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Volumn 9, Issue 3, 2012, Pages 293-310

Chemistry-based functional proteomics for drug target deconvolution

Author keywords

ABPP; affinity chromatography; CCCP; chemistry based functional proteomics; target deconvolution

Indexed keywords

4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; BISINDOLYLMALEIMIDE; BOSUTINIB; DASATINIB; DIAZONAMIDE A; DRUG; GEFITINIB; IMATINIB; NILOTINIB; ORANTINIB; PATEAMINE A; PLADIENOLIDE; QUINOLINE DERIVATIVE; ROSCOVITINE; THALIDOMIDE; UNCLASSIFIED DRUG;

EID: 84864230853     PISSN: 14789450     EISSN: 17448387     Source Type: Journal    
DOI: 10.1586/epr.12.19     Document Type: Review
Times cited : (29)

References (151)
  • 1
    • 13844276627 scopus 로고    scopus 로고
    • Target-based drug discovery: Is something wrong
    • Sams-Dodd F. Target-based drug discovery: Is something wrong? Drug Discov. Today 10(2), 139-147 (2005).
    • (2005) Drug Discov. Today , vol.10 , Issue.2 , pp. 139-147
    • Sams-Dodd, F.1
  • 2
    • 70349971143 scopus 로고    scopus 로고
    • New screens and targets in antibacterial drug discovery
    • Falconer SB, Brown ED. New screens and targets in antibacterial drug discovery. Curr. Opin. Microbiol. 12(5), 497-504 (2009).
    • (2009) Curr. Opin. Microbiol. , vol.12 , Issue.5 , pp. 497-504
    • Falconer, S.B.1    Brown, E.D.2
  • 4
    • 67650708399 scopus 로고    scopus 로고
    • Small-molecule affinity chromatography coupled mass spectrometry for drug target deconvolution
    • Saxena C, Higgs RE, Zhen E, Hale JE. Small-molecule affinity chromatography coupled mass spectrometry for drug target deconvolution. Expert Opin. Drug Discov. 4(7), 701-714 (2009).
    • (2009) Expert Opin. Drug Discov. , vol.4 , Issue.7 , pp. 701-714
    • Saxena, C.1    Higgs, R.E.2    Zhen, E.3    Hale, J.E.4
  • 5
    • 79960983894 scopus 로고    scopus 로고
    • Drug target deconvolution by chemical proteomics
    • Raida M. Drug target deconvolution by chemical proteomics. Curr. Opin. Chem. Biol. 15(4), 570-575 (2011).
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , Issue.4 , pp. 570-575
    • Raida, M.1
  • 6
    • 7244245762 scopus 로고    scopus 로고
    • Finishing the euchromatic sequence of the human genome
    • International Human Genome Sequencing Consortium
    • International Human Genome Sequencing Consortium. Finishing the euchromatic sequence of the human genome. Nature 431(7011), 931-945 (2004).
    • (2004) Nature , vol.431 , Issue.7011 , pp. 931-945
  • 7
    • 0035575637 scopus 로고    scopus 로고
    • Drug discovery of the future: The implications of the human genome project
    • Reiss T. Drug discovery of the future: The implications of the human genome project. Trends Biotechnol. 19(12), 496-499 (2001).
    • (2001) Trends Biotechnol. , vol.19 , Issue.12 , pp. 496-499
    • Reiss, T.1
  • 8
    • 79951481957 scopus 로고    scopus 로고
    • Initial impact of the sequencing of the human genome
    • Lander ES. Initial impact of the sequencing of the human genome. Nature 470(7333), 187-197 (2011).
    • (2011) Nature , vol.470 , Issue.7333 , pp. 187-197
    • Lander, E.S.1
  • 9
    • 13444309096 scopus 로고    scopus 로고
    • Chemical proteomics applied to target identification and drug discovery
    • Verhelst SH, Bogyo M. Chemical proteomics applied to target identification and drug discovery. BioTechniques 38(2), 175-177 (2005).
    • (2005) BioTechniques , vol.38 , Issue.2 , pp. 175-177
    • Verhelst, S.H.1    Bogyo, M.2
  • 10
    • 0037307787 scopus 로고    scopus 로고
    • Chemical proteomics and its application to drug discovery
    • Jeffery DA, Bogyo M. Chemical proteomics and its application to drug discovery. Curr. Opin. Biotechnol. 14(1), 87-95 (2003).
    • (2003) Curr. Opin. Biotechnol. , vol.14 , Issue.1 , pp. 87-95
    • Jeffery, D.A.1    Bogyo, M.2
  • 11
    • 77955942384 scopus 로고    scopus 로고
    • Functional proteomics to dissect tyrosine kinase signalling pathways in cancer
    • Kolch W, Pitt A. Functional proteomics to dissect tyrosine kinase signalling pathways in cancer. Nat. Rev. Cancer 10(9), 618-629 (2010).
    • (2010) Nat. Rev. Cancer , vol.10 , Issue.9 , pp. 618-629
    • Kolch, W.1    Pitt, A.2
  • 12
    • 77953563022 scopus 로고    scopus 로고
    • Integrative oncoproteomics strategies for anticancer drug discovery
    • Liu R, Wang K, Yuan K, Wei Y, Huang C. Integrative oncoproteomics strategies for anticancer drug discovery. Expert Rev. Proteomics 7(3), 411-429 (2010).
    • (2010) Expert Rev. Proteomics , vol.7 , Issue.3 , pp. 411-429
    • Liu, R.1    Wang, K.2    Yuan, K.3    Wei, Y.4    Huang, C.5
  • 13
    • 66849115115 scopus 로고    scopus 로고
    • Advanced proteomic technologies for cancer biomarker discovery
    • Wong SC, Chan CM, Ma BB et al. Advanced proteomic technologies for cancer biomarker discovery. Expert Rev. Proteomics 6(2), 123-134 (2009).
    • (2009) Expert Rev. Proteomics , vol.6 , Issue.2 , pp. 123-134
    • Wong, S.C.1    Chan, C.M.2    Ma, B.B.3
  • 14
    • 66849113517 scopus 로고    scopus 로고
    • Quantitative proteomics and biomarker discovery in human cancer
    • Zhao Y, Lee WN, Xiao GG. Quantitative proteomics and biomarker discovery in human cancer. Expert Rev. Proteomics 6(2), 115-118 (2009).
    • (2009) Expert Rev. Proteomics , vol.6 , Issue.2 , pp. 115-118
    • Zhao, Y.1    Lee, W.N.2    Xiao, G.G.3
  • 15
    • 39649108016 scopus 로고    scopus 로고
    • Proteomics: Advances in biomarker discovery
    • Cowan ML, Vera J. Proteomics: Advances in biomarker discovery. Expert Rev. Proteomics 5(1), 21-23 (2008).
    • (2008) Expert Rev. Proteomics , vol.5 , Issue.1 , pp. 21-23
    • Cowan, M.L.1    Vera, J.2
  • 16
    • 0033604499 scopus 로고    scopus 로고
    • Active site-directed protein regulation
    • Kobe B, Kemp BE. Active site-directed protein regulation. Nature 402(6760), 373-376 (1999).
    • (1999) Nature , vol.402 , Issue.6760 , pp. 373-376
    • Kobe, B.1    Kemp, B.E.2
  • 17
    • 1042287130 scopus 로고    scopus 로고
    • The development and application of methods for activitybased protein profiling
    • Jessani N, Cravatt BF. The development and application of methods for activitybased protein profiling. Curr. Opin. Chem. Biol. 8(1), 54-59 (2004).
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , Issue.1 , pp. 54-59
    • Jessani, N.1    Cravatt, B.F.2
  • 18
    • 70350412263 scopus 로고    scopus 로고
    • Revealing promiscuous drug-target interactions by chemical proteomics
    • Bantscheff M, Scholten A, Heck AJ. Revealing promiscuous drug-target interactions by chemical proteomics. Drug Discov. Today 14(21-22), 1021-1029 (2009).
    • (2009) Drug Discov. Today , vol.14 , Issue.21-22 , pp. 1021-1029
    • Bantscheff, M.1    Scholten, A.2    Heck, A.J.3
  • 19
    • 69249136243 scopus 로고    scopus 로고
    • Target profiling of small molecules by chemical proteomics
    • Rix U, Superti-Furga G. Target profiling of small molecules by chemical proteomics. Nat. Chem. Biol. 5(9), 616-624 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , Issue.9 , pp. 616-624
    • Rix, U.1    Superti-Furga, G.2
  • 20
    • 77955761883 scopus 로고    scopus 로고
    • Application of chemistry-based functional proteomics to screening for novel drug targets
    • Yuan K, Lei Y, Huang C. Application of chemistry-based functional proteomics to screening for novel drug targets. Comb. Chem. High Throughput Screen. 13(5), 414-421 (2010).
