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Volumn 407, Issue 1, 2007, Pages 41-48

Profiling constitutive proteolytic events in vivo

Author keywords

Mass spectrometry; Methionine aminopeptidase (MetAP); Mitochondrial peptidase; N terminal labelling; Peptidase; Protease; Signal peptidase

Indexed keywords

ESCHERICHIA COLI; GENE ENCODING; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PROTEOLYSIS;

EID: 35148891761     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070775     Document Type: Article
Times cited : (141)

References (37)
  • 2
    • 0036302814 scopus 로고    scopus 로고
    • Protease degradomics: A new challenge for proteomics
    • Lopez-Otin, C. and Overall, C. M. (2002) Protease degradomics: a new challenge for proteomics. Nat. Rev. Mol. Cell Biol. 3, 509-519
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 509-519
    • Lopez-Otin, C.1    Overall, C.M.2
  • 3
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signaling by proteolysis
    • Salvesen, G. S. and Dixit, V. M. (1997) Caspases: intracellular signaling by proteolysis. Cell 91, 443-446
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 4
    • 33646576168 scopus 로고    scopus 로고
    • Degradomics: Systems biology of the protease web. Pleiotropic roles of MMPs in cancer
    • Overall, C. M. and Dean, R. A. (2006) Degradomics: systems biology of the protease web. Pleiotropic roles of MMPs in cancer. Cancer Metastasis Rev. 25, 69-75
    • (2006) Cancer Metastasis Rev , vol.25 , pp. 69-75
    • Overall, C.M.1    Dean, R.A.2
  • 6
    • 0028918852 scopus 로고
    • Rapid identification of highly active and selective substrates for stromelysin and matrilysin using bacteriophage peptide display libraries
    • Smith, M., Shi, L. and Navre, M. (1995) Rapid identification of highly active and selective substrates for stromelysin and matrilysin using bacteriophage peptide display libraries. J. Biol. Chem. 270, 6440-6449
    • (1995) J. Biol. Chem , vol.270 , pp. 6440-6449
    • Smith, M.1    Shi, L.2    Navre, M.3
  • 7
    • 0030849093 scopus 로고    scopus 로고
    • A combinatorial approach defines specificities of members of the caspase family and granzyme B: Functional relationships established for key mediators of apoptosis
    • Thornberry, N. A., Rano, T. A., Peterson, E. P., Rasper, D. M., Timkey, T., Garcia-Calvo, M., Houtzager, V. M., Nordstrom, P. A., Roy, S., Vaillancourt, J. P. et al. (1997) A combinatorial approach defines specificities of members of the caspase family and granzyme B: functional relationships established for key mediators of apoptosis. J. Biol. Chem. 272, 17907-17911
    • (1997) J. Biol. Chem , vol.272 , pp. 17907-17911
    • Thornberry, N.A.1    Rano, T.A.2    Peterson, E.P.3    Rasper, D.M.4    Timkey, T.5    Garcia-Calvo, M.6    Houtzager, V.M.7    Nordstrom, P.A.8    Roy, S.9    Vaillancourt, J.P.10
  • 8
    • 0034283578 scopus 로고    scopus 로고
    • Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8
    • Stennicke, H. R., Renatus, M., Meldal, M. and Salvesen, G. S. (2000) Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8. Biochem. J. 350, 563-568
    • (2000) Biochem. J , vol.350 , pp. 563-568
    • Stennicke, H.R.1    Renatus, M.2    Meldal, M.3    Salvesen, G.S.4
  • 10
    • 0034608931 scopus 로고    scopus 로고
    • Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries
    • Harris, J. L., Backes, B. J., Leonetti, F., Mahrus, S., Ellman, J. A. and Craik, C. S. (2000) Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries. Proc. Natl. Acad. Sci. U.S.A. 97, 7754-7759
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 7754-7759
    • Harris, J.L.1    Backes, B.J.2    Leonetti, F.3    Mahrus, S.4    Ellman, J.A.5    Craik, C.S.6
  • 11
