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Volumn 13, Issue 1, 1996, Pages 19-50

Progress with proteome projects: Why all proteins expressed by a genome should be identified and how to do it

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; PROTEIN;

EID: 0030333694     PISSN: 02648725     EISSN: 20465556     Source Type: Journal    
DOI: 10.1080/02648725.1996.10647923     Document Type: Article
Times cited : (1035)

References (153)
  • 1
    • 0021602838 scopus 로고
    • Global approaches to quantitative analysis of gene-expression patterns observed by use of two-dimensional gel electrophoresis
    • Anderson, N. L., Hofmann, J. P., Gemmell, A. and Taylor, J. (1984). Global approaches to quantitative analysis of gene-expression patterns observed by use of two-dimensional gel electrophoresis. Clinical Chemistry, 30, 2031-2036.
    • (1984) Clinical Chemistry , vol.30 , pp. 2031-2036
    • Anderson, N.L.1    Hofmann, J.P.2    Gemmell, A.3    Taylor, J.4
  • 2
    • 0026351384 scopus 로고
    • A two-dimensional gel database of human plasma proteins
    • Anderson, N. L. and anderson, N. G. (1991). A two-dimensional gel database of human plasma proteins. Electrophoresis, 12, 883-906.
    • (1991) Electrophoresis , vol.12 , pp. 883-906
    • Anderson, N.L.1    Anderson, N.G.2
  • 3
    • 0026348925 scopus 로고
    • A two-dimensional gel database of rat liver proteins useful in gene regulation and drug effects studies
    • Anderson, N. L., Esquer-Blasco, R., Hofmann, J. P. and anderson, N. G. (1991). A two-dimensional gel database of rat liver proteins useful in gene regulation and drug effects studies. Electrophoresis. 12, 907-930.
    • (1991) Electrophoresis , vol.12 , pp. 907-930
    • Anderson, N.L.1    Esquer-Blasco, R.2    Hofmann, J.P.3    Anderson, N.G.4
  • 4
    • 77957181125 scopus 로고
    • Covalent protein modifications and gene expression changes in rodent liver following administration of methapyrilene: A study using two-dimensional electrophoresis
    • Anderson, N. L., Copple, D. C., Bendele, R. A., Probst, O. S., Richardson, F. C. (1992). Covalent protein modifications and gene expression changes in rodent liver following administration of methapyrilene: a study using two-dimensional electrophoresis. Fundamental and Applied Toxicology. 18, 570-580.
    • (1992) Fundamental and Applied Toxicology , vol.18 , pp. 570-580
    • Anderson, N.L.1    Copple, D.C.2    Bendele, R.A.3    Probst, O.S.4    Richardson, F.C.5
  • 5
    • 0028240897 scopus 로고
    • A new generation of information retrieval tools for biologists: The example of the expasy www server
    • Appel, R. D., Bairoch, A. and Hochstrasser, D. F. (1994). A new generation of information retrieval tools for biologists: the example of the ExPASy WWW server. Trends in Biochemical Sciences. 19, 258-260.
    • (1994) Trends in Biochemical Sciences , vol.19 , pp. 258-260
    • Appel, R.D.1    Bairoch, A.2    Hochstrasser, D.F.3
  • 9
    • 0028071564 scopus 로고
    • The swiss-prot protein sequence databank: Current status
    • Bairoch, A. and Boeckmann, B. (1994). The SWISS-PROT protein sequence databank: current status. Nucleic Acids Research. 22, 3578-3580.
    • (1994) Nucleic Acids Research , vol.22 , pp. 3578-3580
    • Bairoch, A.1    Boeckmann, B.2
  • 10
    • 0026471243 scopus 로고
    • A human myocardial two-dimensional electrophoresis database: Protein characterisation by microsequcncing and immunoblotting
    • Baker, C. S., Corbett, J. M., May, A. J., Yacoub, M. H. and Dunn, M. J. (1992). A human myocardial two-dimensional electrophoresis database: protein characterisation by microsequcncing and immunoblotting. Electrophoresis. 13, 723-726.
    • (1992) Electrophoresis , vol.13 , pp. 723-726
    • Baker, C.S.1    Corbett, J.M.2    May, A.J.3    Yacoub, M.H.4    Dunn, M.J.5
  • 12
    • 0027213851 scopus 로고
    • Identification of differentially expressed mrna species by an improved display technique (Ddrt-pcr)
    • Bauer, D., Muller, H., Reich, J., Rîedel, H., Ahrenkiel, V., Wartiioe, P. and Strauss, M. (1993). Identification of differentially expressed mRNA species by an improved display technique (DDRT-PCR). Nucleic Acids Research. 21, 4272-4280.
    • (1993) Nucleic Acids Research , vol.21 , pp. 4272-4280
    • Bauer, D.1    Muller, H.2    Reich, J.3    Rîedel, H.4    Ahrenkiel, V.5    Wartiioe, P.6    Strauss, M.7
  • 14
    • 0028940587 scopus 로고
    • Gene number, noise reduction and biological complexity
    • Bird, A. P. (1995). Gene number, noise reduction and biological complexity. Trends in dene tics. 11, 94-100.
    • (1995) Trends in Dene Tics , vol.11 , pp. 94-100
    • Bird, A.P.1
  • 16
    • 0027763435 scopus 로고
    • A nonlinear wide-range immobilized ph gradient for two-dimensional electrophoresis and its definition in a relevant ph scale
    • Bjellqvist, B., Pasquall C., Ravier, F., Sanchez, J-C. and Hochstrasser, D. F. (1993a). A nonlinear wide-range immobilized pH gradient for two-dimensional electrophoresis and its definition in a relevant pH scale. Electrophoresis, 14, 1357-1365.
    • (1993) Electrophoresis , vol.14 , pp. 1357-1365
    • Bjellqvist, B.1    Pasquall, C.2    Ravier, F.3    Sanchez, J.-C.4    Hochstrasser, D.F.5
  • 19
    • 0016203040 scopus 로고
    • A film detection method for tritium-labeled proteins and nucleic acids in polyacrylamide geis
    • Bonner, W. M. and Laskey, R. A. (1974). A film detection method for tritium-labeled proteins and nucleic acids in polyacrylamide geis. European Journal of Biochemistry. 46, 83-88.
    • (1974) European Journal of Biochemistry , vol.46 , pp. 83-88
    • Bonner, W.M.1    Laskey, R.A.2
  • 20
    • 0028131467 scopus 로고
    • Ref52 on global gel navigator: An internet-accessible two-dimensional gel electrophoresis database
    • Boutfell, T., Garrels, J. I., Franza, B. R., Monardo, P. J. and Laïter, G. I. (1994). REF52 on global gel navigator: an internet-accessible two-dimensional gel electrophoresis database. Electrophoresis. 15, 1487-1490.
    • (1994) Electrophoresis , vol.15 , pp. 1487-1490
    • Boutfell, T.1    Garrels, J.I.2    Franza, B.R.3    Monardo, P.J.4    Laïter, G.I.5
  • 22
    • 0027462384 scopus 로고
    • Selective identification and differentiation of n-and o-linked oligosaccharides in glycoproteins by liquid chromatography-mass spectrometry
    • Carr, S. A., Huddleston, M. J. and Bean, M. F. (1993). Selective identification and differentiation of N-and O-linked oligosaccharides in glycoproteins by liquid chromatography-mass spectrometry. Protein Science. 2, 183-196.
