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Volumn 21, Issue 2, 2010, Pages 225-233

Mining the active proteome in plant science and biotechnology

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE PROTEINS; ACTIVE STATE; ACTIVITY-BASED; CYSTEINE PROTEASE; FUNCTIONAL INFORMATION; HIGH-CONTENT; IN-PLANTS; PLANT SCIENCE; PROOF OF CONCEPT; PROTEASOMES; PROTEIN ACTIVITY; PROTEIN DATA; PROTEIN PROFILING; PROTEOMES; SMALL MOLECULES;

EID: 77952672644     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.copbio.2010.02.003     Document Type: Review
Times cited : (31)

References (48)
  • 1
    • 0037306722 scopus 로고    scopus 로고
    • Activity-based proteomics: enzyme chemistry redux
    • Kozarich J.W. Activity-based proteomics: enzyme chemistry redux. Curr Opin Chem Biol 2003, 7:78-83.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 78-83
    • Kozarich, J.W.1
  • 3
    • 11144245547 scopus 로고    scopus 로고
    • Activity-based protein profiling: applications to biomarker discovery, in vivo imaging and drug discovery
    • Berger A.B., Vitorino P.M., Bogyo M. Activity-based protein profiling: applications to biomarker discovery, in vivo imaging and drug discovery. Am J Pharmacogenom 2004, 4:371-381.
    • (2004) Am J Pharmacogenom , vol.4 , pp. 371-381
    • Berger, A.B.1    Vitorino, P.M.2    Bogyo, M.3
  • 4
    • 1042287130 scopus 로고    scopus 로고
    • The development and application of methods for activity-based protein profiling
    • Jessani N., Cravatt B.F. The development and application of methods for activity-based protein profiling. Curr Opin Chem Biol 2004, 8:54-59.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 54-59
    • Jessani, N.1    Cravatt, B.F.2
  • 5
    • 0347087452 scopus 로고    scopus 로고
    • Chemical strategies for activity-based proteomics
    • Speers A.E., Cravatt B.F. Chemical strategies for activity-based proteomics. Chembiochem 2004, 5:41-47.
    • (2004) Chembiochem , vol.5 , pp. 41-47
    • Speers, A.E.1    Cravatt, B.F.2
  • 6
    • 13444309096 scopus 로고    scopus 로고
    • Chemical proteomics applied to target identification and drug discovery
    • Verhelst S.H., Bogyo M. Chemical proteomics applied to target identification and drug discovery. BioTechniques 2005, 38:175-177.
    • (2005) BioTechniques , vol.38 , pp. 175-177
    • Verhelst, S.H.1    Bogyo, M.2
  • 7
    • 33744553115 scopus 로고    scopus 로고
    • Chemical tools for activity-based proteomics
    • Hagenstein M.C., Sewald N. Chemical tools for activity-based proteomics. J Biotechnol 2006, 124:56-73.
    • (2006) J Biotechnol , vol.124 , pp. 56-73
    • Hagenstein, M.C.1    Sewald, N.2
  • 8
    • 50649112213 scopus 로고    scopus 로고
    • Activity-based protein profiling: from enzyme chemistry to proteomic chemistry
    • Cravatt B.F., Wright A.T., Kozarich J.W. Activity-based protein profiling: from enzyme chemistry to proteomic chemistry. Annu Rev Biochem 2008, 77:383-414.
    • (2008) Annu Rev Biochem , vol.77 , pp. 383-414
    • Cravatt, B.F.1    Wright, A.T.2    Kozarich, J.W.3
  • 9
    • 43149105407 scopus 로고    scopus 로고
    • Activity-based protein profiling: new developments and directions in functional proteomics
    • Uttamchandani M., Li J., Sun H., Yao S.Q. Activity-based protein profiling: new developments and directions in functional proteomics. Chembiochem 2008, 9:667-675.
    • (2008) Chembiochem , vol.9 , pp. 667-675
    • Uttamchandani, M.1    Li, J.2    Sun, H.3    Yao, S.Q.4
  • 10
    • 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 2006, 106:3279-3301.
    • (2006) Chem Rev , vol.106 , pp. 3279-3301
    • Evans, M.J.1    Cravatt, B.F.2
  • 11
    • 0033604499 scopus 로고    scopus 로고
    • Active site-directed protein regulation
    • Kobe B., Kemp B.E. Active site-directed protein regulation. Nature 1999, 402:373-376.
