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Volumn 586, Issue 17, 2012, Pages 2723-2731

Beyond hairballs: The use of quantitative mass spectrometry data to understand protein-protein interactions

Author keywords

Affinity purification coupled to mass spectrometry; Interaction networks; Protein protein interactions; Quantitative proteomics; Regulated interactions

Indexed keywords

AFFINITY PURIFICATION COUPLED WITH MASS SPECTROMETRY; DATA ANALYSIS; DATA BASE; FALSE POSITIVE RESULT; INFORMATION PROCESSING; ISOTOPE LABELING; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEOMICS; QUANTITATIVE ANALYSIS; REVIEW;

EID: 84864619937     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.03.065     Document Type: Review
Times cited : (28)

References (117)
  • 3
    • 33846844989 scopus 로고    scopus 로고
    • HORFeome v3.1: A resource of human open reading frames representing over 10,000 human genes
    • 10.1016/j.ygeno.2006.11.012
    • P. Lamesch, N. Li, S. Milstein, C. Fan, T. Hao, G. Szabo, Z. Hu, K. Venkatesan, G. Bethel, and P. Martin HORFeome v3.1: a resource of human open reading frames representing over 10,000 human genes Genomics 89 2007 307 315 10.1016/j.ygeno.2006.11.012
    • (2007) Genomics , vol.89 , pp. 307-315
    • Lamesch, P.1    Li, N.2    Milstein, S.3    Fan, C.4    Hao, T.5    Szabo, G.6    Hu, Z.7    Venkatesan, K.8    Bethel, G.9    Martin, P.10
  • 7
    • 75549087142 scopus 로고    scopus 로고
    • Systematic cloning of an ORFeome using the Gateway system
    • 10.1007/978-1-60761-232-2-2
    • A. Matsuyama, and M. Yoshida Systematic cloning of an ORFeome using the Gateway system Methods Mol. Biol. 577 2009 11 24 10.1007/978-1-60761-232-2-2
    • (2009) Methods Mol. Biol. , vol.577 , pp. 11-24
    • Matsuyama, A.1    Yoshida, M.2
  • 9
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • 10.1038/340245a0
    • S. Fields, and O. Song A novel genetic system to detect protein-protein interactions Nature 340 1989 245 246 10.1038/340245a0
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 11
    • 0033974688 scopus 로고    scopus 로고
    • Toward a protein-protein interaction map of the budding yeast: A comprehensive system to examine two-hybrid interactions in all possible combinations between the yeast proteins
    • T. Ito, K. Tashiro, S. Muta, R. Ozawa, T. Chiba, M. Nishizawa, K. Yamamoto, S. Kuhara, and Y. Sakaki Toward a protein-protein interaction map of the budding yeast: a comprehensive system to examine two-hybrid interactions in all possible combinations between the yeast proteins Proc. Natl. Acad. Sci. U S A 97 2000 1143 1147
    • (2000) Proc. Natl. Acad. Sci. U S A , vol.97 , pp. 1143-1147
    • Ito, T.1    Tashiro, K.2    Muta, S.3    Ozawa, R.4    Chiba, T.5    Nishizawa, M.6    Yamamoto, K.7    Kuhara, S.8    Sakaki, Y.9
  • 12
    • 0035836765 scopus 로고    scopus 로고
    • A comprehensive two-hybrid analysis to explore the yeast protein interactome
    • 10.1073/pnas.061034498
    • T. Ito, T. Chiba, R. Ozawa, M. Yoshida, M. Hattori, and Y. Sakaki A comprehensive two-hybrid analysis to explore the yeast protein interactome Proc. Natl. Acad. Sci. U S A 98 2001 4569 4574 10.1073/pnas.061034498
    • (2001) Proc. Natl. Acad. Sci. U S A , vol.98 , pp. 4569-4574
    • Ito, T.1    Chiba, T.2    Ozawa, R.3    Yoshida, M.4    Hattori, M.5    Sakaki, Y.6
  • 19
  • 22
    • 84857780876 scopus 로고    scopus 로고
    • Evidence for network evolution in an Arabidopsis interactome map
    • Arabidopsis Interactome Mapping Consortium
    • Arabidopsis Interactome Mapping Consortium (2011) Evidence for network evolution in an Arabidopsis interactome map. Science 333, 601-607, doi: http://dx.doi.org/10.1126/science.1203877.
