메뉴 건너뛰기




Volumn 3, Issue 3, 2004, Pages 209-225

Synergistic computational and experimental proteomics approaches for more accurate detection of active serine hydrolases in yeast

Author keywords

[No Author keywords available]

Indexed keywords

DIHYDROFOLATE REDUCTASE; PROTEOME; SERINE DEHYDRATASE; TUMOR SUPPRESSOR PROTEIN;

EID: 2642574128     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M300082-MCP200     Document Type: Review
Times cited : (46)

References (69)
  • 1
    • 0037370476 scopus 로고    scopus 로고
    • The genetics and genomics of cancer
    • Balmain, A., Gray, J., and Ponder, B. (2003) The genetics and genomics of cancer. Nat. Genet. 33, (suppl.) 238-244
    • (2003) Nat. Genet. , vol.33 , Issue.SUPPL. , pp. 238-244
    • Balmain, A.1    Gray, J.2    Ponder, B.3
  • 3
    • 0038404847 scopus 로고    scopus 로고
    • Gene expression profiling detects gene amplification and differentiates tumor types in breast cancer
    • Dressman, M. A., Baras, A., Malinowski, R., Alvis, L. B., Kwon, I., Walz, T. M., and Polymeropoulos, M. H. (2003) Gene expression profiling detects gene amplification and differentiates tumor types in breast cancer. Cancer Res. 63, 2194-2199
    • (2003) Cancer Res. , vol.63 , pp. 2194-2199
    • Dressman, M.A.1    Baras, A.2    Malinowski, R.3    Alvis, L.B.4    Kwon, I.5    Walz, T.M.6    Polymeropoulos, M.H.7
  • 5
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi, S. P., Rochon, Y., Franza, B. R., and Aebersold, R. (1999) Correlation between protein and mRNA abundance in yeast. Mol. Cell Biol. 19, 1720-1730
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 8
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., Wolters, D., and Yates, J. R., 3rd (2001) Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19, 242-247
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 9
    • 0036535357 scopus 로고    scopus 로고
    • Analysis of quantitative proteomic data generated via multi-dimensional protein identification technology
    • Washburn, M. P., Ulaszek, R., Deciu, C., Schieltz, D. M., and Yates, J. R., 3rd (2002) Analysis of quantitative proteomic data generated via multi-dimensional protein identification technology. Anal. Chem. 74, 1650-1657
    • (2002) Anal. Chem. , vol.74 , pp. 1650-1657
    • Washburn, M.P.1    Ulaszek, R.2    Deciu, C.3    Schieltz, D.M.4    Yates III, J.R.5
  • 10
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • Peng, J., Elias, J. E., Thoreen, C. C., Licklider, L. J., and Gygi, S. P. (2003) Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome. J. Proteome Res. 2, 43-50
    • (2003) J. Proteome Res. , vol.2 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 13
    • 0035910063 scopus 로고    scopus 로고
    • Combining multiple structure and sequence alignments to improve sequence detection and alignment: Application to the SH2 domains of Janus kinases
    • Al-Lazikani, B., Sheinerman, F. B., and Honig, B. (2001) Combining multiple structure and sequence alignments to improve sequence detection and alignment: application to the SH2 domains of Janus kinases. Proc. Natl. Acad. Sci. U. S. A. 98, 14796-14801
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 14796-14801
    • Al-Lazikani, B.1    Sheinerman, F.B.2    Honig, B.3
  • 14
    • 0036463587 scopus 로고    scopus 로고
    • Getting more from less: Algorithms for rapid protein identification with multiple short peptide sequences
    • Mackey, A. J., Haystead, T. A., and Pearson, W. R. (2002) Getting more from less: algorithms for rapid protein identification with multiple short peptide sequences. Mol. Cell. Proteomics. 1, 139-147
    • (2002) Mol. Cell. Proteomics. , vol.1 , pp. 139-147
    • Mackey, A.J.1    Haystead, T.A.2    Pearson, W.R.3
  • 15
