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Volumn 10, Issue 1, 1999, Pages 16-21

2D protein electrophoresis: Can it be perfected?

Author keywords

[No Author keywords available]

Indexed keywords

DIAGNOSTIC TEST; DRUG DEVELOPMENT; DRUG INDUSTRY; GENE EXPRESSION; HUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; REVIEW; TWO DIMENSIONAL GEL ELECTROPHORESIS;

EID: 0032948126     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(99)80004-4     Document Type: Article
Times cited : (156)

References (40)
  • 3
    • 0003445692 scopus 로고    scopus 로고
    • M.R. Wilkins, K.L. Williams, R.D. Appel, & D.F. Hochstrasser. Berlin: Springer Verlag. Perhaps the most comprehensive compendium of proteome data published so far. It describes the elements of proteome technology, points towards future developments, and highlights areas of research where proteomic technologies are making an impact.
    • Wilkins MR, Williams KL, Appel RD, Hochstrasser DF Proteomic Research: New Frontiers in Functional Genomics (Principles and Practice). 1997;Springer Verlag, Berlin. Perhaps the most comprehensive compendium of proteome data published so far. It describes the elements of proteome technology, points towards future developments, and highlights areas of research where proteomic technologies are making an impact.
    • (1997) Proteomic Research: New Frontiers in Functional Genomics (Principles and Practice)
  • 4
    • 0003359642 scopus 로고    scopus 로고
    • Strategies in Proteome Research
    • This special issue of Electrophoresis gives an overall perspective of the potential and limitations of the proteome technology. It includes some applications of the technology in cell biology.
    • Williams KL Strategies in Proteome Research. In Electrophoresis. 19:1998;1853-2050. This special issue of Electrophoresis gives an overall perspective of the potential and limitations of the proteome technology. It includes some applications of the technology in cell biology.
    • (1998) In Electrophoresis , vol.19 , pp. 1853-2050
    • Williams, K.L.1
  • 5
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell PH High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 250:1975;4007-4021.
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 6
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell PZ, Goodman HM, O'Farrell PH High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell. 12:1977;1133-1141.
    • (1977) Cell , vol.12 , pp. 1133-1141
    • O'Farrell, P.Z.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 7
    • 0016637146 scopus 로고
    • Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues. A novel approach to testing for induced point mutations in mammals
    • Klose J Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues. A novel approach to testing for induced point mutations in mammals. Humangenetik. 26:1975;231-243.
    • (1975) Humangenetik , vol.26 , pp. 231-243
    • Klose, J.1
  • 9
    • 0031848226 scopus 로고    scopus 로고
    • Proteome and proteomics: New technologies, new concepts, and new words
    • An overview of the beginning of the proteomic field, previously called 'Molecular Anatomy Programme'. In additon, it emphasizes the need for comprehensive quantitative studies of reasonably large datasets.
    • Anderson NL, Anderson NG Proteome and proteomics: new technologies, new concepts, and new words. Electrophoresis. 19:1998;1853-1861. An overview of the beginning of the proteomic field, previously called 'Molecular Anatomy Programme'. In additon, it emphasizes the need for comprehensive quantitative studies of reasonably large datasets.
    • (1998) Electrophoresis , vol.19 , pp. 1853-1861
    • Anderson, N.L.1    Anderson, N.G.2
  • 10
    • 0031848227 scopus 로고    scopus 로고
    • The Australian Proteome Analysis Facility (APAF): Assembling large scale proteomics through integration and automation
    • This paper describes the setting-up of a national core facility for high-throughput proteomics studies. Examples of human tears and Dictiostelium discoideum are given.