    • (2011) Science , vol.333 , pp. 601-607
  • 24
    • 84862670921 scopus 로고    scopus 로고
    • Strategies for membrane interaction proteomics: No mass spectrometry required
    • in press
    • Lam M. and Stagljar, I. Strategies for membrane interaction proteomics: no mass spectrometry required. Proteomics in press.
    • Proteomics
    • Lam, M.1    Stagljar, I.2
  • 25
    • 84862703457 scopus 로고    scopus 로고
    • Interactome mapping for analysis of complex phenotypes: Insights from benchmarking binary interaction assays
    • in press
    • Braun, P. Interactome mapping for analysis of complex phenotypes: insights from benchmarking binary interaction assays. Proteomics in press.
    • Proteomics
    • Braun, P.1
  • 30
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • 10.1016/j.cell.2009.04.042
    • M.E. Sowa, E.J. Bennett, S.P. Gygi, and J.W. Harper Defining the human deubiquitinating enzyme interaction landscape Cell 138 2009 389 403 10.1016/j.cell.2009.04.042
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 31
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • 10.1038/nature09204
    • C. Behrends, M.E. Sowa, S.P. Gygi, and J.W. Harper Network organization of the human autophagy system Nature 466 2010 68 76 10.1038/nature09204
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 34
    • 59149096171 scopus 로고    scopus 로고
    • A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein
    • 10.1074/mcp.M800266-MCP200
    • M. Goudreault, L.M. D'Ambrosio, M.J. Kean, M.J. Mullin, B.G. Larsen, A. Sanchez, S. Chaudhry, G.I. Chen, F. Sicheri, and A.I. Nesvizhskii A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein Mol. Cell Proteomics 8 2009 157 171 10.1074/mcp.M800266-MCP200
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 157-171
    • Goudreault, M.1    D'Ambrosio, L.M.2    Kean, M.J.3    Mullin, M.J.4    Larsen, B.G.5    Sanchez, A.6    Chaudhry, S.7    Chen, G.I.8    Sicheri, F.9    Nesvizhskii, A.I.10
  • 36
    • 58549085778 scopus 로고    scopus 로고
    • An integrated workflow for charting the human interaction proteome: Insights into the PP2A system
    • 10.1038/msb.2008.75
    • T. Glatter, A. Wepf, R. Aebersold, and M. Gstaiger An integrated workflow for charting the human interaction proteome: insights into the PP2A system Mol. Syst. Biol. 5 2009 237 10.1038/msb.2008.75
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 237
    • Glatter, T.1    Wepf, A.2    Aebersold, R.3    Gstaiger, M.4
  • 37
    • 34447321025 scopus 로고    scopus 로고
    • Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme
    • 10.1016/j.molcel.2007.06.027
    • C. Jeronimo, D. Forget, A. Bouchard, Q. Li, G. Chua, C. Poitras, C. Therien, D. Bergeron, S. Bourassa, and J. Greenblatt Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme Mol. Cell 27 2007 262 274 10.1016/j.molcel.2007.06.027
    • (2007) Mol. Cell , vol.27 , pp. 262-274
    • Jeronimo, C.1    Forget, D.2    Bouchard, A.3    Li, Q.4    Chua, G.5    Poitras, C.6    Therien, C.7    Bergeron, D.8    Bourassa, S.9    Greenblatt, J.10
  • 41
    • 80054924599 scopus 로고    scopus 로고
    • Proteomic and functional genomic landscape of receptor tyrosine kinase and ras to extracellular signal-regulated kinase signaling
    • 10.1126/scisignal.2002029
    • A.A. Friedman, G. Tucker, R. Singh, D. Yan, A. Vinayagam, Y. Hu, R. Binari, P. Hong, X. Sun, and M. Porto Proteomic and functional genomic landscape of receptor tyrosine kinase and ras to extracellular signal-regulated kinase signaling Sci. Signal 4 2011 rs10 10.1126/scisignal.2002029
    • (2011) Sci. Signal , vol.4 , pp. 10
