메뉴 건너뛰기




Volumn 8, Issue 3, 2009, Pages 1415-1422

Proteomic analyses using Grifola frondosa metalloendoprotease Lys-N

Author keywords

Grifola frondosa; Immonium ion; Lys N; Metalloendoprotease; Sequence tags

Indexed keywords

IMMONIUM; ION; LYSINE; METALLOPROTEINASE; PEPTIDE; TRYPSIN; UNCLASSIFIED DRUG;

EID: 65249153010     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr800774h     Document Type: Article
Times cited : (35)

References (34)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R.; Mann, M. Mass spectrometry-based proteomics. Nature 2003, 422 (6928), 198-207.
    • (2003) Nature , vol.422 , Issue.6928 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 3
    • 30144440763 scopus 로고    scopus 로고
    • Fragmentation pathways of protonated peptides
    • Rev
    • Paizs, B.; Suhai, S. Fragmentation pathways of protonated peptides. Mass Spectrom. Rev. 2004.
    • (2004) Mass Spectrom
    • Paizs, B.1    Suhai, S.2
  • 4
    • 84987419408 scopus 로고
    • Proposal for a common nomenclature for sequence ions in mass spectra of peptides
    • Roepstorff, P.; Fohlman, J. Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed. Mass Spectrom. 1984, 11 (11), 601.
    • (1984) Biomed. Mass Spectrom , vol.11 , Issue.11 , pp. 601
    • Roepstorff, P.1    Fohlman, J.2
  • 5
    • 0025617140 scopus 로고
    • Appendix 5. Nomenclature for peptide fragment ions (positive ions)
    • Biemann, K. Appendix 5. Nomenclature for peptide fragment ions (positive ions). Methods Enzymol. 1990, 193, 886-7.
    • (1990) Methods Enzymol , vol.193 , pp. 886-887
    • Biemann, K.1
  • 6
    • 0000857494 scopus 로고
    • An approach to correlate tamdem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J.; McCormack, A.; Yates III, J. R. An approach to correlate tamdem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 1994, (5), 976989.
    • (1994) J. Am. Soc. Mass Spectrom , vol.5 , pp. 976989
    • Eng, J.1    McCormack, A.2    Yates III, J.R.3
  • 7
    • 0033434080 scopus 로고    scopus 로고
    • Probability- based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N.; Pappin, D. J.; Creasy, D. M.; Cottrell, J. S. Probability- based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20 (18), 355167.
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 355167
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 8
    • 0029810698 scopus 로고    scopus 로고
    • Influence of Peptide Composition, Gas-Phase Basicity, and Chemical Modification on Fragmentation Efficiency: Evidence for the Mobile Proton Model
    • Dongre, A. R.; Jones, J. L.; Somogyi, A.; Wysocki, V. H. Influence of Peptide Composition, Gas-Phase Basicity, and Chemical Modification on Fragmentation Efficiency: Evidence for the Mobile Proton Model. J. Am. Chem. Soc. 1996, 118 (35), 8365-8374.
    • (1996) J. Am. Chem. Soc , vol.118 , Issue.35 , pp. 8365-8374
    • Dongre, A.R.1    Jones, J.L.2    Somogyi, A.3    Wysocki, V.H.4
  • 9
    • 0026952628 scopus 로고
    • An investigation of fragmentation mechanisms of doubly protonated tryptic peptides
    • Tang, X. J.; Boyd, R. K. An investigation of fragmentation mechanisms of doubly protonated tryptic peptides. Rapid Commun. Mass Spectrom. 1992, 6 (11), 651-7.
    • (1992) Rapid Commun. Mass Spectrom , vol.6 , Issue.11 , pp. 651-657
    • Tang, X.J.1    Boyd, R.K.2
  • 10
    • 0036023990 scopus 로고    scopus 로고
    • Towards understanding some ion intensity relationships for the tandem mass spectra of protonated peptides
    • Paizs, B.; Suhai, S. Towards understanding some ion intensity relationships for the tandem mass spectra of protonated peptides. Rapid Commun. Mass Spectrom. 2002, 16 (17), 1699-702.