    • (2010) Comb. Chem. High Throughput Screen. , vol.13 , Issue.5 , pp. 414-421
    • Yuan, K.1    Lei, Y.2    Huang, C.3
  • 21
    • 78650363876 scopus 로고    scopus 로고
    • Activitybased probes: Discovering new biology and new drug targets
    • Heal WP, Dang TH, Tate EW. Activitybased probes: Discovering new biology and new drug targets. Chem. Soc. Rev. 40(1), 246-257 (2011).
    • (2011) Chem. Soc. Rev. , vol.40 , Issue.1 , pp. 246-257
    • Heal, W.P.1    Dang, T.H.2    Tate, E.W.3
  • 22
    • 35848965006 scopus 로고    scopus 로고
    • Activity-based protein profiling for the functional annotation of enzymes
    • Barglow KT, Cravatt BF. Activity-based protein profiling for the functional annotation of enzymes. Nat. Methods 4(10), 822-827 (2007).
    • (2007) Nat. Methods , vol.4 , Issue.10 , pp. 822-827
    • Barglow, K.T.1    Cravatt, B.F.2
  • 23
    • 33846807650 scopus 로고    scopus 로고
    • Tagging and detection strategies for activity-based proteomics
    • Sadaghiani AM, Verhelst SH, Bogyo M. Tagging and detection strategies for activity-based proteomics. Curr. Opin. Chem. Biol. 11(1), 20-28 (2007).
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , Issue.1 , pp. 20-28
    • Sadaghiani, A.M.1    Verhelst, S.H.2    Bogyo, M.3
  • 24
    • 84857774303 scopus 로고    scopus 로고
    • ABPP methodology: Introduction and overview
    • Nodwell MB, Sieber SA. ABPP methodology: Introduction and overview. Top. Curr. Chem. 324, 1-41 (2012).
    • (2012) Top. Curr. Chem. , vol.324 , Issue.1-41
    • Nodwell, M.B.1    Sieber, S.A.2
  • 26
    • 68749108286 scopus 로고    scopus 로고
    • Small molecule microarray-facilitated screening of affinity-based probes (AfBPs) for gamma-secretase
    • Shi H, Liu K, Xu A, Yao SQ. Small molecule microarray-facilitated screening of affinity-based probes (AfBPs) for gamma-secretase. Chem. Commun. (Camb.) 33, 5030-5032 (2009).
    • (2009) Chem. Commun. (Camb.) , vol.33 , pp. 5030-5032
    • Shi, H.1    Liu, K.2    Xu, A.3    Yao, S.Q.4
  • 27
    • 70350023620 scopus 로고    scopus 로고
    • Functional profiling, identification, and inhibition of plasmepsins in intraerythrocytic malaria parasites
    • Liu K, Shi H, Xiao H et al. Functional profiling, identification, and inhibition of plasmepsins in intraerythrocytic malaria parasites. Angew. Chem. Int. Ed. Engl. 48(44), 8293-8297 (2009).
    • (2009) Angew. Chem. Int. Ed. Engl. , vol.48 , Issue.44 , pp. 8293-8297
    • Liu, K.1    Shi, H.2    Xiao, H.3
  • 28
    • 79952117567 scopus 로고    scopus 로고
    • A method for small molecule microarraybased screening for the rapid discovery of affinity-based probes
    • Shi H, Uttamchandani M, Yao SQ. A method for small molecule microarraybased screening for the rapid discovery of affinity-based probes. Methods Mol. Biol. 669, 57-68 (2010).
    • (2010) Methods Mol. Biol. , vol.669 , pp. 57-68
    • Shi, H.1    Uttamchandani, M.2    Yao, S.Q.3
  • 29
    • 84863116427 scopus 로고    scopus 로고
    • Cell-based proteome profiling of potential dasatinib targets by use of affinity-based probes
    • Shi H, Zhang CJ, Chen GY, Yao SQ. Cell-based proteome profiling of potential dasatinib targets by use of affinity-based probes. J. Am. Chem. Soc. 134(6), 3001-3014 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.6 , pp. 3001-3014
    • Shi, H.1    Zhang, C.J.2    Chen, G.Y.3    Yao, S.Q.4
  • 30
    • 0034621824 scopus 로고    scopus 로고
    • Photoactivated gamma-secretase inhibitors directed to the active site covalently label presenilin 1
    • Li YM, Xu M, Lai MT et al. Photoactivated gamma-secretase inhibitors directed to the active site covalently label presenilin 1. Nature 405(6787), 689-694 (2000).
    • (2000) Nature , vol.405 , Issue.6787 , pp. 689-694
    • Li, Y.M.1    Xu, M.2    Lai, M.T.3
  • 31
    • 33646462162 scopus 로고    scopus 로고
    • Proteomic profiling of metalloprotease activities with cocktails of active-site probes
    • Sieber SA, Niessen S, Hoover HS, Cravatt BF. Proteomic profiling of metalloprotease activities with cocktails of active-site probes. Nat. Chem. Biol. 2(5), 274-281 (2006).
    • (2006) Nat. Chem. Biol. , vol.2 , Issue.5 , pp. 274-281
    • Sieber, S.A.1    Niessen, S.2    Hoover, H.S.3    Cravatt, B.F.4
  • 32
    • 43149105407 scopus 로고    scopus 로고
    • Activity-based protein profiling: New developments and directions in functional proteomics
    • Uttamchandani M, Li J, Sun H, Yao SQ. Activity-based protein profiling: New developments and directions in functional proteomics. Chembiochem 9(5), 667-675 (2008).
    • (2008) Chembiochem , vol.9 , Issue.5 , pp. 667-675
    • Uttamchandani, M.1    Li, J.2    Sun, H.3    Yao, S.Q.4
  • 33
    • 43749107913 scopus 로고    scopus 로고
    • Application of activity-based probes to the study of enzymes involved in cancer progression
    • Paulick MG, Bogyo M. Application of activity-based probes to the study of enzymes involved in cancer progression. Curr. Opin. Genet. Dev. 18(1), 97-106 (2008).
    • (2008) Curr. Opin. Genet. Dev. , vol.18 , Issue.1 , pp. 97-106
    • Paulick, M.G.1    Bogyo, M.2
  • 34
    • 50649112213 scopus 로고    scopus 로고
    • Activity-based protein profiling: From enzyme chemistry to proteomic chemistry
    • Cravatt BF, Wright AT, Kozarich JW. Activity-based protein profiling: From enzyme chemistry to proteomic chemistry. Annu. Rev. Biochem. 77, 383-414 (2008).
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 383-414
    • Cravatt, B.F.1    Wright, A.T.2    Kozarich, J.W.3
  • 35
    • 0348109450 scopus 로고    scopus 로고
    • The growing impact of click chemistry on drug discovery
    • Kolb HC, Sharpless KB. The growing impact of click chemistry on drug discovery. Drug Discov. Today 8(24), 1128-1137 (2003).
    • (2003) Drug Discov. Today , vol.8 , Issue.24 , pp. 1128-1137
    • Kolb, H.C.1    Sharpless, K.B.2
  • 36
    • 0037462106 scopus 로고    scopus 로고
    • Activity-based protein profiling in vivo using a copper i)-catalyzed azide-alkyne [3 + 2] cycloaddition
    • Speers AE, Adam GC, Cravatt BF. Activity-based protein profiling in vivo using a copper(i)-catalyzed azide-alkyne [3 + 2] cycloaddition. J. Am. Chem. Soc. 125(16), 4686-4687 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.16 , pp. 4686-4687
    • Speers, A.E.1    Adam, G.C.2    Cravatt, B.F.3
  • 37
    • 1942522084 scopus 로고    scopus 로고
    • Profiling enzyme activities in vivo using click chemistry methods
    • Speers AE, Cravatt BF. Profiling enzyme activities in vivo using click chemistry methods. Chem. Biol. 11(4), 535-546 (2004).
    • (2004) Chem. Biol. , vol.11 , Issue.4 , pp. 535-546
    • Speers, A.E.1    Cravatt, B.F.2
  • 38
    • 0036678119 scopus 로고    scopus 로고
    • Enzyme activity profiles of the secreted and membrane proteome that depict cancer cell invasiveness
    • Jessani N, Liu Y, Humphrey M, Cravatt BF. Enzyme activity profiles of the secreted and membrane proteome that depict cancer cell invasiveness. Proc. Natl Acad. Sci. USA 99(16), 10335-10340 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , Issue.16 , pp. 10335-10340
    • Jessani, N.1    Liu, Y.2    Humphrey, M.3    Cravatt, B.F.4
  • 39
    • 33749671593 scopus 로고    scopus 로고
    • An enzyme that regulates ether lipid signaling pathways in cancer annotated by multidimensional profiling
    • Chiang KP, Niessen S, Saghatelian A, Cravatt BF. An enzyme that regulates ether lipid signaling pathways in cancer annotated by multidimensional profiling. Chem. Biol. 13(10), 1041-1050 (2006).