    • 0032483312 scopus 로고    scopus 로고
    • Method for prediction of protein function from sequence using the sequence-to-structure-to-function paradigm with application to glutaredoxins/thioredoxins and T1 ribonucleases
    • Fetrow, J. S., and Skolnick, J. (1998) Method for prediction of protein function from sequence using the sequence-to-structure-to-function paradigm with application to glutaredoxins/thioredoxins and T1 ribonucleases. J. Mol. Biol. 281, 949-968
    • (1998) J. Mol. Biol. , vol.281 , pp. 949-968
    • Fetrow, J.S.1    Skolnick, J.2
  • 16
    • 0042674397 scopus 로고    scopus 로고
    • Using a neural network and spatial clustering to predict the location of active sites in enzymes
    • Gutteridge, A., Bartlett, G. J., and Thornton, J. M. (2003) Using a neural network and spatial clustering to predict the location of active sites in enzymes. J. Mol. Biol. 330, 719-734
    • (2003) J. Mol. Biol. , vol.330 , pp. 719-734
    • Gutteridge, A.1    Bartlett, G.J.2    Thornton, J.M.3
  • 17
    • 0037424601 scopus 로고    scopus 로고
    • A model for statistical significance of local similarities in structure
    • Stark, A., Sunyaev, S., and Russell, R. B. (2003) A model for statistical significance of local similarities in structure. J. Mol. Biol. 326, 1307-1316
    • (2003) J. Mol. Biol. , vol.326 , pp. 1307-1316
    • Stark, A.1    Sunyaev, S.2    Russell, R.B.3
  • 19
    • 0035469599 scopus 로고    scopus 로고
    • Direct visualization of serine hydrolase activities in complex proteomes using fluorescent active site-directed probes
    • Patricelli, M. P., Giang, D. K., Stamp, L. M., and Burbaum, J. J. (2001) Direct visualization of serine hydrolase activities in complex proteomes using fluorescent active site-directed probes. Proteomics 1, 1067-1071
    • (2001) Proteomics , vol.1 , pp. 1067-1071
    • Patricelli, M.P.1    Giang, D.K.2    Stamp, L.M.3    Burbaum, J.J.4
  • 20
    • 0035799319 scopus 로고    scopus 로고
    • Profiling serine hydrolase activities in complex proteomes
    • Kidd, D., Liu, Y., and Cravatt, B. F. (2001) Profiling serine hydrolase activities in complex proteomes. Biochemistry 40, 4005-4015
    • (2001) Biochemistry , vol.40 , pp. 4005-4015
    • Kidd, D.1    Liu, Y.2    Cravatt, B.F.3
  • 21
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., and Aebersold, R. (1999) Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17, 994-999
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 23
    • 0038699591 scopus 로고    scopus 로고
    • High-throughput classification of yeast mutants for functional genomics using metabolic footprinting
    • Allen, J., Davey, H. M., Broadhurst, D., Heald, J. K., Rowland, J. J., Oliver, S. G., and Kell, D. B. (2003) High-throughput classification of yeast mutants for functional genomics using metabolic footprinting. Nat. Biotechnol. 21, 692-696
    • (2003) Nat. Biotechnol. , vol.21 , pp. 692-696
    • Allen, J.1    Davey, H.M.2    Broadhurst, D.3    Heald, J.K.4    Rowland, J.J.5    Oliver, S.G.6    Kell, D.B.7
  • 25
    • 0035918511 scopus 로고    scopus 로고
    • Characterization and manipulation of the acyl chain selectivity of fatty acid amide hydrolase
    • Patricelli, M. P., and Cravatt, B. F. (2001) Characterization and manipulation of the acyl chain selectivity of fatty acid amide hydrolase. Biochemistry 40, 6107-6115
    • (2001) Biochemistry , vol.40 , pp. 6107-6115
    • Patricelli, M.P.1    Cravatt, B.F.2
  • 26
    • 0035845487 scopus 로고    scopus 로고
    • An acquired and a native penicillin-binding protein cooperate in building the cell wall of drug-resistant staphylococci
    • Pinho, M. G., de Lencastre, H., and Tomasz, A. (2001) An acquired and a native penicillin-binding protein cooperate in building the cell wall of drug-resistant staphylococci. Proc. Natl. Acad. Sci. U. S. A. 98, 10886-10891