    • Friedman, A.A.1    Tucker, G.2    Singh, R.3    Yan, D.4    Vinayagam, A.5    Hu, Y.6    Binari, R.7    Hong, P.8    Sun, X.9    Porto, M.10
  • 48
    • 57649174475 scopus 로고    scopus 로고
    • PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4
    • 10.1074/jbc.M803443200
    • G.I. Chen, S. Tisayakorn, C. Jorgensen, L.M. D'Ambrosio, M. Goudreault, and A.C. Gingras PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4 J. Biol. Chem. 283 2008 29273 29284 10.1074/jbc.M803443200
    • (2008) J. Biol. Chem. , vol.283 , pp. 29273-29284
    • Chen, G.I.1    Tisayakorn, S.2    Jorgensen, C.3    D'Ambrosio, L.M.4    Goudreault, M.5    Gingras, A.C.6
  • 50
    • 79952676403 scopus 로고    scopus 로고
    • Literature curation of protein interactions: Measuring agreement across major public databases
    • 10.1093/database/baq026
    • A.L. Turinsky, S. Razick, B. Turner, I.M. Donaldson, and S.J. Wodak Literature curation of protein interactions: measuring agreement across major public databases Database (Oxford) 2010 2010 Baq026 10.1093/database/baq026
    • (2010) Database (Oxford) , vol.2010 , pp. 026
    • Turinsky, A.L.1    Razick, S.2    Turner, B.3    Donaldson, I.M.4    Wodak, S.J.5
  • 54
    • 79953713220 scopus 로고    scopus 로고
    • Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5
    • 10.1002/pmic.201000770
    • D.V. Skarra, M. Goudreault, H. Choi, M. Mullin, A.I. Nesvizhskii, A.C. Gingras, and R.E. Honkanen Label-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5 Proteomics 11 2011 1508 1516 10.1002/pmic.201000770
    • (2011) Proteomics , vol.11 , pp. 1508-1516
    • Skarra, D.V.1    Goudreault, M.2    Choi, H.3    Mullin, M.4    Nesvizhskii, A.I.5    Gingras, A.C.6    Honkanen, R.E.7
  • 58
    • 84859620713 scopus 로고    scopus 로고
    • SAINT-MS1: Protein-protein interaction scoring using label-free intensity data in affinity purification-mass spectrometry experiments
    • 10.1021/pr201185r
    • H. Choi, T. Glatter, M. Gstaiger, and A.I. Nesvizhskii SAINT-MS1: protein-protein interaction scoring using label-free intensity data in affinity purification-mass spectrometry experiments J. Proteome Res. 2012 10.1021/pr201185r
    • (2012) J. Proteome Res.
    • Choi, H.1    Glatter, T.2    Gstaiger, M.3    Nesvizhskii, A.I.4
  • 59
    • 77955345941 scopus 로고    scopus 로고
    • Profiling of protein interaction networks of protein complexes using affinity purification and quantitative mass spectrometry
    • 10.1074/mcp.R110.000265
    • R.M. Kaake, X. Wang, and L. Huang Profiling of protein interaction networks of protein complexes using affinity purification and quantitative mass spectrometry Mol. Cell Proteomics 9 2010 1650 1665 10.1074/mcp.R110.000265
    • (2010) Mol. Cell Proteomics , vol.9 , pp. 1650-1665
    • Kaake, R.M.1    Wang, X.2    Huang, L.3
  • 60
    • 67349225422 scopus 로고    scopus 로고
    • New dimensions in the study of protein complexes using quantitative mass spectrometry
    • 10.1016/j.febslet.2009.04.018
    • S. Oeljeklaus, H.E. Meyer, and B. Warscheid New dimensions in the study of protein complexes using quantitative mass spectrometry FEBS Lett. 583 2009 1674 1683 10.1016/j.febslet.2009.04.018
    • (2009) FEBS Lett. , vol.583 , pp. 1674-1683
    • Oeljeklaus, S.1    Meyer, H.E.2    Warscheid, B.3
  • 61
    • 84862655632 scopus 로고    scopus 로고
    • Resolving protein interactions and complexes by affinity purification followed by label-based quantitative mass spectrometry
    • in press
    • Trinkle-Mulcahy, L. (2012) Resolving protein interactions and complexes by affinity purification followed by label-based quantitative mass spectrometry. Proteomics in press.
