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Volumn 1, Issue 6, 1999, Pages 702-711

Probing cellular complexity with proteomics

Author keywords

Cell map proteomics; Expression proteomics; Functional analysis; Interaction network; Mass spectrometry; Organelle; Protein complex

Indexed keywords

MESSENGER RNA;

EID: 0033384057     PISSN: 14648431     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (5)

References (55)
  • 1
    • 0031848226 scopus 로고    scopus 로고
    • Proteome and proteomics: New technologies, new concepts and new words
    • Anderson NL, Anderson NG: Proteome and proteomics: New technologies, new concepts and new words. Electrophoresis (1998) 19:1853-1861.
    • (1998) Electrophoresis , vol.19 , pp. 1853-1861
    • Anderson, N.L.1    Anderson, N.G.2
  • 3
    • 0032784646 scopus 로고    scopus 로고
    • Proteomics: Quantitative and physical mapping of cellular proteins
    • Blackstock WP, Weir MP: Proteomics: quantitative and physical mapping of cellular proteins. Trends Biotechnol (1999) 17:121-127.
    • (1999) Trends Biotechnol , vol.17 , pp. 121-127
    • Blackstock, W.P.1    Weir, M.P.2
  • 4
    • 0000009192 scopus 로고    scopus 로고
    • High-throughput gene expression analysis using SAGE
    • Bertelsen AH, Velculescu VE: High-throughput gene expression analysis using SAGE. Drug Disc Today (1998) 3:152-159.
    • (1998) Drug Disc Today , vol.3 , pp. 152-159
    • Bertelsen, A.H.1    Velculescu, V.E.2
  • 5
    • 0033200398 scopus 로고    scopus 로고
    • Expression profiling: DNA arrays in many guises
    • Granjeaud S, Bertucci F, Jordan BR: Expression profiling: DNA arrays in many guises. Bioessays (1999) 21(9):781-790.
    • (1999) Bioessays , vol.21 , Issue.9 , pp. 781-790
    • Granjeaud, S.1    Bertucci, F.2    Jordan, B.R.3
  • 7
  • 9
    • 0030669030 scopus 로고    scopus 로고
    • Exploring the metabolic and genetic control of gene expression on a genomic scale
    • DeRisi JL, Iyer VR, Brown PO: Exploring the metabolic and genetic control of gene expression on a genomic scale. Science (1997) 278:680-686.
    • (1997) Science , vol.278 , pp. 680-686
    • DeRisi, J.L.1    Iyer, V.R.2    Brown, P.O.3
  • 11
    • 0030895921 scopus 로고    scopus 로고
    • A comparison of selected mRNA and protein abundances in human liver
    • Anderson L, Seilhamer J: A comparison of selected mRNA and protein abundances in human liver. Electrophoresis (1997) 18:533-537.
    • (1997) Electrophoresis , vol.18 , pp. 533-537
    • Anderson, L.1    Seilhamer, J.2
  • 12
    • 0030603251 scopus 로고    scopus 로고
    • Expression profiles of active genes in human and mouse livers
    • Kawamoto S, Matsumoto Y, Mizuno K, Okubo K, Matsubara K: Expression profiles of active genes in human and mouse livers. Gene (1996) 174:151-158.
    • (1996) Gene , vol.174 , pp. 151-158
    • Kawamoto, S.1    Matsumoto, Y.2    Mizuno, K.3    Okubo, K.4    Matsubara, K.5
  • 13
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi SP, Rochon Y, Franza BR, Aebersold R: Correlation between protein and mRNA abundance in yeast. Mol Cell Biol (1999) 19(3):1720-1730.
    • (1999) Mol Cell Biol , vol.19 , Issue.3 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 14
    • 0033388033 scopus 로고    scopus 로고
    • From genome to function: Analysis of multi-protein complexes and protein phosphorylation
    • 199
    • Neubauer G, Wilm M: From genome to function: Analysis of multi-protein complexes and protein phosphorylation. Curr Opin Mol Ther (199) 1 (6):695-701
    • Curr Opin Mol Ther , vol.1 , Issue.6 , pp. 695-701
    • Neubauer, G.1    Wilm, M.2
  • 17
    • 0032923763 scopus 로고    scopus 로고
    • Technology development at the interface of proteome research and genomics: Mapping non-polymorphic proteins on the physical map of mouse chromosomes
    • Nock C, Gauss C, Schalkwyk LC, Klose J, Lehrach H, Himmelbauer H: Technology development at the interface of proteome research and genomics: Mapping non-polymorphic proteins on the physical map of mouse chromosomes. Electrophoresis (1999) 20:1027-1032
