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Review Article

Proteomics and its impact upon biomedical science

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Pages 47-64 | Accepted 22 Nov 2001, Published online: 27 Oct 2016

References

  • Wasinger VC, Cordwell SJ, Cerpa-Poljak A et al. Progress with gene-product mapping of the Mollicutes: Mycoplasma genitalium. Electrophoresis 1995; 16: 1090–4.
  • Wilkins MR, Sanchez J-C, Gooley AA et al. Progress with proteome projects: why all proteins expressed by a genome should be identified and how to do it. Biotechnol Genet Eng Rev 1995; 13: 19–50.
  • Wilkins MR, Pasquali C, Appel RD et al. From proteins to proteomes: large-scale protein identification by two-dimensional electrophoresis and amino acid analysis. BioTechnology 1996; 14: 61–5.
  • Patton WF. Proteome analysis II. Protein subcellular redistribution: linking physiology to genomics via the proteome and separation technologies involved. J Chromatogr B 1999; 722: 203–23.
  • Bradbury J. Proteomics: the next step after genomics? Lancet 2000; 356: 50.
  • Haynes PA, Gygi SP, Figeys D, Aebersold R. Proteome analysis: biological assay or data archive? Electrophoresis 1998; 19: 1862–71.
  • Pandey A, Mann M. Proteomics to study genes and genomes. Nature 2000; 405: 837–46.
  • Gygi SP, Aebersold R. Mass spectrometry and proteomics. Curr Opin Chem Biol 2000; 4: 489–94.
  • Patterson SD. Proteomics: the industrialization of protein chemistry. Curr Opin Biotechnol 2000; 11: 413–8.
  • Banks RE, Dunn MJ, Hochstrasser DF et al. Proteomics: new perspectives, new biomedical opportunities. Lancet 2000: 356: 1749–56.
  • Anderson NG, Matheson A, Anderson NL. Back to the future: the human protein index (HPI) and the agenda for postproteomic biology. Proteomics 2001: 1: 3–12.
  • Gabor Miklos GL, Maleszka R. Integrating molecular medicine with functional proteomics: realities and expectations. Proteomics 2001: 1: 30–41.
  • Tilley A. Proteomics basics. Biomedical Scientist 2001;45:116–7.
  • Tilley A. More proteomics. Biomedical Scientist 2001;45:222–3.
  • Anderson NL, Anderson NG. Proteome and proteomics: new technologies, new concepts, and new words. Electrophoresis 1998; 19: 1853–61.
  • Lopez MF. Proteome analysis: I. Gene products are where the biological action is. J Chromatogr B 1999; 722: 191–202.
  • Blackstock WP, Weir MP. Proteomics: quantitative and physical mapping of cellular proteins. Trends Biotechnol 1999; 17: 121–7.
  • Anderson NL, Matheson AD, Steiner S. Proteomics: applications in basic and applied biology. Curr Opin Biotechnol 2000; 11: 408–12.
  • O’Farrell PH. High-resolution two-dimensional electrophoresis of proteins. J Biol Chem 1975; 250: 4007–21.
  • Scheele GA. Two-dimensional gel analysis of soluble proteins. Characterisation of guinea pig exocrine pancreatic proteins. J Biol Chem 1975; 250: 5375–85.
  • Klose J. Protein mapping by combined isoelectric focusing and electrophoresis in mouse tissues. A novel approach to testing for induced point mutations in mammals. Humangenetik 1975; 26: 231–43.
  • Special Issue. Two-dimensional gel electrophoresis. Clin Chem 1982; 28:737–1092.
  • Special Issue. Two-dimensional electrophoresis: protein mapping. Clin Chem 1984; 30: 1897–2108.
  • Anderson NL, Edwards JJ, Giometti CS et al. High-resolution two-dimensional electrophoretic mapping of human proteins. In: Radola BJ, ed. Electrophoresis Berlin: Walter de Gruyter & Co, 1979:313–28.
  • Anderson NG, Anderson NL. Automatic chemistry and the human protein index. J Autom Chem 1980; 2: 177–8.
  • Wade N. The complete index to man. Science 1981; 211: 33–5.