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 10886-10891
    • Pinho, M.G.1    de Lencastre, H.2    Tomasz, A.3
  • 27
    • 0031800635 scopus 로고    scopus 로고
    • The mammalian carboxylesterases: From molecules to functions
    • Satoh, T., and Hosokawa, M. (1998) The mammalian carboxylesterases: From molecules to functions. Annu. Rev. Pharmacol. Toxicol. 38, 257-288
    • (1998) Annu. Rev. Pharmacol. Toxicol. , vol.38 , pp. 257-288
    • Satoh, T.1    Hosokawa, M.2
  • 28
    • 0032168569 scopus 로고    scopus 로고
    • Catalytic triads and their relatives
    • Dodson, G., and Wlodawer, A. (1998) Catalytic triads and their relatives. Trends Biochem. Sci. 23, 347-352
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 347-352
    • Dodson, G.1    Wlodawer, A.2
  • 29
    • 0031033450 scopus 로고    scopus 로고
    • Catalytic hydroxyl/amine dyads within serine proteases
    • Paetzel, M., and Dalbey, R. E. (1997) Catalytic hydroxyl/amine dyads within serine proteases. Trends Biochem. Sci. 22, 28-31
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 28-31
    • Paetzel, M.1    Dalbey, R.E.2
  • 34
    • 0038817799 scopus 로고    scopus 로고
    • Multimeric threading-based prediction of protein-protein interactions on a genomic scale: Application to the Saccharomyces cerevisiae proteome
    • Lu, L., Arakaki, A. K., Lu, H., and Skolnick, J. (2003) Multimeric threading-based prediction of protein-protein interactions on a genomic scale: Application to the Saccharomyces cerevisiae proteome. Genome Res. 13, 1146-1154
    • (2003) Genome Res. , vol.13 , pp. 1146-1154
    • Lu, L.1    Arakaki, A.K.2    Lu, H.3    Skolnick, J.4
  • 35
    • 0038349948 scopus 로고    scopus 로고
    • Sequencing and comparison of yeast species to identify genes and regulatory elements
    • Kellis, M., Patterson, N., Endrizzi, M., Birren, B., and Lander, E. S. (2003) Sequencing and comparison of yeast species to identify genes and regulatory elements. Nature 423, 241-254
    • (2003) Nature , vol.423 , pp. 241-254
    • Kellis, M.1    Patterson, N.2    Endrizzi, M.3    Birren, B.4    Lander, E.S.5
  • 36
    • 0036789265 scopus 로고    scopus 로고
    • Analyzing yeast protein-protein interaction data obtained from different sources
    • Bader, G. D., and Hogue, C. W. (2002) Analyzing yeast protein-protein interaction data obtained from different sources. Nat. Biotechnol. 20, 991-997
    • (2002) Nat. Biotechnol. , vol.20 , pp. 991-997
    • Bader, G.D.1    Hogue, C.W.2
  • 38
    • 0028983813 scopus 로고
    • Improvement of an "In-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing
    • Hellman, U., Wernstedt, C., Gonez, J., and Heldin, C. H. (1995) Improvement of an "In-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing. Anal. Biochem. 224, 451-455
    • (1995) Anal. Biochem. , vol.224 , pp. 451-455
    • Hellman, U.1    Wernstedt, C.2    Gonez, J.3    Heldin, C.H.4
  • 39
    • 0031812223 scopus 로고    scopus 로고
    • Use of liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS) for routine identification of enzymatically digested proteins separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Stone, K. L., DeAngelis, R., LoPresti, M., Jones, J., Papov, V. V., and Williams, K. R. (1998) Use of liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS) for routine identification of enzymatically digested proteins separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Electrophoresis 19, 1046-1052
    • (1998) Electrophoresis , vol.19 , pp. 1046-1052
    • Stone, K.L.1    DeAngelis, R.2    LoPresti, M.3    Jones, J.4    Papov, V.V.5    Williams, K.R.6
  • 41
    • 0032475938 scopus 로고    scopus 로고
