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Volumn 125, Issue 19, 2012, Pages 4555-4566

Quantitative proteomics and dynamic imaging reveal that G3BP-mediated stress granule assembly is poly(ADP-ribose)-dependent following exposure to MNNG-induced DNA alkylation

Author keywords

G3BP; pADPr; Quantitative proteomics; SILAC; Stress granules

Indexed keywords

BINDING PROTEIN; G3BP PROTEIN; LEPTOMYCIN B; POLY(ADENOSINE DIPHOSPHATE RIBOSE); PROTEIN SH3; UNCLASSIFIED DRUG;

EID: 84872189805     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.106963     Document Type: Article
Times cited : (67)

References (58)
  • 1
    • 79958164837 scopus 로고    scopus 로고
    • A guide through the computational analysis of isotope-labeled mass spectrometry-based quantitative proteomics data: an application study
    • Albaum, S. P., Hahne, H., Otto, A., Haußmann, U., Becher, D., Poetsch, A., Goesmann, A. and Nattkemper, T. W. (2011). A guide through the computational analysis of isotope-labeled mass spectrometry-based quantitative proteomics data: an application study. Proteome Sci. 9, 30.
    • (2011) Proteome Sci , vol.9 , pp. 30
    • Albaum, S.P.1    Hahne, H.2    Otto, A.3    Haußmann, U.4    Becher, D.5    Poetsch, A.6    Goesmann, A.7    Nattkemper, T.W.8
  • 2
    • 0024428970 scopus 로고
    • Poly(ADP-ribose) catabolism in mammalian cells exposed to DNA-damaging agents
    • Alvarez-Gonzalez, R. and Althaus, F. R. (1989). Poly(ADP-ribose) catabolism in mammalian cells exposed to DNA-damaging agents. Mutat. Res. 218, 67-74.
    • (1989) Mutat. Res. , vol.218 , pp. 67-74
    • Alvarez-Gonzalez, R.1    Althaus, F.R.2
  • 4
    • 0037101945 scopus 로고    scopus 로고
    • Stressful initiations
    • Anderson, P. and Kedersha, N. (2002). Stressful initiations. J. Cell Sci. 115, 3227-3234.
    • (2002) J. Cell Sci. , vol.115 , pp. 3227-3234
    • Anderson, P.1    Kedersha, N.2
  • 5
    • 66249103703 scopus 로고    scopus 로고
    • RNA granules: post-transcriptional and epigenetic modulators of gene expression
    • Anderson, P. and Kedersha, N. (2009). RNA granules: post-transcriptional and epigenetic modulators of gene expression. Nat. Rev. Mol. Cell Biol. 10, 430-436.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 430-436
    • Anderson, P.1    Kedersha, N.2
  • 7
    • 57649233085 scopus 로고    scopus 로고
    • Mitochondrial and nuclear cross talk in cell death: parthanatos
    • Andrabi, S. A., Dawson, T. M. and Dawson, V. L. (2008). Mitochondrial and nuclear cross talk in cell death: parthanatos. Ann. N. Y. Acad. Sci. 1147, 233-241.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1147 , pp. 233-241
    • Andrabi, S.A.1    Dawson, T.M.2    Dawson, V.L.3
  • 11
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADPribosyl) ation reactions in the regulation of nuclear functions
    • D'Amours, D., Desnoyers, S., D'Silva, I. and Poirier, G. G. (1999). Poly(ADPribosyl) ation reactions in the regulation of nuclear functions. Biochem. J. 342, 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
  • 14
    • 65449145195 scopus 로고    scopus 로고
    • Inhibition of poly(ADP-ribose) polymerase-1 by arsenite interferes with repair of oxidative DNA damage
    • Ding, W., Liu, W., Cooper, K. L., Qin, X. J., de Souza Bergo, P. L., Hudson, L. G. and Liu, K. J. (2009). Inhibition of poly(ADP-ribose) polymerase-1 by arsenite interferes with repair of oxidative DNA damage. J. Biol. Chem. 284, 6809-6817.
    • (2009) J. Biol. Chem. , vol.284 , pp. 6809-6817
    • Ding, W.1    Liu, W.2    Cooper, K.L.3    Qin, X.J.4    de Souza Bergo, P.L.5    Hudson, L.G.6    Liu, K.J.7
  • 15
    • 0018906390 scopus 로고
    • (ADP-ribose)n participates in DNA excision repair
    • Durkacz, B. W., Omidiji, O., Gray, D. A. and Shall, S. (1980). (ADP-ribose)n participates in DNA excision repair. Nature 283, 593-596.