    • (1993) Protein Science , vol.2 , pp. 183-196
    • Carr, S.A.1    Huddleston, M.J.2    Bean, M.F.3
  • 23
    • 0020643575 scopus 로고
    • Staining of the ca:+ binding proteins, ealseque. Sterin. Calmodulin, troponin c. And s-100, with the cationic dye slains-ali'
    • Campbell, K. P., Maclennan, D. H. and Jorgensen, A. O. (1983). Staining of the Ca:+ binding proteins, ealseque. sterin. calmodulin, troponin C. and S-100, with the cationic dye Slains-ali'. Journal of Biological Chemistry, 258, 11267-11273.
    • (1983) Journal of Biological Chemistry , vol.258 , pp. 11267-11273
    • Campbell, K.P.1    Maclennan, D.H.2    Jorgensen, A.O.3
  • 24
    • 0025328253 scopus 로고
    • A two-dimensional gel protein database of noncultured total normal human epidermal keratinocytes: Identification of proteins strongly up-regulated in psoriatic epidermis
    • Celis, J. E., Cruger, D., Km, J., Dejgarrd, K., Lauridsen, J. B., Ratz, G. P., Bassi, G., Celis, A., Rasmussen, U. M., Bauw, G. and Vandekerkiiove, J. (1990a). A two-dimensional gel protein database of noncultured total normal human epidermal keratinocytes: identification of proteins strongly up-regulated in psoriatic epidermis. Electrophoresis, 11, 242-254.
    • (1990) Electrophoresis , vol.11 , pp. 242-254
    • Celis, J.E.1    Cruger, D.2    Km, J.3    Dejgarrd, K.4    Lauridsen, J.B.5    Ratz, G.P.6    Bassi, G.7    Celis, A.8    Rasmussen, U.M.9    Bauw, G.10    Vandekerkiiove, J.11
  • 27
    • 0028302333 scopus 로고
    • A qualitative and quantitative protein database approach identified individual and groups of functionally related proteins that are differentially regulated in simian virus 40 (Sv40) transformed human keratinocytes: An overview of the functional changes associated with the transformed phenotype
    • Celis, J. E. and Olsen, E. (1994). A qualitative and quantitative protein database approach identified individual and groups of functionally related proteins that are differentially regulated in simian virus 40 (SV40) transformed human keratinocytes: an overview of the functional changes associated with the transformed phenotype. Electrophoresis. 15, 309-344.
    • (1994) Electrophoresis , vol.15 , pp. 309-344
    • Celis, J.E.1    Olsen, E.2
  • 28
    • 0027992574 scopus 로고
    • Positional reproducibility of protein spots in two-dimsensional polyacrylamide electrophoresis using immobilzed ph gradient isolelectric focusing in the first dimension-an interlaboratory comparison
    • Corliett, J. M., Dunn, M. J., Posch, A. and Görg, A. (1994a). Positional reproducibility of protein spots in two-dimsensional polyacrylamide electrophoresis using immobilzed pH gradient isolelectric focusing in the first dimension-an interlaboratory comparison. Electrophoresis. 15, 1205-1211.
    • (1994) Electrophoresis , vol.15 , pp. 1205-1211
    • Corliett, J.M.1    Dunn, M.J.2    Posch, A.3    Görg, A.4
  • 29
    • 0027940134 scopus 로고
    • The human myocardial two-dimensional gel protein database: Update 1994
    • Corbett, J. M., Wheeler, C. H., Baker, C. S., Yacouu, M. H. and Dunn, M. J. (1994b). The human myocardial two-dimensional gel protein database: update 1994. Electrophoresis. 15, 1459-1465.
    • (1994) Electrophoresis , vol.15 , pp. 1459-1465
    • Corbett, J.M.1    Wheeler, C.H.2    Baker, C.S.3    Yacouu, M.H.4    Dunn, M.J.5
  • 30
    • 0028917303 scopus 로고
    • Cross-species identification of proteins separated by two-dimensional electrophoresis using maldi-tof and amino acid composition
    • Cordwell, S., Wilkins, M. R., Cerpa-Poijak, A., Gooley, A. A., Duncan, M., Williams, K. L. and Humphery-Smith, I. (1995). Cross-species identification of proteins separated by two-dimensional electrophoresis using MALDI-TOF and amino acid composition. Electrophoresis, 15, 438-443.
    • (1995) Electrophoresis , vol.15 , pp. 438-443
    • Cordwell, S.1    Wilkins, M.R.2    Cerpa-Poijak, A.3    Gooley, A.A.4    Duncan, M.5    Williams, K.L.6    Humphery-Smith, I.7
  • 31
    • 0028429419 scopus 로고
    • Protein identification by peptide mass fingerprinting
    • Cottrell, J. S. (1994). Protein identification by peptide mass fingerprinting. Peptide research, 7, 115-124.
    • (1994) Peptide Research , vol.7 , pp. 115-124
    • Cottrell, J.S.1
  • 32
    • 0025262186 scopus 로고
    • In situ chemical cleavage of proteins immobilized to glass-fiber and polyvinylidenefluoride membranes: Cleavage at tryptophan residues with 2-(2'-nilrophenylsulfenyl)-3-methyl-3'-bromoindolenine toobtain internal amino acid sequence
    • Crimmins, D. L., Mccourt, D. W., Thoma, R. S., Scott, M. G., Macke, K. and Schwartz, B. D. (1990). In situ chemical cleavage of proteins immobilized to glass-fiber and polyvinylidenefluoride membranes: cleavage at tryptophan residues with 2-(2'-nilrophenylsulfenyl)-3-methyl-3'-bromoindolenine toobtain internal amino acid sequence. Analytical Biochemistry. 187, 27-38.
    • (1990) Analytical Biochemistry , vol.187 , pp. 27-38
    • Crimmins, D.L.1    McCourt, D.W.2    Thoma, R.S.3    Scott, M.G.4    Macke, K.5    Schwartz, B.D.6
  • 33
    • 0027256659 scopus 로고
    • Glycan microheterogeneity of alpha i-antitrypsin in serum and meconium from normal and cystic fibrosis patients by crossed innminoafíinoeleetrophoresis with different lectins (Con a, lca, wga)
    • Durtlel, S. and Revol, A. (1993). Glycan microheterogeneity of alpha I-antitrypsin in serum and meconium from normal and cystic fibrosis patients by crossed innminoafíinoeleetrophoresis with different lectins (Con A, LCA, WGA). Clinical and Chemical Acta, 215, 173-187.
    • (1993) Clinical and Chemical Acta , vol.215 , pp. 173-187
    • Durtlel, S.1    Revol, A.2
  • 34
    • 0024204979 scopus 로고
    • Identification of mouse brain proteins after two-dimensional electrophoresis and electro-blotting by microsequence analysis and amino acid composition
    • Eckerskorn, C., Jungblit, P., Mewes, W., Klose, J. and Loitspeicii, F. (1988). Identification of mouse brain proteins after two-dimensional electrophoresis and electro-blotting by microsequence analysis and amino acid composition. Electrophoresis, 9, 830-838.
