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Volumn 1, Issue 6, 2007, Pages 2856-2860

In-gel digestion for mass spectrometric characterization of proteins and proteomes

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 34548178909     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2006.468     Document Type: Article
Times cited : (3979)

References (23)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R. & Mann, M. Mass spectrometry-based proteomics. Nature 422, 198-207 (2003).
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 2
    • 85047698600 scopus 로고    scopus 로고
    • Archived polyacrylamide gels as a resource for proteome characterization by mass spectrometry
    • Shevchenko, A., Loboda, A., Ens, W., Schraven, B. & Standing, K.G. Archived polyacrylamide gels as a resource for proteome characterization by mass spectrometry. Electrophoresis 22, 1194-1203 (2001).
    • (2001) Electrophoresis , vol.22 , pp. 1194-1203
    • Shevchenko, A.1    Loboda, A.2    Ens, W.3    Schraven, B.4    Standing, K.G.5
  • 3
    • 0037444512 scopus 로고    scopus 로고
    • Fast-response proteomics by accelerated in-gel digestion of proteins
    • Havlis, J., Thomas, H., Sebela, M. & Shevchenko, A. Fast-response proteomics by accelerated in-gel digestion of proteins. Anal. Chem. 75, 1300-1306 (2003).
    • (2003) Anal. Chem , vol.75 , pp. 1300-1306
    • Havlis, J.1    Thomas, H.2    Sebela, M.3    Shevchenko, A.4
  • 4
    • 2642569251 scopus 로고    scopus 로고
    • Absolute quantification of proteins in solutions and in polyacrylamide gels by mass spectrometry
    • Havlis, J. & Shevchenko, A. Absolute quantification of proteins in solutions and in polyacrylamide gels by mass spectrometry. Anal. Chem. 76, 3029-3036 (2004).
    • (2004) Anal. Chem , vol.76 , pp. 3029-3036
    • Havlis, J.1    Shevchenko, A.2
  • 5
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. & Mann, M. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858 (1996).
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 6
    • 0035384687 scopus 로고    scopus 로고
    • 18O labeling for comparative proteomics: Model studies with two serotypes of adenovirus
    • 18O labeling for comparative proteomics: Model studies with two serotypes of adenovirus. Anal. Chem. 73, 2836-2842 (2001).
    • (2001) Anal. Chem , vol.73 , pp. 2836-2842
    • Yao, X.1    Freas, A.2    Ramirez, J.3    Demirev, P.A.4    Fenselau, C.5
  • 7
    • 0035884102 scopus 로고    scopus 로고
    • Evaluation of the efficiency of in-gel digestion of proteins by peptide isotopic labeling and MALDI mass spectrometry
    • Shevchenko, A. & Shevchenko, A. Evaluation of the efficiency of in-gel digestion of proteins by peptide isotopic labeling and MALDI mass spectrometry. Anal. Biochem. 296, 279-283 (2001).
    • (2001) Anal. Biochem , vol.296 , pp. 279-283
    • Shevchenko, A.1    Shevchenko, A.2
  • 8
    • 34548862160 scopus 로고    scopus 로고
    • 18O labeled isotopic clusters
    • in the press
    • 18O labeled isotopic clusters. Mol. Cell Proteomics in the press (2006).
    • (2006) Mol. Cell Proteomics
    • Mason, C.J.1
  • 9
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S.E. et al. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell Proteomics 1, 376-386 (2002).
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1
  • 10
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong, S.-E. & Mann, M. A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat. Protocols 1, 2650-2660 (2006).
    • (2006) Nat. Protocols , vol.1 , pp. 2650-2660
    • Ong, S.-E.1    Mann, M.2
  • 11
    • 0033649230 scopus 로고    scopus 로고
    • De novo peptide sequencing by nanoelectrospray tandem mass spectrometry using triple quadrupole and quadrupole/time-of-flight instruments
    • Shevchenko, A., Chernushevich, I., Wilm, M. & Mann, M. De novo peptide sequencing by nanoelectrospray tandem mass spectrometry using triple quadrupole and quadrupole/time-of-flight instruments. Methods Mol. Biol. 146, 1-16 (2000).
    • (2000) Methods Mol. Biol , vol.146 , pp. 1-16
    • Shevchenko, A.1    Chernushevich, I.2    Wilm, M.3    Mann, M.4
  • 12
    • 0037317228 scopus 로고    scopus 로고
    • Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • Rappsilber, J., Ishihama, Y. & Mann, M. Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics. Anal. Chem. 75, 663-670 (2003).
    • (2003) Anal. Chem , vol.75 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 13
    • 0030960366 scopus 로고    scopus 로고
