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Volumn 11, Issue 2, 2012, Pages 796-807

Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CYCLIN DEPENDENT KINASE INHIBITOR; LYSINE; PROTEOME; UBIQUITIN;

EID: 84856637551     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr200668y     Document Type: Article
Times cited : (35)

References (50)
  • 2
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. M. Mechanisms underlying ubiquitination Annu. Rev. Biochem. 2001, 70, 503-533
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 3
    • 2142663061 scopus 로고    scopus 로고
    • Ubiquitin as a central cellular regulator
    • 2 p following S
    • Finley, D.; Ciechanover, A.; Varshavsky, A. Ubiquitin as a central cellular regulator Cell 2004, 116 (2 Suppl) S29-S32 2 p following S
    • (2004) Cell , vol.116 , Issue.2 SUPPL.
    • Finley, D.1    Ciechanover, A.2    Varshavsky, A.3
  • 4
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade
    • Scheffner, M.; Nuber, U.; Huibregtse, J. M. Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade Nature 1995, 373 (6509) 81-83
    • (1995) Nature , vol.373 , Issue.6509 , pp. 81-83
    • Scheffner, M.1    Nuber, U.2    Huibregtse, J.M.3
  • 5
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R.; Mann, M. Mass spectrometry-based proteomics Nature 2003, 422 (6928) 198-207
    • (2003) Nature , vol.422 , Issue.6928 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 6
    • 35848970747 scopus 로고    scopus 로고
    • Mapping protein post-translational modifications with mass spectrometry
    • Witze, E. S.; Old, W. M.; Resing, K. A.; Ahn, N. G. Mapping protein post-translational modifications with mass spectrometry Nat. Methods 2007, 4 (10) 798-806
    • (2007) Nat. Methods , vol.4 , Issue.10 , pp. 798-806
    • Witze, E.S.1    Old, W.M.2    Resing, K.A.3    Ahn, N.G.4
  • 7
    • 77952956167 scopus 로고    scopus 로고
    • Decoding signalling networks by mass spectrometry-based proteomics
    • Choudhary, C.; Mann, M. Decoding signalling networks by mass spectrometry-based proteomics Nat. Rev. Mol. Cell. Biol. 2010, 11 (6) 427-439
    • (2010) Nat. Rev. Mol. Cell. Biol. , vol.11 , Issue.6 , pp. 427-439
    • Choudhary, C.1    Mann, M.2
  • 8
    • 0037161303 scopus 로고    scopus 로고
    • Direct identification of a G protein ubiquitination site by mass spectrometry
    • Marotti, L. A., Jr.; Newitt, R.; Wang, Y.; Aebersold, R.; Dohlman, H. G. Direct identification of a G protein ubiquitination site by mass spectrometry Biochemistry 2002, 41 (16) 5067-5074
    • (2002) Biochemistry , vol.41 , Issue.16 , pp. 5067-5074
    • Marotti Jr., L.A.1    Newitt, R.2    Wang, Y.3    Aebersold, R.4    Dohlman, H.G.5
  • 10
    • 33845441117 scopus 로고    scopus 로고
    • Dissecting the ubiquitin pathway by mass spectrometry
    • Xu, P.; Peng, J. Dissecting the ubiquitin pathway by mass spectrometry Biochim. Biophys. Acta 2006, 1764 (12) 1940-1947
    • (2006) Biochim. Biophys. Acta , vol.1764 , Issue.12 , pp. 1940-1947
    • Xu, P.1    Peng, J.2
  • 11
    • 20444384069 scopus 로고    scopus 로고
    • Analysis of polyubiquitin conjugates reveals that the Rpn10 substrate receptor contributes to the turnover of multiple proteasome targets
    • Mayor, T.; Lipford, J. R.; Graumann, J.; Smith, G. T.; Deshaies, R. J. Analysis of polyubiquitin conjugates reveals that the Rpn10 substrate receptor contributes to the turnover of multiple proteasome targets Mol. Cell. Proteomics 2005, 4 (6) 741-751
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.6 , pp. 741-751
    • Mayor, T.1    Lipford, J.R.2    Graumann, J.3    Smith, G.T.4    Deshaies, R.J.5
  • 12
    • 33645703441 scopus 로고    scopus 로고
    • A tandem affinity tag for two-step purification under fully denaturing conditions: Application in ubiquitin profiling and protein complex identification combined with in vivocross-linking
    • Tagwerker, C.; Flick, K.; Cui, M.; Guerrero, C.; Dou, Y.; Auer, B.; Baldi, P.; Huang, L.; Kaiser, P. A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking Mol. Cell. Proteomics 2006, 5 (4) 737-748
    • (2006) Mol. Cell. Proteomics , vol.5 , Issue.4 , pp. 737-748
    • Tagwerker, C.1    Flick, K.2    Cui, M.3    Guerrero, C.4    Dou, Y.5    Auer, B.6    Baldi, P.7    Huang, L.8    Kaiser, P.9
  • 13
    • 55949136614 scopus 로고    scopus 로고
    • Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry
    • Meierhofer, D.; Wang, X.; Huang, L.; Kaiser, P. Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry J. Proteome Res. 2008, 7 (10) 4566-4576
    • (2008) J. Proteome Res. , vol.7 , Issue.10 , pp. 4566-4576
    • Meierhofer, D.1    Wang, X.2    Huang, L.3    Kaiser, P.4
  • 16
    • 29144505073 scopus 로고    scopus 로고
    • Proteomic analysis of ubiquitinated proteins from human MCF-7 breast cancer cells by immunoaffinity purification and mass spectrometry
    • Vasilescu, J.; Smith, J. C.; Ethier, M.; Figeys, D. Proteomic analysis of ubiquitinated proteins from human MCF-7 breast cancer cells by immunoaffinity purification and mass spectrometry J. Proteome Res. 2005, 4 (6) 2192-2200
    • (2005) J. Proteome Res. , vol.4 , Issue.6 , pp. 2192-2200
    • Vasilescu, J.1    Smith, J.C.2    Ethier, M.3    Figeys, D.4
  • 20
    • 70449084692 scopus 로고    scopus 로고
    • Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities
    • Hjerpe, R.; Aillet, F.; Lopitz-Otsoa, F.; Lang, V.; England, P.; Rodriguez, M. S. Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities EMBO Rep. 2009, 10 (11) 1250-1258
    • (2009) EMBO Rep. , vol.10 , Issue.11 , pp. 1250-1258
    • Hjerpe, R.1    Aillet, F.2    Lopitz-Otsoa, F.3    Lang, V.4    England, P.5    Rodriguez, M.S.6
  • 22
    • 78651225388 scopus 로고    scopus 로고
    • Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
    • Xu, G.; Paige, J. S.; Jaffrey, S. R. Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling Nat. Biotechnol. 2010, 28 (8) 868-873
    • (2010) Nat. Biotechnol. , vol.28 , Issue.8 , pp. 868-873
    • Xu, G.1    Paige, J.S.2    Jaffrey, S.R.3
  • 24
    • 0037453306 scopus 로고    scopus 로고
    • Preferential interaction of TIP120A with Cul1 that is not modified by NEDD8 and not associated with Skp1
    • Oshikawa, K.; Matsumoto, M.; Yada, M.; Kamura, T.; Hatakeyama, S.; Nakayama, K. I. Preferential interaction of TIP120A with Cul1 that is not modified by NEDD8 and not associated with Skp1 Biochem. Biophys. Res. Commun. 2003, 303 (4) 1209-1216
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , Issue.4 , pp. 1209-1216
    • Oshikawa, K.1    Matsumoto, M.2    Yada, M.3    Kamura, T.4    Hatakeyama, S.5    Nakayama, K.I.6
  • 25
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • Rappsilber, J.; Mann, M.; Ishihama, Y. Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips Nat. Protoc. 2007, 2 (8) 1896-1906
    • (2007) Nat. Protoc. , vol.2 , Issue.8 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 26
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama, Y.; Oda, Y.; Tabata, T.; Sato, T.; Nagasu, T.; Rappsilber, J.; Mann, M. Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein Mol. Cell. Proteomics 2005, 4 (9) 1265-1272
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.9 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5    Rappsilber, J.6    Mann, M.7
  • 27
    • 77949518999 scopus 로고    scopus 로고
    • EmPAI Calc - For the estimation of protein abundance from large-scale identification data by liquid chromatography-tandem mass spectrometry
    • Shinoda, K.; Tomita, M.; Ishihama, Y. emPAI Calc - for the estimation of protein abundance from large-scale identification data by liquid chromatography-tandem mass spectrometry Bioinformatics 2010, 26 (4) 576-577
    • (2010) Bioinformatics , vol.26 , Issue.4 , pp. 576-577
    • Shinoda, K.1    Tomita, M.2    Ishihama, Y.3
  • 28
  • 30
    • 0037673562 scopus 로고    scopus 로고
    • The comparative proteomics of ubiquitination in mouse
    • Semple, C. A. The comparative proteomics of ubiquitination in mouse Genome Res. 2003, 13 (6B) 1389-1394
    • (2003) Genome Res. , vol.13 , Issue.6 B , pp. 1389-1394
    • Semple, C.A.1
  • 33
    • 65549120715 scopus 로고    scopus 로고
    • Modes of p53 regulation
    • Kruse, J. P.; Gu, W. Modes of p53 regulation Cell 2009, 137 (4) 609-622
    • (2009) Cell , vol.137 , Issue.4 , pp. 609-622
    • Kruse, J.P.1    Gu, W.2
  • 35
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson, E. S. Protein modification by SUMO Annu. Rev. Biochem. 2004, 73, 355-382
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 36
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary, C.; Kumar, C.; Gnad, F.; Nielsen, M. L.; Rehman, M.; Walther, T. C.; Olsen, J. V.; Mann, M. Lysine acetylation targets protein complexes and co-regulates major cellular functions Science 2009, 325 (5942) 834-840