    • (1980) Nature , vol.283 , pp. 593-596
    • Durkacz, B.W.1    Omidiji, O.2    Gray, D.A.3    Shall, S.4
  • 16
    • 0038641860 scopus 로고    scopus 로고
    • A proteomic approach to the identification of heterogeneous nuclear ribonucleoproteins as a new family of poly(ADP-ribose)-binding proteins
    • Gagné, J. P., Hunter, J. M., Labrecque, B., Chabot, B. and Poirier, G. G. (2003). A proteomic approach to the identification of heterogeneous nuclear ribonucleoproteins as a new family of poly(ADP-ribose)-binding proteins. Biochem. J. 371, 331-340.
    • (2003) Biochem. J. , vol.371 , pp. 331-340
    • Gagné, J.P.1    Hunter, J.M.2    Labrecque, B.3    Chabot, B.4    Poirier, G.G.5
  • 17
    • 29644440131 scopus 로고    scopus 로고
    • Poly(ADP-ribose) glycohydrolase is a component of the FMRPassociated messenger ribonucleoparticles
    • Gagné, J. P., Bonicalzi, M. E., Gagné, P., Ouellet, M. E., Hendzel, M. J. and Poirier, G. G. (2005). Poly(ADP-ribose) glycohydrolase is a component of the FMRPassociated messenger ribonucleoparticles. Biochem. J. 392, 499-509.
    • (2005) Biochem. J. , vol.392 , pp. 499-509
    • Gagné, J.P.1    Bonicalzi, M.E.2    Gagné, P.3    Ouellet, M.E.4    Hendzel, M.J.5    Poirier, G.G.6
  • 18
    • 58749112769 scopus 로고    scopus 로고
    • Proteome-wide identification of poly(ADP-ribose) binding proteins and poly(ADP-ribose)-associated protein complexes
    • Gagné, J. P., Isabelle, M., Lo, K. S., Bourassa, S., Hendzel, M. J., Dawson, V. L., Dawson, T. M. and Poirier, G. G. (2008). Proteome-wide identification of poly(ADP-ribose) binding proteins and poly(ADP-ribose)-associated protein complexes. Nucleic Acids Res. 36, 6959-6976.
    • (2008) Nucleic Acids Res , vol.36 , pp. 6959-6976
    • Gagné, 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
  • 20
    • 36248971198 scopus 로고    scopus 로고
    • How arginine-rich domains coordinate mRNA maturation events
    • Godin, K. S. and Varani, G. (2007). How arginine-rich domains coordinate mRNA maturation events. RNA Biol. 4, 69-75.
    • (2007) RNA Biol , vol.4 , pp. 69-75
    • Godin, K.S.1    Varani, G.2
  • 21
    • 33644984966 scopus 로고    scopus 로고
    • Dynamic relocation of poly(ADP-ribose) glycohydrolase isoforms during radiation-induced DNA damage
    • Haince, J. F., Ouellet, M. E., McDonald, D., Hendzel, M. J. and Poirier, G. G. (2006). Dynamic relocation of poly(ADP-ribose) glycohydrolase isoforms during radiation-induced DNA damage. Biochim. Biophys. Acta 1763, 226-237.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 226-237
    • Haince, J.F.1    Ouellet, M.E.2    McDonald, D.3    Hendzel, M.J.4    Poirier, G.G.5
  • 22
  • 23
    • 40649095957 scopus 로고    scopus 로고
    • Quantitative proteomics using stable isotope labeling with amino acids in cell culture
    • Harsha, H. C., Molina, H. and Pandey, A. (2008). Quantitative proteomics using stable isotope labeling with amino acids in cell culture. Nat. Protoc. 3, 505-516.
    • (2008) Nat. Protoc. , vol.3 , pp. 505-516
    • Harsha, H.C.1    Molina, H.2    Pandey, A.3
  • 24
    • 38449088040 scopus 로고    scopus 로고
    • The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases
    • Hassa, P. O. and Hottiger, M. O. (2008). The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases. Front. Biosci. 13, 3046-3082.
    • (2008) Front. Biosci. , vol.13 , pp. 3046-3082
    • Hassa, P.O.1    Hottiger, M.O.2
  • 25
    • 57849139691 scopus 로고    scopus 로고
    • Playing tag with quantitative proteomics
    • Iliuk, A., Galan, J. and Tao, W. A. (2009). Playing tag with quantitative proteomics. Anal. Bioanal. Chem. 393, 503-513.