    • (2012) Proteomics
    • Trinkle-Mulcahy, L.1
  • 62
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • 10.1073/pnas.0832254100
    • S.A. Gerber, J. Rush, O. Stemman, M.W. Kirschner, and S.P. Gygi Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS Proc. Natl. Acad. Sci. U S A 100 2003 6940 6945 10.1073/pnas.0832254100
    • (2003) Proc. Natl. Acad. Sci. U S A , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 64
    • 23144442824 scopus 로고    scopus 로고
    • Multiplexed absolute quantification in proteomics using artificial QCAT proteins of concatenated signature peptides
    • 10.1038/nmeth774
    • R.J. Beynon, M.K. Doherty, J.M. Pratt, and S.J. Gaskell Multiplexed absolute quantification in proteomics using artificial QCAT proteins of concatenated signature peptides Nat. Methods 2 2005 587 589 10.1038/nmeth774
    • (2005) Nat. Methods , vol.2 , pp. 587-589
    • Beynon, R.J.1    Doherty, M.K.2    Pratt, J.M.3    Gaskell, S.J.4
  • 65
    • 34548427053 scopus 로고    scopus 로고
    • Absolute multiplexed quantitative analysis of protein expression during muscle development using QconCAT
    • 10.1074/mcp.M600456-MCP200
    • J. Rivers, D.M. Simpson, D.H. Robertson, S.J. Gaskell, and R.J. Beynon Absolute multiplexed quantitative analysis of protein expression during muscle development using QconCAT Mol. Cell Proteomics 6 2007 1416 1427 10.1074/mcp.M600456-MCP200
    • (2007) Mol. Cell Proteomics , vol.6 , pp. 1416-1427
    • Rivers, J.1    Simpson, D.M.2    Robertson, D.H.3    Gaskell, S.J.4    Beynon, R.J.5
  • 66
    • 33748319353 scopus 로고    scopus 로고
    • Statistical analysis of membrane proteome expression changes in Saccharomyces cerevisiae
    • 10.1021/pr060161n
    • B. Zybailov, A.L. Mosley, M.E. Sardiu, M.K. Coleman, L. Florens, and M.P. Washburn Statistical analysis of membrane proteome expression changes in Saccharomyces cerevisiae J. Proteome Res. 5 2006 2339 2347 10.1021/pr060161n
    • (2006) J. Proteome Res. , vol.5 , pp. 2339-2347
    • Zybailov, B.1    Mosley, A.L.2    Sardiu, M.E.3    Coleman, M.K.4    Florens, L.5    Washburn, M.P.6
  • 67
    • 58149299336 scopus 로고    scopus 로고
    • Significance analysis of spectral count data in label-free shotgun proteomics
    • 10.1074/mcp.M800203-MCP200
    • H. Choi, D. Fermin, and A.I. Nesvizhskii Significance analysis of spectral count data in label-free shotgun proteomics Mol. Cell Proteomics 7 2008 2373 2385 10.1074/mcp.M800203-MCP200
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 2373-2385
    • Choi, H.1    Fermin, D.2    Nesvizhskii, A.I.3
  • 68
    • 74049132731 scopus 로고    scopus 로고
    • Label-free, normalized quantification of complex mass spectrometry data for proteomic analysis
    • 10.1038/nbt.1592
    • N.M. Griffin, J. Yu, F. Long, P. Oh, S. Shore, Y. Li, J.A. Koziol, and J.E. Schnitzer Label-free, normalized quantification of complex mass spectrometry data for proteomic analysis Nat. Biotechnol. 28 2010 83 89 10.1038/nbt.1592
    • (2010) Nat. Biotechnol. , vol.28 , pp. 83-89
    • Griffin, N.M.1    Yu, J.2    Long, F.3    Oh, P.4    Shore, S.5    Li, Y.6    Koziol, J.A.7    Schnitzer, J.E.8
  • 69
    • 77952344256 scopus 로고    scopus 로고
    • Quantitative proteomics combined with BAC TransgeneOmics reveals in vivo protein interactions
    • 10.1083/jcb.200911091
    • N.C. Hubner, A.W. Bird, J. Cox, B. Splettstoesser, P. Bandilla, I. Poser, A. Hyman, and M. Mann Quantitative proteomics combined with BAC TransgeneOmics reveals in vivo protein interactions J. Cell Biol. 189 2010 739 754 10.1083/jcb.200911091
    • (2010) J. Cell Biol. , vol.189 , pp. 739-754
    • Hubner, N.C.1    Bird, A.W.2    Cox, J.3    Splettstoesser, B.4    Bandilla, P.5    Poser, I.6    Hyman, A.7    Mann, M.8
  • 70
    • 33947182552 scopus 로고    scopus 로고
    • An integrated mass spectrometric and computational framework for the analysis of protein interaction networks