    • (1988) Electrophoresis , vol.9 , pp. 830-838
    • Eckerskorn, C.1    Jungblit, P.2    Mewes, W.3    Klose, J.4    Loitspeicii, F.5
  • 35
    • 0026464562 scopus 로고
    • Mass speetrometric analysis of blotted proteins after gel electrophoretic separation by matrix-assisted laser desorption/ ionization
    • Eckerskorn, C., Strupat, K., Karas, M., Hillenkamp, F. and Loitspeicii, F. (1992). Mass speetrometric analysis of blotted proteins after gel electrophoretic separation by matrix-assisted laser desorption/ ionization. Electrophoresis. 13, 664-665.
    • (1992) Electrophoresis , vol.13 , pp. 664-665
    • Eckerskorn, C.1    Strupat, K.2    Karas, M.3    Hillenkamp, F.4    Loitspeicii, F.5
  • 36
    • 0027431544 scopus 로고
    • Structural characterisation of blotting membranes and the influence of membrane parameters for electroblotting and subsequent amino acid sequence analysis of proteins
    • Eckerskorn, C. and Lottspeicii, P. (1991). Structural characterisation of blotting membranes and the influence of membrane parameters for electroblotting and subsequent amino acid sequence analysis of proteins. Electrophoresis. 14, 831-838.
    • (1991) Electrophoresis , vol.14 , pp. 831-838
    • Eckerskorn, C.1    Lottspeicii, P.2
  • 37
    • 0020819344 scopus 로고
    • Preparative isoelectric focusing in immobilized ph gradients. I. General principles and methodology
    • Ek, K., Bjellqvist, B. J. and Richeth, P. O. (1983). Preparative isoelectric focusing in immobilized pH gradients. I. General principles and methodology. Journal of Biochemical ant Biophysical Methods. 8, 135-155.
    • (1983) Journal of Biochemical Ant Biophysical Methods , vol.8 , pp. 135-155
    • Ek, K.1    Bjellqvist, B.J.2    Richeth, P.O.3
  • 40
    • 0024978195 scopus 로고
    • The quest system for quantitative analysis of two-dimensional gels
    • Garrels, J. I. (1989). The QUEST system for quantitative analysis of two-dimensional gels. Journal of Biological Chemistry. 264, 5269-5282.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 5269-5282
    • Garrels, J.I.1
  • 42
    • 0025609749 scopus 로고
    • Quantitative exploration of the ref52 protein database: Cluster analysis reveals the major protein expression profiles in responses to growth regulation, serum stimulation, and viral transformation
    • Garrels, J. I., Franza, B. R., Chang, C. and Laiter, G. (1990). Quantitative exploration of the REF52 protein database: cluster analysis reveals the major protein expression profiles in responses to growth regulation, serum stimulation, and viral transformation. Electrophoresis. II. 1114-1130.
    • (1990) Electrophoresis , vol.2 , pp. 1114-1130
    • Garrels, J.I.1    Franza, B.R.2    Chang, C.3    Laiter, G.4
  • 45
    • 0008806375 scopus 로고
    • Amino acid analysis of pvdf-bound proteins
    • R. H. Ageletti. Ed.), Academic Press, San Diego
    • Gharaadagi, F., Atherton, D., Demoit, M. and Mische, S. M. (1992). Amino acid analysis of PVDF-bound proteins, in Techniques in Protein Chemistry III (R. H. Ageletti. Ed.). pp 249-260. Academic Press, San Diego.
    • (1992) Techniques in Protein Chemistry III , pp. 249-260
    • Gharaadagi, F.1    Atherton, D.2    Demoit, M.3    Mische, S.M.4
  • 46
    • 0027300119 scopus 로고
    • Effects of chronic ethanol on enzymes regulating sialylation and desialylation of transferrin in ruls
    • Ghosh, P., Okoh, C., Liu, Q. H. and Lakshman, M. R. (1993). Effects of chronic ethanol on enzymes regulating sialylation and desialylation of transferrin in ruls. Alcoholism; Clinical and Expérimental Research. 17, 576-579.
    • (1993) Alcoholism; Clinical and Expérimental Research , vol.17 , pp. 576-579
    • Ghosh, P.1    Okoh, C.2    Liu, Q.H.3    Lakshman, M.R.4
  • 47
    • 0025733509 scopus 로고
    • Quantitation of human leukocyte proteins after silver staining: A study with two-dimensional electrophoresis
    • Giometti, C. S., Gbmmeil, M. A., Tollaksen, S. L. and Taylor, J. (1991). Quantitation of human leukocyte proteins after silver staining: a study with two-dimensional electrophoresis. Electrophoresis. 12, 536-543.
    • (1991) Electrophoresis , vol.12 , pp. 536-543
    • Giometti, C.S.1    Gbmmeil, M.A.2    Tollaksen, S.L.3    Taylor, J.4
  • 48
    • 0027065015 scopus 로고
    • Mouse liver protein database: A catalog of proteins detected by two-dimensional gel electrophoresis
    • Giometti, C. S., Taylor, J. and Tollaksen, S. L. (1992). Mouse liver protein database: a catalog of proteins detected by two-dimensional gel electrophoresis. Electrophoresis. 13, 970-991.
    • (1992) Electrophoresis , vol.13 , pp. 970-991
    • Giometti, C.S.1    Taylor, J.2    Tollaksen, S.L.3
  • 52
    • 0026638318 scopus 로고
    • Size polymorphisms due to changes in the number of o-glycosylated tandem repeats in the dictyostelium discoideum glycoprotein psa
    • Gooley, A. A., Marsiichalek, R. and Williams, K. L. (1992). Size polymorphisms due to changes in the number of O-glycosylated tandem repeats in the Dictyostelium discoideum glycoprotein PsA. Genetics. 130, 749-756.
    • (1992) Genetics , vol.130 , pp. 749-756
    • Gooley, A.A.1    Marsiichalek, R.2    Williams, K.L.3
  • 53
    • 0023768475 scopus 로고
    • The current stale of two-dimensional electrophoresis with immobilized ph gradients
    • Görg, A., Postel, W. and Gunther, S. (1988). The current stale of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis. 9, 531-546.
    • (1988) Electrophoresis , vol.9 , pp. 531-546
    • Görg, A.1    Postel, W.2    Gunther, S.3
  • 54
    • 0023842078 scopus 로고
    • Approach to stationary two-dimensional pattern: Influence of focusing time and immobiline/carrier ampholyte concentrations
    • Gorg, A., Postel, W., Gunther, S., Weser, J., Strahler, J. R., Hanash, S. M., Someklot, L. and Kuroe, R. (1988). Approach to stationary two-dimensional pattern: influence of focusing time and immobiline/carrier ampholyte concentrations. Electrophoresis, 9, 37-46.
    • (1988) Electrophoresis , vol.9 , pp. 37-46
    • Gorg, A.1    Postel, W.2    Gunther, S.3    Weser, J.4    Strahler, J.R.5    Hanash, S.M.6    Someklot, L.7    Kuroe, R.8
  • 55
    • 0028070242 scopus 로고
    • Analysis of glycoproteins separated by two-dimensional gel electrophoresis using lectin blotting revealed by ehemiluminescence
    • Gravel, P., Golaz, O., Walzer, C., Hochstrasser, D. F., Turler, H., and Balant, L. P. (1994). Analysis of glycoproteins separated by two-dimensional gel electrophoresis using lectin blotting revealed by ehemiluminescence. Analytical Biochemistry, 221, 66-71.