    • Functional analysis of the Escherichia coli genome using the sequence-to-structure-to-function paradigm: Identification of proteins exhibiting the glutaredoxin/thioredoxin disulfide oxidoreductase activity
    • Fetrow, J. S., Godzik, A., and Skolnick, J. (1998) Functional analysis of the Escherichia coli genome using the sequence-to-structure-to-function paradigm: Identification of proteins exhibiting the glutaredoxin/thioredoxin disulfide oxidoreductase activity. J. Mol. Biol. 282, 703-711
    • (1998) J. Mol. Biol. , vol.282 , pp. 703-711
    • Fetrow, J.S.1    Godzik, A.2    Skolnick, J.3
  • 42
    • 0032852375 scopus 로고    scopus 로고
    • Three-dimensional structures of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis
    • Zuegg, J., Gruber, K., Gugganig, M., Wagner, U. G., and Kratky, C. (1999) Three-dimensional structures of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis. Protein Sci. 8, 1990-2000
    • (1999) Protein Sci. , vol.8 , pp. 1990-2000
    • Zuegg, J.1    Gruber, K.2    Gugganig, M.3    Wagner, U.G.4    Kratky, C.5
  • 43
    • 0032847750 scopus 로고    scopus 로고
    • Atomic resolution crystal structure of hydroxynitrile lyase from Hevea brasiliensis
    • Gruber, K., Gugganig, M., Wagner, U. G., and Kratky, C. (1999) Atomic resolution crystal structure of hydroxynitrile lyase from Hevea brasiliensis. Biol. Chem. 380, 993-1000
    • (1999) Biol. Chem. , vol.380 , pp. 993-1000
    • Gruber, K.1    Gugganig, M.2    Wagner, U.G.3    Kratky, C.4
  • 44
    • 0035866002 scopus 로고    scopus 로고
    • Defrosting the frozen approximation: PROSPECTOR - A new approach to threading
    • Skolnick, J., and Kihara, D. (2001) Defrosting the frozen approximation: PROSPECTOR - A new approach to threading. Proteins 42, 319-331
    • (2001) Proteins , vol.42 , pp. 319-331
    • Skolnick, J.1    Kihara, D.2
  • 46
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 51
    • 0030925920 scopus 로고    scopus 로고
    • Pfam: A comprehensive database of protein domain families based on seed alignments
    • Sonnhammer, E. L., Eddy, S. R., and Durbin, R. (1997) Pfam: A comprehensive database of protein domain families based on seed alignments. Proteins Struct. Funct. Gen. 28, 405-420
    • (1997) Proteins Struct. Funct. Gen. , vol.28 , pp. 405-420
    • Sonnhammer, E.L.1    Eddy, S.R.2    Durbin, R.3
  • 52
    • 0030013081 scopus 로고    scopus 로고
    • Blocks database and its applications
    • Henikoff, J. G., and Henikoff, S. (1996) Blocks database and its applications. Methods Enzymol. 266, 88-105
    • (1996) Methods Enzymol. , vol.266 , pp. 88-105
    • Henikoff, J.G.1    Henikoff, S.2
  • 56
    • 0032411227 scopus 로고    scopus 로고
    • Functional analysis of the Escherichia coli genome for members of the alpha/beta hydrolase family
    • Zhang, L., Godzik, A., Skolnick, J., and Fetrow, J. S. (1998) Functional analysis of the Escherichia coli genome for members of the alpha/beta hydrolase family. Fold Des. 3, 535-548
    • (1998) Fold Des. , vol.3 , pp. 535-548
    • Zhang, L.1    Godzik, A.2    Skolnick, J.3    Fetrow, J.S.4
  • 57
    • 0032843737 scopus 로고    scopus 로고
    • Structure-based functional motif identifies a potential disulfide oxidoreductase active site in the serine/threonine protein phosphatase-1 subfamily
    • Fetrow, J. S., Siew, N., and Skolnick, J. (1999) Structure-based functional motif identifies a potential disulfide oxidoreductase active site in the serine/threonine protein phosphatase-1 subfamily. FASEB J. 13, 1866-1874
    • (1999) FASEB J. , vol.13 , pp. 1866-1874
    • Fetrow, J.S.1    Siew, N.2    Skolnick, J.3
  • 58
    • 0031866670 scopus 로고    scopus 로고
    • aCHEdb: The database system for ESTHER, the alpha/beta fold family of proteins and the Cholinesterase gene server
