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Volumn 3, Issue 8, 2007, Pages 554-566

Identification of Conus amadis disulfide isomerase: Minimum sequence length of peptide fragments necessary for protein annotation

Author keywords

[No Author keywords available]

Indexed keywords

CONUS AMADIS; GASTROPODA;

EID: 34547230228     PISSN: 1742206X     EISSN: 17422051     Source Type: Journal    
DOI: 10.1039/b705382g     Document Type: Article
Times cited : (17)

References (39)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • R. Aebersold M. Mann Mass spectrometry-based proteomics Nature 2003 422 198 207
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 2
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • B. Domon R. Aebersold Mass spectrometry and protein analysis Science 2006 312 212 217
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 3
    • 0042854999 scopus 로고    scopus 로고
    • Proteome analysis by mass spectrometry
    • P. L. Ferguson R. D. Smith Proteome analysis by mass spectrometry Annu. Rev. Biochem. 2003 32 399 424
    • (2003) Annu. Rev. Biochem. , vol.32 , pp. 399-424
    • Ferguson, P.L.1    Smith, R.D.2
  • 4
    • 0029927505 scopus 로고    scopus 로고
    • Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels
    • A. Shevchenko M. Wilm O. Vorm M. Mann Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels Anal. Chem. 1996 68 850 858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 5
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • M. Wilm A. Shevchenko T. Houthaeve S. Breit L. Schweigerer T. Fotsis M. Mann Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry Nature 1996 379 466 469
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 6
    • 0032190378 scopus 로고    scopus 로고
    • Protein identification at the low femtomole level from silver-stained gels using a new fritless electrospray interface for liquid chromatography- microspray and nanospray mass spectrometry
    • C. L. Gatlin G. R. Kleemann L. G. Hays A. J. Link J. R. Yates, 3rd Protein identification at the low femtomole level from silver-stained gels using a new fritless electrospray interface for liquid chromatography-microspray and nanospray mass spectrometry Anal. Biochem. 1998 263 93 101
    • (1998) Anal. Biochem. , vol.263 , pp. 93-101
    • Gatlin, C.L.1    Kleemann, G.R.2    Hays, L.G.3    Link, A.J.4    Yates III, J.R.5
  • 7
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • D. N. Perkins D. J. Pappin D. M. Creasy J. S. Cottrell Probability-based protein identification by searching sequence databases using mass spectrometry data Electrophoresis 1999 20 3551 3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 8
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • J. K. Eng A. L. McCormack J. R. Yates, 3rd An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database J. Am. Soc. Mass Spectrom. 1994 5 976 989
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 9
    • 0028575316 scopus 로고
    • Error-tolerant identification of peptides in sequence databases by peptide sequence tags
    • M. Mann M. Wilm Error-tolerant identification of peptides in sequence databases by peptide sequence tags Anal. Chem. 1994 66 4390 4399
    • (1994) Anal. Chem. , vol.66 , pp. 4390-4399
    • Mann, M.1    Wilm, M.2
  • 10
    • 24044491542 scopus 로고    scopus 로고
    • Comprehensive Analysis of a Multidimensional Liquid Chromatography Mass Spectrometry Dataset Acquired on a Quadrupole Selecting Quadrupole Collision Cell, Time-of-flight Mass Spectrometer. II. New Developments in Protein Prospector Allow for Reliable and Comprehensive Automatic Analysis of Large Datasets
    • R. J. Chalkley P. R. Baker L. Huang K. C. Hansen N. P. Allen M. Rexach A. L. Burlingame Comprehensive Analysis of a Multidimensional Liquid Chromatography Mass Spectrometry Dataset Acquired on a Quadrupole Selecting Quadrupole Collision Cell, Time-of-flight Mass Spectrometer. II. New Developments in Protein Prospector Allow for Reliable and Comprehensive Automatic Analysis of Large Datasets Mol. Cell. Proteomics 2005 4 1194 1204
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1194-1204