    • (1999) Electrophoresis , vol.20 , pp. 1027-1032
    • Nock, C.1    Gauss, C.2    Schalkwyk, L.C.3    Klose, J.4    Lehrach, H.5    Himmelbauer, H.6
  • 18
    • 0033040670 scopus 로고    scopus 로고
    • Five stages of the Human Genome Project
    • Strohman RC: Five stages of the Human Genome Project. Nature Biotechnol (1999) 17:112.
    • (1999) Nature Biotechnol , vol.17 , pp. 112
    • Strohman, R.C.1
  • 19
    • 0029020259 scopus 로고
    • Two-dimensional electrophoresis of proteins: An updated protocol and implications for a functional analysis of the genome
    • Klose J, Kobalz U: Two-dimensional electrophoresis of proteins: an updated protocol and implications for a functional analysis of the genome. Electrophoresis (1995) 16:1034-1059.
    • (1995) Electrophoresis , vol.16 , pp. 1034-1059
    • Klose, J.1    Kobalz, U.2
  • 20
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M: Mass spectrometric sequencing of proteins 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
  • 21
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu M, Morgan ME, Minden JS: Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis (1997) 18:2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 24
    • 0031127851 scopus 로고    scopus 로고
    • Cell biology and the genome projects - A concerted strategy for characterizing multiprotein complexes by using mass spectrometry
    • Lamond AI, Mann M: Cell biology and the genome projects - a concerted strategy for characterizing multiprotein complexes by using mass spectrometry. Trends Cell Biol (1997) 7:139-142.
    • (1997) Trends Cell Biol , vol.7 , pp. 139-142
    • Lamond, A.I.1    Mann, M.2
  • 25
    • 0032603342 scopus 로고    scopus 로고
    • Sample preparation methods for mass spectrometric peptide mapping directly from 2-DE gels
    • Link A (Ed), Humana Press, New Jersey
    • Jensen ON, Wilm M, Shevchenko A, Mann M: Sample preparation methods for mass spectrometric peptide mapping directly from 2-DE gels. In: Methods in Molecular Biology. Link A (Ed), Humana Press, New Jersey (1999):513-530.
    • (1999) Methods in Molecular Biology , pp. 513-530
    • Jensen, O.N.1    Wilm, M.2    Shevchenko, A.3    Mann, M.4
  • 26
    • 0031298696 scopus 로고    scopus 로고
    • Identification of the components of simple protein mixtures by high-accuracy peptide mass mapping and database searching
    • Jensen ON, Podtelejnikov AV, Mann M: Identification of the components of simple protein mixtures by high-accuracy peptide mass mapping and database searching. Anal Chem (1997) 69:4741-4750.
    • (1997) Anal Chem , vol.69 , pp. 4741-4750
    • Jensen, O.N.1    Podtelejnikov, A.V.2    Mann, M.3
  • 28
    • 0029685702 scopus 로고    scopus 로고
    • Analytical properties of the nanoelectrospray ion source
    • Wilm M, Mann M: Analytical properties of the nanoelectrospray ion source. Anal Chem (1996) 68:1-8.
    • (1996) Anal Chem , vol.68 , pp. 1-8
    • Wilm, M.1    Mann, M.2
  • 29
    • 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) 66:4390-4399.
    • (1994) Anal Chem , vol.66 , pp. 4390-4399
    • Mann, M.1    Wilm, M.2
  • 30
    • 0032603760 scopus 로고    scopus 로고
    • Peptide sequencing of 2DE gel-isolated proteins by nanoelectrospray tandem mass spectrometry
    • Link A (Ed), Humana Press, New Jersey
    • Jensen ON, Wilm M, Shevchenko A, Mann M: Peptide sequencing of 2DE gel-isolated proteins by nanoelectrospray tandem mass spectrometry. In: Methods in Molecular Biology. Link A (Ed), Humana Press, New Jersey (1999):571-588.
    • (1999) Methods in Molecular Biology , pp. 571-588
    • Jensen, O.N.1    Wilm, M.2    Shevchenko, A.3    Mann, M.4
  • 31
    • 0032612351 scopus 로고    scopus 로고
    • Automated protein identification using microcolumn liquid chromatography-tandem mass spectrometry
    • Link A (Ed), Humana Press, New Jersey
    • Yates JR, Carmack E, Hays L, Link AJ: Automated protein identification using microcolumn liquid chromatography-tandem mass spectrometry. In: Methods in Molecular Biology. Link A (Ed), Humana Press, New Jersey (1999):553-569.