  • Anderson NG, Anderson NL. The human protein index. Clin Chem 1982; 28: 739–48.
  • Taylor J, Anderson NL, Scandora AE, Willard KE, Anderson NG. Design and implementation of a prototype human protein index. Clin Chem 1982; 28: 861–6.
  • Anderson NG, Anderson NL. The human protein index project and the molecular pathology database. Medical Laboratory 1982; 11: 75–94.
  • Patterson SD. From electrophoretically separated protein to identification: strategies for sequence and mass analysis. Anal Biochem 1994; 221: 1–15.
  • Gevaert K, Vandekerckhove J. Protein identification methods in proteomics. Electrophoresis 2000; 21: 1145–54.
  • Jungblat P, Dzionara M, Klose J, Wittmann-Leibold B. Identification of tissue proteins by amino acid analysis after purification by two-dimensional electrophoresis. J Protein Chem 1992; 11: 603–12.
  • Shaw G. Rapid identification of proteins. Proc Natl Acad Sci USA 1993; 90: 5138–42.
  • Hobohm U, Houthaeve T, Sander C. Amino acid analysis and protein database compositional search as a rapid and inexpensive method to identify proteins. Anal Biochem 1994; 222: 202–9.
  • Henzel WJ, Billeci TM, Stults JT, Wong SC, Grimley C, WatanabeC. Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc Natl Acad Sci USA 1993; 90: 5011–5.
  • Pappin DJC, Hojrup P, Bleasby AJ. Rapid identification of proteins by peptide-mass fingerprinting. Curr Biol 1993; 3: 327–32.
  • James P, Quadroni M, Carafoli E, Gonnet G. Protein identification by mass-profile fingerprinting. Biochem Biophys Res Commun 1993; 195: 58–64.
  • Mann M, Hojrup P, Roepstorff P. Use of mass spectrometric molecular weight information to identify proteins in sequence databases. Biol Mass Spectrom 1993; 22: 338–45.
  • Yates JR, Speicher S, Griffin PR, Hunkapiller T. Peptide mass maps: a highly informative approach to protein identification. Anal Biochem 1993; 214: 397–408.
  • Mørtz E, Vorm O, Mann M, Roepstorff P. Identification of proteins in polyacrylamide gels by mass spectrometric peptide mapping combined with database search. Biol Mass Spectrom 1994; 23: 249–61.
  • Patterson SD, Aebersold R. Mass spectrometric approaches for the identification of gel-separated proteins. Electrophoresis 1995; 16: 1791–814.
  • Lahm H-W, Langen H. Mass spectrometry: A tool for the identification of proteins separated by gels. Electrophoresis 2000; 21: 2105–14.
  • Chalmers MJ, Gaskell SJ. Advances in mass spectrometry for proteome analysis. Curr Opin Biotechnol 2000; 11: 384–90.
  • Cordwell S, Wilkins MR, Cerpa-Poljak A et al. Cross-species identification of protein separated by two-dimensional electrophoresis using MALDI-TOF and amino acid composition. Electrophoresis 1995; 16: 438–43.
  • Mann M, Wilm M. Error tolerance identification of peptides in sequence databases by peptide sequence tags. Anal Chem 1994; 66: 4390–9.
  • Matsudaira P. Sequence of picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem 1987; 262: 10035–8.
  • Rosefeld J, Cappdevielle J, Guillemot JC, Ferrara P. In-gel digestion of proteins for internal sequence analysis after oneor two-dimensional gel electrophoresis. Anal Biochem 1992; 203: 173–9.
  • Jeno P, Mini T, Moes S, Hintermann E, Horst M. Internal sequences from proteins digested in polyacrylamide gels. Anal Biochem 1995; 224: 75–82.
  • Hellman U, Wernstedt C, Gonez J, Heldin C-H. Improvement of an in-gel digestion for the micropreparation of internal protein fragments for amino acid sequencing. Anal Biochem 1995; 224: 451–5.
  • Johnson RS, Walsh KA. Sequence analysis of peptide mixtures by automated integration of Edman and mass spectrometric data. Protein Sci 1992; 1: 1083–91.