    • (1999) Nature , vol.402 , pp. 373-376
    • Kobe, B.1    Kemp, B.E.2
  • 12
    • 0033835372 scopus 로고    scopus 로고
    • Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools
    • Greenbaum D., Medzihradszky K.F., Burlingame A., Bogyo M. Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools. Chem Biol 2000, 7:569-581.
    • (2000) Chem Biol , vol.7 , pp. 569-581
    • Greenbaum, D.1    Medzihradszky, K.F.2    Burlingame, A.3    Bogyo, M.4
  • 16
    • 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 1999, 96:14696-14699.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14696-14699
    • Liu, Y.1    Patricelli, M.P.2    Cravatt, B.F.3
  • 17
    • 0035799319 scopus 로고    scopus 로고
    • Profiling serine hydrolase activities in complex proteomes
    • Kidd D., Liu Y., Cravatt B.F. Profiling serine hydrolase activities in complex proteomes. Biochemistry 2001, 40:4005-4015.
    • (2001) Biochemistry , vol.40 , pp. 4005-4015
    • Kidd, D.1    Liu, Y.2    Cravatt, B.F.3
  • 18
    • 34547129626 scopus 로고    scopus 로고
    • Role of a carboxylesterase in herbicide bioactivation in Arabidopsis thaliana
    • Gershater M.C., Cummins I., Edwards R. Role of a carboxylesterase in herbicide bioactivation in Arabidopsis thaliana. J Biol Chem 2007, 282:21460-21466.
    • (2007) J Biol Chem , vol.282 , pp. 21460-21466
    • Gershater, M.C.1    Cummins, I.2    Edwards, R.3
  • 19
    • 67449102606 scopus 로고    scopus 로고
    • Diversity of serine hydrolase activities of unchallenged and Botrytis-infected Arabidopsis thaliana
    • Kaschani F., Gu C., Niessen S., Hoover H., Cravatt B.F., van der Hoorn R.A. Diversity of serine hydrolase activities of unchallenged and Botrytis-infected Arabidopsis thaliana. Mol Cell Proteomics 2009, 8:1082-1093.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1082-1093
    • Kaschani, F.1    Gu, C.2    Niessen, S.3    Hoover, H.4    Cravatt, B.F.5    van der Hoorn, R.A.6
  • 20
    • 0033831542 scopus 로고    scopus 로고
    • Cloning of the SNG1 gene of Arabidopsis reveals a role for a serine carboxypeptidase-like protein as an acyltransferase in secondary metabolism
    • Lehfeldt C., Shirley A.M., Meyer K., Ruegger M.O., Cusumano J.C., Viitanen P.V., Strack D., Chapple C. Cloning of the SNG1 gene of Arabidopsis reveals a role for a serine carboxypeptidase-like protein as an acyltransferase in secondary metabolism. Plant Cell 2000, 12:1295-1306.
    • (2000) Plant Cell , vol.12 , pp. 1295-1306
    • Lehfeldt, C.1    Shirley, A.M.2    Meyer, K.3    Ruegger, M.O.4    Cusumano, J.C.5    Viitanen, P.V.6    Strack, D.7    Chapple, C.8
  • 22
    • 26944443700 scopus 로고    scopus 로고
    • Tripeptidyl peptidase II. An oligomeric protease complex from Arabidopsis
    • Book A.J., Yang P., Scalf M., Smith L.M., Vierstra R.D. Tripeptidyl peptidase II. An oligomeric protease complex from Arabidopsis. Plant Physiol 2005, 138:1046-1057.
    • (2005) Plant Physiol , vol.138 , pp. 1046-1057
    • Book, A.J.1    Yang, P.2    Scalf, M.3    Smith, L.M.4    Vierstra, R.D.5
  • 24
    • 0034819479 scopus 로고    scopus 로고
    • Extended peptide-based inhibitors efficiently target the proteasome and reveal overlapping specificities of the catalytic beta-subunits
    • Kessler B.M., Tortorella D., Altun M., Kisselev A.F., Fiebiger E., Hekking B.G., Ploegh H.L., Overkleeft H.S. Extended peptide-based inhibitors efficiently target the proteasome and reveal overlapping specificities of the catalytic beta-subunits. Chem Biol 2001, 8:913-929.