    • Chalkley, R.J.1    Baker, P.R.2    Huang, L.3    Hansen, K.C.4    Allen, N.P.5    Rexach, M.6    Burlingame, A.L.7
  • 11
    • 0035326344 scopus 로고    scopus 로고
    • Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching
    • A. Shevchenko S. Sunyaev A. Loboda A. Shevchenko P. Bork W. Ens K. G. Standing Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching Anal. Chem. 2001 73 1917 1926
    • (2001) Anal. Chem. , vol.73 , pp. 1917-1926
    • Shevchenko, A.1    Sunyaev, S.2    Loboda, A.3    Shevchenko, A.4    Bork, P.5    Ens, W.6    Standing, K.G.7
  • 12
    • 0347989461 scopus 로고    scopus 로고
    • Conus venoms: A rich source of novel ion channel-targeted peptides
    • H. Terlau B. M. Olivera Conus venoms: a rich source of novel ion channel-targeted peptides Physiol. Rev. 2004 84 41 68
    • (2004) Physiol. Rev. , vol.84 , pp. 41-68
    • Terlau, H.1    Olivera, B.M.2
  • 13
    • 0001021863 scopus 로고
    • Conus peptides as chemical probes for receptors and ion channels
    • R. A. Myers L. J. Cruz J. E. Rivier B. M. Olivera Conus peptides as chemical probes for receptors and ion channels Chem. Rev. 1993 93 1923 1936
    • (1993) Chem. Rev. , vol.93 , pp. 1923-1936
    • Myers, R.A.1    Cruz, L.J.2    Rivier, J.E.3    Olivera, B.M.4
  • 15
    • 29344443859 scopus 로고    scopus 로고
    • Conotoxins and the posttranslational modification of secreted gene products
    • O. Buczek G. Bulaj B. M. Olivera Conotoxins and the posttranslational modification of secreted gene products Cell. Mol. Life Sci. 2005 62 3067 3079
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 3067-3079
    • Buczek, O.1    Bulaj, G.2    Olivera, B.M.3
  • 16
    • 0033198875 scopus 로고    scopus 로고
    • Post-translationally modified neuropeptides from Conus venoms
    • A. G. Craig P. Bandyopadhyay B. M. Olivera Post-translationally modified neuropeptides from Conus venoms Eur. J. Biochem. 1999 264 271 275
    • (1999) Eur. J. Biochem. , vol.264 , pp. 271-275
    • Craig, A.G.1    Bandyopadhyay, P.2    Olivera, B.M.3
  • 18
    • 0029856411 scopus 로고    scopus 로고
    • Folding of omega-conotoxins. 2. Influence of precursor sequences and protein disulfide isomerase
    • C. M. Price W. R. Gray D. P. Goldenberg Folding of omega-conotoxins. 2. Influence of precursor sequences and protein disulfide isomerase Biochemistry 1996 35 15547 57
    • (1996) Biochemistry , vol.35 , pp. 15547-15557
    • Price, C.M.1    Gray, W.R.2    Goldenberg, D.P.3
  • 19
    • 0942279699 scopus 로고    scopus 로고
    • Propeptide does not act as an intramolecular chaperone but facilitates protein disulfide isomerase-assisted folding of a conotoxin precursor
    • O. Buczek B. M. Olivera G. Bulaj Propeptide does not act as an intramolecular chaperone but facilitates protein disulfide isomerase-assisted folding of a conotoxin precursor Biochemistry 2004 43 1093 1101
    • (2004) Biochemistry , vol.43 , pp. 1093-1101
    • Buczek, O.1    Olivera, B.M.2    Bulaj, G.3
  • 21
    • 0030724094 scopus 로고    scopus 로고
    • Protein disulfide isomerase and assisted protein folding
    • H. F. Gilbert Protein disulfide isomerase and assisted protein folding J. Biol. Chem. 1997 272 29399 29402
    • (1997) J. Biol. Chem. , vol.272 , pp. 29399-29402
    • Gilbert, H.F.1
  • 23
    • 0036842559 scopus 로고    scopus 로고
    • Formation and transfer of disulfide bonds in living cells
    • C. S. Sevier C. A. Kaiser Formation and transfer of disulfide bonds in living cells Nat. Rev. Mol. Cell Biol. 2002 3 836 847
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 836-847
    • Sevier, C.S.1    Kaiser, C.A.2
  • 24
    • 0027959156 scopus 로고
    • Protein disulfide isomerase: Building bridges in protein folding
    • R. B. Freedman T. R. Hirst M. F. Tuite Protein disulfide isomerase: building bridges in protein folding Trends Biochem. Sci. 1994 19 331 336
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 29
    • 0029397704 scopus 로고
    • Sequence-Specific Fragmentation of Matrix-Assisted Laser-Desorbed Protein/Peptide Ions
    • R. S. Brown J. J. Lennon Sequence-Specific Fragmentation of Matrix-Assisted Laser-Desorbed Protein/Peptide Ions Anal. Chem. 1995 67 3990 3999