    • 10.1038/nbt1289
    • O. Rinner, L.N. Mueller, M. Hubalek, M. Muller, M. Gstaiger, and R. Aebersold An integrated mass spectrometric and computational framework for the analysis of protein interaction networks Nat. Biotechnol. 25 2007 345 352 10.1038/nbt1289
    • (2007) Nat. Biotechnol. , vol.25 , pp. 345-352
    • Rinner, O.1    Mueller, L.N.2    Hubalek, M.3    Muller, M.4    Gstaiger, M.5    Aebersold, R.6
  • 72
    • 61449237172 scopus 로고    scopus 로고
    • Quantitative interaction proteomics using mass spectrometry
    • 10.1038/nmeth.1302
    • A. Wepf, T. Glatter, A. Schmidt, R. Aebersold, and M. Gstaiger Quantitative interaction proteomics using mass spectrometry Nat. Methods 6 2009 203 205 10.1038/nmeth.1302
    • (2009) Nat. Methods , vol.6 , pp. 203-205
    • Wepf, A.1    Glatter, T.2    Schmidt, A.3    Aebersold, R.4    Gstaiger, M.5
  • 75
    • 33745925880 scopus 로고    scopus 로고
    • Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase
    • 10.1073/pnas.0602400103
    • S.E. Moyer, P.W. Lewis, and M.R. Botchan Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase Proc. Natl. Acad. Sci. U S A 103 2006 10236 10241 10.1073/pnas.0602400103
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 10236-10241
    • Moyer, S.E.1    Lewis, P.W.2    Botchan, M.R.3
  • 78
    • 84862646149 scopus 로고    scopus 로고
    • Mapping physical interactions within chromatin by proteomic approaches
    • in press
    • Lambert, J.P., Pawson, T. and Gingras, A.C. (2012) Mapping physical interactions within chromatin by proteomic approaches. Proteomics in press.
    • (2012) Proteomics
    • Lambert, J.P.1    Pawson, T.2    Gingras, A.C.3
  • 80
    • 66149100528 scopus 로고    scopus 로고
    • A novel proteomics approach for the discovery of chromatin-associated protein networks
    • 10.1074/mcp.M800447-MCP200
    • J.P. Lambert, L. Mitchell, A. Rudner, K. Baetz, and D. Figeys A novel proteomics approach for the discovery of chromatin-associated protein networks Mol. Cell Proteomics 8 2009 870 882 10.1074/mcp.M800447-MCP200
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 870-882
    • Lambert, J.P.1    Mitchell, L.2    Rudner, A.3    Baetz, K.4    Figeys, D.5
  • 86
    • 39049117451 scopus 로고    scopus 로고
    • Identifying dynamic interactors of protein complexes by quantitative mass spectrometry
    • 10.1074/mcp.M700261-MCP200
    • X. Wang, and L. Huang Identifying dynamic interactors of protein complexes by quantitative mass spectrometry Mol. Cell Proteomics 7 2008 46 57 10.1074/mcp.M700261-MCP200
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 46-57
    • Wang, X.1    Huang, L.2
  • 87
    • 43849110454 scopus 로고    scopus 로고
    • Quantitative proteomics reveals regulation of dynamic components within TATA-binding protein (TBP) transcription complexes
    • 10.1074/mcp.M700306-MCP200
    • F. Mousson, A. Kolkman, W.W. Pijnappel, H.T. Timmers, and A.J. Heck Quantitative proteomics reveals regulation of dynamic components within TATA-binding protein (TBP) transcription complexes Mol. Cell Proteomics 7 2008 845 852 10.1074/mcp.M700306-MCP200
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 845-852
    • Mousson, F.1    Kolkman, A.2    Pijnappel, W.W.3    Timmers, H.T.4    Heck, A.J.5
  • 88
    • 84859576245 scopus 로고    scopus 로고
    • Identification of core components and transient interactors of the peroxisomal importomer by dual-track stable isotope labeling with amino acids in cell culture analysis
    • 10.1021/pr3000333
    • S. Oeljeklaus, B.S. Reinartz, J. Wolf, S. Wiese, J. Tonillo, K. Podwojski, K. Kuhlmann, C. Stephan, H.E. Meyer, and W. Schliebs Identification of core components and transient interactors of the peroxisomal importomer by dual-track stable isotope labeling with amino acids in cell culture analysis J. Proteome Res. 2012 10.1021/pr3000333
    • (2012) J. Proteome Res.