    • Rapid "de novo" peptide sequencing by a combination of nanoelectrospray, isotopic labelling and a quadrupole/ time-of-flight mass spectrometer
    • Shevchenko, A. et al. Rapid "de novo" peptide sequencing by a combination of nanoelectrospray, isotopic labelling and a quadrupole/ time-of-flight mass spectrometer. Rapid Commun. Mass Spectrom. 11, 1015-1024 (1997).
    • (1997) Rapid Commun. Mass Spectrom , vol.11 , pp. 1015-1024
    • Shevchenko, A.1
  • 14
    • 0001092477 scopus 로고    scopus 로고
    • Nanoelectrospray tandem mass spectrometry and sequence similarity searching for identification of proteins from organisms with unknown genomes
    • Shevchenko, A., Sunyaev, S., Liska, A. & Bork, P. Nanoelectrospray tandem mass spectrometry and sequence similarity searching for identification of proteins from organisms with unknown genomes. Methods Mol. Biol. 211, 221-234 (2003).
    • (2003) Methods Mol. Biol , vol.211 , pp. 221-234
    • Shevchenko, A.1    Sunyaev, S.2    Liska, A.3    Bork, P.4
  • 15
    • 2442513210 scopus 로고    scopus 로고
    • Dried-droplet probe preparation on AnchorChip targets for navigating the acquisition of matrixassisted laser desorption/ionization time-of-flight spectra by fluorescence of matrix/analyte crystals
    • Thomas, H., Havlis, J., Peychl, J. & Shevchenko, A. Dried-droplet probe preparation on AnchorChip targets for navigating the acquisition of matrixassisted laser desorption/ionization time-of-flight spectra by fluorescence of matrix/analyte crystals. Rapid Commun. Mass Spectrom. 18, 923-930 (2004).
    • (2004) Rapid Commun. Mass Spectrom , vol.18 , pp. 923-930
    • Thomas, H.1    Havlis, J.2    Peychl, J.3    Shevchenko, A.4
  • 16
    • 33748294162 scopus 로고    scopus 로고
    • Rapid validation of protein identifications with the borderline statistical confidence via de novo sequencing and MS BLAST searches
    • Wielsch, N. et al. Rapid validation of protein identifications with the borderline statistical confidence via de novo sequencing and MS BLAST searches. J. Proteome Res. 5, 2448-2456 (2006).
    • (2006) J. Proteome Res , vol.5 , pp. 2448-2456
    • Wielsch, N.1
  • 17
    • 17844401751 scopus 로고    scopus 로고
    • SUMO modification of the ubiquitin-conjugating enzyme E2-25K
    • Pichler, A. et al. SUMO modification of the ubiquitin-conjugating enzyme E2-25K. Nat. Struct. Mol. Biol. 12, 264-269 (2005).
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 264-269
    • Pichler, A.1
  • 18
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S.E. & Mann, M. Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 1, 252-262 (2005).
    • (2005) Nat. Chem. Biol , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 19
    • 33745591083 scopus 로고    scopus 로고
    • Status of complete proteome analysis by mass spectrometry: SILAC labeled yeast as a model system
    • de Godoy, L.M. et al. Status of complete proteome analysis by mass spectrometry: SILAC labeled yeast as a model system. Genome Biol. 7, R50 (2006).
    • (2006) Genome Biol , vol.7
    • de Godoy, L.M.1
  • 20
    • 0344212101 scopus 로고    scopus 로고
    • An improved method for tracking and reducing the void volume in nano HPLC-MS with micro trapping columns
    • Mitulovic, G. et al. An improved method for tracking and reducing the void volume in nano HPLC-MS with micro trapping columns. Anal. Bioanal. Chem. 376, 946-951 (2003).
    • (2003) Anal. Bioanal. Chem , vol.376 , pp. 946-951
    • Mitulovic, G.1
  • 21
    • 33744454670 scopus 로고    scopus 로고
    • Thermostable trypsin conjugates for high-throughput proteomics: Synthesis and performance evaluation
    • Sebela, M. et al. Thermostable trypsin conjugates for high-throughput proteomics: Synthesis and performance evaluation. Proteomics 6, 2959-2963 (2006).
    • (2006) Proteomics , vol.6 , pp. 2959-2963
    • Sebela, M.1
  • 22
    • 4544370533 scopus 로고    scopus 로고
    • Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation
    • Olsen, J.V. & Mann, M. Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation. Proc. Natl. Acad. Sci. USA 101, 13417-13422 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13417-13422
    • Olsen, J.V.1    Mann, M.2
  • 23
    • 4444335470 scopus 로고    scopus 로고
    • The abc's (and xyz's) of peptide sequencing
    • Steen, H. & Mann, M. The abc's (and xyz's) of peptide sequencing. Nat. Rev. Mol. Cell Biol. 5, 699-711 (2004).
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 699-711
    • Steen, H.1    Mann, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.