    • 0035853116 scopus 로고    scopus 로고
    • Global analysis of proteasomal substrate specificity using positional-scanning libraries of covalent inhibitors
    • Nazif, T. and Bogyo, M. (2001) Global analysis of proteasomal substrate specificity using positional-scanning libraries of covalent inhibitors. Proc. Natl. Acad. Sci. U.S.A. 98, 2967-2972
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 2967-2972
    • Nazif, T.1    Bogyo, M.2
  • 12
    • 0034946412 scopus 로고    scopus 로고
    • Determination of protease cleavage site motifs using mixture-based oriented peptide libraries
    • Turk, B. E., Huang, L. L., Piro, E. T. and Cantley, L. C. (2001) Determination of protease cleavage site motifs using mixture-based oriented peptide libraries. Nat. Biotechnol. 19, 661-667
    • (2001) Nat. Biotechnol , vol.19 , pp. 661-667
    • Turk, B.E.1    Huang, L.L.2    Piro, E.T.3    Cantley, L.C.4
  • 15
    • 0033619787 scopus 로고    scopus 로고
    • Mitochondrial processing peptidase: Multiple-site recognition of precursor proteins
    • Ito, A. (1999) Mitochondrial processing peptidase: multiple-site recognition of precursor proteins. Biochem. Biophys. Res. Commun. 265, 611-616
    • (1999) Biochem. Biophys. Res. Commun , vol.265 , pp. 611-616
    • Ito, A.1
  • 16
    • 0028819132 scopus 로고
    • Evidence that two zinc fingers in the methionine aminopeptidase from Saccharomyces cerevisiae are important for normal growth
    • Zuo, S., Guo, Q., Ling, C. and Chang, Y. H. (1995) Evidence that two zinc fingers in the methionine aminopeptidase from Saccharomyces cerevisiae are important for normal growth. Mol. Gen. Genet. 246, 247-253
    • (1995) Mol. Gen. Genet , vol.246 , pp. 247-253
    • Zuo, S.1    Guo, Q.2    Ling, C.3    Chang, Y.H.4
  • 18
    • 0000917949 scopus 로고
    • Guanidination of proteins
    • Kimmel, J. R. (1967) Guanidination of proteins. Methods Enzymol. 11, 584-589
    • (1967) Methods Enzymol , vol.11 , pp. 584-589
    • Kimmel, J.R.1
  • 19
    • 0033647183 scopus 로고    scopus 로고
    • Enhancing the intensities of lysine-terminated tryptic peptide ions in matrix-assisted laser desorption/ionization mass spectrometry
    • Beardsley, R. L., Karty, J. A. and Reilly, J. P. (2000) Enhancing the intensities of lysine-terminated tryptic peptide ions in matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun. Mass Spectrom. 14, 2147-2153
    • (2000) Rapid Commun. Mass Spectrom , vol.14 , pp. 2147-2153
    • Beardsley, R.L.1    Karty, J.A.2    Reilly, J.P.3
  • 22
    • 24044513966 scopus 로고    scopus 로고
    • Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations
    • Elias, J. E., Haas, W., Faherty, B. K. and Gygi, S. P. (2005) Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations. Nat. Methods 2, 667-675
    • (2005) Nat. Methods , vol.2 , pp. 667-675
    • Elias, J.E.1    Haas, W.2    Faherty, B.K.3    Gygi, S.P.4
  • 23
    • 0037462954 scopus 로고    scopus 로고
    • N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins
    • Polevoda, B. and Sherman, F. (2003) N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins. J. Mol. Biol. 325, 595-622
    • (2003) J. Mol. Biol , vol.325 , pp. 595-622
    • Polevoda, B.1    Sherman, F.2
  • 24
    • 0344815737 scopus 로고
    • Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid
    • Hirel, P. H., Schmitter, M. J., Dessen, P., Fayat, G. and Blanquet, S. (1989) Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid. Proc. Natl. Acad. Sci. U.S.A. 86, 8247-8251
    • (1989) Proc. Natl. Acad. Sci. U.S.A , vol.86 , pp. 8247-8251
    • Hirel, P.H.1    Schmitter, M.J.2    Dessen, P.3    Fayat, G.4    Blanquet, S.5
  • 26
  • 28
    • 0038475878 scopus 로고    scopus 로고