    • Oeljeklaus, S.1    Reinartz, B.S.2    Wolf, J.3    Wiese, S.4    Tonillo, J.5    Podwojski, K.6    Kuhlmann, K.7    Stephan, C.8    Meyer, H.E.9    Schliebs, W.10
  • 89
    • 34248999095 scopus 로고    scopus 로고
    • Affinity-purification mass spectrometry (AP-MS) of serine/threonine phosphatases
    • 10.1016/j.ymeth.2007.02.018
    • G.I. Chen, and A.C. Gingras Affinity-purification mass spectrometry (AP-MS) of serine/threonine phosphatases Methods 42 2007 298 305 10.1016/j.ymeth.2007.02.018
    • (2007) Methods , vol.42 , pp. 298-305
    • Chen, G.I.1    Gingras, A.C.2
  • 90
    • 77956058146 scopus 로고    scopus 로고
    • Investigation of protein-protein interactions in living cells by chemical crosslinking and mass spectrometry
    • 10.1007/s00216-009-3405-5
    • A. Sinz Investigation of protein-protein interactions in living cells by chemical crosslinking and mass spectrometry Anal. Bioanal. Chem. 397 2010 3433 3440 10.1007/s00216-009-3405-5
    • (2010) Anal. Bioanal. Chem. , vol.397 , pp. 3433-3440
    • Sinz, A.1
  • 91
    • 78149438179 scopus 로고    scopus 로고
    • Crosslinking combined with mass spectrometry for structural proteomics
    • 10.1002/mas.20293
    • E.V. Petrotchenko, and C.H. Borchers Crosslinking combined with mass spectrometry for structural proteomics Mass Spectrom. Rev. 29 2010 862 876 10.1002/mas.20293
    • (2010) Mass Spectrom. Rev. , vol.29 , pp. 862-876
    • Petrotchenko, E.V.1    Borchers, C.H.2
  • 92
    • 84857938427 scopus 로고    scopus 로고
    • Joining forces: Integrating proteomics and cross-linking with the mass spectrometry of intact complexes
    • 10.1074/mcp.R111.014027 R111 014027
    • F. Stengel, R. Aebersold, and C.V. Robinson Joining forces: integrating proteomics and cross-linking with the mass spectrometry of intact complexes Mol. Cell Proteomics 11 2012 10.1074/mcp.R111.014027 R111 014027
    • (2012) Mol. Cell Proteomics , vol.11
    • Stengel, F.1    Aebersold, R.2    Robinson, C.V.3
  • 93
    • 77955381399 scopus 로고    scopus 로고
    • Probing native protein structures by chemical cross-linking, mass spectrometry, and bioinformatics
    • 10.1074/mcp.R000001-MCP201
    • A. Leitner, T. Walzthoeni, A. Kahraman, F. Herzog, O. Rinner, M. Beck, and R. Aebersold Probing native protein structures by chemical cross-linking, mass spectrometry, and bioinformatics Mol. Cell Proteomics 9 2010 1634 1649 10.1074/mcp.R000001-MCP201
    • (2010) Mol. Cell Proteomics , vol.9 , pp. 1634-1649
    • Leitner, A.1    Walzthoeni, T.2    Kahraman, A.3    Herzog, F.4    Rinner, O.5    Beck, M.6    Aebersold, R.7
  • 94
    • 79851513173 scopus 로고    scopus 로고
    • The beginning of a beautiful friendship: Cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes
    • 10.1016/j.jsb.2010.10.014
    • J. Rappsilber The beginning of a beautiful friendship: cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes J. Struct. Biol. 173 2011 530 540 10.1016/j.jsb.2010.10.014
    • (2011) J. Struct. Biol. , vol.173 , pp. 530-540