    • Walsh BJ, Molloy MP, Williams KL The Australian Proteome Analysis Facility (APAF): assembling large scale proteomics through integration and automation. Electrophoresis. 19:1998;1883-1890. This paper describes the setting-up of a national core facility for high-throughput proteomics studies. Examples of human tears and Dictiostelium discoideum are given.
    • (1998) Electrophoresis , vol.19 , pp. 1883-1890
    • Walsh, B.J.1    Molloy, M.P.2    Williams, K.L.3
  • 11
    • 0031776341 scopus 로고    scopus 로고
    • Proteomics: Key technology in drug discovery
    • Celis JE Proteomics: key technology in drug discovery. Drug Discov Today. 3:1998;193-195.
    • (1998) Drug Discov Today , vol.3 , pp. 193-195
    • Celis, J.E.1
  • 13
    • 0344536990 scopus 로고    scopus 로고
    • J.E. Celis, N. Carter, T. Hunter, D. Shotton, K. Simons, & J.V. Small. New York: Academic Press
    • Celis JE, Carter N, Hunter T, Shotton D, Simons K, Small JV Cell Biology: A laboratory Handbook, vol 4, edn 2. 1997;Academic Press, New York.
    • (1997) Cell Biology: A Laboratory Handbook, Vol 4, Edn 2.
  • 14
    • 0023008914 scopus 로고
    • Electroblotting onto activated glass. High efficiency preparation of proteins from analytical sodium dodecyl sulfate-polyacrylamide gels for direct sequence analysis
    • Aebersold RH, Teplow DB, Hood LE, Kent SB Electroblotting onto activated glass. High efficiency preparation of proteins from analytical sodium dodecyl sulfate-polyacrylamide gels for direct sequence analysis. J Biol Chem. 261:1986;4229-4238.
    • (1986) J Biol Chem , vol.261 , pp. 4229-4238
    • Aebersold, R.H.1    Teplow, D.B.2    Hood, L.E.3    Kent, S.B.4
  • 15
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem. 262:1987;10035-10038.
    • (1987) J Biol Chem , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 17
    • 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. 66:1994;4390-4399.
    • (1994) Anal Chem , vol.66 , pp. 4390-4399
    • Mann, M.1    Wilm, M.2
  • 18
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates JR, Eng JK, McCormack AL, Schieltz D Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal Chem. 67:1995;1426-1436.
    • (1995) Anal Chem , vol.67 , pp. 1426-1436
    • Yates, J.R.1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 19
    • 53249145476 scopus 로고    scopus 로고
    • Peptide sequencing by mass spectrometry for homology searches and cloning genes
    • The authors describe how to sequence peptide fragments from proteins recovered from gels using mass spectrometry at the low picomole to fentomole levels.
    • Schevchenko A, Wilm M, Mann M Peptide sequencing by mass spectrometry for homology searches and cloning genes. J Protein Chem. 16:1997;481-490. The authors describe how to sequence peptide fragments from proteins recovered from gels using mass spectrometry at the low picomole to fentomole levels.
    • (1997) J Protein Chem , vol.16 , pp. 481-490
    • Schevchenko, A.1    Wilm, M.2    Mann, M.3
  • 20
    • 0343406659 scopus 로고    scopus 로고
    • Determination of antibody specificity by Western blotting and immunoprecipitation
    • J.E. Celis, N. Carter, T. Hunter, K. Simons, & J.V. Small. New York: Academic Press
    • Celis JE, Lauridsen JB, Basse B Determination of antibody specificity by Western blotting and immunoprecipitation. Celis JE, Carter N, Hunter T, Simons K, Small JV. Cell Biology: A Laboratory Handbook, edn 2. 1997;429-438 Academic Press, New York.
    • (1997) Cell Biology: A Laboratory Handbook, Edn 2. , pp. 429-438
    • Celis, J.E.1    Lauridsen, J.B.2    Basse, B.3
  • 23
    • 0020085946 scopus 로고
    • How many proteins are there in a typical mammalian cell?
    • Duncan R, McConkey EH How many proteins are there in a typical mammalian cell? Clin Chem. 28:1982;749-755.
    • (1982) Clin Chem , vol.28 , pp. 749-755
    • Duncan, R.1    McConkey, E.H.2
  • 24
    • 0025763235 scopus 로고
    • Human cellular protein patterns and their link to genome DNA sequence data: Usefulness of two-dimensional gel electrophoresis and microsequencing
    • Celis JE, Rasmussen HH, Leffers H, Madsen P, Honore B, Gesser B, Dejgaard K, Vandekerckhove J Human cellular protein patterns and their link to genome DNA sequence data: usefulness of two-dimensional gel electrophoresis and microsequencing. FASEB J. 5:1991;2200-2208.