    • (1994) Analytical Biochemistry , vol.221 , pp. 66-71
    • Gravel, P.1    Golaz, O.2    Walzer, C.3    Hochstrasser, D.F.4    Turler, H.5    Balant, L.P.6
  • 56
    • 0024086860 scopus 로고
    • Acid phosphatase typing for breeding nematode-resistant tomatoes by isoelectric focusing willi an ultranarrow immobilized ph gradient
    • Gunther, S., Postei, W., Wiering, H. and Görg, A. (1988). Acid phosphatase typing for breeding nematode-resistant tomatoes by isoelectric focusing willi an ultranarrow immobilized pH gradient. Electrophoresis. 9, 618-620.
    • (1988) Electrophoresis. , vol.9 , pp. 618-620
    • Gunther, S.1    Postei, W.2    Wiering, H.3    Görg, A.4
  • 60
    • 0028983813 scopus 로고
    • Improvement of an in-gel digestion for the micropreparation of internal protein fragments for amino acid sequencing
    • Hellman, U., Wernstedt, C., Gonez, J. and Heldin, C-H. (1995). Improvement of an in-gel digestion for the micropreparation of internal protein fragments for amino acid sequencing. Analytical Biochemistry, 224, 451-455.
    • (1995) Analytical Biochemistry , vol.224 , pp. 451-455
    • Hellman, U.1    Wernstedt, C.2    Gonez, J.3    Heldin, C.-H.4
  • 62
    • 0027244568 scopus 로고
    • Analytical and micropreparative peptide mapping by high performance liquid chromatography/ electrospray mass spectrometry of proteins purified by gel electrophoresis
    • Hess, D., Covey, T. C., Winz, R., Brownsey, R. W. and Aebersold, R. (1993). Analytical and micropreparative peptide mapping by high performance liquid chromatography/ electrospray mass spectrometry of proteins purified by gel electrophoresis. Protein Science, 2, 1342-1351.
    • (1993) Protein Science , vol.2 , pp. 1342-1351
    • Hess, D.1    Covey, T.C.2    Winz, R.3    Brownsey, R.W.4    Aebersold, R.5
  • 63
    • 0028020715 scopus 로고
    • Amino acid analysis and protein database compositional search as a rapid and inexpensive method to identify proteins
    • Hobohm, U., Houthaeve, T. and Sanüer, C. (1994). Amino acid analysis and protein database compositional search as a rapid and inexpensive method to identify proteins. Analytical Biochemistry. 222, 202-209.
    • (1994) Analytical Biochemistry , vol.222 , pp. 202-209
    • Hobohm, U.1    Houthaeve, T.2    Sanüer, C.3
  • 65
    • 0023676995 scopus 로고
    • Development of polyacrylamide gels that improve the separation of proteins and their detection by silver staining
    • Hochstrasser, D. F., Patchornik, A., and Merril, C. R. (1988). Development of polyacrylamide gels that improve the separation of proteins and their detection by silver staining. Analytical Biochemistry. 173, 412-423.
    • (1988) Analytical Biochemistry , vol.173 , pp. 412-423
    • Hochstrasser, D.F.1    Patchornik, A.2    Merril, C.R.3
  • 66
    • 0026043017 scopus 로고
    • Preparative isoeleetrofocusing and highresolutiontwo-dimensional electrophoresis for coneemration and purification of proteins
    • Hochstrasser, A. C., James, R. W., Pomeita, D. and Hochstrasser, D. F. (1991a). Preparative isoeleetrofocusing and highresolutiontwo-dimensional electrophoresis for coneemration and purification of proteins. Applied and Theoretical Electrophoresis, 1, 333-337.
    • (1991) Applied and Theoretical Electrophoresis , vol.1 , pp. 333-337
    • Hochstrasser, A.C.1    James, R.W.2    Pomeita, D.3    Hochstrasser, D.F.4
  • 70
    • 0027139249 scopus 로고
    • Interferon-gamma up-regulates a unique set of proteins in human keratinocytes. Molecular cloning and expression of the cdna encoding the rgd-sequencc containing protein igup 1-5 111
    • Honore, B., Leffers, H., Madsen, P, and Celis, J. E. (1993). Interferon-gamma up-regulates a unique set of proteins in human keratinocytes. Molecular cloning and expression of the cDNA encoding the RGD-sequencc containing protein IGUP 1-5 111. European Journal of Biochemistry. 218, 421-430.
    • (1993) European Journal of Biochemistry , vol.218 , pp. 421-430
    • Honore, B.1    Leffers, H.2    Madsen, P.3    Celis, J.E.4
  • 71
    • 0027918090 scopus 로고
    • Site-specific carbohydrate identification in recombinant proteins using mald-tof ms
    • Huberty, M. C., Vatu, J. E., Yu, W. and Martin, S. A. (1993). Site-specific carbohydrate identification in recombinant proteins using MALD-TOF MS. Analytical Chemistry. 65, 2791-2800.
    • (1993) Analytical Chemistry , vol.65 , pp. 2791-2800
    • Huberty, M.C.1    Vatu, J.E.2    Yu, W.3    Martin, S.A.4
  • 73
    • 0023777627 scopus 로고
    • India ink staining of proteins on nylon and hydrophobic membranes
    • Hughes, J. H., Mack, K. and Hamparian, V. V. (1988). India ink staining of proteins on nylon and hydrophobic membranes. Analytical Biochemistry, 173, 18-25.
    • (1988) Analytical Biochemistry , vol.173 , pp. 18-25
    • Hughes, J.H.1    Mack, K.2    Hamparian, V.V.3
  • 75
    • 0028272130 scopus 로고
    • Two-dimensional electrophoretic analysis of proteins expressed by normal and cancerous human crypts: Application of mass spectrometry to peptide-mass fingerprinting
    • Ji, H., Whitehead, R. H., Reid, G. E., Moritz, R. L., Ward, L. D. and Simpson, R. J. (1994). Two-dimensional electrophoretic analysis of proteins expressed by normal and cancerous human crypts: application of mass spectrometry to peptide-mass fingerprinting. Electrophoresis. 15, 391-405.
    • (1994) Electrophoresis , vol.15 , pp. 391-405
    • Ji, H.1    Whitehead, R.H.2    Reid, G.E.3    Moritz, R.L.4    Ward, L.D.5    Simpson, R.J.6
  • 76
    • 0027085825 scopus 로고
    • Sequence analysis of peptide mixtures by automated integration of ednian and mass spectrometric data
    • Johnson, R. S. and Walsh, K. A. (1992). Sequence analysis of peptide mixtures by automated integration of Ednian and mass spectrometric data. Protein Science. 1, 1083-1091.
    • (1992) Protein Science , vol.1 , pp. 1083-1091
    • Johnson, R.S.1    Walsh, K.A.2
  • 77
    • 0025336478 scopus 로고
    • Autoradiography using storage phosphor technology
    • Johnston, R. F., Pickeit, S. C. and Barker, D. L. (1990). Autoradiography using storage phosphor technology. Electrophoresis, 11, 355-360.