    • (2006) Chem. Biol. , vol.13 , Issue.10 , pp. 1041-1050
    • Chiang, K.P.1    Niessen, S.2    Saghatelian, A.3    Cravatt, B.F.4
  • 40
    • 0038361307 scopus 로고    scopus 로고
    • Discovering potent and selective reversible inhibitors of enzymes in complex proteomes
    • Leung D, Hardouin C, Boger DL, Cravatt BF. Discovering potent and selective reversible inhibitors of enzymes in complex proteomes. Nat. Biotechnol. 21(6), 687-691 (2003).
    • (2003) Nat. Biotechnol. , vol.21 , Issue.6 , pp. 687-691
    • Leung, D.1    Hardouin, C.2    Boger, D.L.3    Cravatt, B.F.4
  • 41
    • 79955396596 scopus 로고    scopus 로고
    • A potent and selective inhibitor of KIAA1363/AADACL1 that impairs prostate cancer pathogenesis
    • Chang JW, Nomura DK, Cravatt BF. A potent and selective inhibitor of KIAA1363/AADACL1 that impairs prostate cancer pathogenesis. Chem. Biol. 18(4), 476-484 (2011).
    • (2011) Chem. Biol. , vol.18 , Issue.4 , pp. 476-484
    • Chang, J.W.1    Nomura, D.K.2    Cravatt, B.F.3
  • 42
    • 79955388237 scopus 로고    scopus 로고
    • Activity-based profiling for drug discovery
    • Serwa R, Tate EW. Activity-based profiling for drug discovery. Chem. Biol. 18(4), 407-409 (2011).
    • (2011) Chem. Biol. , vol.18 , Issue.4 , pp. 407-409
    • Serwa, R.1    Tate, E.W.2
  • 43
    • 55049133250 scopus 로고    scopus 로고
    • Metadegradomics: Toward in vivo quantitative degradomics of proteolytic post-translational modifications of the cancer proteome
    • Doucet A, Butler GS, Rodríguez D, Prudova A, Overall CM. Metadegradomics: Toward in vivo quantitative degradomics of proteolytic post-translational modifications of the cancer proteome. Mol. Cell Proteomics 7(10), 1925-1951 (2008).
    • (2008) Mol. Cell Proteomics , vol.7 , Issue.10 , pp. 1925-1951
    • Doucet, A.1    Butler, G.S.2    Rodríguez, D.3    Prudova, A.4    Overall, C.M.5
  • 44
    • 0034651996 scopus 로고    scopus 로고
    • Unraveling the role of proteases in cancer
    • Koblinski JE, Ahram M, Sloane BF. Unraveling the role of proteases in cancer. Clin. Chim. Acta 291(2), 113-135 (2000).
    • (2000) Clin. Chim. Acta , vol.291 , Issue.2 , pp. 113-135
    • Koblinski, J.E.1    Ahram, M.2    Sloane, B.F.3
  • 45
    • 0034628448 scopus 로고    scopus 로고
    • Protease inhibitors: Current status and future prospects
    • Leung D, Abbenante G, Fairlie DP. Protease inhibitors: Current status and future prospects. J. Med. Chem. 43(3), 305-341 (2000).
    • (2000) J. Med. Chem. , vol.43 , Issue.3 , pp. 305-341
    • Leung, D.1    Abbenante, G.2    Fairlie, D.P.3
  • 46
    • 77955983759 scopus 로고    scopus 로고
    • Activity-based protein profiling for biochemical pathway discovery in cancer
    • Nomura DK, Dix MM, Cravatt BF. Activity-based protein profiling for biochemical pathway discovery in cancer. Nat. Rev. Cancer 10(9), 630-638 (2010).
    • (2010) Nat. Rev. Cancer , vol.10 , Issue.9 , pp. 630-638
    • Nomura, D.K.1    Dix, M.M.2    Cravatt, B.F.3
  • 47
    • 54349106665 scopus 로고    scopus 로고
    • Activity-based probes as a tool for functional proteomic analysis of proteases
    • Fonovic M, Bogyo M. Activity-based probes as a tool for functional proteomic analysis of proteases. Expert Rev. Proteomics 5(5), 721-730 (2008).
    • (2008) Expert Rev. Proteomics , vol.5 , Issue.5 , pp. 721-730
    • Fonovic, M.1    Bogyo, M.2
  • 48
    • 51349154761 scopus 로고    scopus 로고
    • Activity based chemical proteomics: Profiling proteases as drug targets
    • Heal WP, Wickramasinghe SR, Tate EW. Activity based chemical proteomics: Profiling proteases as drug targets. Curr. Drug Discov. Technol. 5(3), 200-212 (2008).
    • (2008) Curr. Drug Discov. Technol. , vol.5 , Issue.3 , pp. 200-212
    • Heal, W.P.1    Wickramasinghe, S.R.2    Tate, E.W.3
  • 49
    • 0033593013 scopus 로고    scopus 로고
    • Activitybased protein profiling: The serine hydrolases
    • Liu Y, Patricelli MP, Cravatt BF. Activitybased protein profiling: The serine hydrolases. Proc. Natl Acad. Sci. USA 96(26), 14694-14699 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , Issue.26 , pp. 14694-14699
    • Liu, Y.1    Patricelli, M.P.2    Cravatt, B.F.3
  • 50
    • 0035799319 scopus 로고    scopus 로고
    • Profiling serine hydrolase activities in complex proteomes
    • Kidd D, Liu Y, Cravatt BF. Profiling serine hydrolase activities in complex proteomes. Biochemistry 40(13), 4005-4015 (2001).
    • (2001) Biochemistry , vol.40 , Issue.13 , pp. 4005-4015
    • Kidd, D.1    Liu, Y.2    Cravatt, B.F.3
  • 51
    • 73149109062 scopus 로고    scopus 로고
    • Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis
    • Nomura DK, Long JZ, Niessen S, Hoover HS, Ng SW, Cravatt BF. Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis. Cell 140(1), 49-61 (2010).
    • (2010) Cell , vol.140 , Issue.1 , pp. 49-61
    • Nomura, D.K.1    Long, J.Z.2    Niessen, S.3    Hoover, H.S.4    Ng, S.W.5    Cravatt, B.F.6
  • 52
    • 76649109937 scopus 로고    scopus 로고
    • RBBP9: A tumor-associated serine hydrolase activity required for pancreatic neoplasia
    • Shields DJ, Niessen S, Murphy EA et al. RBBP9: A tumor-associated serine hydrolase activity required for pancreatic neoplasia. Proc. Natl Acad. Sci. USA 107(5), 2189-2194 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , Issue.5 , pp. 2189-2194
    • Shields, D.J.1    Niessen, S.2    Murphy, E.A.3
  • 53
    • 0033835372 scopus 로고    scopus 로고
    • Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools
    • Greenbaum D, Medzihradszky KF, Burlingame A, Bogyo M. Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools. Chem. Biol. 7(8), 569-581 (2000).
    • (2000) Chem. Biol. , vol.7 , Issue.8 , pp. 569-581
    • Greenbaum, D.1    Medzihradszky, K.F.2    Burlingame, A.3    Bogyo, M.4
  • 54
    • 2342603891 scopus 로고    scopus 로고
    • Cathepsin cysteine proteases are effectors of invasive growth and angiogenesis during multistage tumorigenesis
    • Joyce JA, Baruch A, Chehade K et al. Cathepsin cysteine proteases are effectors of invasive growth and angiogenesis during multistage tumorigenesis. Cancer Cell 5(5), 443-453 (2004).
    • (2004) Cancer Cell , vol.5 , Issue.5 , pp. 443-453
    • Joyce, J.A.1    Baruch, A.2    Chehade, K.3
  • 55
    • 29444460784 scopus 로고    scopus 로고
    • Activity-based probes that target diverse cysteine protease families
    • Kato D, Boatright KM, Berger AB et al. Activity-based probes that target diverse cysteine protease families. Nat. Chem. Biol. 1(1), 33-38 (2005).
    • (2005) Nat. Chem. Biol. , vol.1 , Issue.1 , pp. 33-38
    • Kato, D.1    Boatright, K.M.2    Berger, A.B.3
  • 56
    • 33746972404 scopus 로고    scopus 로고
    • Identification of early intermediates of caspase activation using selective inhibitors and activity-based probes
    • Berger AB, Witte MD, Denault JB et al. Identification of early intermediates of caspase activation using selective inhibitors and activity-based probes. Mol. Cell 23(4), 509-521 (2006).
    • (2006) Mol. Cell , vol.23 , Issue.4 , pp. 509-521
    • Berger, A.B.1    Witte, M.D.2    Denault, J.B.3
  • 57
    • 68349148319 scopus 로고    scopus 로고
    • Noninvasive optical imaging of apoptosis by caspase-targeted activity-based probes
    • Edgington LE, Berger AB, Blum G et al. Noninvasive optical imaging of apoptosis by caspase-targeted activity-based probes. Nat. Med. 15(8), 967-973 (2009).