  • Bartlet-Jones M, Jeffery WA, Hansen HF, Pappin DJC. Peptide ladder sequencing by mass spectrometry using a novel volatile degradation reagent. Rapid Comm Mass Spectrom 1994; 8: 737–42.
  • Eckerskorn C, Jungblut P, Mewes W, Klose J, Lottspeich F. Identification of mouse brain proteins after two-dimensional electrophoresis and electroblotting by microsequence analysis and amino acid composition. Electrophoresis 1988; 9: 830–8.
  • Sibbald PR, Sommerfeldt H, Argos P. Identification of proteins in sequence databases from amino acid composition. Anal Biochem 1991; 198: 330–3.
  • Wilkins MR, Ou K, Appel RD et al. Rapid protein identification using N-terminal ‘sequence tag’ and amino acid analysis. Biochem Biophys Res Commun 1996; 221: 609–13.
  • Yates JR, Eng JK, McCormack AL, Shieltz D. Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal Chem 1995; 67: 1426–36.
  • Chait BT, Wang R, Beavis RC, Kent SBH. Protein ladder sequencing. Science 1993; 262: 89–92.
  • Tsugita A, TakamotoK, Kamo M, Iwadate H. C-terminal sequencing of protein. A novel partial acid hydrolysis and analysis by mass spectrometry. Eur J Biochem 1992; 206: 691–6.
  • Thiede B, Wittmann-Liebold B, Bienert M, Krause E. MALDI-MS for C-terminal sequence determination of peptides and proteins degraded by carboxypeptidase Y and P. FEBS Lett 1995; 357: 65–9.
  • Bonetto V, Bergman AC, Jornvall H, Sillard R. C-terminal sequence determination of modified peptides by MALDI-MS. J Protein Chem 1997; 16: 371–4.
  • Dongre AR, Eng JK, Yates JR. Emerging tandem mass spectrometry techniques for the rapid identification of proteins. Trends Biotechnol 1997; 15: 418–25.
  • Jensen ON, Wilm M, Schevchenko A, Mann M. Peptide sequencing of 2-DE gel-isolated proteins by nanospray tandem mass spectrometry. Methods Mol Biol 1999; 112: 571–88.
  • Merchant M, Weinberger SR. Recent advancements in surface-enhanced laser desorption/ionization-time of flight-mass spectrometry. Electrophoresis 2000; 21: 1164–7.
  • Krutchinsky AN, Zhang W, Chait BT. Rapidly switchable MALDI and electrospray quadrupole time-of-flight mass spectrometry for protein identification. J Am Soc Mass Spectrom 2000; 11: 493–504.
  • Shevchenko A, Loboda A, Shevchenko A, Ens W, Standing KG. MALDI quadrupole time-of-flight mass spectrometry: a powerful tool for proteomic research. Anal Chem 2000; 72: 2132–41.
  • Medzihradszky KF, Campbell JM, Baldwin MA et al. The characteristics of peptide collision-induced dissociation using a high-performance MALDI-TOF/TOF tandem mass spectrometer. Anal Chem 2000; 72: 552–8.
  • Vestal M, Juhasz P, Hines W, Martin S. A new delayed extraction MALDI-TOF MS-MS for characterisation of protein digests. In: Burlingame AL, Carr SA, Baldwin MA, eds. Mass spectrometry in biology and medicine 2000. New Jersey: Humana Press, 2000:1–16.
  • Davies H, Lomas L, Austen B. Profiling of amyloid beta peptide variants using SELDI protein chip arrays. BioTechniques 1999; 27: 1258–61.
  • Giometti CS, Gemmell MA, Tollaksen SL, Taylor J. Quantitation of human leukocyte proteins after silver staining: a study with two-dimensional electrophoresis. Electrophoresis 1991; 12: 536–43.
  • Rodriguez LV, Gersten DM, Ramagli LS, Johnston DA. Towards stoichiometric silver staining of proteins resolved in complex two-dimensional electrophoresis gels: Real-time analysis of pattern development. Electrophoresis 1993; 14: 628–37.
  • Berggren K, Steinberg TH, Lauber WM et al. A luminescent ruthenium complex for ultrasensitive detection of proteins immobilized on membrane supports. Anal Biochem 1999; 276: 129–43.