    • Rappsilber, J.1
  • 96
    • 80054760401 scopus 로고    scopus 로고
    • Protein-fragment complementation assays for large-scale analysis, functional dissection and dynamic studies of protein-protein interactions in living cells
    • 10.1007/978-1-61779-160-4-25
    • S.W. Michnick, P.H. Ear, C. Landry, M.K. Malleshaiah, and V. Messier Protein-fragment complementation assays for large-scale analysis, functional dissection and dynamic studies of protein-protein interactions in living cells Methods Mol. Biol. 756 2011 395 425 10.1007/978-1-61779-160-4-25
    • (2011) Methods Mol. Biol. , vol.756 , pp. 395-425
    • Michnick, S.W.1    Ear, P.H.2    Landry, C.3    Malleshaiah, M.K.4    Messier, V.5
  • 97
    • 77956048943 scopus 로고    scopus 로고
    • A toolkit of protein-fragment complementation assays for studying and dissecting large-scale and dynamic protein-protein interactions in living cells
    • 10.1016/S0076-6879(10)70014-8
    • S.W. Michnick, P.H. Ear, C. Landry, M.K. Malleshaiah, and V. Messier A toolkit of protein-fragment complementation assays for studying and dissecting large-scale and dynamic protein-protein interactions in living cells Methods Enzymol. 470 2010 335 368 10.1016/S0076-6879(10)70014-8
    • (2010) Methods Enzymol. , vol.470 , pp. 335-368
    • Michnick, S.W.1    Ear, P.H.2    Landry, C.3    Malleshaiah, M.K.4    Messier, V.5
  • 98
    • 79959851876 scopus 로고    scopus 로고
    • A roadmap to generate renewable protein binders to the human proteome
    • 10.1038/nmeth.1607
    • K. Colwill, and S. Graslund A roadmap to generate renewable protein binders to the human proteome Nat. Methods 8 2011 551 558 10.1038/nmeth.1607
    • (2011) Nat. Methods , vol.8 , pp. 551-558
    • Colwill, K.1    Graslund, S.2
  • 101
    • 40749116015 scopus 로고    scopus 로고
    • Automated production of recombinant human proteins as resource for proteome research
    • 10.1186/1477-5956-6-4
    • T. Kohl, C. Schmidt, S. Wiemann, A. Poustka, and U. Korf Automated production of recombinant human proteins as resource for proteome research Proteome Sci. 6 2008 4 10.1186/1477-5956-6-4
    • (2008) Proteome Sci. , vol.6 , pp. 4
    • Kohl, T.1    Schmidt, C.2    Wiemann, S.3    Poustka, A.4    Korf, U.5
  • 103
    • 70349564237 scopus 로고    scopus 로고
    • Profiling protein interaction networks with functional protein microarrays
    • 10.1007/978-1-60761-175-2-4
    • D.R. Mattoon, and B. Schweitzer Profiling protein interaction networks with functional protein microarrays Methods Mol. Biol. 563 2009 63 74 10.1007/978-1-60761-175-2-4
    • (2009) Methods Mol. Biol. , vol.563 , pp. 63-74
    • Mattoon, D.R.1    Schweitzer, B.2
  • 105
    • 84862663706 scopus 로고    scopus 로고
    • Integrating mass spectrometry of intact protein complexes into structural proteomics
    • in press
    • Suk-Joon, H. and Ruotolo, B. (2012) Integrating mass spectrometry of intact protein complexes into structural proteomics. Proteomics in press.