    • (2009) Nat. Med. , vol.15 , Issue.8 , pp. 967-973
    • Edgington, L.E.1    Berger, A.B.2    Blum, G.3
  • 58
    • 13444275087 scopus 로고    scopus 로고
    • Chemistry-based functional proteomics: Mechanism-based activity-profiling tools for ubiquitin and ubiquitin-like specific proteases
    • Hemelaar J, Galardy PJ, Borodovsky A, Kessler BM, Ploegh HL, Ovaa H. Chemistry-based functional proteomics: Mechanism-based activity-profiling tools for ubiquitin and ubiquitin-like specific proteases. J. Proteome Res. 3(2), 268-276 (2004).
    • (2004) J. Proteome Res. , vol.3 , Issue.2 , pp. 268-276
    • Hemelaar, J.1    Galardy, P.J.2    Borodovsky, A.3    Kessler, B.M.4    Ploegh, H.L.5    Ovaa, H.6
  • 59
    • 33745606169 scopus 로고    scopus 로고
    • Putting proteomics on target: Activity-based profiling of ubiquitin and ubiquitin-like processing enzymes
    • Kessler BM. Putting proteomics on target: Activity-based profiling of ubiquitin and ubiquitin-like processing enzymes. Expert Rev. Proteomics 3(2), 213-221 (2006).
    • (2006) Expert Rev. Proteomics , vol.3 , Issue.2 , pp. 213-221
    • Kessler, B.M.1
  • 60
    • 38949108670 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes
    • Klionsky DJ, Abeliovich H, Agostinis P et al. Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes. Autophagy 4(2), 151-175 (2008).
    • (2008) Autophagy , vol.4 , Issue.2 , pp. 151-175
    • Klionsky, D.J.1    Abeliovich, H.2    Agostinis, P.3
  • 61
    • 0347695019 scopus 로고    scopus 로고
    • A single protease, Apg4B, is specific for the autophagy-related ubiquitinlike proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L
    • Hemelaar J, Lelyveld VS, Kessler BM, Ploegh HL. A single protease, Apg4B, is specific for the autophagy-related ubiquitinlike proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L. J. Biol. Chem. 278(51), 51841-51850 (2003).
    • (2003) J. Biol. Chem. , vol.278 , Issue.51 , pp. 51841-51850
    • Hemelaar, J.1    Lelyveld, V.S.2    Kessler, B.M.3    Ploegh, H.L.4
  • 62
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: Emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau JR, Lima CD. The SUMO pathway: Emerging mechanisms that shape specificity, conjugation and recognition. Nat. Rev. Mol. Cell Biol. 11(12), 861-871 (2010).
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , Issue.12 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 63
    • 10744227299 scopus 로고    scopus 로고
    • Specific and covalent targeting of conjugating and deconjugating enzymes of ubiquitin-like proteins
    • Hemelaar J, Borodovsky A, Kessler BM et al. Specific and covalent targeting of conjugating and deconjugating enzymes of ubiquitin-like proteins. Mol. Cell. Biol. 24(1), 84-95 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , Issue.1 , pp. 84-95
    • Hemelaar, J.1    Borodovsky, A.2    Kessler, B.M.3
  • 64
    • 0033974998 scopus 로고    scopus 로고
    • A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae
    • Makarova KS, Aravind L, Koonin EV. A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae. Trends Biochem. Sci. 25(2), 50-52 (2000).
    • (2000) Trends Biochem. Sci. , vol.25 , Issue.2 , pp. 50-52
    • Makarova, K.S.1    Aravind, L.2    Koonin, E.V.3
  • 65
    • 0036775490 scopus 로고    scopus 로고
    • Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family
    • Borodovsky A, Ovaa H, Kolli N et al. Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family. Chem. Biol. 9(10), 1149-1159 (2002).
    • (2002) Chem. Biol. , vol.9 , Issue.10 , pp. 1149-1159
    • Borodovsky, A.1    Ovaa, H.2    Kolli, N.3
  • 66
    • 23744434659 scopus 로고    scopus 로고
    • A deubiquitinating enzyme encoded by HSV-1 belongs to a family of cysteine proteases that is conserved across the family Herpesviridae
    • Kattenhorn LM, Korbel GA, Kessler BM, Spooner E, Ploegh HL. A deubiquitinating enzyme encoded by HSV-1 belongs to a family of cysteine proteases that is conserved across the family Herpesviridae. Mol. Cell 19(4), 547-557 (2005).
    • (2005) Mol. Cell , vol.19 , Issue.4 , pp. 547-557
    • Kattenhorn, L.M.1    Korbel, G.A.2    Kessler, B.M.3    Spooner, E.4    Ploegh, H.L.5
  • 67
    • 7744233875 scopus 로고    scopus 로고
    • Developing photoactive affinity probes for proteomic profiling: Hydroxamate-based probes for metalloproteases
    • Chan EW, Chattopadhaya S, Panicker RC, Huang X, Yao SQ. Developing photoactive affinity probes for proteomic profiling: Hydroxamate-based probes for metalloproteases. J. Am. Chem. Soc. 126(44), 14435-14446 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.44 , pp. 14435-14446
    • Chan, E.W.1    Chattopadhaya, S.2    Panicker, R.C.3    Huang, X.4    Yao, S.Q.5
  • 69
    • 33846649707 scopus 로고    scopus 로고
    • Activity-based probes for proteomic profiling of histone deacetylase complexes
    • Salisbury CM, Cravatt BF. Activity-based probes for proteomic profiling of histone deacetylase complexes. Proc. Natl Acad. Sci. USA 104(4), 1171-1176 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , Issue.4 , pp. 1171-1176
    • Salisbury, C.M.1    Cravatt, B.F.2
  • 70
    • 39549102872 scopus 로고    scopus 로고
    • Optimization of activity-based probes for proteomic profiling of histone deacetylase complexes
    • Salisbury CM, Cravatt BF. Optimization of activity-based probes for proteomic profiling of histone deacetylase complexes. J. Am. Chem. Soc. 130(7), 2184-2194 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , Issue.7 , pp. 2184-2194
    • Salisbury, C.M.1    Cravatt, B.F.2
  • 71
    • 79959476700 scopus 로고    scopus 로고
    • The evolution of protein kinase inhibitors from antagonists to agonists of cellular signaling
    • Dar AC, Shokat KM. The evolution of protein kinase inhibitors from antagonists to agonists of cellular signaling. Annu. Rev. Biochem. 80, 769-795 (2011).
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 769-795
    • Dar, A.C.1    Shokat, K.M.2
  • 72
    • 67949124765 scopus 로고    scopus 로고
    • Drug discovery and protein tyrosine phosphatases
    • Blaskovich MA. Drug discovery and protein tyrosine phosphatases. Curr. Med. Chem. 16(17), 2095-2176 (2009).
    • (2009) Curr. Med. Chem. , vol.16 , Issue.17 , pp. 2095-2176
    • Blaskovich, M.A.1
  • 75
    • 0020696906 scopus 로고
    • Affinity labeling of purine nucleotide sites in proteins
    • Colman RF. Affinity labeling of purine nucleotide sites in proteins. Annu. Rev. Biochem. 52, 67-91 (1983).
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 67-91
    • Colman, R.F.1
  • 76
    • 33846248354 scopus 로고    scopus 로고
    • Functional interrogation of the kinome using nucleotide acyl phosphates
    • Patricelli MP, Szardenings AK, Liyanage M et al. Functional interrogation of the kinome using nucleotide acyl phosphates. Biochemistry 46(2), 350-358 (2007).
    • (2007) Biochemistry , vol.46 , Issue.2 , pp. 350-358
    • Patricelli, M.P.1    Szardenings, A.K.2    Liyanage, M.3
  • 79
    • 3242759075 scopus 로고    scopus 로고
    • Design and synthesis of AX7574: A microcystin-derived, fluorescent probe for serine/threonine phosphatases
    • Shreder KR, Liu Y, Nomanhboy T et al. Design and synthesis of AX7574: A microcystin-derived, fluorescent probe for serine/threonine phosphatases. Bioconjug. Chem. 15(4), 790-798 (2004).
    • (2004) Bioconjug. Chem. , vol.15 , Issue.4 , pp. 790-798
    • Shreder, K.R.1    Liu, Y.2    Nomanhboy, T.3
  • 80
    • 70349128914 scopus 로고    scopus 로고
    • Profiling protein tyrosine phosphatase activity with mechanistic probes
    • Krishnamurthy D, Barrios AM. Profiling protein tyrosine phosphatase activity with mechanistic probes. Curr. Opin. Chem. Biol. 13(4), 375-381 (2009).
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , Issue.4 , pp. 375-381
    • Krishnamurthy, D.1    Barrios, A.M.2
  • 81
    • 66149144747 scopus 로고    scopus 로고
    • Activitybased protein profiling of protein tyrosine phosphatases
    • Walls C, Zhou B, Zhang ZY. Activitybased protein profiling of protein tyrosine phosphatases. Methods Mol. Biol. 519, 417-429 (2009).