  • Patton WF. A thousand points of light: the application of fluorescence detection technologies to two-dimensional gel electrophoresis and proteomics. Electrophoresis 2000; 21: 1123–44.
  • Berggren K, Chernokalskaya E, Steinberg TH et al. Backgroundfree, high sensitivity staining of proteins in one- and two-dimensional sodium dodecyl sulfate-polyacrylamide gels using a luminescent ruthenium complex. Electrophoresis 2000; 21: 2509–21.
  • Garrels JI. The QUEST system for quantitative analysis of two-dimensional electrophoresis gels. J Biol Chem 1989; 264: 5269–82.
  • Celis JE, Gesser B, Rasmussen HH et al. Comprehensive two-dimensional gel protein databases offer a global approach to the analysis of human cells: the transformed amnion cells (AMA) master database and its link to genome DNA sequence data. Electrophoresis 1990; 11: 989–1071.
  • Celis JE, Olsen E. A qualitative and quantitative protein database approach identifies 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 1994; 15: 309–44.
  • Gygi SP, Rist B, Aebersold R. Measuring gene expression by quantitative proteome analysis. Curr Opin Biotechnol 2000; 11: 396–401.
  • 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: 6591–6.
  • Gygi SP, Rist B, Gerber SA, Turecek F, Gelb MH, Aebersold R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 1999; 17: 994–9.
  • Munchbach M, Quadroni M, Miotto G, James P. Quantitation and facilitated de novo sequencing of proteins by isotopic N-terminal labelling of peptides with a fragmentation-directing moiety. Anal Chem 2000; 72: 4047–57.
  • Appel RD, Bairoch A, Hochstrasser DF. A new generation of information retrieval tools for biologists: the example of the ExPASy WWW server. TIBS 1994; 19: 258–60.
  • Hochstrasser DF, Appel RD, Golaz O, Pasquali C, Sanchez J-C, Bairoch A. Sharing of worldwide spread knowledge using hypermedia facilities and fast communication protocols (mosaic and world wide web): the example of ExPASy. Methods Inf Med 1995; 34: 75–8.
  • Anderson NL, Taylor J, Scandora AE, Coulter BP, Anderson NG. The TYCHO system for computer analysis of two-dimensional gel electrophoresis patterns. Clin Chem 1981; 27: 1807–20.
  • Olson AD, Miller MJ. ELSIE 4: quantitative computer analysis of sets of two-dimensional gel electrophoretograms. Anal Biochem 1988; 169: 49–70
  • Lemkin PF, Wu Y, Upton K. An efficient disk-based data structure for rapid searching of quantitative two-dimensional gel databases. Electrophoresis 1993; 14: 1341–50.
  • Wu Y, Lemkin PF, Upton K. A fast spot segmentation algorithm for two-dimensional gel electrophoresis analysis. Electrophoresis 1993; 14: 1351–6.
  • Monardo PJ, Boutell T, Garrels JI, Latter GI. A distributed system for two-dimensional gel analysis. Comput Appl Biosci 1994; 10: 137–43.
  • Appel RD, Palagi PM, Walther D et al. MELANIE II – a third-generation software package for analysis of two-dimensional electrophoresis images. 1. Features and user interface. Electrophoresis 1997; 18: 2724–34.
  • Appel RD, Vargas JR, Palagi PM, Walther D, Hochstrasser DF. MELANIE II – a third-generation software package for analysis of two-dimensional electrophoresis images. 2. Algorithms. Electrophoresis 1997; 18: 2735–48.
  • Fenyö D. Identifying the proteome: software tools. Curr Opin Biotechnol 2000; 11: 391–5.
  • Clauser KR, Hall SC, Smith DM et al. Rapid mass spectrometric peptide sequencing and mass matching for characterization of human melanoma proteins isolated by two-dimensional PAGE. Proc Natl Acad Sci USA 1995; 92: 5072–6.
  • Clauser KR, Baker P, Burlingame AL. Role of accurate mass measurement (± 10 ppm) in protein identification strategies employing MS or MS/MS and database searching. Anal Chem 1999; 71: 2871–82.
  • Fenyö D, Qin J, Chait BT. Protein identification using mass spectrometric information. Electrophoresis 1998; 19: 998–1005.