    • (2009) Anal. Bioanal. Chem. , vol.393 , pp. 503-513
    • Iliuk, A.1    Galan, J.2    Tao, W.A.3
  • 26
    • 67649855305 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation of heterogeneous nuclear ribonucleoproteins modulates splicing
    • Ji, Y. and Tulin, A. V. (2009). Poly(ADP-ribosyl)ation of heterogeneous nuclear ribonucleoproteins modulates splicing. Nucleic Acids Res. 37, 3501-3513.
    • (2009) Nucleic Acids Res , vol.37 , pp. 3501-3513
    • Ji, Y.1    Tulin, A.V.2
  • 27
    • 0036863320 scopus 로고    scopus 로고
    • Stress granules: sites of mRNA triage that regulate mRNA stability and translatability
    • Kedersha, N. and Anderson, P. (2002). Stress granules: sites of mRNA triage that regulate mRNA stability and translatability. Biochem. Soc. Trans. 30, 963-969.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 963-969
    • Kedersha, N.1    Anderson, P.2
  • 29
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A., Nesvizhskii, A. I., Kolker, E. and Aebersold, R. (2002). Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 74, 5383-5392.
    • (2002) Anal. Chem. , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 30
    • 24344454692 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal
    • Kim, M. Y., Zhang, T. and Kraus, W. L. (2005). Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal. Genes Dev. 19, 1951-1967.
    • (2005) Genes Dev , vol.19 , pp. 1951-1967
    • Kim, M.Y.1    Zhang, T.2    Kraus, W.L.3
  • 31
    • 0037302958 scopus 로고    scopus 로고
    • Mammalian stress granules represent sites of accumulation of stalled translation initiation complexes
    • Kimball, S. R., Horetsky, R. L., Ron, D., Jefferson, L. S. and Harding, H. P. (2003). Mammalian stress granules represent sites of accumulation of stalled translation initiation complexes. Am. J. Physiol. Cell Physiol. 284, C273-C284.
    • (2003) Am. J. Physiol. Cell Physiol. , vol.284
    • Kimball, S.R.1    Horetsky, R.L.2    Ron, D.3    Jefferson, L.S.4    Harding, H.P.5
  • 32
    • 61449101465 scopus 로고    scopus 로고
    • Poly (ADP-ribose) polymerase 1 is required for protein localization to Cajal body
    • Kotova, E., Jarnik, M. and Tulin, A. V. (2009). Poly (ADP-ribose) polymerase 1 is required for protein localization to Cajal body. PLoS Genet. 5, e1000387.
    • (2009) PLoS Genet , vol.5
    • Kotova, E.1    Jarnik, M.2    Tulin, A.V.3
  • 33
    • 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. and Chang, P. (2011). Poly(ADP-ribose) regulates stress responses and microRNA activity in the cytoplasm. Mol. Cell 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
  • 34
    • 0028865245 scopus 로고
    • Post-translational modification of poly(ADP-ribose) polymerase induced by DNA strand breaks
    • Lindahl, T., Satoh, M. S., Poirier, G. G. and Klungland, A. (1995). Post-translational modification of poly(ADP-ribose) polymerase induced by DNA strand breaks. Trends Biochem. Sci. 20, 405-411.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 405-411
    • Lindahl, T.1    Satoh, M.S.2    Poirier, G.G.3    Klungland, A.4
  • 35
    • 50649093361 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to the splicing factor ASF/SF2 and regulates its phosphorylation by DNA topoisomerase I
    • Malanga, M., Czubaty, A., Girstun, A., Staron, K. and Althaus, F. R. (2008). Poly(ADP-ribose) binds to the splicing factor ASF/SF2 and regulates its phosphorylation by DNA topoisomerase I. J. Biol. Chem. 283, 19991-19998.
    • (2008) J. Biol. Chem. , vol.283 , pp. 19991-19998
    • Malanga, M.1    Czubaty, A.2    Girstun, A.3    Staron, K.4    Althaus, F.R.5
  • 36
    • 0020759349 scopus 로고
    • Immunoaffinity fractionation of the poly(ADP-ribosyl)ated domains of chromatin
    • Malik, N., Miwa, M., Sugimura, T., Thraves, P. and Smulson, M. (1983). Immunoaffinity fractionation of the poly(ADP-ribosyl)ated domains of chromatin. Proc. Natl. Acad. Sci. USA 80, 2554-2558.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2554-2558
    • Malik, N.1    Miwa, M.2    Sugimura, T.3    Thraves, P.4    Smulson, M.5
  • 37
    • 75549091918 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor proteome reveals chromatin-regulatory partners
    • Montes de Oca, R., Shoemaker, C. J., Gucek, M., Cole, R. N. and Wilson, K. L. (2009). Barrier-to-autointegration factor proteome reveals chromatin-regulatory partners. PLoS ONE 4, e7050.
