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Volumn 2, Issue 6, 2007, Pages 1414-1425

Tandem orthogonal proteolysis-activity-based protein profiling (TOP-ABPP) - A general method for mapping sites of probe modification in proteomes

Author keywords

[No Author keywords available]

Indexed keywords

PROTEOME; REAGENT;

EID: 34250746414     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2007.194     Document Type: Article
Times cited : (206)

References (28)
  • 1
    • 0031848226 scopus 로고    scopus 로고
    • Proteome and proteomics: New technologies, new concepts, and new words
    • Anderson, N.L. & Anderson, N.G. Proteome and proteomics: New technologies, new concepts, and new words. Electrophoresis 19 1853-1861 (1998).
    • (1998) Electrophoresis , vol.19 , pp. 1853-1861
    • Anderson, N.L.1    Anderson, N.G.2
  • 2
    • 0034923505 scopus 로고    scopus 로고
    • Analysis of proteins and proteomes by mass spectrometry
    • Mann, M., Hendrickson, R.C. & Pandey, A. Analysis of proteins and proteomes by mass spectrometry. Annu. Rev. Biochem. 70, 437-473 (2001).
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 437-473
    • Mann, M.1    Hendrickson, R.C.2    Pandey, A.3
  • 3
    • 0033604499 scopus 로고    scopus 로고
    • Active site-directed protein regulation
    • Kobe, B. & Kemp, B.E. Active site-directed protein regulation. Nature 402, 373-376 (1999).
    • (1999) Nature , vol.402 , pp. 373-376
    • Kobe, B.1    Kemp, B.E.2
  • 4
    • 33748595526 scopus 로고    scopus 로고
    • Mechanism-based profiling of enzyme families
    • Evans, M.J. & Cravatt, B.F. Mechanism-based profiling of enzyme families. Chem. Rev. 106, 3279-3301 (2006).
    • (2006) Chem. Rev , vol.106 , pp. 3279-3301
    • Evans, M.J.1    Cravatt, B.F.2
  • 5
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda, Y., Nagasu, T. & Chait, B.T. Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat. Biotechnol. 19, 379-382 (2001).
    • (2001) Nat. Biotechnol , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 6
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou, H., Watts, J.D. & Aebersold, R. A systematic approach to the analysis of protein phosphorylation. Nat. Biotechnol. 19, 375-378 (2001).
    • (2001) Nat. Biotechnol , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3
  • 10
    • 0347087452 scopus 로고    scopus 로고
    • Chemical strategies for activity-based proteomics
    • Speers, A.E. & Cravatt, B.F. Chemical strategies for activity-based proteomics. Chembiochem 5, 41-47 (2004).
    • (2004) Chembiochem , vol.5 , pp. 41-47
    • Speers, A.E.1    Cravatt, B.F.2
  • 11
    • 0033593013 scopus 로고    scopus 로고
    • Activity-based protein profiling: The serine hydrolases
    • Liu, Y., Patricelli, M.P. & Cravatt, B.F. Activity-based protein profiling: The serine hydrolases. Proc. Natl. Acad. Sci. USA 96 14694-14699 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14694-14699
    • Liu, Y.1    Patricelli, M.P.2    Cravatt, B.F.3
  • 12
    • 29444460784 scopus 로고    scopus 로고
    • Activity-based probes that target diverse cysteine protease families
    • Kato, D. et al. Activity-based probes that target diverse cysteine protease families. Nat. Chem. Biol. 1, 33-38 (2005).
    • (2005) Nat. Chem. Biol , vol.1 , pp. 33-38
    • Kato, D.1
  • 13
    • 33846248354 scopus 로고    scopus 로고
    • Functional interrogation of the kinome using nucleotide acyl phosphates
    • Patricelli, M.P. et al. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry 46, 350-358 (2007).
    • (2007) Biochemistry , vol.46 , pp. 350-358
    • Patricelli, M.P.1
  • 14
    • 0036022519 scopus 로고    scopus 로고
    • Proteomic profiling of mechanistically distinct enzyme classes using a common chemotype
    • Adam, G.C., Sorensen, E.J. & Cravatt, B.F. Proteomic profiling of mechanistically distinct enzyme classes using a common chemotype. Nat. Biotechnol. 20, 805-809 (2002).
    • (2002) Nat. Biotechnol , vol.20 , pp. 805-809
    • Adam, G.C.1    Sorensen, E.J.2    Cravatt, B.F.3
  • 15
    • 8844268481 scopus 로고    scopus 로고
    • Discovering disease-associated enzymes by proteome reactivity profiling
    • Barglow, K.T. & Cravatt, B.F. Discovering disease-associated enzymes by proteome reactivity profiling. Chem. Biol. 11, 1523-31 (2004).
    • (2004) Chem. Biol , vol.11 , pp. 1523-1531
    • Barglow, K.T.1    Cravatt, B.F.2
  • 16
    • 27144510184 scopus 로고    scopus 로고