  • Wilkins MR, Gasteiger E, Tonella L et al. Protein identification with N and C-terminal sequence tags in proteome projects. J Mol Biol 1998; 278: 599–608.
  • Wilkins MR, Gasteiger E, Wheeler CH et al. Multiple parameter cross-species protein identification using MultiIdent – a world wide web-accessible tool. Electrophoresis 1998; 19: 3199–206.
  • Gras R, Muller M, Gasteiger E et al. Improving protein identification from peptide mass fingerprinting through a parameterized multi-level scoring algorithm and an optimized peak detection. Electrophoresis 1999; 20: 3535–50.
  • Wilkins MR, Gasteiger E, Bairoch A et al. Protein identification and analysis tools in the ExPASy server. Methods Mol Biol 1999; 112: 531–52.
  • Perkins DN, Pappin DJ, Creasy DM, Cottrell JS. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999; 20: 3551–67.
  • Zhang W, Chait BT. ProFound: an expert system for protein identification using mass spectrometric peptide mapping information. Anal Chem 2000; 72: 2482–9.
  • Erikssom J, Chait BT, Fenyö D. A statistical basis for testing the significance of mass spectrometric protein identification results. Anal Chem 2000; 72: 999–1005.
  • Hoogland C, Sanchez J-C, Tonella L et al. The 1999 SWISS-2DPAGE database update. Nucleic Acids Res 2000; 28: 286–8.
  • Pleissner K-P, Soeding P, Sander S et al. Dilated cardiomyopathyassociated proteins and their presentation in a WWW-accessible two-dimensional gel protein database. Electrophoresis 1997; 18: 802–8.
  • Evans G, Wheeler CH, Corbett JM, Dunn MJ. Construction of HSC-2DPAGE: a two-dimensional gel electrophoresis database of heart proteins. Electrophoresis 1997; 18: 471–9.
  • Otto A, Benndorf R, Wittmann-Liebold B, Jungblut P. Identification of proteins on two-dimensional gels for the construction of a human heart 2-DE database. J Prot Chem 1994; 13: 478–80.
  • Celis JE, Østergaard M, Jensen NA, Gromova I, Rasmussen HH, Gromov P. Human and mouse proteomic databases: novel resources in the protein universe. FEBS Letts 1998; 430: 64–72.
  • Liberatori S, Bini L, De Felice C et al. A two-dimensional protein map of human amniotic fluid at 17 weeks gestation. Electrophoresis 1997; 18: 2816–22.
  • Bini L, Magi B, Marzocchi B et al. Protein expression profiles in human breast ductal carcinoma and histologically normal tissue. Electrophoresis 1997; 18: 2832–41.
  • Stulik J, Koupilova K, Österreicher J et al. Protein abundance alterations in matched sets of microscopically normal colon mucosa and colorectal carcinoma. Electrophoresis 1999; 20: 3638–46.
  • Rasmussen RK, Ji H, Eddes JS, Moritz RL, Reid GE, Simpson RJ. Database of proteins from the human breast carcinoma cell line MDA-MB231. Electrophoresis 1997; 18: 588–98.
  • Poirer F, Imam N, Pontet M, Joubert-Caron R, Caron M. The BPP (protein biochemistry and proteomics) two-dimensional electrophoresis database. J Chromatogr B Biomed Sci Appl 2001; 753: 23–8.
  • Toda T, Kaji K, Kimura N. TMIG-2DPAGE: a new concept of two-dimensional gel protein database for research on ageing. Electrophoresis 1998; 19: 344–8.
  • Wattiez R, Hermans C, Cruyt C, Bernard A, Falmagne P. Human bronchoalveolar lavage fluid protein 2-DE database: study of interstitial lung diseases. Electrophoresis 2000; 21: 2703–12.
  • Thalmann I, Kohut RI, Ryu JH, Thalmann R. High-resolution two-dimensional electrophoresis: technique and potential applicability to the study of inner ear disease. Am J Otol 1995; 16: 153–7.
  • Rabilloud T, Kieffer S, Procaccio V et al. Two-dimensional electrophoresis of human placental mitochondria and protein identification by mass spectrometry: toward a human mitochondrial proteome. Electrophoresis 1998; 19: 1006–14.