    • (1990) Electrophoresis , vol.11 , pp. 355-360
    • Johnston, R.F.1    Pickeit, S.C.2    Barker, D.L.3
  • 78
    • 0026752199 scopus 로고
    • Identification of tissue proteins by amino acid analysis after purification by two-dimensional electrophoresis
    • Jungblut, P., Dzionara, M., Ki, Ose, J. and Wiitmann-Leibold, B. (1992). Identification of tissue proteins by amino acid analysis after purification by two-dimensional electrophoresis. Journal of Protein Chemistry. 11, 603-612.
    • (1992) Journal of Protein Chemistry , vol.11 , pp. 603-612
    • Jungblut, P.1    Dzionara, M.2    Ki Ose, J.3    Wiitmann-Leibold, B.4
  • 80
    • 0023669069 scopus 로고
    • The physical map of the whole e. Cali chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic library
    • Koiiara, Y., Akiyama, K. and Isono, K. (1987). The physical map of the whole E. cali chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell. 50, 495-508.
    • (1987) Cell , vol.50 , pp. 495-508
    • Koiiara, Y.1    Akiyama, K.2    Isono, K.3
  • 81
    • 0016637146 scopus 로고
    • Protein mapping by combined isoelectric focusing and electrophoresis in mouse tissues. A novel approach to testing for individual point mutations in mammals
    • Kiose, J. (1975). Protein mapping by combined isoelectric focusing and electrophoresis in mouse tissues. A novel approach to testing for individual point mutations in mammals. Human Genetik. 26, 231-243.
    • (1975) Human Genetik , vol.26 , pp. 231-243
    • Kiose, J.1
  • 82
    • 0025915957 scopus 로고
    • Quantitative analysis of protein synthesis in mouse embryos i: Extensive re-programming at the one-and two-celt stages
    • Latham, K. E., Garrels, J. I., Chang, C. and Solter, D. (1991). Quantitative analysis of protein synthesis in mouse embryos I: extensive re-programming at the one-and two-celt stages. Development. 2, 921-932.
    • (1991) Development , vol.2 , pp. 921-932
    • Latham, K.E.1    Garrels, J.I.2    Chang, C.3    Solter, D.4
  • 83
    • 0026436999 scopus 로고
    • Analysis of embryonic mouse development: Construction of a high-resolution, two-dimensional gel protein database
    • Latham, K. E., Garrels, J. I., Chang, C. and Solter, D. (1992). Analysis of embryonic mouse development: construction of a high-resolution, two-dimensional gel protein database. Applied and Theoretical Electrophoresis. 2, 163-170.
    • (1992) Applied and Theoretical Electrophoresis , vol.2 , pp. 163-170
    • Latham, K.E.1    Garrels, J.I.2    Chang, C.3    Solter, D.4
  • 85
    • 0027378908 scopus 로고
    • Electrospray ionization mass spectrometry from sodium dodecyl su 1 fate-poly aery lamide gel electrophoresis: Application to the topology of the sarcoplasmic reticulum ca atpase
    • Le Maire, M., Descuamps, S., Möller, J. V., Le Caer, J. P. and Rossier, J. (1993). Electrospray ionization mass spectrometry from sodium dodecyl su 1 fate-poly aery lamide gel electrophoresis: application to the topology of the sarcoplasmic reticulum Ca ATPase. Analytical Biochemistry. 214, 50-57.
    • (1993) Analytical Biochemistry , vol.214 , pp. 50-57
    • Le Maire, M.1    Descuamps, S.2    Möller, J.V.3    Le Caer, J.P.4    Rossier, J.5
  • 86
    • 0024571609 scopus 로고
    • Database and search techniques for two-dimensional gel protein data: A comparison of paradigms for exploratory data analysis and prospects for biological modelling
    • Lem Kin, P. F. and Lester, E. P. (1989). Database and search techniques for two-dimensional gel protein data: a comparison of paradigms for exploratory data analysis and prospects for biological modelling. Electrophoresis. 10, 122-140.
    • (1989) Electrophoresis , vol.10 , pp. 122-140
    • Lem Kin, P.F.1    Lester, E.P.2
  • 87
    • 0027769618 scopus 로고
    • An efficient disk-based dala structure for rapid searching of quantitative two-dimensional gel databases
    • Lemkin, P. F., Wu, Y. and Ufton, K. (1993). An efficient disk-based dala structure for rapid searching of quantitative two-dimensional gel databases. Electrophoresis. 14, 1341-1350.
    • (1993) Electrophoresis , vol.14 , pp. 1341-1350
    • Lemkin, P.F.1    Wu, Y.2    Ufton, K.3
  • 88
    • 0024468526 scopus 로고
    • Quantification of proteins in the subnanogram and nanogram range: Comparison of the aurodye, ferridye. And india ink staining methods
    • Li, K.W., Geraerts, W. P., Vanelk, R. and Koose, J. (1989). Quantification of proteins in the subnanogram and nanogram range: comparison of the AuroDye, FerriDye. and india ink staining methods. Analytical Biochemistry. 182, 44-47.
    • (1989) Analytical Biochemistry , vol.182 , pp. 44-47
    • Li, K.W.1    Geraerts, W.P.2    Vanelk, R.3    Koose, J.4
  • 89
    • 0026674886 scopus 로고
    • Dif ferential display of eukaryotic messenger rna by means of the polymerase chain reaction
    • Liang, P. and Pardee, A. B. (1992). Dif ferential display of eukaryotic messenger RNA by means of the polymerase chain reaction. Science. 257, 967-971.
    • (1992) Science , vol.257 , pp. 967-971
    • Liang, P.1    Pardee, A.B.2
  • 90
    • 0002948611 scopus 로고
    • Sequence database searching by mass specirometric data
    • (R. Kellner, F. Lottspeich. and H. E. Mever, Eds), VCH. Weinheim
    • Mann, M. (1995). Sequence database searching by mass specirometric data. In Microcharacierisation of Proteins (R. Kellner, F. Lottspeich. and H. E. Mever, Eds), pp 223-245. VCH. Weinheim.
    • (1995) Microcharacierisation of Proteins , pp. 223-245
    • Mann, M.1
  • 91
    • 0027608882 scopus 로고
    • Use of mass speelrometric molecular weight information to identify proteins insequence databases
    • Mann, M., Hojrup, P. and Roepstorff, P. (1993). Use of mass speelrometric molecular weight information to identify proteins insequence databases. Biological mass spectrometry, 22, 338-345.
    • (1993) Biological Mass Spectrometry , vol.22 , pp. 338-345
    • Mann, M.1    Hojrup, P.2    Roepstorff, P.3
  • 92
    • 0028575316 scopus 로고
    • Error tolerant identification of peptides in sequence databases by peptide sequence tags
    • Mann, M. and Wilm, M. (1994). Error tolerant identification of peptides in sequence databases by peptide sequence tags. Analytical Chemistry, 66, 4390-4399.
    • (1994) Analytical Chemistry , vol.66 , pp. 4390-4399
    • Mann, M.1    Wilm, M.2
  • 93
    • 0023664635 scopus 로고
    • Sequence of picomole quantities of proteins electroblotted onto polyvinylidcne difluoride nviinbranes
    • Matsudaira, P. (1987). Sequence of picomole quantities of proteins electroblotted onto polyvinylidcne difluoride nviinbranes. Journal of Biotogical Chemistry, 262, 10035-10038.