    • Cousin, X., Hotelier, T., Giles, K., Toutant, J. P., and Chatonnet, A. (1998) aCHEdb: The database system for ESTHER, the alpha/beta fold family of proteins and the Cholinesterase gene server. Nucleic Acids Res. 26, 226-228
    • (1998) Nucleic Acids Res. , vol.26 , pp. 226-228
    • Cousin, X.1    Hotelier, T.2    Giles, K.3    Toutant, J.P.4    Chatonnet, A.5
  • 59
    • 0037397491 scopus 로고    scopus 로고
    • Functional profiling of the proteome with affinity labels
    • Campbell, D. A., and Szardenings, A. K. (2003) Functional profiling of the proteome with affinity labels. Curr. Opin. Chem. Biol. 7, 296-303
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 296-303
    • Campbell, D.A.1    Szardenings, A.K.2
  • 60
    • 0037306722 scopus 로고    scopus 로고
    • Activity-based proteomics: Enzyme chemistry redux
    • Kozarich, J. W. (2003) Activity-based proteomics: Enzyme chemistry redux. Curr. Opin. Chem. Biol. 7, 78-83
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 78-83
    • Kozarich, J.W.1
  • 61
    • 0033553570 scopus 로고    scopus 로고
    • A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A
    • Ogris, E., Du, X., Nelson, K. C., Mak, E. K., Yu, X. X., Lane, W. S., and Pallas, D. C. (1999) A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A. J. Biol. Chem. 274, 14382-14391
    • (1999) J. Biol. Chem. , vol.274 , pp. 14382-14391
    • Ogris, E.1    Du, X.2    Nelson, K.C.3    Mak, E.K.4    Yu, X.X.5    Lane, W.S.6    Pallas, D.C.7
  • 62
    • 0028914607 scopus 로고
    • Substrate and product binding sites of yeast fatty acid synthase. Stoichiometry and binding kinetics of wild-type and in vitro mutated enzymes
    • Schuster, H., Rautenstrauss, B., Mittag, M., Stratmann, D., and Schweizer, E. (1995) Substrate and product binding sites of yeast fatty acid synthase. Stoichiometry and binding kinetics of wild-type and in vitro mutated enzymes. Eur. J. Biochem. 228, 417-424
    • (1995) Eur. J. Biochem. , vol.228 , pp. 417-424
    • Schuster, H.1    Rautenstrauss, B.2    Mittag, M.3    Stratmann, D.4    Schweizer, E.5
  • 63
    • 0024239166 scopus 로고
    • Primary structure of the multifunctional alpha subunit protein of yeast fatty acid synthase derived from FAS2 gene sequence
    • Mohamed, A. H., Chirala, S. S., Mody, N. H., Huang, W. Y., and Wakil, S. J. (1988) Primary structure of the multifunctional alpha subunit protein of yeast fatty acid synthase derived from FAS2 gene sequence. J. Biol. Chem. 263, 12315-12325
    • (1988) J. Biol. Chem. , vol.263 , pp. 12315-12325
    • Mohamed, A.H.1    Chirala, S.S.2    Mody, N.H.3    Huang, W.Y.4    Wakil, S.J.5
  • 64
    • 0028059576 scopus 로고
    • The isolation and characterization of the gene (dfr1) encoding dihydrofolate reductase (DHFR) in Schizosaccharomyces pombe
    • Bertani, L. E., and Campbell, J. L. (1994) The isolation and characterization of the gene (dfr1) encoding dihydrofolate reductase (DHFR) in Schizosaccharomyces pombe. Gene 147, 131-135
    • (1994) Gene , vol.147 , pp. 131-135
    • Bertani, L.E.1    Campbell, J.L.2
  • 68
    • 0036308741 scopus 로고    scopus 로고
    • Enzyme function low conserved than anticipated
    • Rost, B. (2002) Enzyme function low conserved than anticipated. J. Mol. Biol. 318, 595-608
    • (2002) J. Mol. Biol. , vol.318 , pp. 595-608
    • Rost, B.1
  • 69
    • 0034767547 scopus 로고    scopus 로고
    • Annotation transfer for genomics: Measuring functional divergence in multi-domain proteins
    • Hegyi, H., and Gerstein, M. (2001) Annotation transfer for genomics: Measuring functional divergence in multi-domain proteins. Genome Res. 11, 1632-1640
    • (2001) Genome Res. , vol.11 , pp. 1632-1640
    • Hegyi, H.1    Gerstein, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.