    • (2001) Chem Biol , vol.8 , pp. 913-929
    • Kessler, B.M.1    Tortorella, D.2    Altun, M.3    Kisselev, A.F.4    Fiebiger, E.5    Hekking, B.G.6    Ploegh, H.L.7    Overkleeft, H.S.8
  • 26
    • 77952669583 scopus 로고    scopus 로고
    • Proteasome activity profiling: a simple, robust and versatile method revealing subunit-selective inhibitors and cytoplasmic, defense-induced proteasome activities. Plant J. in press.
    • Gu C, Kolodziejek I, Misas-Villamil J, Shindo T, Colby T, Verdoes M, Richau KH, Schmidt J, Overkleeft HS, Van der Hoorn RA: Proteasome activity profiling: a simple, robust and versatile method revealing subunit-selective inhibitors and cytoplasmic, defense-induced proteasome activities. Plant J. in press.
    • Gu, C.1    Kolodziejek, I.2    Misas-Villamil, J.3    Shindo, T.4    Colby, T.5    Verdoes, M.6    Richau, KH.7    Schmidt, J.8    Overkleeft, HS.9    Van der Hoorn, RA.10
  • 27
    • 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 2004, 11:535-546.
    • (2004) Chem Biol , vol.11 , pp. 535-546
    • Speers, A.E.1    Cravatt, B.F.2
  • 28
    • 0031888036 scopus 로고    scopus 로고
    • High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrometry
    • Ducret A., Van Oostveen I., Eng J.K., Yates J.R., Aebersold R. High throughput protein characterization by automated reverse-phase chromatography/electrospray tandem mass spectrometry. Protein Sci 1998, 7:706-719.
    • (1998) Protein Sci , vol.7 , pp. 706-719
    • Ducret, A.1    Van Oostveen, I.2    Eng, J.K.3    Yates, J.R.4    Aebersold, R.5
  • 29
    • 20444455284 scopus 로고    scopus 로고
    • A vacuolar processing enzyme, deltaVPE, is involved in seed coat formation at the early stage of seed development
    • Nakaune S., Yamada K., Kondo M., Kato T., Tabata S., Nishimura M., Hara-Nishimura I. A vacuolar processing enzyme, deltaVPE, is involved in seed coat formation at the early stage of seed development. Plant Cell 2005, 17:876-887.
    • (2005) Plant Cell , vol.17 , pp. 876-887
    • Nakaune, S.1    Yamada, K.2    Kondo, M.3    Kato, T.4    Tabata, S.5    Nishimura, M.6    Hara-Nishimura, I.7
  • 31
    • 34247186321 scopus 로고    scopus 로고
    • Vacuolar cysteine proteases of wheat (Triticum aestivum L.) are common to leaf senescence induced by different factors
    • Martinez D.E., Bartoli C.G., Grbic V., Guiamet J.J. Vacuolar cysteine proteases of wheat (Triticum aestivum L.) are common to leaf senescence induced by different factors. J Exp Bot 2007, 58:1099-1107.
    • (2007) J Exp Bot , vol.58 , pp. 1099-1107
    • Martinez, D.E.1    Bartoli, C.G.2    Grbic, V.3    Guiamet, J.J.4
  • 32
    • 15544377824 scopus 로고    scopus 로고
    • Endosomal proteases facilitate the fusion of endosomes with vacuoles at the final step of the endocytotic pathway
    • Yamada K., Fuji K., Shimada T., Nishimura M., Hara-Nishimura I. Endosomal proteases facilitate the fusion of endosomes with vacuoles at the final step of the endocytotic pathway. Plant J 2005, 41:888-898.
    • (2005) Plant J , vol.41 , pp. 888-898
    • Yamada, K.1    Fuji, K.2    Shimada, T.3    Nishimura, M.4    Hara-Nishimura, I.5
  • 33
    • 33846379634 scopus 로고    scopus 로고
    • A Phytophthora infestans cystatin-like protein targets a novel tomato papain-like apoplastic protease
    • Tian M., Win J., Song J., van der Hoorn R., van der Knaap E., Kamoun S. A Phytophthora infestans cystatin-like protein targets a novel tomato papain-like apoplastic protease. Plant Physiol 2007, 143:364-377.