    • (1991) FASEB J , vol.5 , pp. 2200-2208
    • Celis, J.E.1    Rasmussen, H.H.2    Leffers, H.3    Madsen, P.4    Honore, B.5    Gesser, B.6    Dejgaard, K.7    Vandekerckhove, J.8
  • 26
    • 0003445692 scopus 로고    scopus 로고
    • The importance of protein co- And post-translational modifications in proteome projects
    • M.R. Wilkins, K.L. Williams, R.D. Appel, & D.F. Hochstrasser. Berlin: Springer Verlag. This overviews post-translational modifications and outlines important features that distinguish proteomic from genomic projects. It also describes procedures to determine the nature and localization of the modifications.
    • Gooley AA, Packer NH The importance of protein co- and post-translational modifications in proteome projects. Wilkins MR, Williams KL, Appel RD, Hochstrasser DF Proteome Research: New Frontiers in Functional Genomics (Principles and Practice). 1997;Springer Verlag, Berlin. This overviews post-translational modifications and outlines important features that distinguish proteomic from genomic projects. It also describes procedures to determine the nature and localization of the modifications.
    • (1997) Proteome Research: New Frontiers in Functional Genomics (Principles and Practice)
    • Gooley, A.A.1    Packer, N.H.2
  • 28
    • 0023768475 scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Görg A, Postel W, Gunther S The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis. 9:1988;531-546.
    • (1988) Electrophoresis , vol.9 , pp. 531-546
    • Görg, A.1    Postel, W.2    Gunther, S.3
  • 29
    • 0030736779 scopus 로고    scopus 로고
    • Isoelectric focusing in immobilised pH gradients: An update
    • A review of the latest developments on isoelectric focusing in immobilised pH gradients; it highlights the advantages of combining this technique with SDS-PAGE to obtain a high resolution gel separation procedure.
    • Righetti PG, Bossi A Isoelectric focusing in immobilised pH gradients: an update. J Chromatogr B Biomed Sci Appl. 699:1997;77-89. A review of the latest developments on isoelectric focusing in immobilised pH gradients; it highlights the advantages of combining this technique with SDS-PAGE to obtain a high resolution gel separation procedure.
    • (1997) J Chromatogr B Biomed Sci Appl , vol.699 , pp. 77-89
    • Righetti, P.G.1    Bossi, A.2
  • 30
    • 0031837579 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of proteins in an immobilized pH 4-12 gradient
    • Görg A, Boguth G, Obermaier C, Weiss W Two-dimensional electrophoresis of proteins in an immobilized pH 4-12 gradient. Electrophoresis. 19:1998;1516-1519.
    • (1998) Electrophoresis , vol.19 , pp. 1516-1519
    • Görg, A.1    Boguth, G.2    Obermaier, C.3    Weiss, W.4
  • 31
    • 0031553992 scopus 로고    scopus 로고
    • Isoelectric focusing in immobilized pH gradients: Recent analytical and preparative developments
    • Righetti PG, Bossi A Isoelectric focusing in immobilized pH gradients: recent analytical and preparative developments. Anal Biochem. 247:1997;1-10.
    • (1997) Anal Biochem , vol.247 , pp. 1-10
    • Righetti, P.G.1    Bossi, A.2
  • 32
    • 0028302337 scopus 로고
    • Reference points for comparisons of two-dimensional maps of proteins from different human cell types defined in a pH scale where isoelectric points correlate with polypeptide compositions
    • Bjellqvist B, Basse B, Olsen E, Celis JE Reference points for comparisons of two-dimensional maps of proteins from different human cell types defined in a pH scale where isoelectric points correlate with polypeptide compositions. Electrophoresis. 15:1994;529-539.
    • (1994) Electrophoresis , vol.15 , pp. 529-539
    • Bjellqvist, B.1    Basse, B.2    Olsen, E.3    Celis, J.E.4
  • 33
    • 0031812473 scopus 로고    scopus 로고
    • Correlation of acidic and basic carrier ampholyte and immobilized pH gradient two-dimensional gel electrophoresis patterns based on mass spectrometric protein identification
    • A thorough comparison between yeast protein patterns obtained by using carrier ampholyte- and IPG-based 2D gel technology. It clearly emphasizes the need of using protein identification techniques (MALDI-MS) to assess the identity of polypeptides having similar coordinates, that is molecular weight and pI.