    • (2009) Science , vol.325 , Issue.5942 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6    Olsen, J.V.7    Mann, M.8
  • 37
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: Emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau, J. R.; Lima, C. D. The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition Nat. Rev. Mol. Cell. Biol. 2010, 11 (12) 861-871
    • (2010) Nat. Rev. Mol. Cell. Biol. , vol.11 , Issue.12 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 38
    • 78650177028 scopus 로고    scopus 로고
    • The epigenome as a therapeutic target in prostate cancer
    • Perry, A. S.; Watson, R. W.; Lawler, M.; Hollywood, D. The epigenome as a therapeutic target in prostate cancer Nat. Rev. Urol. 2010, 7 (12) 668-680
    • (2010) Nat. Rev. Urol. , vol.7 , Issue.12 , pp. 668-680
    • Perry, A.S.1    Watson, R.W.2    Lawler, M.3    Hollywood, D.4
  • 41
    • 78751662908 scopus 로고    scopus 로고
    • The Polycomb complex PRC2 and its mark in life
    • Margueron, R.; Reinberg, D. The Polycomb complex PRC2 and its mark in life Nature 2011, 469 (7330) 343-349
    • (2011) Nature , vol.469 , Issue.7330 , pp. 343-349
    • Margueron, R.1    Reinberg, D.2
  • 42
    • 79751469547 scopus 로고    scopus 로고
    • NEDD8 pathways in cancer, Sine Quibus Non
    • Watson, I. R.; Irwin, M. S.; Ohh, M. NEDD8 pathways in cancer, Sine Quibus Non Cancer Cell 2011, 19 (2) 168-176
    • (2011) Cancer Cell , vol.19 , Issue.2 , pp. 168-176
    • Watson, I.R.1    Irwin, M.S.2    Ohh, M.3
  • 43
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IκBα inhibits NF-κB activation
    • Desterro, J. M.; Rodriguez, M. S.; Hay, R. T. SUMO-1 modification of IκBα inhibits NF-κB activation Mol. Cell 1998, 2 (2) 233-239
    • (1998) Mol. Cell , vol.2 , Issue.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 44
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • Kouzarides, T. Acetylation: a regulatory modification to rival phosphorylation? EMBO J. 2000, 19 (6) 1176-1179
    • (2000) EMBO J. , vol.19 , Issue.6 , pp. 1176-1179
    • Kouzarides, T.1
  • 45
    • 21244449061 scopus 로고    scopus 로고
    • Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p
    • Papouli, E.; Chen, S.; Davies, A. A.; Huttner, D.; Krejci, L.; Sung, P.; Ulrich, H. D. Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p Mol. Cell 2005, 19 (1) 123-133
    • (2005) Mol. Cell , vol.19 , Issue.1 , pp. 123-133
    • Papouli, E.1    Chen, S.2    Davies, A.A.3    Huttner, D.4    Krejci, L.5    Sung, P.6    Ulrich, H.D.7
  • 46
    • 49349107518 scopus 로고    scopus 로고
    • Lysine acetylation: Codified crosstalk with other posttranslational modifications
    • Yang, X. J.; Seto, E. Lysine acetylation: codified crosstalk with other posttranslational modifications Mol. Cell 2008, 31 (4) 449-461
    • (2008) Mol. Cell , vol.31 , Issue.4 , pp. 449-461
    • Yang, X.J.1    Seto, E.2
  • 47
    • 65649101212 scopus 로고    scopus 로고
    • Crosstalk between sumoylation and acetylation regulates p53-dependent chromatin transcription and DNA binding
    • Wu, S. Y.; Chiang, C. M. Crosstalk between sumoylation and acetylation regulates p53-dependent chromatin transcription and DNA binding EMBO J. 2009, 28 (9) 1246-1259
    • (2009) EMBO J. , vol.28 , Issue.9 , pp. 1246-1259
    • Wu, S.Y.1    Chiang, C.M.2
  • 48
    • 0029024015 scopus 로고
    • Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27
    • Pagano, M.; Tam, S. W.; Theodoras, A. M.; Beer-Romero, P.; Del Sal, G.; Chau, V.; Yew, P. R.; Draetta, G. F.; Rolfe, M. Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27 Science 1995, 269 (5224) 682-685
    • (1995) Science , vol.269 , Issue.5224 , pp. 682-685
    • Pagano, M.1    Tam, S.W.2    Theodoras, A.M.3    Beer-Romero, P.4    Del Sal, G.5    Chau, V.6    Yew, P.R.7    Draetta, G.F.8    Rolfe, M.9
  • 49
    • 33646345376 scopus 로고    scopus 로고
    • Ubiquitin ligases: Cell-cycle control and cancer
    • Nakayama, K. I.; Nakayama, K. Ubiquitin ligases: cell-cycle control and cancer Nat. Rev. Cancer 2006, 6 (5) 369-381
    • (2006) Nat. Rev. Cancer , vol.6 , Issue.5 , pp. 369-381
    • Nakayama, K.I.1    Nakayama, K.2


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