    • (2009) Methods Mol. Biol. , vol.519 , pp. 417-429
    • Walls, C.1    Zhou, B.2    Zhang, Z.Y.3
  • 83
    • 15944395145 scopus 로고    scopus 로고
    • Insights into host responses against pathogens from transcriptional profiling
    • Jenner RG, Young RA. Insights into host responses against pathogens from transcriptional profiling. Nat. Rev. Microbiol. 3(4), 281-294 (2005).
    • (2005) Nat. Rev. Microbiol. , vol.3 , Issue.4 , pp. 281-294
    • Jenner, R.G.1    Young, R.A.2
  • 85
    • 23744458104 scopus 로고    scopus 로고
    • New insights into viral structure and virus-cell interactions through proteomics
    • Bernhard OK, Diefenbach RJ, Cunningham AL. New insights into viral structure and virus-cell interactions through proteomics. Expert Rev. Proteomics 2(4), 577-588 (2005).
    • (2005) Expert Rev. Proteomics , vol.2 , Issue.4 , pp. 577-588
    • Bernhard, O.K.1    Diefenbach, R.J.2    Cunningham, A.L.3
  • 87
    • 76149144007 scopus 로고    scopus 로고
    • Activity-based proteome profiling of hepatoma cells during hepatitis C virus replication using protease substrate probes
    • Blais DR, Brûlotte M, Qian Y, Bélanger S, Yao SQ, Pezacki JP. Activity-based proteome profiling of hepatoma cells during hepatitis C virus replication using protease substrate probes. J. Proteome Res. 9(2), 912-923 (2010).
    • (2010) J. Proteome Res. , vol.9 , Issue.2 , pp. 912-923
    • Blais, D.R.1    Brûlotte, M.2    Qian, Y.3    Bélanger, S.4    Yao, S.Q.5    Pezacki, J.P.6
  • 88
    • 77955495228 scopus 로고    scopus 로고
    • Activity-based protein profiling identifies a host enzyme, carboxylesterase 1, which is differentially active during hepatitis C virus replication
    • Blais DR, Lyn RK, Joyce MA et al. Activity-based protein profiling identifies a host enzyme, carboxylesterase 1, which is differentially active during hepatitis C virus replication. J. Biol. Chem. 285(33), 25602-25612 (2010).
    • (2010) J. Biol. Chem. , vol.285 , Issue.33 , pp. 25602-25612
    • Blais, D.R.1    Lyn, R.K.2    Joyce, M.A.3
  • 89
    • 77949496042 scopus 로고    scopus 로고
    • Activity-based protein profiling of the hepatitis C virus replication in Huh-7 hepatoma cells using a non-directed active site probe
    • Singaravelu R, Blais DR, McKay CS, Pezacki JP. Activity-based protein profiling of the hepatitis C virus replication in Huh-7 hepatoma cells using a non-directed active site probe. Proteome Sci. 8, 5 (2010).
    • (2010) Proteome Sci. , vol.8 , pp. 5
    • Singaravelu, R.1    Blais, D.R.2    McKay, C.S.3    Pezacki, J.P.4
  • 90
    • 27544498863 scopus 로고    scopus 로고
    • Design of a mechanism-based probe for neuraminidase to capture influenza viruses
    • Lu CP, Ren CT, Lai YN et al. Design of a mechanism-based probe for neuraminidase to capture influenza viruses. Angew. Chem. Int. Ed. Engl. 44(42), 6888-6892 (2005).
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , Issue.42 , pp. 6888-6892
    • Lu, C.P.1    Ren, C.T.2    Lai, Y.N.3
  • 91
    • 1442355024 scopus 로고    scopus 로고
    • Activity-based ubiquitin-specific protease (USP) profiling of virus-infected and malignant human cells
    • Ovaa H, Kessler BM, Rolén U, Galardy PJ, Ploegh HL, Masucci MG. Activity-based ubiquitin-specific protease (USP) profiling of virus-infected and malignant human cells. Proc. Natl Acad. Sci. USA 101(8), 2253-2258 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , Issue.8 , pp. 2253-2258
    • Ovaa, H.1    Kessler, B.M.2    Rolén, U.3    Galardy, P.J.4    Ploegh, H.L.5    Masucci, M.G.6
  • 92
    • 33645449857 scopus 로고    scopus 로고
    • Activity profiling of deubiquitinating enzymes in cervical carcinoma biopsies and cell lines
    • Rolén U, Kobzeva V, Gasparjan N et al. Activity profiling of deubiquitinating enzymes in cervical carcinoma biopsies and cell lines. Mol. Carcinog. 45(4), 260-269 (2006).
    • (2006) Mol. Carcinog. , vol.45 , Issue.4 , pp. 260-269
    • Rolén, U.1    Kobzeva, V.2    Gasparjan, N.3
  • 93
    • 84055191473 scopus 로고    scopus 로고
    • Proteomic profiling and potential cellular target identification of K11777, a clinical cysteine protease inhibitor, in Trypanosoma brucei
    • Yang PY, Wang M, He CY, Yao SQ. Proteomic profiling and potential cellular target identification of K11777, a clinical cysteine protease inhibitor, in Trypanosoma brucei. Chem. Commun. (Camb.) 48(6), 835-837 (2012).
    • (2012) Chem. Commun. (Camb.) , vol.48 , Issue.6 , pp. 835-837
    • Yang, P.Y.1    Wang, M.2    He, C.Y.3    Yao, S.Q.4
  • 94
    • 80053498767 scopus 로고    scopus 로고
    • Proteome profiling reveals potential cellular targets of staurosporine using a clickable cell-permeable probe
    • Shi H, Cheng X, Sze SK, Yao SQ. Proteome profiling reveals potential cellular targets of staurosporine using a clickable cell-permeable probe. Chem. Commun. (Camb.) 47(40), 11306-11308 (2011).
    • (2011) Chem. Commun. (Camb.) , vol.47 , Issue.40 , pp. 11306-11308
    • Shi, H.1    Cheng, X.2    Sze, S.K.3    Yao, S.Q.4
  • 95
    • 10744221240 scopus 로고    scopus 로고
    • Chemistry in living cells: Detection of active proteasomes by a two-step labeling strategy
    • Ovaa H, Van Swieten PF, Kessler BM et al. Chemistry in living cells: Detection of active proteasomes by a two-step labeling strategy. Angew. Chem. Int. Ed. Engl. 42(31), 3626-3629 (2003).
    • (2003) Angew. Chem. Int. Ed. Engl. , vol.42 , Issue.31 , pp. 3626-3629
    • Ovaa, H.1    Van Swieten, P.F.2    Kessler, B.M.3
  • 96
    • 34548628220 scopus 로고    scopus 로고
    • Chemical proteomic probes for profiling cytochrome p450 activities and drug interactions in vivo
    • Wright AT, Cravatt BF. Chemical proteomic probes for profiling cytochrome p450 activities and drug interactions in vivo. Chem. Biol. 14(9), 1043-1051 (2007).
    • (2007) Chem. Biol. , vol.14 , Issue.9 , pp. 1043-1051
    • Wright, A.T.1    Cravatt, B.F.2
  • 97
    • 27144510184 scopus 로고    scopus 로고
    • Target discovery in smallmolecule cell-based screens by in situ proteome reactivity profiling
    • Evans MJ, Saghatelian A, Sorensen EJ, Cravatt BF. Target discovery in smallmolecule cell-based screens by in situ proteome reactivity profiling. Nat. Biotechnol. 23(10), 1303-1307 (2005).
    • (2005) Nat. Biotechnol. , vol.23 , Issue.10 , pp. 1303-1307
    • Evans, M.J.1    Saghatelian, A.2    Sorensen, E.J.3    Cravatt, B.F.4
  • 98
    • 74949101629 scopus 로고    scopus 로고
    • Activity-based proteome profiling of potential cellular targets of Orlistat-an FDA-approved drug with anti-tumor activities
    • Yang PY, Liu K, Ngai MH, Lear MJ, Wenk MR, Yao SQ. Activity-based proteome profiling of potential cellular targets of Orlistat-an FDA-approved drug with anti-tumor activities. J. Am. Chem. Soc. 132(2), 656-666 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , Issue.2 , pp. 656-666
    • Yang, P.Y.1    Liu, K.2    Ngai, M.H.3    Lear, M.J.4    Wenk, M.R.5    Yao, S.Q.6
  • 99
    • 84855816228 scopus 로고    scopus 로고
    • Development and characterization of improved β-lactonebased anti-virulence drugs targeting ClpP
    • Zeiler E, Korotkov VS, Lorenz-Baath K, Böttcher T, Sieber SA. Development and characterization of improved β-lactonebased anti-virulence drugs targeting ClpP. Bioorg. Med. Chem. 20(2), 583-591 (2012).