    • Factors governing nonoverlapping substrate specificity by mitochondrial inner membrane peptidase
    • Luo, W., Chen, X., Fang, H. and Green, N. (2003) Factors governing nonoverlapping substrate specificity by mitochondrial inner membrane peptidase. J. Biol. Chem. 278, 4943-4948
    • (2003) J. Biol. Chem , vol.278 , pp. 4943-4948
    • Luo, W.1    Chen, X.2    Fang, H.3    Green, N.4
  • 30
    • 84944076792 scopus 로고    scopus 로고
    • Membrane alanyl aminopeptidase
    • Barrett, A. J, Rawlings, N. D. and Woessner, J. F, eds, pp, Elsevier, London
    • Turner, A. J. (2004) Membrane alanyl aminopeptidase. In Handbook of Proteolytic Enzymes (Barrett, A. J., Rawlings, N. D. and Woessner, J. F., eds.), pp. 289-294, Elsevier, London
    • (2004) Handbook of Proteolytic Enzymes , pp. 289-294
    • Turner, A.J.1
  • 31
    • 20444421293 scopus 로고    scopus 로고
    • Fibroblast activation protein-α and dipeptidyl peptidase IV (CD26): Cell-surface proteases that activate cell signaling and are potential targets for cancer therapy
    • Kelly, T. (2005) Fibroblast activation protein-α and dipeptidyl peptidase IV (CD26): cell-surface proteases that activate cell signaling and are potential targets for cancer therapy Drug Resist. Updat. 8, 51-58
    • (2005) Drug Resist. Updat , vol.8 , pp. 51-58
    • Kelly, T.1
  • 32
    • 0037869031 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibitors for the treatment of impaired glucose tolerance and type 2 diabetes
    • Wiedeman, P. E. and Trevillyan, J. M. (2003) Dipeptidyl peptidase IV inhibitors for the treatment of impaired glucose tolerance and type 2 diabetes. Curr. Opin. Invest. Drugs 4, 412-420
    • (2003) Curr. Opin. Invest. Drugs , vol.4 , pp. 412-420
    • Wiedeman, P.E.1    Trevillyan, J.M.2
  • 33
    • 0030805979 scopus 로고    scopus 로고
    • Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12
    • Link, A. J., Robison, K. and Church, G. M. (1997) Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 18, 1259-1313
    • (1997) Electrophoresis , vol.18 , pp. 1259-1313
    • Link, A.J.1    Robison, K.2    Church, G.M.3
  • 34
    • 0038333588 scopus 로고    scopus 로고
    • Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides
    • Gevaert, K., Goethals, M., Martens, L., Van Damme, J., Staes, A., Thomas, G. R. and Vandekerckhove, J. (2003) Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat. Biotechnol. 21, 566-569
    • (2003) Nat. Biotechnol , vol.21 , pp. 566-569
    • Gevaert, K.1    Goethals, M.2    Martens, L.3    Van Damme, J.4    Staes, A.5    Thomas, G.R.6    Vandekerckhove, J.7
  • 35
    • 30944438540 scopus 로고    scopus 로고
    • Positional proteomics: Selective recovery and analysis of N-terminal proteolytic peptides
    • McDonald, L., Robertson, D. H., Hurst, J. L. and Beynon, R. J. (2005) Positional proteomics: selective recovery and analysis of N-terminal proteolytic peptides. Nat. Methods 2, 955-957
    • (2005) Nat. Methods , vol.2 , pp. 955-957
    • McDonald, L.1    Robertson, D.H.2    Hurst, J.L.3    Beynon, R.J.4
  • 36
    • 0037380768 scopus 로고    scopus 로고
    • Fluorescent two-dimensional difference gel electrophoresis and mass spectrometry identify age-related protein expression differences for the primary visual cortex of kitten and adult cat
    • Van den Bergh, G., Clerens, S., Cnops, L., Vandesande, F. and Arckens, L. (2003) Fluorescent two-dimensional difference gel electrophoresis and mass spectrometry identify age-related protein expression differences for the primary visual cortex of kitten and adult cat. J. Neurochem. 85, 193-205
    • (2003) J. Neurochem , vol.85 , pp. 193-205
    • Van den Bergh, G.1    Clerens, S.2    Cnops, L.3    Vandesande, F.4    Arckens, L.5


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