    • (2002) Rapid Commun. Mass Spectrom , vol.16 , Issue.17 , pp. 1699-1702
    • Paizs, B.1    Suhai, S.2
  • 11
    • 0034501099 scopus 로고    scopus 로고
    • Mobile and localized protons: A framework for understanding peptide dissociation
    • Wysocki, V. H.; Tsaprailis, G.; Smith, L. L.; Breci, L. A. Mobile and localized protons: a framework for understanding peptide dissociation. J. Mass Spectrom. 2000, 35 (12), 1399-406.
    • (2000) J. Mass Spectrom , vol.35 , Issue.12 , pp. 1399-1406
    • Wysocki, V.H.1    Tsaprailis, G.2    Smith, L.L.3    Breci, L.A.4
  • 12
    • 1442324456 scopus 로고    scopus 로고
    • Tabb, D. L.; Huang, Y.; Wysocki, V. H.; Yates, J. R. 3rd, Influence of basic residue content on fragment ion peak intensities in low- energy collision-induced dissociation spectra of peptides. Anal. Chem. 2004, 76 (5), 1243-8.
    • Tabb, D. L.; Huang, Y.; Wysocki, V. H.; Yates, J. R. 3rd, Influence of basic residue content on fragment ion peak intensities in low- energy collision-induced dissociation spectra of peptides. Anal. Chem. 2004, 76 (5), 1243-8.
  • 13
    • 0036989672 scopus 로고    scopus 로고
    • PCR cloning and heterologous expression of cDNA encoding a peptidyl-Lys met- alloendopeptidase precursor of Grifola frondosa
    • Saito, T.; Dohmae, N.; Tsujimoto, M.; Takio, K. PCR cloning and heterologous expression of cDNA encoding a peptidyl-Lys met- alloendopeptidase precursor of Grifola frondosa. J. Gen. Appl. Microbiol. 2002, 48 (5), 287-92.
    • (2002) J. Gen. Appl. Microbiol , vol.48 , Issue.5 , pp. 287-292
    • Saito, T.1    Dohmae, N.2    Tsujimoto, M.3    Takio, K.4
  • 14
    • 0035096928 scopus 로고    scopus 로고
    • Structure of a new 'aspzincin' metalloendopeptidase from Grifola frondosa: Implications for the catalytic mechanism and substrate specificity based on several different crystal forms
    • Hori, T.; Kumasaka, T.; Yamamoto, M.; Nonaka, N.; Tanaka, N.; Hashimoto, Y.; Ueki, U.; Takio, K. Structure of a new 'aspzincin' metalloendopeptidase from Grifola frondosa: implications for the catalytic mechanism and substrate specificity based on several different crystal forms. Acta Crystallogr. D: Biol. Crystallogr. 2001, 57 (Pt 3), 361-8.
    • (2001) Acta Crystallogr. D: Biol. Crystallogr , vol.57 , Issue.PART 3 , pp. 361-368
    • Hori, T.1    Kumasaka, T.2    Yamamoto, M.3    Nonaka, N.4    Tanaka, N.5    Hashimoto, Y.6    Ueki, U.7    Takio, K.8
  • 15
    • 0030775983 scopus 로고    scopus 로고
    • Amino acid sequences of metalloendopeptidases specific for acyl-lysine bonds from Grifola frondosa and Pleurotus ostreatus fruiting bodies
    • Nonaka, T.; Dohmae, N.; Hashimoto, Y.; Takio, K. Amino acid sequences of metalloendopeptidases specific for acyl-lysine bonds from Grifola frondosa and Pleurotus ostreatus fruiting bodies. J. Biol. Chem. 1997, 272 (48), 30032-9.
    • (1997) J. Biol. Chem , vol.272 , Issue.48 , pp. 30032-30039
    • Nonaka, T.1    Dohmae, N.2    Hashimoto, Y.3    Takio, K.4
  • 16
    • 0035259134 scopus 로고    scopus 로고
    • Purification and characterization of an aminopeptidase from the edible basidiomycete Grifola frondosa
    • Nishiwaki, T.; Hayashi, K. Purification and characterization of an aminopeptidase from the edible basidiomycete Grifola frondosa. Biosci. Biotechnol. Biochem. 2001, 65 (2), 424-7.
    • (2001) Biosci. Biotechnol. Biochem , vol.65 , Issue.2 , pp. 424-427
    • Nishiwaki, T.1    Hayashi, K.2
  • 17
    • 0031872472 scopus 로고    scopus 로고
    • Kinetic characterization of lysine-specific metalloendopeptidases from Grifola frondosa and Pleurotus ostreatus fruiting bodies