    • (2012) Bioorg. Med. Chem. , vol.20 , Issue.2 , pp. 583-591
    • Zeiler, E.1    Korotkov, V.S.2    Lorenz-Baath, K.3    Böttcher, T.4    Sieber, S.A.5
  • 100
    • 55549091103 scopus 로고    scopus 로고
    • Beta-lactones as specific inhibitors of ClpP attenuate the production of extracellular virulence factors of Staphylococcus aureus
    • Böttcher T, Sieber SA. Beta-lactones as specific inhibitors of ClpP attenuate the production of extracellular virulence factors of Staphylococcus aureus. J. Am. Chem. Soc. 130(44), 14400-14401 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , Issue.44 , pp. 14400-14401
    • Böttcher, T.1    Sieber, S.A.2
  • 101
    • 53549118638 scopus 로고    scopus 로고
    • Beta-lactams as selective chemical probes for the in vivo labeling of bacterial enzymes involved in cell wall biosyn thesis, antibiotic resistance, and virulence
    • Staub I, Sieber SA. Beta-lactams as selective chemical probes for the in vivo labeling of bacterial enzymes involved in cell wall biosynthesis, antibiotic resistance, and virulence. J. Am. Chem. Soc. 130(40), 13400-13409 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , Issue.40 , pp. 13400-13409
    • Staub, I.1    Sieber, S.A.2
  • 102
    • 70149092317 scopus 로고    scopus 로고
    • Beta-lactam probes as selective chemical-proteomic tools for the identification and functional characterization of resistance associated enzymes in MRSA
    • Staub I, Sieber SA. Beta-lactam probes as selective chemical-proteomic tools for the identification and functional characterization of resistance associated enzymes in MRSA. J. Am. Chem. Soc. 131(17), 6271-6276 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , Issue.17 , pp. 6271-6276
    • Staub, I.1    Sieber, S.A.2
  • 103
    • 49949106029 scopus 로고    scopus 로고
    • Beta-lactone probes identify a papain-like peptide ligase in Arabidopsis thaliana
    • Wang Z, Gu C, Colby T et al. Beta-lactone probes identify a papain-like peptide ligase in Arabidopsis thaliana. Nat. Chem. Biol. 4(9), 557-563 (2008).
    • (2008) Nat. Chem. Biol. , vol.4 , Issue.9 , pp. 557-563
    • Wang, Z.1    Gu, C.2    Colby, T.3
  • 104
    • 34250746414 scopus 로고    scopus 로고
    • Tandem orthogonal proteolysis-activitybased protein profiling (TOP-ABPP) - A general method for mapping sites of probe modification in proteomes
    • Weerapana E, Speers AE, Cravatt BF. Tandem orthogonal proteolysis-activitybased protein profiling (TOP-ABPP) - A general method for mapping sites of probe modification in proteomes. Nat. Protoc. 2(6), 1414-1425 (2007).
    • (2007) Nat. Protoc. , vol.2 , Issue.6 , pp. 1414-1425
    • Weerapana, E.1    Speers, A.E.2    Cravatt, B.F.3
  • 105
    • 22244445882 scopus 로고    scopus 로고
    • A tandem orthogonal proteolysis strategy for high-content chemical proteomics
    • Speers AE, Cravatt BF. A tandem orthogonal proteolysis strategy for high-content chemical proteomics. J. Am. Chem. Soc. 127(28), 10018-10019 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.28 , pp. 10018-10019
    • Speers, A.E.1    Cravatt, B.F.2
  • 106
    • 11144245547 scopus 로고    scopus 로고
    • Activity-based protein profiling: Applications to biomarker discovery, in vivo imaging and drug discovery
    • Berger AB, Vitorino PM, Bogyo M. Activity-based protein profiling: Applications to biomarker discovery, in vivo imaging and drug discovery. Am. J. Pharmacogenomics 4(6), 371-381 (2004).
    • (2004) Am. J. Pharmacogenomics , vol.4 , Issue.6 , pp. 371-381
    • Berger, A.B.1    Vitorino, P.M.2    Bogyo, M.3
  • 107
    • 33644825565 scopus 로고    scopus 로고
    • Dynamic imaging of protease activity with fluorescently quenched activity-based probes
    • Blum G, Mullins SR, Keren K et al. Dynamic imaging of protease activity with fluorescently quenched activity-based probes. Nat. Chem. Biol. 1(4), 203-209 (2005).
    • (2005) Nat. Chem. Biol. , vol.1 , Issue.4 , pp. 203-209
    • Blum, G.1    Mullins, S.R.2    Keren, K.3
  • 108
    • 34548666006 scopus 로고    scopus 로고
    • Noninvasive optical imaging of cysteine protease activity using fluorescently quenched activity-based probes
    • Blum G, von Degenfeld G, Merchant MJ, Blau HM, Bogyo M. Noninvasive optical imaging of cysteine protease activity using fluorescently quenched activity-based probes. Nat. Chem. Biol. 3(10), 668-677 (2007).
    • (2007) Nat. Chem. Biol. , vol.3 , Issue.10 , pp. 668-677
    • Blum, G.1    Von Degenfeld, G.2    Merchant, M.J.3    Blau, H.M.4    Bogyo, M.5
  • 109
    • 79961138638 scopus 로고    scopus 로고
    • Multicolor, one- and two-photon imaging of enzymatic activities in live cells with fluorescently quenched activity-based probes (qABPs)
    • Hu M, Li L, Wu H et al. Multicolor, one- and two-photon imaging of enzymatic activities in live cells with fluorescently quenched activity-based probes (qABPs). J. Am. Chem. Soc. 133(31), 12009-12020 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , Issue.31 , pp. 12009-12020
    • Hu, M.1    Li, L.2    Wu, H.3
  • 110
    • 34748889841 scopus 로고    scopus 로고
    • Use of multidimensional separation protocols for the purification of trace components in complex biological samples for proteomics analysis
    • discussion 189
    • Nice EC, Rothacker J, Weinstock J, Lim L, Catimel B. Use of multidimensional separation protocols for the purification of trace components in complex biological samples for proteomics analysis. J. Chromatogr. A 1168(1-2), 190-210; discussion 189 (2007).
    • (2007) J. Chromatogr. , vol.A1168 , Issue.1-2 , pp. 190-210
    • Nice, E.C.1    Rothacker, J.2    Weinstock, J.3    Lim, L.4    Catimel, B.5
  • 111
    • 33847016153 scopus 로고    scopus 로고
    • Identification of intracellular targets of small molecular weight chemical compounds using affinity chromatography
    • Guiffant D, Tribouillard D, Gug F et al. Identification of intracellular targets of small molecular weight chemical compounds using affinity chromatography. Biotechnol. J. 2(1), 68-75 (2007).
    • (2007) Biotechnol. J. , vol.2 , Issue.1 , pp. 68-75
    • Guiffant, D.1    Tribouillard, D.2    Gug, F.3
  • 112
    • 84355162943 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of host cell lipid rafts modified by HBV infection
    • Xie N, Huang K, Zhang T et al. Comprehensive proteomic analysis of host cell lipid rafts modified by HBV infection. J. Proteomics 75(3), 725-739 (2012).
    • (2012) J. Proteomics , vol.75 , Issue.3 , pp. 725-739
    • Xie, N.1    Huang, K.2    Zhang, T.3
  • 113
    • 57249103219 scopus 로고    scopus 로고
    • Comparative plasma membrane-associated proteomics of immortalized human hepatocytes
    • Gou LT, Tong AP, Chen LJ et al. Comparative plasma membrane-associated proteomics of immortalized human hepatocytes. Biochemistry Mosc. 73(11), 1200-1206 (2008).
    • (2008) Biochemistry Mosc. , vol.73 , Issue.11 , pp. 1200-1206
    • Gou, L.T.1    Tong, A.P.2    Chen, L.J.3
  • 114
    • 40849130043 scopus 로고    scopus 로고
    • Proteomic methods for drug target discovery
    • Sleno L, Emili A. Proteomic methods for drug target discovery. Curr. Opin. Chem. Biol. 12(1), 46-54 (2008).
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , Issue.1 , pp. 46-54
    • Sleno, L.1    Emili, A.2
  • 115
    • 33646052014 scopus 로고    scopus 로고
    • A versatile method of identifying specific binding proteins on affinity resins
    • Yamamoto K, Yamazaki A, Takeuchi M, Tanaka A. A versatile method of identifying specific binding proteins on affinity resins. Anal. Biochem. 352(1), 15-23 (2006).
    • (2006) Anal. Biochem. , vol.352 , Issue.1 , pp. 15-23
    • Yamamoto, K.1    Yamazaki, A.2    Takeuchi, M.3    Tanaka, A.4
  • 116
    • 24744461426 scopus 로고    scopus 로고
    • Kinase selectivity profiling by inhibitor affinity chromatography
    • Valsasina B, Kalisz HM, Isacchi A. Kinase selectivity profiling by inhibitor affinity chromatography. Expert Rev. Proteomics 1(3), 303-315 (2004).