  • Bini L, Sanchez-Campillo M, Santucci A et al. Mapping of Chlamydia trachomatis proteins by Immobiline-polyacrylamide two-dimensional electrophoresis: spot identification by N-terminal sequencing and immunoblotting. Electrophoresis 1996; 17: 185–90.
  • Mollenkopf H-J, Jungblut PR, Raupach B et al. A dynamic bacterial 2D-PAGE database: the mycobacterial proteome via internet. Electrophoresis 1999; 20: 2172–80.
  • Cash P, Argo E, Langford P, Kroll SJ. Development of an haemophilus 2D protein database. Electrophoresis 1997; 18: 1472–82.
  • Rosenkrands I, Weldingh K, Jacobsen S et al. Mapping and identification of Mycobacterium tuberculosis proteins by two-dimensional electrophoresis. Electrophoresis 2000; 21: 935–48.
  • Fischer HG, Stachelhaus S, Sahm M, Meyer HE, Reichmann G. GRA7, an excretory 29 kDa Toxoplasma gondii dense granule antigen released by infected host cells. Mol Biochem Parasitol 1998; 91: 251–62.
  • Cash P. Proteomics in medical microbiology. Electrophoresis 2000; 21: 1187–1201.
  • Cordwell SJ, Nouwens AS, Walsh BJ. Comparative proteomics of bacterial pathogens. Proteomics 2001; 1: 461–72.
  • Fountoulakis M, Takacs B, Langen H. Two-dimensional map of basic proteins of Haemophilus influenzae. Electrophoresis 1998; 19: 761–6.
  • Fountoulakis M, Juranville JF, Roder D, Evers S, Berndt P, Langen H. Reference map of the low molecular mass proteins of Haemophilus influenzae. Electrophoresis 1998; 19: 1819–27.
  • Williams KM. The cell walls of methylotrophs PhD Thesis, University of Newcastle upon Tyne, 1984.
  • Jackson P, Thornley MJ, Thompson RJ. A study by high-resolution two-dimensional polyacrylamide gel electrophoresis of relationships between Neisseria gonorrhoeae and other bacteria. J Gen Microbiol 1984; 130: 3189–201.
  • Andersen H, Christiansen G, Christiansen C. Electrophoretic analysis of proteins from Mycoplasma capricolum and related serotypes using extracts from intact cells and from minicells containing cloned mycoplasma DNA. J Gen Microbiol 1984; 130: 1409–18.
  • Watson HL, Davidson MK, Cox NR, Davis JK, Dyvig K, Cassell GH. Protein variability among strains of Mycoplasma pulmonis. Infect Immunol 1987; 55: 2838–40.
  • Dunn BE, Perez-Perez GI, Blaser MJ. Two-dimensional gel electrophoresis and immunoblotting of Campylobacter pylori proteins. Infect Immunol 1989; 57: 1825–33.
  • Cash P, Argo E, Bruce KD. Characterisation of Haemophilus influenzae proteins by two-dimensional gel electrophoresis. Electrophoresis 1995; 16: 135–48.
  • Gorman T, Phan-Thanh L. Identification and classification of Listeria by two-dimensional protein mapping. Res Microbiol 1995; 146: 143–54.
  • Enroth H, Akerlund T, Sillen A, Engstrand L. Clustering of clinical strains of Helicobacter pylori analyzed by two-dimensional electrophoresis. Clin Diagn Lab Immunol 2000; 7: 301–6.
  • Jungblut PR, Bumann D, Haas G et al. Comparative proteome analysis of Helicobacter pylori. Mol Microbiol 2000; 36: 710–25.
  • Hansen EJ, Wilson RM, Baseman JB. Two-dimensional gel electrophoretic comparison of proteins from virulent and avirulent strains of Mycoplasma pneumoniae. Infect Immunol 1979; 24: 468–75.
  • Sowa BA, Kelly KA, Ficht TA, Adams LG. Virulence-associated proteins of Brucella abortus identified by paired two-dimensional gel electrophoretic comparisons of virulent, vaccine and LPSdeficient strains. Appl Theor Electrophor 1992; 3: 33–40.