    • (1987) Journal of Biotogical Chemistry , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 95
    • 0028180250 scopus 로고
    • Identification of proteins in polyacrylamide gels by mass spectrornetric peptide mapping combined with database search
    • Mortz, E., Vorm, O., Mann, M. and Roepstorff, P. (1994). Identification of proteins in polyacrylamide gels by mass spectrornetric peptide mapping combined with database search. Biological Mass Spectrometry, 23, 249-261.
    • (1994) Biological Mass Spectrometry , vol.23 , pp. 249-261
    • Mortz, E.1    Vorm, O.2    Mann, M.3    Roepstorff, P.4
  • 96
    • 0026019503 scopus 로고
    • Measurement of picomoles of phosphoamino acids by high performance liquid chromatography
    • Murthy, L. R. and Iqbal, K. (1991). Measurement of picomoles of phosphoamino acids by high performance liquid chromatography. Analytical Biochemistry, 193, 299-305.
    • (1991) Analytical Biochemistry , vol.193 , pp. 299-305
    • Murthy, L.R.1    Iqbal, K.2
  • 97
    • 0027829703 scopus 로고
    • Comparison of the bioimage visage 2000 and the gellab-ii two-dimensional electrophoresis image analysis systems
    • Myrick, J. E., Lemkin, P. F., Robinson, M. K. and Upton, K. M. (1993). Comparison of the Bioimage Visage 2000 and the GELLAB-II two-dimensional electrophoresis image analysis systems. Applied and Theoretical Electrophoresis, 3, 335-346.
    • (1993) Applied and Theoretical Electrophoresis , vol.3 , pp. 335-346
    • Myrick, J.E.1    Lemkin, P.F.2    Robinson, M.K.3    Upton, K.M.4
  • 98
    • 0024504492 scopus 로고
    • Genomically linked ccilular protein databases derived from two-dimensional polyacrylamide gel electrophoresis
    • Neidhardt, F. C., Appleby, D. B., Sankar, P., Hution, M. E. and Phillips, T. A. (1989). Genomically linked ccilular protein databases derived from two-dimensional polyacrylamide gel electrophoresis. Electrophoresis. 10, 116-122.
    • (1989) Electrophoresis , vol.10 , pp. 116-122
    • Neidhardt, F.C.1    Appleby, D.B.2    Sankar, P.3    Hution, M.E.4    Phillips, T.A.5
  • 99
    • 0018717153 scopus 로고
    • Protein fingerprinting by sds-gel electrophoresis after partial fragmentation with cnbr
    • Ni Kodem, V. and Fresco, J. R. (1979). Protein fingerprinting by SDS-gel electrophoresis after partial fragmentation with CNBr. Analytical Biochemistry. 97, 382-386.
    • (1979) Analytical Biochemistry , vol.97 , pp. 382-386
    • Ni Kodem, V.1    Fresco, J.R.2
  • 100
    • 0026495698 scopus 로고
    • Applications of an automated apparatus for two-dimensional clectrophoresis. Model tep-i. For microsequence analysis of proteins
    • Nokihara, K., Morita, N. and Kuriki, T. (1992). Applications of an automated apparatus for two-dimensional clectrophoresis. Model TEP-I. for microsequence analysis of proteins. Electrophoresis. 13, 701-707.
    • (1992) Electrophoresis , vol.13 , pp. 701-707
    • Nokihara, K.1    Morita, N.2    Kuriki, T.3
  • 101
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. H. (1975). High resolution two-dimensional electrophoresis of proteins. Journal of Biological Chemistry. 250, 4007-4021.
    • (1975) Journal of Biological Chemistry. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 102
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell, P. Z., Goodman, H. M. and O'Farrell, P. H. (1977). High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell, 12, 1133-1142.
    • (1977) Cell , vol.12 , pp. 1133-1142
    • O'Farrell, P.Z.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 103
    • 0026572003 scopus 로고
    • Hie complete dna sequence of yeast chromosome hi
    • Oliver Et At. (1992). Hie complete DNA sequence of yeast chromosome HI. Nature 357, 38-46.
    • (1992) Nature , vol.357 , pp. 38-46
    • Oliver1
  • 104
    • 0023869984 scopus 로고
    • Elsie 4: Quantitative computer analysis of sets of two-dimensional gel electrophoretograms
    • Olsen, A. D. and Miller M. J. (1988). Elsie 4: quantitative computer analysis of sets of two-dimensional gel electrophoretograms. Analytical Biochemistry, 169, 49-70.
    • (1988) Analytical Biochemistry , vol.169 , pp. 49-70
    • Olsen, A.D.1    Miller, M.J.2
  • 105
    • 0026601551 scopus 로고
    • Imidazole-sds-zn reverse staining of proteins in gels containing or not sds and microsequence of individual unmodified electroblotted proteins
    • Ortiz, M. L., Calero, M., Fernandez-Patron, C., Patron, C. F., Castellanos, L. and Mendez, E. (1992). imidazole-SDS-Zn reverse staining of proteins in gels containing or not SDS and microsequence of individual unmodified electroblotted proteins. FEBS Lettersers, 296, 300-304.
    • (1992) FEBS Lettersers , vol.296 , pp. 300-304
    • Ortiz, M.L.1    Calero, M.2    Fernandez-Patron, C.3    Patron, C.F.4    Castellanos, L.5    Mendez, E.6
  • 107
    • 85024066022 scopus 로고
    • Improved high-performance liquidchromatography of amino acidsderivatised with 9-fluoreny i methyl chloroformate
    • press
    • Ou, K., Wilkins, M. R., Yan, J. X., Gooley, A. A., Fung, Y., Sheumack, D. and Williams, K. L. (1995). Improved high-performance liquidchromatography of amino acidsderivatised with 9-fluoreny I methyl chloroformate. Journal of Chromatography (in press).
    • (1995) Journal of Chromatography
    • Ou, K.1    Wilkins, M.R.2    Yan, J.X.3    Gooley, A.A.4    Fung, Y.5    Sheumack, D.6    Williams, K.L.7
  • 109
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • Pappin, D. J. C., Hojrup, P. and Bliashy, A. J. (1993). Rapid identification of proteins by peptide-mass fingerprinting. Current Biology, 3, 327-332.
    • (1993) Current Biology , vol.3 , pp. 327-332
    • Pappin, D.1    Hojrup, P.2    Bliashy, A.J.3
  • 110
    • 0028142375 scopus 로고
    • From electrophoretieally separated protein to identification: Strategies for sequence and mass analysis
    • Patterson, S. D. (1994). From electrophoretieally separated protein to identification: strategies for sequence and mass analysis. Analytical Biochemistry, 221, 1-15.
    • (1994) Analytical Biochemistry , vol.221 , pp. 1-15
    • Patterson, S.D.1
  • 111
    • 0027133538 scopus 로고
    • Evaluation of storage phosphor imaging for quantitative analysis of 2-d gels using the quest ii system
    • Patterson, S. D. and Latter, G. I. (1993). Evaluation of storage phosphor imaging for quantitative analysis of 2-D gels using the Quest II system. BioTechnolues, 15, 1076-1083.
    • (1993) Biotechnolues , vol.15 , pp. 1076-1083
    • Patterson, S.D.1    Latter, G.I.2
  • 112
    • 0027374888 scopus 로고
    • Glycosylation sites identified by solid-phase edman degradation: O-linked glycosylation motifs on human glycophorin a
    • Pisano, A., Redmond, J. W., Williams, K. L. and Gooley, A. A. (1993). Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A. Glycohiology. 3, 429-435.