    • (2004) Expert Rev. Proteomics , vol.1 , Issue.3 , pp. 303-315
    • Valsasina, B.1    Kalisz, H.M.2    Isacchi, A.3
  • 117
    • 9144219693 scopus 로고    scopus 로고
    • An efficient proteomics method to identify the cellular targets of protein kinase inhibitors
    • Godl K, Wissing J, Kurtenbach A et al. An efficient proteomics method to identify the cellular targets of protein kinase inhibitors. Proc. Natl Acad. Sci. USA 100(26), 15434-15439 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , Issue.26 , pp. 15434-15439
    • Godl, K.1    Wissing, J.2    Kurtenbach, A.3
  • 118
    • 19944432043 scopus 로고    scopus 로고
    • Cellular targets of gefitinib
    • Brehmer D, Greff Z, Godl K et al. Cellular targets of gefitinib. Cancer Res. 65(2), 379-382 (2005).
    • (2005) Cancer Res. , vol.65 , Issue.2 , pp. 379-382
    • Brehmer, D.1    Greff, Z.2    Godl, K.3
  • 119
    • 23044510618 scopus 로고    scopus 로고
    • Proteomic characterization of the angiogenesis inhibitor SU6668 reveals multiple impacts on cellular kinase signaling
    • Godl K, Gruss OJ, Eickhoff J et al. Proteomic characterization of the angiogenesis inhibitor SU6668 reveals multiple impacts on cellular kinase signaling. Cancer Res. 65(15), 6919-6926 (2005).
    • (2005) Cancer Res. , vol.65 , Issue.15 , pp. 6919-6926
    • Godl, K.1    Gruss, O.J.2    Eickhoff, J.3
  • 120
    • 2442455834 scopus 로고    scopus 로고
    • Proteome-wide identification of cellular targets affected by bisindolylmaleimide-type protein kinase C inhibitors
    • Brehmer D, Godl K, Zech B, Wissing J, Daub H. Proteome-wide identification of cellular targets affected by bisindolylmaleimide-type protein kinase C inhibitors. Mol. Cell Proteomics 3(5), 490-500 (2004).
    • (2004) Mol. Cell Proteomics , vol.3 , Issue.5 , pp. 490-500
    • Brehmer, D.1    Godl, K.2    Zech, B.3    Wissing, J.4    Daub, H.5
  • 121
    • 24744437350 scopus 로고    scopus 로고
    • Roscovitine targets, protein kinases and pyridoxal kinase
    • Bach S, Knockaert M, Reinhardt J et al. Roscovitine targets, protein kinases and pyridoxal kinase. J. Biol. Chem. 280(35), 31208-31219 (2005).
    • (2005) J. Biol. Chem. , vol.280 , Issue.35 , pp. 31208-31219
    • Bach, S.1    Knockaert, M.2    Reinhardt, J.3
  • 122
    • 0033614446 scopus 로고    scopus 로고
    • Chronic myeloid leukemia
    • Sawyers CL. Chronic myeloid leukemia. N. Engl. J. Med. 340(17), 1330-1340 (1999).
    • (1999) N. Engl. J. Med. , vol.340 , Issue.17 , pp. 1330-1340
    • Sawyers, C.L.1
  • 123
    • 37049014938 scopus 로고    scopus 로고
    • Chemical proteomic profiles of the BCR-ABL inhibitors imatinib, nilotinib, and dasatinib reveal novel kinase and nonkinase targets
    • Rix U, Hantschel O, Dürnberger G et al. Chemical proteomic profiles of the BCR-ABL inhibitors imatinib, nilotinib, and dasatinib reveal novel kinase and nonkinase targets. Blood 110(12), 4055-4063 (2007).
    • (2007) Blood , vol.110 , Issue.12 , pp. 4055-4063
    • Rix, U.1    Hantschel, O.2    Dürnberger, G.3
  • 124
    • 34548097263 scopus 로고    scopus 로고
    • The Btk tyrosine kinase is a major target of the Bcr-Abl inhibitor dasatinib
    • Hantschel O, Rix U, Schmidt U et al. The Btk tyrosine kinase is a major target of the Bcr-Abl inhibitor dasatinib. Proc. Natl Acad. Sci. USA 104(33), 13283-13288 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , Issue.33 , pp. 13283-13288
    • Hantschel, O.1    Rix, U.2    Schmidt, U.3
  • 125
    • 62549166213 scopus 로고    scopus 로고
    • Global target profile of the kinase inhibitor bosutinib in primary chronic myeloid leukemia cells
    • Remsing Rix LL, Rix U, Colinge J et al. Global target profile of the kinase inhibitor bosutinib in primary chronic myeloid leukemia cells. Leukemia 23(3), 477-485 (2009).
    • (2009) Leukemia , vol.23 , Issue.3 , pp. 477-485
    • Remsing Rix, L.L.1    Rix, U.2    Colinge, J.3
  • 126
    • 78649790001 scopus 로고    scopus 로고
    • Chemical kinomics: A powerful strategy for target deconvolution
    • Kim DH, Sim T. Chemical kinomics: A powerful strategy for target deconvolution. BMB Rep. 43(11), 711-719 (2010).
    • (2010) BMB Rep. , vol.43 , Issue.11 , pp. 711-719
    • Kim, D.H.1    Sim, T.2
  • 127
    • 34948875686 scopus 로고    scopus 로고
    • Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors
    • Bantscheff M, Eberhard D, Abraham Y et al. Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors. Nat. Biotechnol. 25(9), 1035-1044 (2007).
    • (2007) Nat. Biotechnol. , vol.25 , Issue.9 , pp. 1035-1044
    • Bantscheff, M.1    Eberhard, D.2    Abraham, Y.3
  • 128
    • 83055168499 scopus 로고    scopus 로고
    • Quantitative chemical proteomics reveals new potential drug targets in head and neck cancer
    • Wu Z, Doondeea JB, Gholami AM et al. Quantitative chemical proteomics reveals new potential drug targets in head and neck cancer. Mol. Cell Proteomics 10(12), M111.011635 (2011).
    • (2011) Mol. Cell Proteomics , vol.10 , Issue.12
    • Wu, Z.1    Doondeea, J.B.2    Gholami, A.M.3
  • 129
    • 48349138726 scopus 로고    scopus 로고
    • Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle
    • Daub H, Olsen JV, Bairlein M et al. Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol. Cell 31(3), 438-448 (2008).
    • (2008) Mol. Cell , vol.31 , Issue.3 , pp. 438-448
    • Daub, H.1    Olsen, J.V.2    Bairlein, M.3
  • 130
    • 5644255983 scopus 로고    scopus 로고
    • Quality, not quantity: The role of natural products and chemical proteomics in modern drug discovery
    • Piggott AM, Karuso P. Quality, not quantity: The role of natural products and chemical proteomics in modern drug discovery. Comb. Chem. High Throughput Screen. 7(7), 607-630 (2004).
    • (2004) Comb. Chem. High Throughput Screen. , vol.7 , Issue.7 , pp. 607-630
    • Piggott, A.M.1    Karuso, P.2
  • 131
    • 34548104659 scopus 로고    scopus 로고
    • Splicing factor SF3b as a target of the antitumor natural product pladienolide
    • Kotake Y, Sagane K, Owa T et al. Splicing factor SF3b as a target of the antitumor natural product pladienolide. Nat. Chem. Biol. 3(9), 570-575 (2007).
    • (2007) Nat. Chem. Biol. , vol.3 , Issue.9 , pp. 570-575
    • Kotake, Y.1    Sagane, K.2    Owa, T.3
  • 132
    • 23044457401 scopus 로고    scopus 로고
    • Stimulation of mammalian translation initiation factor eIF4A activity by a small molecule inhibitor of eukaryotic translation
    • Bordeleau ME, Matthews J, Wojnar JM et al. Stimulation of mammalian translation initiation factor eIF4A activity by a small molecule inhibitor of eukaryotic translation. Proc. Natl Acad. Sci. USA 102(30), 10460-10465 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , Issue.30 , pp. 10460-10465
    • Bordeleau, M.E.1    Matthews, J.2    Wojnar, J.M.3
  • 133
    • 33847788820 scopus 로고    scopus 로고
    • Diazonamide toxins reveal an unexpected function for ornithine delta-amino transferase in mitotic cell division
    • Wang G, Shang L, Burgett AW, Harran PG, Wang X. Diazonamide toxins reveal an unexpected function for ornithine delta-amino transferase in mitotic cell division. Proc. Natl Acad. Sci. USA 104(7), 2068-2073 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , Issue.7 , pp. 2068-2073
    • Wang, G.1    Shang, L.2    Burgett, A.W.3    Harran, P.G.4    Wang, X.5
  • 134
    • 0036892305 scopus 로고    scopus 로고
    • Discovery of novel targets of quinoline drugs in the human purine binding proteome
    • Graves PR, Kwiek JJ, Fadden P et al. Discovery of novel targets of quinoline drugs in the human purine binding proteome. Mol. Pharmacol. 62(6), 1364-1372 (2002).