    • Nawrocki A, Larsen MR, Podtelejnikov AV, Jensen ON, Mann M, Roepstorff P, Görg A, Fey SJ, Larsen PM Correlation of acidic and basic carrier ampholyte and immobilized pH gradient two-dimensional gel electrophoresis patterns based on mass spectrometric protein identification. Electrophoresis. 19:1998;1024-1035. A thorough comparison between yeast protein patterns obtained by using carrier ampholyte- and IPG-based 2D gel technology. It clearly emphasizes the need of using protein identification techniques (MALDI-MS) to assess the identity of polypeptides having similar coordinates, that is molecular weight and pI.
    • (1998) Electrophoresis , vol.19 , pp. 1024-1035
    • Nawrocki, A.1    Larsen, M.R.2    Podtelejnikov, A.V.3    Jensen, O.N.4    Mann, M.5    Roepstorff, P.6    Görg, A.7    Fey, S.J.8    Larsen, P.M.9
  • 34
    • 0037563355 scopus 로고    scopus 로고
    • Very alkaline immobilised pH gradients for two-dimensional electrophoresis of ribosomal and nuclear proteins
    • HeLa, mouse liver ribosomes and chicken erythrocyte histones were separated using highly reproducible very alkaline pH gradients.
    • Görg A, Obermaier C, Boguth G, Csodas A, Diaz JJ, Madjar JJ Very alkaline immobilised pH gradients for two-dimensional electrophoresis of ribosomal and nuclear proteins. Electrophoresis. 18:1997;328-337. HeLa, mouse liver ribosomes and chicken erythrocyte histones were separated using highly reproducible very alkaline pH gradients.
    • (1997) Electrophoresis , vol.18 , pp. 328-337
    • Görg, A.1    Obermaier, C.2    Boguth, G.3    Csodas, A.4    Diaz, J.J.5    Madjar, J.J.6
  • 35
    • 0029020259 scopus 로고
    • Two-dimensional electrophoresis of proteins: An update protocol and implications for a functional analysis of the genome
    • Klose J, Kobalz U Two-dimensional electrophoresis of proteins: an update protocol and implications for a functional analysis of the genome. Electrophoresis. 16:1995;1034-1059.
    • (1995) Electrophoresis , vol.16 , pp. 1034-1059
    • Klose, J.1    Kobalz, U.2
  • 36
    • 0031571355 scopus 로고    scopus 로고
    • Two-dimensional analysis of recombinant E. coli proteins using capillary isoelectric focusing electrospray ionization mass spectrometry
    • Tang W, Harrata AK, Lee CS Two-dimensional analysis of recombinant E. coli proteins using capillary isoelectric focusing electrospray ionization mass spectrometry. Anal Chem. 69:1997;3177-3182.
    • (1997) Anal Chem , vol.69 , pp. 3177-3182
    • Tang, W.1    Harrata, A.K.2    Lee, C.S.3
  • 37
    • 0030957650 scopus 로고    scopus 로고
    • Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients
    • Detergents and chaotropes are used to improve the solubility and 2D gel resolution of membrane proteins.
    • Rabilloud T, Adessi C, Giraudel A, Lunardi J Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis. 18:1997;307-316. Detergents and chaotropes are used to improve the solubility and 2D gel resolution of membrane proteins.
    • (1997) Electrophoresis , vol.18 , pp. 307-316
    • Rabilloud, T.1    Adessi, C.2    Giraudel, A.3    Lunardi, J.4
  • 39
    • 0005125401 scopus 로고    scopus 로고
    • Blot overlay assay for identification of GTP-binding proteins
    • J.E. Celis, N. Carter, T. Hunter, D. Shotton, K. Simons, & J.V. Small. New York: Academic Press
    • Gromov P, Celis JE Blot overlay assay for identification of GTP-binding proteins. Celis JE, Carter N, Hunter T, Shotton D, Simons K, Small JV. Cell Biology: A Laboratory Handbook, edn 2. 1997;Academic Press, New York.
    • (1997) Cell Biology: A Laboratory Handbook, Edn 2.
    • Gromov, P.1    Celis, J.E.2
  • 40
    • 0030219531 scopus 로고    scopus 로고
    • Application of SYPRO orange and SYPRO red protein gel stains
    • Steinberg TH, Haugland RP, Singer VL Application of SYPRO orange and SYPRO red protein gel stains. Anal Biochem. 239:1996;238-245.
    • (1996) Anal Biochem , vol.239 , pp. 238-245
    • Steinberg, T.H.1    Haugland, R.P.2    Singer, V.L.3


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