    • (2009) PLoS ONE , vol.4
    • Montes de Oca, R.1    Shoemaker, C.J.2    Gucek, M.3    Cole, R.N.4    Wilson, K.L.5
  • 38
    • 79960206370 scopus 로고    scopus 로고
    • PARG is recruited to DNA damage sites through poly(ADP-ribose)- and PCNAdependent mechanisms
    • Mortusewicz, O., Fouquerel, E., Amé, J. C., Leonhardt, H. and Schreiber, V. (2011). PARG is recruited to DNA damage sites through poly(ADP-ribose)- and PCNAdependent mechanisms. Nucleic Acids Res. 39, 5045-5056.
    • (2011) Nucleic Acids Res , vol.39 , pp. 5045-5056
    • Mortusewicz, O.1    Fouquerel, E.2    Amé, J.C.3    Leonhardt, H.4    Schreiber, V.5
  • 39
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii, A. I., Keller, A., Kolker, E. and Aebersold, R. (2003). A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 75, 4646-4658.
    • (2003) Anal. Chem. , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 40
    • 45749126026 scopus 로고    scopus 로고
    • C. elegans La-related protein, LARP-1, localizes to germline P bodies and attenuates Ras-MAPK signaling during oogenesis
    • Nykamp, K., Lee, M. H. and Kimble, J. (2008). C. elegans La-related protein, LARP-1, localizes to germline P bodies and attenuates Ras-MAPK signaling during oogenesis. RNA 14, 1378-1389.
    • (2008) RNA , vol.14 , pp. 1378-1389
    • Nykamp, K.1    Lee, M.H.2    Kimble, J.3
  • 41
    • 34250372908 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture for quantitative proteomics
    • Ong, S. E. and Mann, M. (2007). Stable isotope labeling by amino acids in cell culture for quantitative proteomics. Methods Mol. Biol. 359, 37-52.
    • (2007) Methods Mol. Biol. , vol.359 , pp. 37-52
    • Ong, S.E.1    Mann, M.2
  • 42
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A. and Mann, M. (2002). Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 43
    • 20544475918 scopus 로고    scopus 로고
    • Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: determining the PARG catalytic domain
    • Patel, C. N., Koh, D. W., Jacobson, M. K. and Oliveira, M. A. (2005). Identification of three critical acidic residues of poly(ADP-ribose) glycohydrolase involved in catalysis: determining the PARG catalytic domain. Biochem. J. 388, 493-500.
    • (2005) Biochem. J. , vol.388 , pp. 493-500
    • Patel, C.N.1    Koh, D.W.2    Jacobson, M.K.3    Oliveira, M.A.4
  • 44
    • 0034731455 scopus 로고    scopus 로고
    • Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins
    • Pleschke, J. M., Kleczkowska, H. E., Strohm, M. and Althaus, F. R. (2000). Poly(ADP-ribose) binds to specific domains in DNA damage checkpoint proteins. J. Biol. Chem. 275, 40974-40980.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40974-40980
    • Pleschke, J.M.1    Kleczkowska, H.E.2    Strohm, M.3    Althaus, F.R.4
  • 45
    • 1642308537 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ated chromatin domains: access granted
    • Rouleau, M., Aubin, R. A. and Poirier, G. G. (2004). Poly(ADP-ribosyl)ated chromatin domains: access granted. J. Cell Sci. 117, 815-825.
    • (2004) J. Cell Sci. , vol.117 , pp. 815-825
    • Rouleau, M.1    Aubin, R.A.2    Poirier, G.G.3
  • 48
    • 4243068535 scopus 로고    scopus 로고
    • The therapeutic effects of PJ34 [N-(6-oxo-5,6-dihydrophenanthridin-2-yl)-N,N-dimethylacetamide.HCl], a selective inhibitor of poly(ADP-ribose) polymerase, in experimental allergic encephalomyelitis are associated with immunomodulation
    • Scott, G. S., Kean, R. B., Mikheeva, T., Fabis, M. J., Mabley, J. G., Szabó, C. and Hooper, D. C. (2004). The therapeutic effects of PJ34 [N-(6-oxo-5,6-dihydrophenanthridin-2-yl)-N,N-dimethylacetamide.HCl], a selective inhibitor of poly(ADP-ribose) polymerase, in experimental allergic encephalomyelitis are associated with immunomodulation. J. Pharmacol. Exp. Ther. 310, 1053-1061.