    • Nonaka, T.; Hashimoto, Y.; Takio, K. Kinetic characterization of lysine-specific metalloendopeptidases from Grifola frondosa and Pleurotus ostreatus fruiting bodies. J. Biochem. 1998, 124 (1), 15762.
    • (1998) J. Biochem , vol.124 , Issue.1 , pp. 15762
    • Nonaka, T.1    Hashimoto, Y.2    Takio, K.3
  • 19
    • 27644463394 scopus 로고    scopus 로고
    • 18O labeling for comparative pro- teomics: Application to cytokine/lipolysaccharide-treated human retinal pigment epithelium cell line
    • 18O labeling for comparative pro- teomics: application to cytokine/lipolysaccharide-treated human retinal pigment epithelium cell line. Mol. Cell. Proteomics 2005, 4 (10), 1550-7.
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.10 , pp. 1550-1557
    • Rao, K.C.1    Palamalai, V.2    Dunlevy, J.R.3    Miyagi, M.4
  • 20
    • 42949113985 scopus 로고    scopus 로고
    • Straightforward ladder sequencing of peptides using a Lys-N metalloen- dopeptidase
    • Taouatas, N.; Drugan, M. M.; Heck, A. J.; Mohammed, S. Straightforward ladder sequencing of peptides using a Lys-N metalloen- dopeptidase. Nat. Methods 2008, 5 (5), 405-7.
    • (2008) Nat. Methods , vol.5 , Issue.5 , pp. 405-407
    • Taouatas, N.1    Drugan, M.M.2    Heck, A.J.3    Mohammed, S.4
  • 22
    • 23044442790 scopus 로고    scopus 로고
    • Investigation of neutral loss during collision-induced dissociation of peptide ions
    • Martin, D. B.; Eng, J. K.; Nesvizhskii, A. I.; Gemmill, A.; Aebersold, R. Investigation of neutral loss during collision-induced dissociation of peptide ions. Anal. Chem. 2005, 77 (15), 4870-82.
    • (2005) Anal. Chem , vol.77 , Issue.15 , pp. 4870-4882
    • Martin, D.B.1    Eng, J.K.2    Nesvizhskii, A.I.3    Gemmill, A.4    Aebersold, R.5
  • 23
    • 33746930864 scopus 로고    scopus 로고
    • A uniform proteomics MS/MS analysis platform utilizing open XML file formats
    • Keller, A.; Eng, J.; Zhang, N.; Li, X. J.; Aebersold, R. A uniform proteomics MS/MS analysis platform utilizing open XML file formats. Mol. Syst. Biol. 2005, 1, 2005-0017.
    • (2005) Mol. Syst. Biol , vol.1 , pp. 2005-0017
    • Keller, A.1    Eng, J.2    Zhang, N.3    Li, X.J.4    Aebersold, R.5
  • 24
    • 33750631580 scopus 로고    scopus 로고
    • Efficient fractionation and improved protein identification by peptide OFFGEL electrophoresis
    • Horth, P.; Miller, C. A.; Preckel, T.; Wenz, C. Efficient fractionation and improved protein identification by peptide OFFGEL electrophoresis. Mol. Cell. Proteomics 2006, 5 (10), 1968-74.
    • (2006) Mol. Cell. Proteomics , vol.5 , Issue.10 , pp. 1968-1974
    • Horth, P.1    Miller, C.A.2    Preckel, T.3    Wenz, C.4
  • 25
    • 34249329535 scopus 로고    scopus 로고
    • Modeling the isoelectric focusing of peptides in an OFFGEL multicompartment cell
    • Lam, H. T.; Josserand, J.; Lion, N.; Girault, H. H. Modeling the isoelectric focusing of peptides in an OFFGEL multicompartment cell. J. Proteome Res. 2007, 6 (5), 1666-76.
    • (2007) J. Proteome Res , vol.6 , Issue.5 , pp. 1666-1676
    • Lam, H.T.1    Josserand, J.2    Lion, N.3    Girault, H.H.4
  • 26
    • 0037274605 scopus 로고    scopus 로고
    • Multiple enzymatic digestion for enhanced sequence coverage of proteins in complex proteomic mixtures using capillary LC with ion trap MS/MS
    • Choudhary, G.; Wu, S. L.; Shieh, P.; Hancock, W. S. Multiple enzymatic digestion for enhanced sequence coverage of proteins in complex proteomic mixtures using capillary LC with ion trap MS/MS. J. Proteome Res. 2003, 2 (1), 59-67.
    • (2003) J. Proteome Res , vol.2 , Issue.1 , pp. 59-67
    • Choudhary, G.1    Wu, S.L.2    Shieh, P.3    Hancock, W.S.4
  • 27
    • 0034652301 scopus 로고    scopus 로고