    • (1995) Anal. Chem. , vol.67 , pp. 3990-3999
    • Brown, R.S.1    Lennon, J.J.2
  • 30
    • 0027692925 scopus 로고
    • Identification of the facile gas-phase cleavage of the Asp-Pro and Asp-Xxx peptide bonds in matrix-assisted laser desorption time-of-flight mass spectrometry
    • W. Yu J. E. Vath M. C. Huberty S. A. Martin Identification of the facile gas-phase cleavage of the Asp-Pro and Asp-Xxx peptide bonds in matrix-assisted laser desorption time-of-flight mass spectrometry Anal. Chem. 1993 65 3015 3023
    • (1993) Anal. Chem. , vol.65 , pp. 3015-3023
    • Yu, W.1    Vath, J.E.2    Huberty, M.C.3    Martin, S.A.4
  • 31
    • 0037253223 scopus 로고    scopus 로고
    • Expanding the organismal scope of proteomics: Cross-species protein identification by mass spectrometry and its implications
    • A. J. Liska A. Shevchenko Expanding the organismal scope of proteomics: cross-species protein identification by mass spectrometry and its implications Proteomics 2003 3 19 28
    • (2003) Proteomics , vol.3 , pp. 19-28
    • Liska, A.J.1    Shevchenko, A.2
  • 32
    • 0041731780 scopus 로고    scopus 로고
    • Isolation and characterization of a cone snail protease with homology to CRISP proteins of the pathogenesis-related protein superfamily
    • T. J. Milne G. Abbenante J. D. Tyndall J. Halliday R. J. Lewis Isolation and characterization of a cone snail protease with homology to CRISP proteins of the pathogenesis-related protein superfamily J. Biol. Chem. 2003 278 31105 31110
    • (2003) J. Biol. Chem. , vol.278 , pp. 31105-31110
    • Milne, T.J.1    Abbenante, G.2    Tyndall, J.D.3    Halliday, J.4    Lewis, R.J.5
  • 33
    • 0029979976 scopus 로고    scopus 로고
    • Influence of Matrix Solution Conditions on the MALDI-MS Analysis of Peptides and Proteins
    • S. L. Cohen B. T. Chait Influence of Matrix Solution Conditions on the MALDI-MS Analysis of Peptides and Proteins Anal. Chem. 1996 68 31 37
    • (1996) Anal. Chem. , vol.68 , pp. 31-37
    • Cohen, S.L.1    Chait, B.T.2
  • 34
    • 0025670535 scopus 로고
    • Sequencing of peptides by tandem mass spectrometry and high-energy collision-induced dissociation
    • K. Biemann Sequencing of peptides by tandem mass spectrometry and high-energy collision-induced dissociation Methods Enzymol. 1990 193 455 479
    • (1990) Methods Enzymol. , vol.193 , pp. 455-479
    • Biemann, K.1
  • 35
    • 4444335470 scopus 로고    scopus 로고
    • The abc's (and xyz's) of peptide sequencing
    • H. Steen M. Mann The abc's (and xyz's) of peptide sequencing Nat. Rev. Mol. Cell Biol. 2004 5 699 711
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 37
    • 0023449998 scopus 로고
    • Novel fragmentation process of peptides by collision-induced decomposition in a tandem mass spectrometer: Differentiation of leucine and isoleucine
    • R. S. Jonson S. A. Martin K. Biemann J. T. Stults J. T. Watson Novel fragmentation process of peptides by collision-induced decomposition in a tandem mass spectrometer: differentiation of leucine and isoleucine Anal. Chem. 1987 59 2621 2625
    • (1987) Anal. Chem. , vol.59 , pp. 2621-2625
    • Jonson, R.S.1    Martin, S.A.2    Biemann, K.3    Stults, J.T.4    Watson, J.T.5
  • 38
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • J. D. Thompson T. J. Gibson F. Plewniak F. Jeanmougin D. G. Higgins The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res. 1997 25 4876 4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 39
    • 33846571319 scopus 로고    scopus 로고
    • Improved collision-induced dissociation analysis of peptides by matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometry through 3-sulfobenzoic acid succinimidyl ester labeling
    • W. R. Alley, Jr. Y. Mechref I. Klouckova M. V. Novotny Improved collision-induced dissociation analysis of peptides by matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometry through 3-sulfobenzoic acid succinimidyl ester labeling J. Proteome Res. 2007 6 124 132
    • (2007) J. Proteome Res. , vol.6 , pp. 124-132
    • Alley Jr., W.R.1    Mechref, Y.2    Klouckova, I.3    Novotny, M.V.4


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