    • (2002) Mol. Pharmacol. , vol.62 , Issue.6 , pp. 1364-1372
    • Graves, P.R.1    Kwiek, J.J.2    Fadden, P.3
  • 135
    • 0002963496 scopus 로고    scopus 로고
    • Arsenic compounds as anticancer agents
    • Wang ZY. Arsenic compounds as anticancer agents. Cancer Chemother. Pharmacol. 48(Suppl. 1), S72-S76 (2001).
    • (2001) Cancer Chemother. Pharmacol. , vol.48 , Issue.SUPPL.1
    • Wang, Z.Y.1
  • 136
    • 77950826446 scopus 로고    scopus 로고
    • Arsenic trioxide controls the fate of the PMLRARalpha oncoprotein by directly binding PML
    • Zhang XW, Yan XJ, Zhou ZR et al. Arsenic trioxide controls the fate of the PMLRARalpha oncoprotein by directly binding PML. Science 328(5975), 240-243 (2010).
    • (2010) Science , vol.328 , Issue.5975 , pp. 240-243
    • Zhang, X.W.1    Yan, X.J.2    Zhou, Z.R.3
  • 137
    • 0035203218 scopus 로고    scopus 로고
    • Thalidomide: 40 years on
    • Diggle GE. Thalidomide: 40 years on. Int. J. Clin. Pract. 55(9), 627-631 (2001).
    • (2001) Int. J. Clin. Pract. , vol.55 , Issue.9 , pp. 627-631
    • Diggle, G.E.1
  • 138
    • 61349139994 scopus 로고    scopus 로고
    • Development and application of high-performance affinity beads: Toward chemical biology and drug discovery
    • Sakamoto S, Kabe Y, Hatakeyama M, Yamaguchi Y, Handa H. Development and application of high-performance affinity beads: Toward chemical biology and drug discovery. Chem. Rec. 9(1), 66-85 (2009).
    • (2009) Chem. Rec. , vol.9 , Issue.1 , pp. 66-85
    • Sakamoto, S.1    Kabe, Y.2    Hatakeyama, M.3    Yamaguchi, Y.4    Handa, H.5
  • 139
    • 77949350034 scopus 로고    scopus 로고
    • Identification of a primary target of thalidomide teratogenicity
    • Ito T, Ando H, Suzuki T et al. Identification of a primary target of thalidomide teratogenicity. Science 327(5971), 1345-1350 (2010).
    • (2010) Science , vol.327 , Issue.5971 , pp. 1345-1350
    • Ito, T.1    Ando, H.2    Suzuki, T.3
  • 140
    • 53049102175 scopus 로고    scopus 로고
    • An immuno-chemo-proteomics method for drug target deconvolution
    • Saxena C, Zhen E, Higgs RE, Hale JE. An immuno-chemo-proteomics method for drug target deconvolution. J. Proteome Res. 7(8), 3490-3497 (2008).
    • (2008) J. Proteome Res. , vol.7 , Issue.8 , pp. 3490-3497
    • Saxena, C.1    Zhen, E.2    Higgs, R.E.3    Hale, J.E.4
  • 141
    • 68549083829 scopus 로고    scopus 로고
    • Capture of drug targets from live cells using a multipurpose immuno-chemo-proteomics tool
    • Saxena C, Bonacci TM, Huss KL, Bloem LJ, Higgs RE, Hale JE. Capture of drug targets from live cells using a multipurpose immuno-chemo-proteomics tool. J. Proteome Res. 8(8), 3951-3957 (2009).
    • (2009) J. Proteome Res. , vol.8 , Issue.8 , pp. 3951-3957
    • Saxena, C.1    Bonacci, T.M.2    Huss, K.L.3    Bloem, L.J.4    Higgs, R.E.5    Hale, J.E.6
  • 142
    • 0037312648 scopus 로고    scopus 로고
    • Directed immobilization of peptide ligands to accessible pore sites by conjugation with a placeholder molecule
    • Hahn R, Berger E, Pflegerl K, Jungbauer A. Directed immobilization of peptide ligands to accessible pore sites by conjugation with a placeholder molecule. Anal. Chem. 75(3), 543-548 (2003).
    • (2003) Anal. Chem. , vol.75 , Issue.3 , pp. 543-548
    • Hahn, R.1    Berger, E.2    Pflegerl, K.3    Jungbauer, A.4
  • 143
    • 74849088596 scopus 로고    scopus 로고
    • Capture compound mass spectrometry sheds light on the molecular mechanisms of liver toxicity of two Parkinson drugs
    • Fischer JJ, Michaelis S, Schrey AK et al. Capture compound mass spectrometry sheds light on the molecular mechanisms of liver toxicity of two Parkinson drugs. Toxicol. Sci. 113(1), 243-253 (2010).
    • (2010) Toxicol. Sci. , vol.113 , Issue.1 , pp. 243-253
    • Fischer, J.J.1    Michaelis, S.2    Schrey, A.K.3
  • 144
    • 67449105851 scopus 로고    scopus 로고
    • Selectivity in enrichment of cAMPdependent protein kinase regulatory subunits type I and type II and their interactors using modified cAMP affinity resins
    • Aye TT, Mohammed S, Van den Toorn HW et al. Selectivity in enrichment of cAMPdependent protein kinase regulatory subunits type I and type II and their interactors using modified cAMP affinity resins. Mol. Cell Proteomics 8(5), 1016-1028 (2009).
    • (2009) Mol. Cell Proteomics , vol.8 , Issue.5 , pp. 1016-1028
    • Aye, T.T.1    Mohammed, S.2    Van Den Toorn, H.W.3
  • 145
    • 77649092461 scopus 로고    scopus 로고
    • Proteomic identification of binding partners for the brain metabolite lanthionine ketimine (LK) and documentation of LK effects on microglia and motoneuron cell cultures
    • Hensley K, Christov A, Kamat S et al. Proteomic identification of binding partners for the brain metabolite lanthionine ketimine (LK) and documentation of LK effects on microglia and motoneuron cell cultures. J. Neurosci. 30(8), 2979-2988 (2010).
    • (2010) J. Neurosci. , vol.30 , Issue.8 , pp. 2979-2988
    • Hensley, K.1    Christov, A.2    Kamat, S.3
  • 146
    • 59149084542 scopus 로고    scopus 로고
    • Targeted proteomic strategy for clinical biomarker discovery
    • Schiess R, Wollscheid B, Aebersold R. Targeted proteomic strategy for clinical biomarker discovery. Mol. Oncol. 3(1), 33-44 (2009).
    • (2009) Mol. Oncol. , vol.3 , Issue.1 , pp. 33-44
    • Schiess, R.1    Wollscheid, B.2    Aebersold, R.3
  • 147
    • 0031171961 scopus 로고    scopus 로고
    • Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin
    • Griffith EC, Su Z, Turk BE et al. Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin. Chem. Biol. 4(6), 461-471 (1997).
    • (1997) Chem. Biol. , vol.4 , Issue.6 , pp. 461-471
    • Griffith, E.C.1    Su, Z.2    Turk, B.E.3
  • 148
    • 33644845444 scopus 로고    scopus 로고
    • Mass spectrometry and isotopes: A century of research and discussion
    • Budzikiewicz H, Grigsby RD. Mass spectrometry and isotopes: A century of research and discussion. Mass Spectrom. Rev. 25(1), 146-157 (2006).
    • (2006) Mass Spectrom. Rev. , vol.25 , Issue.1 , pp. 146-157
    • Budzikiewicz, H.1    Grigsby, R.D.2
  • 150
    • 33846856907 scopus 로고    scopus 로고
    • Synthesis and characterization of 5'-p-fluorosulfonylbenzoyl-2' (or 3')-(biotinyl)adenosine as an activity-based probe for protein kinases
    • Ratcliffe SJ, Yi T, Khandekar SS. Synthesis and characterization of 5'-p-fluorosulfonylbenzoyl-2' (or 3')-(biotinyl)adenosine as an activity-based probe for protein kinases. J. Biomol. Screen. 12(1), 126-132 (2007).
    • (2007) J. Biomol. Screen. , vol.12 , Issue.1 , pp. 126-132
    • Ratcliffe, S.J.1    Yi, T.2    Khandekar, S.S.3
  • 151
    • 33845302336 scopus 로고    scopus 로고
    • Plasmodium falciparum chloroquine resistance marker protein (Pfcrmp) may be a chloroquine target protein in nucleus
    • Li GD. Plasmodium falciparum chloroquine resistance marker protein (Pfcrmp) may be a chloroquine target protein in nucleus. Med. Hypotheses 68(2), 332-334 (2007).
    • (2007) Med. Hypotheses , vol.68 , Issue.2 , pp. 332-334
    • Li, G.D.1


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