    • (1993) Glycohiology. , vol.3 , pp. 429-435
    • Pisano, A.1    Redmond, J.W.2    Williams, K.L.3    Gooley, A.A.4
  • 113
    • 0026733421 scopus 로고
    • A comparison between low background silver diamine and silver nitrate protein stains
    • Rabilloud, T. (1992). A comparison between low background silver diamine and silver nitrate protein stains. Electrophoresis, 13, 429-439.
    • (1992) Electrophoresis , vol.13 , pp. 429-439
    • Rabilloud, T.1
  • 114
    • 0027070806 scopus 로고
    • Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes
    • Rasmussen, H. H., Van Damme, J., Puype, M., Cesser, B., Celis, J. E. and Vandekerck-Iiove, J. (1992). Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 13, 960-969.
    • (1992) Electrophoresis , vol.13 , pp. 960-969
    • Rasmussen, H.H.1    Van Damme, J.2    Puype, M.3    Cesser, B.4    Celis, J.E.5    Vandekerck-Iiove, J.6
  • 115
    • 0028240519 scopus 로고
    • Identification of transformation sensitive proteins recorded in human two-dimensional gei protein databases by mass-spectrometrie peptide mapping alone and in combination with microsequencing
    • Rasmussen, H. H., Mortz, E., Mann, M., Roepstoref, P. and Culls, J. E. (1994). Identification of transformation sensitive proteins recorded in human two-dimensional gei protein databases by mass-spectrometrie peptide mapping alone and in combination with microsequencing. Electrophoresis, 15, 406-416.
    • (1994) Electrophoresis , vol.15 , pp. 406-416
    • Rasmussen, H.H.1    Mortz, E.2    Mann, M.3    Roepstoref, P.4    Culls, J.E.5
  • 116
    • 0028078498 scopus 로고
    • Dose-responscs in rat hepatic protein modification and expression following exposure to the rat hepatocarcinogen metliapyriiene
    • Richardson, F. C., Horn, D. M. and anderson, N. L. (1994). Dose-responscs in rat hepatic protein modification and expression following exposure to the rat hepatocarcinogen metliapyriiene. Carcinogenesis. 15, 325-329.
    • (1994) Carcinogenesis , vol.15 , pp. 325-329
    • Richardson, F.C.1    Horn, D.M.2    Anderson, N.L.3
  • 117
    • 0004292561 scopus 로고
    • Irnmobilied ph gradients: Theory and methodology
    • R. H. Burdon and P. H, van Knippenberg. Eds) Elsevier. Amsterdam
    • Righetti, P. G. (1990). Irnmobilied pH gradients: theory and methodology. In Laboratory Techniques in Biochemistry and Molecular Biology R. H. Burdon and P. H, van Knippenberg. Eds Elsevier. Amsterdam.
    • (1990) Laboratory Techniques in Biochemistry and Molecular Biology
    • Righetti, P.G.1
  • 119
    • 0027248790 scopus 로고
    • Towards stoichiometric silver staining of proteins resolved in complex two-dimensional electrophoresis gels: Real-time analysis of pattern development
    • Rodrigulz, L. V., Gernsten, D. M., Ramagli, L. S. and Johnston, D. A. (1993). Towards stoichiometric silver staining of proteins resolved in complex two-dimensional electrophoresis gels: real-time analysis of pattern development. Electrophoresis. 14, 628-637.
    • (1993) Electrophoresis , vol.14 , pp. 628-637
    • Rodrigulz, L.V.1    Gernsten, D.M.2    Ramagli, L.S.3    Johnston, D.A.4
  • 120
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after one-or two-dimensional gel electrophoresis
    • Rosenfeld, J., Capdevielle, J., Guillemot, J. C. and Ferrara, P. (1992). In-gel digestion of proteins for internal sequence analysis after one-or two-dimensional gel electrophoresis. Analytical Biochemistry. 203, 173-179.
    • (1992) Analytical Biochemistry , vol.203 , pp. 173-179
    • Rosenfeld, J.1    Capdevielle, J.2    Guillemot, J.C.3    Ferrara, P.4
  • 123
    • 0016767686 scopus 로고
    • Two-dimensional analysis of soluble proteins
    • Scheele, G. J. (1975). Two-dimensional analysis of soluble proteins. Biochemistry. 250, 5375-5385.
    • (1975) Biochemistry , vol.250 , pp. 5375-5385
    • Scheele, G.J.1
  • 125
    • 0025938679 scopus 로고
    • Identification of proteins in scquencc databases from amino acid composition
    • Smbald, P. R., Sommereeldt, H. and Argos, P. (1991). Identification of proteins in scquencc databases from amino acid composition. Analytical Biochemistry. 198, 330-333.
    • (1991) Analytical Biochemistry , vol.198 , pp. 330-333
    • Smbald, P.R.1    Sommereeldt, H.2    Argos, P.3
  • 128
  • 129
    • 12044260066 scopus 로고
    • Matrix-assisted laser desorption ionization mass spectrometry of proteins electroblotted after polyacrylamide gel electrophoresis
    • Strupat, K., Karas, M., Hillenkamp, F., Eckerskorn, C. and Loitspeich, F. (1994). Matrix-assisted laser desorption ionization mass spectrometry of proteins electroblotted after polyacrylamide gel electrophoresis. Analytical Chemistry. 66, 464-470.
    • (1994) Analytical Chemistry , vol.66 , pp. 464-470
    • Strupat, K.1    Karas, M.2    Hillenkamp, F.3    Eckerskorn, C.4    Loitspeich, F.5
  • 132
    • 0023129266 scopus 로고
    • Protein blotting on nitrocellulose: Some important aspects of the resolution and detection of antigens in complex extracts
    • Tovey, E. R., Ford, S. A. and Baldo, B. A. (1987). Protein blotting on nitrocellulose: some important aspects of the resolution and detection of antigens in complex extracts. Journal of Biochemical and Biophysical Methods. 14, 1-17.
    • (1987) Journal of Biochemical and Biophysical Methods , vol.14 , pp. 1-17
    • Tovey, E.R.1    Ford, S.A.2    Baldo, B.A.3
  • 133
    • 0027461194 scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis of proteins labeled with the fluorophore monobromobimane prior to first-dimensional isoelectric focusing: Imaging of the fluorescent prolein spot patterns using a cooled charge-coupled device
    • Urwin, V. E. and Jackson, P. (1993). Two-dimensional polyacrylamide gel electrophoresis of proteins labeled with the fluorophore monobromobimane prior to first-dimensional isoelectric focusing: imaging of the fluorescent prolein spot patterns using a cooled charge-coupled device. Analytical Biochemistry. 209, 57-62.
    • (1993) Analytical Biochemistry , vol.209 , pp. 57-62
    • Urwin, V.E.1    Jackson, P.2
  • 134
    • 0025648952 scopus 로고
    • Gene-protein database of escherichica coli k-12: Edition 3
    • Vanbogelen, R. A., Hutton, M. E. and Neidhardt, F. C. (1990). Gene-protein database of Escherichica coli K-12: edition 3. Electrophoresis, 11, 1131-1166.