    • Gatlin, C. L.; Eng, J. K.; Cross, S. T.; Detter, J. C.; Yates, J. R. 3rd, Automated identification of amino acid sequence variations in proteins by HPLC/microspray tandem mass spectrometry. Anal. Chem. 2000, 72 (4), 757-63.
    • Gatlin, C. L.; Eng, J. K.; Cross, S. T.; Detter, J. C.; Yates, J. R. 3rd, Automated identification of amino acid sequence variations in proteins by HPLC/microspray tandem mass spectrometry. Anal. Chem. 2000, 72 (4), 757-63.
  • 28
    • 31844455267 scopus 로고    scopus 로고
    • Obtaining high sequence coverage in matrix-assisted laser desorption time-of-flight mass spectrometry for studies of protein modification: Analysis of human serum albumin as a model
    • Wa, C.; Cerny, R.; Hage, D. S. Obtaining high sequence coverage in matrix-assisted laser desorption time-of-flight mass spectrometry for studies of protein modification: analysis of human serum albumin as a model. Anal. Biochem. 2006, 349 (2), 229-41.
    • (2006) Anal. Biochem , vol.349 , Issue.2 , pp. 229-241
    • Wa, C.1    Cerny, R.2    Hage, D.S.3
  • 29
    • 0034516862 scopus 로고    scopus 로고
    • Dissociation of the peptide bond in protonated peptides
    • Polce, M. J.; Ren, D.; Wesdemiotis, C. Dissociation of the peptide bond in protonated peptides. J. Mass Spectrom. 2000, 35 (12), 1391-8.
    • (2000) J. Mass Spectrom , vol.35 , Issue.12 , pp. 1391-1398
    • Polce, M.J.1    Ren, D.2    Wesdemiotis, C.3
  • 30
    • 0032231991 scopus 로고    scopus 로고
    • Origin of product ions in the MS/MS spectra of peptides in a quadrupole ion trap
    • Vachet, R. W.; Ray, K. L.; Glish, G. L. Origin of product ions in the MS/MS spectra of peptides in a quadrupole ion trap. J. Am. Soc. Mass Spectrom. 1998, 9 (4), 341-4.
    • (1998) J. Am. Soc. Mass Spectrom , vol.9 , Issue.4 , pp. 341-344
    • Vachet, R.W.1    Ray, K.L.2    Glish, G.L.3
  • 31
    • 49049104638 scopus 로고    scopus 로고
    • Quantification of the Compositional Information Provided by Immonium Ions on a Quadrupole-Time-of-Flight Mass Spectrometer
    • Hohmann, L. J.; Eng, J. K.; Gemmill, A.; Klimek, J.; Vitek, O.; Reid, G. E.; Martin, D. B. Quantification of the Compositional Information Provided by Immonium Ions on a Quadrupole-Time-of-Flight Mass Spectrometer. Anal. Chem. 2008.
    • (2008) Anal. Chem
    • Hohmann, L.J.1    Eng, J.K.2    Gemmill, A.3    Klimek, J.4    Vitek, O.5    Reid, G.E.6    Martin, D.B.7
  • 32
    • 0028575316 scopus 로고
    • Error-tolerant identification of peptides in sequence databases by peptide sequence tags
    • Mann, M.; Wilm, M. Error-tolerant identification of peptides in sequence databases by peptide sequence tags. Anal. Chem. 1994, 66 (24), 4390-9.
    • (1994) Anal. Chem , vol.66 , Issue.24 , pp. 4390-4399
    • Mann, M.1    Wilm, M.2
  • 33
    • 0345600791 scopus 로고    scopus 로고
    • Tabb, D. L.; Saraf, A.; Yates, J. R. 3rd, GutenTag: high-throughput sequence tagging via an empirically derived fragmentation model. Anal. Chem. 2003, 75 (23), 6415-21.
    • Tabb, D. L.; Saraf, A.; Yates, J. R. 3rd, GutenTag: high-throughput sequence tagging via an empirically derived fragmentation model. Anal. Chem. 2003, 75 (23), 6415-21.
  • 34
    • 55249118638 scopus 로고    scopus 로고
    • Tabb, D. L.; Ma, Z. Q.; Martin, D. B.; Ham, A. J.; Chambers, M. C. DirecTag: Accurate Sequence Tags from Peptide MS/MS through Statistical Scoring. J. Proteome Res. 2008, 7 (9), 3838-46.
    • Tabb, D. L.; Ma, Z. Q.; Martin, D. B.; Ham, A. J.; Chambers, M. C. DirecTag: Accurate Sequence Tags from Peptide MS/MS through Statistical Scoring. J. Proteome Res. 2008, 7 (9), 3838-46.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.