (2010) J Mass Spectrom , vol.45 , Issue.6 , pp. 664-669
    • Fedorova, M.1    Frolov, A.2    Hoffmann, R.3
  • 134
    • 34548336772 scopus 로고    scopus 로고
    • Higher-energy C-trap dissociation for peptide modification analysis
    • DOI 10.1038/nmeth1060, PII NMETH1060
    • J. V. Olsen, B. Macek, O. Lange, A. Makarov, S. Horning and M. Mann: Higher-energy C-trap dissociation for peptide modification analysis. Nat Methods, 4(9), 709-12 (2007). (Pubitemid 47338163)
    • (2007) Nature Methods , vol.4 , Issue.9 , pp. 709-712
    • Olsen, J.V.1    MacEk, B.2    Lange, O.3    Makarov, A.4    Horning, S.5    Mann, M.6
  • 135
    • 57449099068 scopus 로고    scopus 로고
    • Precision proteomics: The case for high resolution and high mass accuracy
    • M. Mann and N. L. Kelleher: Precision proteomics: the case for high resolution and high mass accuracy. Proc Natl Acad Sci USA, 105(47), 18132-8 (2008).
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.47 , pp. 18132-18138
    • Mann, M.1    Kelleher, N.L.2
  • 136
    • 83055182135 scopus 로고    scopus 로고
    • Evaluation of HCD- and CID-type fragmentation within their respective detection platforms for murine phosphoproteomics
    • M. P. Jedrychowski, E. L. Huttlin, W. Haas, M. E. Sowa, R. Rad and S. P. Gygi: Evaluation of HCD- and CID-type fragmentation within their respective detection platforms for murine phosphoproteomics. Mol Cell Proteomics, 10(12), M111 009910 (2011).
    • (2011) Mol Cell Proteomics , vol.10 M111 , Issue.12 , pp. 009910
    • Jedrychowski, M.P.1    Huttlin, E.L.2    Haas, W.3    Sowa, M.E.4    Rad, R.5    Gygi, S.P.6
  • 137
    • 84875939839 scopus 로고    scopus 로고
    • Mapping PARP-1 auto-ADP-ribosylation sites by liquid chromatography- tandem mass spectrometry
    • J. D. Chapman, J. P. Gagne, G. G. Poirier and D. R. Goodlett: Mapping PARP-1 auto-ADP-ribosylation sites by liquid chromatography-tandem mass spectrometry. J Proteome Res (2013).
    • (2013) J Proteome Res
    • Chapman, J.D.1    Gagne, J.P.2    Poirier, G.G.3    Goodlett, D.R.4
  • 138
    • 0030854373 scopus 로고    scopus 로고
    • Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching
    • DOI 10.1021/bi971055p
    • V. Rolli, M. O'Farrell, J. Menissier-de Murcia and G. de Murcia: Random mutagenesis of the poly(ADPribose) polymerase catalytic domain reveals amino acids involved in polymer branching. Biochemistry, 36(40), 12147-54 (1997). (Pubitemid 27440951)
    • (1997) Biochemistry , vol.36 , Issue.40 , pp. 12147-12154
    • Rolli, V.1    O'Farrell, M.2    Menissier-De Murcia, J.3    De Murcia, G.4
  • 139
    • 0028852624 scopus 로고
    • Role of glutamic acid 988 of human poly-ADP-ribose polymerase in polymer formation. Evidence for active site similarities to the ADP-ribosylating toxins
    • G. T. Marsischky, B. A. Wilson and R. J. Collier: Role of glutamic acid 988 of human poly-ADP-ribose polymerase in polymer formation. Evidence for active site similarities to the ADP-ribosylating toxins. J Biol Chem, 270(7), 3247-54 (1995).
    • (1995) J Biol Chem , vol.270 , Issue.7 , pp. 3247-3254
    • Marsischky, G.T.1    Wilson, B.A.2    Collier, R.J.3
  • 140
    • 70349935191 scopus 로고    scopus 로고
    • Identification of the ADP-ribosylation sites in the PARP-1 automodification domain: Analysis and implications
    • Z. Tao, P. Gao and H. Liu: Identification of the ADP-ribosylation sites in the PARP-1 automodification domain: analysis and implications. J Am Chem Soc, 131(40), 14258-14260 (2009).
    • (2009) J Am Chem Soc , vol.131 , Issue.40 , pp. 14258-14260
    • Tao, Z.1    Gao, P.2    Liu, H.3
  • 141
    • 84884906084 scopus 로고    scopus 로고
    • Sitespecific characterization of the Asp- and Glu-ADPribosylated proteome
    • Y. Zhang, J. Wang, M. Ding and Y. Yu: Sitespecific characterization of the Asp- and Glu-ADPribosylated proteome. Nat Methods, 10(10), 981-4 (2013).
    • (2013) Nat Methods , vol.10 , Issue.10 , pp. 981-984
    • Zhang, Y.1    Wang, J.2    Ding, M.3    Yu, Y.4
  • 142
    • 0020856418 scopus 로고
    • Evaluation of immobilized boronates for studies of adenine and pyridine nucleotide metabolism
    • R. Alvarez-Gonzalez, H. Juarez-Salinas, E. L. Jacobson and M. K. Jacobson: Evaluation of immobilized boronates for studies of adenine and pyridine nucleotide metabolism. Anal Biochem, 135(1), 69-77 (1983).
    • (1983) Anal Biochem , vol.135 , Issue.1 , pp. 69-77
    • Alvarez-Gonzalez, R.1    Juarez-Salinas, H.2    Jacobson, E.L.3    Jacobson, M.K.4
  • 143
    • 0021111995 scopus 로고
    • Amino acidspecific ADP-ribosylation
    • J. Moss, D. A. Yost and S. J. Stanley: Amino acidspecific ADP-ribosylation. J Biol Chem, 258(10), 6466-70 (1983).
    • (1983) J Biol Chem , vol.258 , Issue.10 , pp. 6466-6470
    • Moss, J.1    Yost, D.A.2    Stanley, S.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.