    • (1999) Methods in Molecular Biology , pp. 553-569
    • Yates, J.R.1    Carmack, E.2    Hays, L.3    Link, A.J.4
  • 32
    • 0033168122 scopus 로고    scopus 로고
    • Identification of proteins in complexes by solid-phase microextraction/multistep elution/capillary electrophoresis/tandem mass spectrometry
    • Tong W, Link A, Eng JK, Yates JR: Identification of proteins in complexes by solid-phase microextraction/multistep elution/capillary electrophoresis/tandem mass spectrometry. Anal Chem (1999) 71:2270-2278.
    • (1999) Anal Chem , vol.71 , pp. 2270-2278
    • Tong, W.1    Link, A.2    Eng, J.K.3    Yates, J.R.4
  • 33
    • 0032402208 scopus 로고    scopus 로고
    • A microscale electrospray interface incorporating a monolithic poly(styrene-divinylbenzene) support for on-line liquid chromatography/tandem mass spectrometry analysis of peptides and proteins
    • Moore RE, Licklider L, Schumann D, Lee TD: A microscale electrospray interface incorporating a monolithic poly(styrene-divinylbenzene) support for on-line liquid chromatography/tandem mass spectrometry analysis of peptides and proteins. Anal Chem (1998) 70:4879-4884.
    • (1998) Anal Chem , vol.70 , pp. 4879-4884
    • Moore, R.E.1    Licklider, L.2    Schumann, D.3    Lee, T.D.4
  • 35
    • 0032930639 scopus 로고    scopus 로고
    • Mapping of phosphorylation sites of gel-isolated proteins by nanoelectrospray tandem mass spectrometry: Potentials and limitations
    • Neubauer G, Mann M: Mapping of phosphorylation sites of gel-isolated proteins by nanoelectrospray tandem mass spectrometry: potentials and limitations. Anal Chem (1999) 71:235-242.
    • (1999) Anal Chem , vol.71 , pp. 235-242
    • Neubauer, G.1    Mann, M.2
  • 37
    • 0033535961 scopus 로고    scopus 로고
    • Accurate quantitation of protein expression and site-specific phosphorylation
    • Oda Y, Huang K, Cross FR, Cowburn D, Chait BT: Accurate quantitation of protein expression and site-specific phosphorylation. Proc Natl Acad Sci USA (1999) 96:6591-6596.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6591-6596
    • Oda, Y.1    Huang, K.2    Cross, F.R.3    Cowburn, D.4    Chait, B.T.5
  • 38
    • 0030960366 scopus 로고    scopus 로고
    • Rapid 'de novo' peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer
    • Shevchenko A, Chemushevich I, Ens W, Standing KG, Thomson B, Wilm M, Mann M: Rapid 'de novo' peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer. Rapid Commun Mass Spectrom (1997) 11:1015-1024.
    • (1997) Rapid Commun Mass Spectrom , vol.11 , pp. 1015-1024
    • Shevchenko, A.1    Chemushevich, I.2    Ens, W.3    Standing, K.G.4    Thomson, B.5    Wilm, M.6    Mann, M.7
  • 39
    • 0032535467 scopus 로고    scopus 로고
    • Modification of cysteine residues by alkylation. A tool in peptide mapping and protein identification
    • Sechi S, Chait BT: Modification of cysteine residues by alkylation. A tool in peptide mapping and protein identification. Anal Chem (1998) 70:5150-5158.
    • (1998) Anal Chem , vol.70 , pp. 5150-5158
    • Sechi, S.1    Chait, B.T.2
  • 40
    • 0033569552 scopus 로고    scopus 로고
    • Biosequence exegesis.
    • Boguski MS: Biosequence exegesis. (1999) Science 286:453-455.
    • (1999) Science , vol.286 , pp. 453-455
    • Boguski, M.S.1
  • 44
    • 0032504104 scopus 로고    scopus 로고
    • A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation
    • Grant PA, Schieltz D, Pray-Grant MG, Steger DJ, Reese JC, Yates JR, Workman JL: A subset of TAF(II)s are integral components of the SAGA complex required for nucleosome acetylation and transcriptional stimulation. Cell (1998) 94:45-53.
    • (1998) Cell , vol.94 , pp. 45-53
    • Grant, P.A.1    Schieltz, D.2    Pray-Grant, M.G.3    Steger, D.J.4    Reese, J.C.5    Yates, J.R.6    Workman, J.L.7
  • 45
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut G, Shevchenko A, Rutz B, Wilm M, Mann M, Séraphin B: A generic protein purification method for protein complex characterization and proteome exploration. Nature Biotechnol (1999) 17:1030-1032.