    • (2007) Plant Physiol , vol.143 , pp. 364-377
    • Tian, M.1    Win, J.2    Song, J.3    van der Hoorn, R.4    van der Knaap, E.5    Kamoun, S.6
  • 34
    • 0036777957 scopus 로고    scopus 로고
    • The importance of the proteasome and subsequent proteolytic steps in the generation of antigenic peptides
    • Goldberg A.L., Cascio P., Saric T., Rock K.L. The importance of the proteasome and subsequent proteolytic steps in the generation of antigenic peptides. Mol Immunol 2002, 39:147-164.
    • (2002) Mol Immunol , vol.39 , pp. 147-164
    • Goldberg, A.L.1    Cascio, P.2    Saric, T.3    Rock, K.L.4
  • 40
    • 0037177596 scopus 로고    scopus 로고
    • A tomato cysteine protease required for Cf-2-dependent disease resistance and suppression of autonecrosis
    • Kruger J., Thomas C.M., Golstein C., Dixon M.S., Smoker M., Tang S., Mulder L., Jones J.D. A tomato cysteine protease required for Cf-2-dependent disease resistance and suppression of autonecrosis. Science 2002, 296:744-747.
    • (2002) Science , vol.296 , pp. 744-747
    • Kruger, J.1    Thomas, C.M.2    Golstein, C.3    Dixon, M.S.4    Smoker, M.5    Tang, S.6    Mulder, L.7    Jones, J.D.8
  • 41
    • 34548628220 scopus 로고    scopus 로고
    • Chemical proteomics probes for profiling cytochrome P450 activities and drug interactions in vivo
    • Wright A.T., Cravatt B.F. Chemical proteomics probes for profiling cytochrome P450 activities and drug interactions in vivo. Chem Biol 2007, 14:1043-1051.
    • (2007) Chem Biol , vol.14 , pp. 1043-1051
    • Wright, A.T.1    Cravatt, B.F.2
  • 42
    • 77949533354 scopus 로고    scopus 로고
    • Boothroyd JC: 4-bromophenacyl bromide specifically inhibits rhoptry secretion during Toxoplasma invasion
    • Ravindran S., Lodoen M.B., Verhelst S.H.L., Bogyo M. Boothroyd JC: 4-bromophenacyl bromide specifically inhibits rhoptry secretion during Toxoplasma invasion. PlosOne 2009, 4:e8143.
    • (2009) PlosOne , vol.4
    • Ravindran, S.1    Lodoen, M.B.2    Verhelst, S.H.L.3    Bogyo, M.4
  • 44
    • 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 2005, 127:10018-10019.
    • (2005) J Am Chem Soc , vol.127 , pp. 10018-10019
    • Speers, A.E.1    Cravatt, B.F.2
  • 45
    • 34247273992 scopus 로고    scopus 로고
    • A mild chemically cleavable linker system for functional proteomic applications
    • Verhelst S.H., Fonovic M., Bogyo M. A mild chemically cleavable linker system for functional proteomic applications. Angew Chem Int Ed Engl 2007, 46:1284-1286.
    • (2007) Angew Chem Int Ed Engl , vol.46 , pp. 1284-1286
    • Verhelst, S.H.1    Fonovic, M.2    Bogyo, M.3
  • 46
    • 67651091698 scopus 로고    scopus 로고
    • Useful tools for biomolecule isolation, detection, and identification: acylhydrazone-based cleavable linkers
    • Park K.D., Liu R., Kohn H. Useful tools for biomolecule isolation, detection, and identification: acylhydrazone-based cleavable linkers. Chem Biol 2009, 16:763-772.
    • (2009) Chem Biol , vol.16 , pp. 763-772
    • Park, K.D.1    Liu, R.2    Kohn, H.3
  • 47
    • 33846807650 scopus 로고    scopus 로고
    • Tagging and detection strategies for activity-based proteomics
    • Sadaghiani A.M., Verhelst S.H., Bogyo M. Tagging and detection strategies for activity-based proteomics. Curr Opin Chem Biol 2007, 14:20-28.
    • (2007) Curr Opin Chem Biol , vol.14 , pp. 20-28
    • Sadaghiani, A.M.1    Verhelst, S.H.2    Bogyo, M.3


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