    • (1990) Electrophoresis , vol.11 , pp. 1131-1166
    • Vanbogelen, R.A.1    Hutton, M.E.2    Neidhardt, F.C.3
  • 135
    • 0026329604 scopus 로고
    • The gene-protein database of escherichia coli: Edition 4
    • Vanbogelen, R. A. and Nhidiiardt, P. C. (1991). The gene-protein database of Escherichia coli: edition 4. Electrophoresis. 12, 955-994.
    • (1991) Electrophoresis , vol.12 , pp. 955-994
    • Vanbogelen, R.A.1    Nhidiiardt, P.C.2
  • 137
    • 0025363196 scopus 로고
    • Comparative two-dimensional gel analysis and microsequencing identifies gelsolin as one of the jnost prominent downregulated markers of transformed human fibroblast and epithelial ceils
    • Vandekerkhove, J., Bauw, G., Vancompernolle, K., Honore, B. and Celis, J. (1990). Comparative two-dimensional gel analysis and microsequencing identifies gelsolin as one of the jnost prominent downregulated markers of transformed human fibroblast and epithelial ceils. Journal of Cell Biology, 111, 95-102.
    • (1990) Journal of Cell Biology , vol.111 , pp. 95-102
    • Vandekerkhove, J.1    Bauw, G.2    Vancompernolle, K.3    Honore, B.4    Celis, J.5
  • 138
    • 0026568372 scopus 로고
    • Peptide mapping and microsequencing of proteins separated by sds-page after limited in situ hydrolysis
    • Vanelethren, J. R., Raymackers, J. G., Van Bun, S. M and Mehus, L. A. (1992). Peptide mapping and microsequencing of proteins separated by SDS-PAGE after limited in situ hydrolysis. BioTechniques, 12, 550-557.
    • (1992) Biotechniques , vol.12 , pp. 550-557
    • Vanelethren, J.R.1    Raymackers, J.G.2    Van Bun, S.M.3    Mehus, L.A.4
  • 139
    • 0001305955 scopus 로고
    • Improved muss accuracy in matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry of peptides
    • Vorm, O. and Mann, M., (1994). Improved muss accuracy in matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry of peptides. Journal of the American Society for Mass Spectrometry, 5, 955-958.
    • (1994) Journal of the American Society for Mass Spectrometry , vol.5 , pp. 955-958
    • Vorm, O.1    Mann, M.2
  • 140
    • 0000094029 scopus 로고
    • Improved resolution and very high sensitivity in maldi tof of matrix surfaces made by fast evaporation
    • Vorm, O., Roepstorek P. and Mann, M. (1994). Improved resolution and very high sensitivity in MALDI TOF of matrix surfaces made by fast evaporation. Analytical Chemistry, 66, 3281-3287.
    • (1994) Analytical Chemistry , vol.66 , pp. 3281-3287
    • Vorm, O.1    Roepstorek, P.2    Mann, M.3
  • 141
    • 0026693227 scopus 로고
    • Uhramicrodeiection of proteins in polyacrylamide gels
    • Wallace, A. and Saluz, H. P. (1992a). Uhramicrodeiection of proteins in polyacrylamide gels. Analytical Biochemistry, 203, 27-34.
    • (1992) Analytical Biochemistry , vol.203 , pp. 27-34
    • Wallace, A.1    Saluz, H.P.2
  • 142
    • 0027122766 scopus 로고
    • Beyond silver staining
    • Wallaœ, A. and Saliez, H. P. (1992b). Beyond silver staining. Nature. 357, 608-609.
    • (1992) Nature , vol.357 , pp. 608-609
    • Wallaœ, A.1    Saliez, H.P.2
  • 143
    • 0028904159 scopus 로고
    • Identification of macrophage activation associated proteins by two-dimensional electrophoresis and micro-sequencing
    • Walsh, B. J., Gooley, A. A., Williams, K. L. and Breit, S. N. (1995). Identification of macrophage activation associated proteins by two-dimensional electrophoresis and micro-sequencing. Journal of Leukocyte Biology, 57, 507-512.
    • (1995) Journal of Leukocyte Biology , vol.57 , pp. 507-512
    • Walsh, B.J.1    Gooley, A.A.2    Williams, K.L.3    Breit, S.N.4
  • 145
    • 0027456341 scopus 로고
    • Monosaccharide and oligosaccharide analysis of proteins transferred to polyvinylidene fluoride membranes after sodium dodccyl sulfate-polyacrylamidc gel electrophoresis
    • Weitzhandler, M., Kadlecek, D., Avdalovic, N., Forte, J. G., Chow, D. and Townsenix R. R. (1993). Monosaccharide and oligosaccharide analysis of proteins transferred to polyvinylidene fluoride membranes after sodium dodccyl sulfate-polyacrylamidc gel electrophoresis. Journal of Biological Chemistry, 268, 5121-5130.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 5121-5130
    • Weitzhandler, M.1    Kadlecek, D.2    Avdalovic, N.3    Forte, J.G.4    Chow, D.5    Townsenix, R.R.6
  • 150
    • 0027763434 scopus 로고
    • A fast spot segmentation algorithm for two-dimensional gel electrophoresis analysis
    • Wu, Y., Lemkin, P. F. and Upton, K. (1993). A fast spot segmentation algorithm for two-dimensional gel electrophoresis analysis. Electrophoresis, 14, 1351-1356.
    • (1993) Electrophoresis , vol.14 , pp. 1351-1356
    • Wu, Y.1    Lemkin, P.F.2    Upton, K.3
  • 151
    • 0024043998 scopus 로고
    • Preparation of colloidal gold for staining proteins electrotransferred onto nitrocellulose membranes
    • Yamaguchi, K. and Asakawa, H. (1988). Preparation of colloidal gold for staining proteins electrotransferred onto nitrocellulose membranes. Analytical Biochemistry. 172, 104-107.
    • (1988) Analytical Biochemistry , vol.172 , pp. 104-107
    • Yamaguchi, K.1    Asakawa, H.2
  • 152
    • 0027503288 scopus 로고
    • Sugar chains of serum transferrin from patients with carbohydrate deficient glycoprotein syndrome. Evidence of asparaginc-n-linked oligosaccharide transfer deficiency
    • Yamashita, K., Ikdeo, H., Ohkura, T., Fükushima, K., Yuasa, K., Ohno, K. and Takeshita, K. (1993). Sugar chains of serum transferrin from patients with carbohydrate deficient glycoprotein syndrome. Evidence of asparaginc-N-linked oligosaccharide transfer deficiency. Journal of Biological Chemistry, 268, 5783-5789.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 5783-5789
    • Yamashita, K.1    Ikdeo, H.2    Ohkura, T.3    Fükushima, K.4    Yuasa, K.5    Ohno, K.6    Takeshita, K.7
  • 153
    • 0027375364 scopus 로고
    • Peptide mass maps: A highly informative approach to protein identification
    • Yates, J. R., Speicher, S., Griffin, P. R. and Hinkapiller, T. (1993). Peptide mass maps: a highly informative approach to protein identification. Analytical Biochemistry 214, 397-408.
    • (1993) Analytical Biochemistry , vol.214 , pp. 397-408
    • Yates, J.R.1    Speicher, S.2    Griffin, P.R.3    Hinkapiller, T.4


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