    • (1999) Nature Biotechnol , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Séraphin, B.6
  • 46
    • 0032511150 scopus 로고    scopus 로고
    • An ESP1/PDS1 complex regulates loss of sister chromatid cohesion at the metaphase to anaphase transition in yeast
    • Ciosk R, Zachariae W, Michaelis C, Shevchenko A, Mann M, Nasmyth K: An ESP1/PDS1 complex regulates loss of sister chromatid cohesion at the metaphase to anaphase transition in yeast. Cell (1998) 93:1067-1076.
    • (1998) Cell , vol.93 , pp. 1067-1076
    • Ciosk, R.1    Zachariae, W.2    Michaelis, C.3    Shevchenko, A.4    Mann, M.5    Nasmyth, K.6
  • 47
    • 0032404491 scopus 로고    scopus 로고
    • The impact of two-hybrid and related methods on biotechnology
    • Colas P, Brent R: The impact of two-hybrid and related methods on biotechnology. Trends Biotechnol (1998) 16:355-363.
    • (1998) Trends Biotechnol , vol.16 , pp. 355-363
    • Colas, P.1    Brent, R.2
  • 48
    • 0033557224 scopus 로고    scopus 로고
    • Yeast forward and reverse 'n'-hybrid systems
    • Vidai M, Legrain P: Yeast forward and reverse 'n'-hybrid systems. Nucleic Acids Res (1999) 27:919-929.
    • (1999) Nucleic Acids Res , vol.27 , pp. 919-929
    • Vidai, M.1    Legrain, P.2
  • 49
    • 0030963019 scopus 로고    scopus 로고
    • Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens
    • Fromont-Racine M, Rain JC, Legrain P: Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens. Nature Genet (1997) 16:277-282.
    • (1997) Nature Genet , vol.16 , pp. 277-282
    • Fromont-Racine, M.1    Rain, J.C.2    Legrain, P.3
  • 50
    • 0031029388 scopus 로고    scopus 로고
    • Identification of the proteins of the yeast U1 small nuclear ribonucleoprotein complex by mass spectrometry
    • Neubauer G, Gottschalk A, Fabrizio P, Seraphin B, Luhrmann R, Mann M: Identification of the proteins of the yeast U1 small nuclear ribonucleoprotein complex by mass spectrometry. Proc Natl Acad Sci USA (1997) 94:385-390.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 385-390
    • Neubauer, G.1    Gottschalk, A.2    Fabrizio, P.3    Seraphin, B.4    Luhrmann, R.5    Mann, M.6
  • 51
    • 0031750102 scopus 로고    scopus 로고
    • Analysis of the Saccharomyces spindle pole by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry
    • Wigge PA, Jensen ON, Holmes S, Soues S, Mann M, Kilmartin JV: Analysis of the Saccharomyces spindle pole by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. J Cell Biol (1998) 141:967-977.
    • (1998) J Cell Biol , vol.141 , pp. 967-977
    • Wigge, P.A.1    Jensen, O.N.2    Holmes, S.3    Soues, S.4    Mann, M.5    Kilmartin, J.V.6
  • 53
    • 0031417668 scopus 로고    scopus 로고
    • Identification of components of trans-Golgi network-derived transport vesicles and detergent-insoluble complexes by nanoelectrospray tandem mass spectrometry
    • Shevchenko A, Keller P, Scheiffele P, Mann M, Simons K: Identification of components of trans-Golgi network-derived transport vesicles and detergent-insoluble complexes by nanoelectrospray tandem mass spectrometry. Electrophoresis (1997) 18:2591-2600.
    • (1997) Electrophoresis , vol.18 , pp. 2591-2600
    • Shevchenko, A.1    Keller, P.2    Scheiffele, P.3    Mann, M.4    Simons, K.5
  • 54
    • 0031956851 scopus 로고    scopus 로고
    • Exploring the mechanisms of antigen processing by cell fractionation
    • Pierre P, Mellman I: Exploring the mechanisms of antigen processing by cell fractionation. Curr Opin Immunol (1998) 10:145-153.
    • (1998) Curr Opin Immunol , vol.10 , pp. 145-153
    • Pierre, P.1    Mellman, I.2
  • 55
    • 0030817279 scopus 로고    scopus 로고
    • RNA-peptide fusions for the in vitro selection of peptides and proteins
    • Roberts RW, Szostak JW: RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc Natl Acad Sci USA (1997) 94:12297-12302.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12297-12302
    • Roberts, R.W.1    Szostak, J.W.2


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