  • Mahairas GG, Sabo PJ, Hickey MJ, Singh DC, Stover CK. Molecular analysis of genetic differences between Mycobacterium bovis BCG and virulent M. bovis. J Bacteriol 1996; 178: 1274–82.
  • Urquhart BL, Atsalos TE, Roach D et al. ‘Proteomic contigs’ of Mycobacterium tuberculosis and Mycobacterium bovis (BCG) using novel immobilised pH gradients. Electrophoresis 1997; 18: 1384–92.
  • Jungblut PR, Schaible UE, Mollenkopf HJ et al. Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: towards functional genomics of microbial pathogens. Mol Microbiol 1999; 33: 1103–17.
  • Sturgill-Koszycki S, Haddix PL, Russell DG. The interaction between mycobacterium and the macrophage analyzed by two-dimensional polyacrylamide gel electrophoresis. Electrophoresis 1997; 18: 2558–65.
  • Marshall T, Latner AL. High-resolution electrophoresis of extracts of a baby hamster kidney cell line before and after transformation by polyoma virus. Electrophoresis 1983; 4: 354–8.
  • Duncan RF. Protein synthesis initiation factor modifications during viral infections: implications for translational control. Electrophoresis 1990; 11: 219–27.
  • Kettman J, Hoot G, Kuhn L, Lefkovits I. Polyoma-induced thymic epithelial tumors: analysis by 2D gel electrophoresis of tumors upon labelling the entire tumor bearing host. Thymus 1990; 15: 167–97.
  • Argo E, Gimenez B, Cash P. Non-cytopathic infection of rhabdomyosarcoma cells by coxsackie B5 virus. Arch Virol 1992; 126: 215–29.
  • Greco A, Bienvenut W, Sanchez J-C et al. Identification of ribosome-associated viral and cellular basic proteins during the course of infection with herpes simplex virus type 1. Proteomics 2001; 1: 545–9.
  • McAtee CP, Lim MY, Fung K et al. Identification of potential diagnostic and vaccine candidates of Helicobacter pylori by two-dimensional gel electrophoresis, sequence analysis and serum profiling. Clin Diagn Lab Immunol 1998; 5: 537–42
  • McAtee CP, Fry KE, Berg DE. Identification of potential diagnostic and vaccine candidates of Helicobacter pylori by ‘proteome’ technologies. Helicobacter 1998; 3: 163–9.
  • Bumann, Meyer TF, Jungblut PR. Proteome analysis of the common human pathogen Helicobacter pylori. Proteomics 2001; 1: 473–9.
  • Lemos JA, Giambiagi-Demarval M, Castro AC. Expression of heat-shock proteins in Streptococcus pyogenes and their immunoreactivity with sera from patients with streptococcal diseases. J Med Microbiol 1998; 47: 711–5.
  • Jungblut PR, Grabher G, Stoffler G. Comprehensive detection of immunorelevant Borrelia garinii antigens by two-dimensional electrophoresis. Electrophoresis 1999; 20: 3611–22.
  • Geissler S, Sokolowska-Kohler W, Bollmann R, Jungblut PR, Presber W. Toxoplasma gondii infection: analysis of serological response by 2-DE immunoblotting. FEMS Immunol Med Microbiol 1999; 25: 299–311.
  • Sonnenberg MG, Belisle JT. Definition of Mycobacterium tuberculosis culture filtrate proteins by two-dimensional polyacrylamide gel electrophoresis, N-terminal amino acid sequencing, and electrospray mass spectrometry. Infect Immunol 1997; 65: 4515–24.
  • Rosenkrands I, Rasmussen PB, Carnio M, Jacobsen S, Theisen M, Andersen P. Identification and characterization of a 29-kilodalton protein from Mycobacterium tuberculosis culture filtrate recognized by mouse memory effector cells. Infect Immunol 1998; 66: 2728–35.
  • Samanich KM, Belisle JT, Sonnenberg MG, Keen MA, Zolla-Pazner S, Laal S. Delineation of human antibody responses to culture filtrate antigens of Mycobacterium tuberculosis. J Infect Dis 1998; 178: 1534–8.