    • (2012) Proteomics
    • Suk-Joon, H.1    Ruotolo, B.2
  • 109
    • 70350212549 scopus 로고    scopus 로고
    • Determining protein complex connectivity using a probabilistic deletion network derived from quantitative proteomics
    • 10.1371/journal.pone.0007310
    • M.E. Sardiu, J.M. Gilmore, M.J. Carrozza, B. Li, J.L. Workman, L. Florens, and M.P. Washburn Determining protein complex connectivity using a probabilistic deletion network derived from quantitative proteomics PLoS One 4 2009 e7310 10.1371/journal.pone.0007310
    • (2009) PLoS One , vol.4 , pp. 7310
    • Sardiu, M.E.1    Gilmore, J.M.2    Carrozza, M.J.3    Li, B.4    Workman, J.L.5    Florens, L.6    Washburn, M.P.7
  • 111
    • 80755126865 scopus 로고    scopus 로고
    • Mapping a dynamic innate immunity protein interaction network regulating type i interferon production
    • 10.1016/j.immuni.2011.06.014
    • S. Li, L. Wang, M. Berman, Y.Y. Kong, and M.E. Dorf Mapping a dynamic innate immunity protein interaction network regulating type I interferon production Immunity 35 2011 426 440 10.1016/j.immuni.2011.06.014
    • (2011) Immunity , vol.35 , pp. 426-440
    • Li, S.1    Wang, L.2    Berman, M.3    Kong, Y.Y.4    Dorf, M.E.5
  • 112
    • 65549169528 scopus 로고    scopus 로고
    • Quantitative proteomics reveals a dynamic interactome and phase-specific phosphorylation in the Neurospora circadian clock
    • 10.1016/j.molcel.2009.04.023
    • C.L. Baker, A.N. Kettenbach, J.J. Loros, S.A. Gerber, and J.C. Dunlap Quantitative proteomics reveals a dynamic interactome and phase-specific phosphorylation in the Neurospora circadian clock Mol Cell 34 2009 354 363 10.1016/j.molcel.2009.04.023
    • (2009) Mol Cell , vol.34 , pp. 354-363
    • Baker, C.L.1    Kettenbach, A.N.2    Loros, J.J.3    Gerber, S.A.4    Dunlap, J.C.5
  • 114
    • 78751675280 scopus 로고    scopus 로고
    • Targeted proteomics by selected reaction monitoring mass spectrometry: Applications to systems biology and biomarker discovery
    • 10.1039/c0mb00159g
    • S. Elschenbroich, and T. Kislinger Targeted proteomics by selected reaction monitoring mass spectrometry: applications to systems biology and biomarker discovery Mol. Biosyst. 7 2011 292 303 10.1039/c0mb00159g
    • (2011) Mol. Biosyst. , vol.7 , pp. 292-303
    • Elschenbroich, S.1    Kislinger, T.2
  • 116
    • 54049090766 scopus 로고    scopus 로고
    • Selected reaction monitoring for quantitative proteomics: A tutorial
    • 10.1038/msb.2008.61
    • V. Lange, P. Picotti, B. Domon, and R. Aebersold Selected reaction monitoring for quantitative proteomics: a tutorial Mol. Syst. Biol. 4 2008 222 10.1038/msb.2008.61
    • (2008) Mol. Syst. Biol. , vol.4 , pp. 222
    • Lange, V.1    Picotti, P.2    Domon, B.3    Aebersold, R.4
  • 117
    • 84861860481 scopus 로고    scopus 로고
    • Targeted data extraction of the MS/MS spectra generated by data independent acquisition: A new concept for consistent and accurate proteome analysis
    • 10.1074/mcp.O111.016717
    • L.C. Gillet, P. Navarro, S. Tate, H. Roest, N. Selevsek, L. Reiter, R. Bonner, and R. Aebersold Targeted data extraction of the MS/MS spectra generated by data independent acquisition: a new concept for consistent and accurate proteome analysis Mol. Cell Proteomics 2012 10.1074/mcp.O111.016717
    • (2012) Mol. Cell Proteomics
    • Gillet, L.C.1    Navarro, P.2    Tate, S.3    Roest, H.4    Selevsek, N.5    Reiter, L.6    Bonner, R.7    Aebersold, R.8


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