    • (2004) J. Pharmacol. Exp. Ther. , vol.310 , pp. 1053-1061
    • Scott, G.S.1    Kean, R.B.2    Mikheeva, T.3    Fabis, M.J.4    Mabley, J.G.5    Szabó, C.6    Hooper, D.C.7
  • 49
    • 79951906633 scopus 로고    scopus 로고
    • SIRT3 substrate specificity determined by peptide arrays and machine learning
    • Smith, B. C., Settles, B., Hallows, W. C., Craven, M. W. and Denu, J. M. (2011). SIRT3 substrate specificity determined by peptide arrays and machine learning. ACS Chem. Biol. 6, 146-157.
    • (2011) ACS Chem. Biol. , vol.6 , pp. 146-157
    • Smith, B.C.1    Settles, B.2    Hallows, W.C.3    Craven, M.W.4    Denu, J.M.5
  • 51
    • 0034775591 scopus 로고    scopus 로고
    • RasGAP-associated endoribonuclease G3Bp: selective RNA degradation and phosphorylation-dependent localization
    • Tourrière, H., Gallouzi, I. E., Chebli, K., Capony, J. P., Mouaikel, J., van der Geer, P. and Tazi, J. (2001). RasGAP-associated endoribonuclease G3Bp: selective RNA degradation and phosphorylation-dependent localization. Mol. Cell. Biol. 21, 7747-7760.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7747-7760
    • Tourrière, H.1    Gallouzi, I.E.2    Chebli, K.3    Capony, J.P.4    Mouaikel, J.5    van der Geer, P.6    Tazi, J.7
  • 53
    • 0037462597 scopus 로고    scopus 로고
    • Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci
    • Tulin, A. and Spradling, A. (2003). Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci. Science 299, 560-562.
    • (2003) Science , vol.299 , pp. 560-562
    • Tulin, A.1    Spradling, A.2
  • 54
    • 0141619287 scopus 로고    scopus 로고
    • Radiosensitization and DNA repair inhibition by the combined use of novel inhibitors of DNA-dependent protein kinase and poly(ADP-ribose) polymerase-1
    • Veuger, S. J., Curtin, N. J., Richardson, C. J., Smith, G. C. and Durkacz, B. W. (2003). Radiosensitization and DNA repair inhibition by the combined use of novel inhibitors of DNA-dependent protein kinase and poly(ADP-ribose) polymerase-1. Cancer Res. 63, 6008-6015.
    • (2003) Cancer Res , vol.63 , pp. 6008-6015
    • Veuger, S.J.1    Curtin, N.J.2    Richardson, C.J.3    Smith, G.C.4    Durkacz, B.W.5
  • 55
    • 67649526000 scopus 로고    scopus 로고
    • Poly(ADP-ribose) signals to mitochondrial AIF: a key event in parthanatos
    • Wang, Y., Dawson, V. L. and Dawson, T. M. (2009). Poly(ADP-ribose) signals to mitochondrial AIF: a key event in parthanatos. Exp. Neurol. 218, 193-202.
    • (2009) Exp. Neurol. , vol.218 , pp. 193-202
    • Wang, Y.1    Dawson, V.L.2    Dawson, T.M.3
  • 56
    • 79953840957 scopus 로고    scopus 로고
    • Poly(ADP-ribose) (PAR) binding to apoptosis-inducing factor is critical for PAR polymerase-1-dependent cell death (parthanatos)
    • Wang, Y., Kim, N. S., Haince, J. F., Kang, H. C., David, K. K., Andrabi, S. A., Poirier, G. G., Dawson, V. L. and Dawson, T. M. (2011). Poly(ADP-ribose) (PAR) binding to apoptosis-inducing factor is critical for PAR polymerase-1-dependent cell death (parthanatos). Sci. Signal. 4, ra20.
    • (2011) Sci. Signal. , vol.4
    • Wang, Y.1    Kim, N.S.2    Haince, J.F.3    Kang, H.C.4    David, K.K.5    Andrabi, S.A.6    Poirier, G.G.7    Dawson, V.L.8    Dawson, T.M.9
  • 58
    • 4544348052 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation as a DNA damage-induced post-translational modification regulating poly(ADP-ribose) polymerase-1-topoisomerase I interaction
    • Yung, T. M., Sato, S. and Satoh, M. S. (2004). Poly(ADP-ribosyl)ation as a DNA damage-induced post-translational modification regulating poly(ADP-ribose) polymerase-1-topoisomerase I interaction. J. Biol. Chem. 279, 39686-39696.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39686-39696
    • Yung, T.M.1    Sato, S.2    Satoh, M.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.