    • Target discovery in small-molecule cell-based screens by in situ proteome reactivity profiling
    • Evans, M.J., Saghatelian, A., Sorensen, E.J. & Cravatt, B.F. Target discovery in small-molecule cell-based screens by in situ proteome reactivity profiling. Nat. Biotechnol. 23, 1303-1307 (2005).
    • (2005) Nat. Biotechnol , vol.23 , pp. 1303-1307
    • Evans, M.J.1    Saghatelian, A.2    Sorensen, E.J.3    Cravatt, B.F.4
  • 17
    • 0037462106 scopus 로고    scopus 로고
    • Speers, A.E., Adam, G.C. & Cravatt, B.F. Activity-based protein profiling in vivo using a copper(i)-catalyzed azide-alkyne [3 + 2] cycloaddition. J. Am. Chem. Soc. 125, 4686-4687 (2003).
    • Speers, A.E., Adam, G.C. & Cravatt, B.F. Activity-based protein profiling in vivo using a copper(i)-catalyzed azide-alkyne [3 + 2] cycloaddition. J. Am. Chem. Soc. 125, 4686-4687 (2003).
  • 18
    • 1942522084 scopus 로고    scopus 로고
    • Profiling enzyme activities in vivo using click chemistry methods
    • Speers, A.E. & Cravatt, B.F. Profiling enzyme activities in vivo using click chemistry methods. Chem. Biol. 11, 535-546 (2004).
    • (2004) Chem. Biol , vol.11 , pp. 535-546
    • Speers, A.E.1    Cravatt, B.F.2
  • 19
    • 0000096835 scopus 로고    scopus 로고
    • Click chemistry: Diverse chemical function from a few good reactions
    • Kolb, H.C., Finn, M.G. & Sharpless, K.B. Click chemistry: Diverse chemical function from a few good reactions. Angew. Chem. Int. Ed. Engl. 40, 2004-2021 (2001).
    • (2001) Angew. Chem. Int. Ed. Engl , vol.40 , pp. 2004-2021
    • Kolb, H.C.1    Finn, M.G.2    Sharpless, K.B.3
  • 20
    • 22244445882 scopus 로고    scopus 로고
    • A tandem orthogonal proteolysis strategy for high-content chemical proteomics
    • Speers, A.E. & Cravatt, B.F. A tandem orthogonal proteolysis strategy for high-content chemical proteomics. J. Am. Chem. Soc. 127, 10018-10019 (2005).
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 10018-10019
    • Speers, A.E.1    Cravatt, B.F.2
  • 21
    • 0024708229 scopus 로고
    • Molecular genetic analysis of a plant virus polyprotein cleavage site: A model
    • Dougherty, W.G., Cary, S.M. & Parks, T.D. Molecular genetic analysis of a plant virus polyprotein cleavage site: A model. Virology 171 356-364 (1989).
    • (1989) Virology , vol.171 , pp. 356-364
    • Dougherty, W.G.1    Cary, S.M.2    Parks, T.D.3
  • 22
    • 0035106351 scopus 로고    scopus 로고
    • 3rd large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M.P., Wolters, D. & Yates, J.R. 3rd large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19, 242-247 (2001).
    • (2001) Nat. Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 24
    • 17044407508 scopus 로고    scopus 로고
    • High-resolution functional proteomics by active-site peptide profiling
    • Okerberg, E.S. et al. High-resolution functional proteomics by active-site peptide profiling. Proc, Natl. Acad. Sci. USA 102 4996-5001 (2005).
    • (2005) Proc, Natl. Acad. Sci. USA , vol.102 , pp. 4996-5001
    • Okerberg, E.S.1
  • 25
    • 24044520992 scopus 로고    scopus 로고
    • A streamlined platform for high-content functional proteomics of primary human specimens
    • Jessani, N. et al. A streamlined platform for high-content functional proteomics of primary human specimens. Nat. Methods 2, 691-697 (2005).
    • (2005) Nat. Methods , vol.2 , pp. 691-697
    • Jessani, N.1
  • 26
    • 3242731195 scopus 로고    scopus 로고
    • Liu, H., Sadygov, R.G. & Yates, J.R. 3rd A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem. 76, 4193-4201 (2004).
    • Liu, H., Sadygov, R.G. & Yates, J.R. 3rd A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem. 76, 4193-4201 (2004).
  • 27
    • 27644543078 scopus 로고    scopus 로고
    • Comparison of label-free methods for quantifying human proteins by shotgun proteomics
    • Old, W.M. et al. Comparison of label-free methods for quantifying human proteins by shotgun proteomics. Mol. Cell. Proteomics 4 1487-1502 (2005).
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1487-1502
    • Old, W.M.1
  • 28
    • 14744299376 scopus 로고    scopus 로고
    • The role of electron capture dissociation in biomolecular analysis
    • Cooper, H.J., Hakansson, K. & Marshall, A.G. The role of electron capture dissociation in biomolecular analysis. Mass Spectrom. Rev. 24, 201-222 (2005).
    • (2005) Mass Spectrom. Rev , vol.24 , pp. 201-222
    • Cooper, H.J.1    Hakansson, K.2    Marshall, A.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.