  • Vurma-Rapp U, Kayser FH, Hadorn K, Wiederkehr F. Mechanism of imipenem resistance acquired by three Pseudomonas aeruginosa strains during imipenem therapy. Eur J Clin Microbiol Infect Dis 1990; 9: 580–7.
  • Abadi FJ, Carter PE, Cash P, Pennington TH. Rifampin resistance in Neisseria meningitidis due to alterations in membrane permeability. Antimicro Agents Chemother 1996; 40: 646–51.
  • Cash P, Argo E, Ford L, Lawrie L, McKenzie H. A proteomic analysis of erythromycin resistance in Streptococcus pneumoniae. Electrophoresis 1999; 20: 2259–68.
  • Marichal P, Vanden Bossche H, Odds FC et al. Molecular biological characterization of an azole-resistant Candida glabrata isolate. Antimicro Agents Chemother 1997; 41: 2229–37.
  • Jung E, Heller M, Sanchez J-C, Hochstrasser DF. Proteomics meets cell biology: the establishment of subcellular proteomes. Electrophoresis 2000; 21: 3369–77.
  • Scharfe C, Zaccaria P, Hoertnagel K et al. MITOP, the mitochondrial proteome database: 2000 update. Nucleic Acids Res 2000; 28: 155–8.
  • Jung E, Hoogland C, Chiappe D, Sanchez J-C, Hochstrasser DF. The establishment of a human liver nuclei two-dimensional electrophoresis reference map. Electrophoresis 2000; 21: 3483–7.
  • Muller EC, Schumann M, Rickers A, Bommert K, Wittmann-Liebold B, Otto A. Study of Burkitt lymphoma cell line proteins by high-resolution two-dimensional gel electrophoresis and nanospray mass spectrometry. Electrophoresis 1999; 20: 320–30.
  • Gerner C, Holzmann K, Grimm R, Sauermann G. Similarity between nuclear matrix proteins of various cells revealed by an improved isolation method. J Cell Biochem 1998; 71: 363–74.
  • Gerner C, Sauermann G. Nuclear matrix proteins specific for subtypes of human hematopoietic cells. J Cell Biochem 1999; 72: 470–82.
  • Gerner C, Holzmann K, Meissner M, Gotzmann J, Grimm R, Sauermann G. Reassembling proteins and chaperones in human nuclear matrix protein fractions. J Cell Biochem 1999; 74: 145–51.
  • Chataway TK, Whittle AM, Lewis MD et al. Two-dimensional mapping and microsequencing of lysosomal proteins from human placenta. Placenta 1998; 19: 643–54.
  • Neubauer G, King A, Rappsilber J et al. Mass spectrometry and EST-database searching allows characterization of the multiprotein spliceosome complex. Nat Genet 1998; 20: 46–50.
  • Hanson BJ, Schulenberg B, Patton WF, Capaldi RA. A novel subfractionation approach for mitochondrial proteins: a threedimensional mitochondrial proteome map. Electrophoresis 2001; 22: 950–9.
  • Pasquali C, Fialka I, Huber LA. Subcellular fractionation, electromigration analysis and mapping of organelles. J Chromatogr B Biomed Sci Appl 1999; 722: 89–102.
  • Alaiya AA, Franzen B, Auer G, Linder S. Cancer proteomics: from identification of novel markers to creation of artificial learning models for tumor classification. Electrophoresis 2000; 21: 1210–7.
  • Celis JE, Wolf H, Østergaard M. Bladder squamous cell carcinoma biomarkers derived from proteomics. Electrophoresis 2000; 21: 2115–21.
  • Østergaard M, Rasmussen HH, Nielsen HV et al. Proteome profiling of bladder squamous cell carcinomas: identification of markers that define their degree of differentiation. Cancer Res 1997; 57: 4111–7.
  • Celis JE, Østergaard M, Rasmussen HH et al. A comprehensive protein resource for the study of bladder cancer: <http://biobase.dk/cgi-bin/celis>. Electrophoresis 1999; 20: 300–9.
  • Celis JE, Celis P, Østergaard M et al. Proteomics and immunohistochemistry define some of the steps involved in the squamous differentiation of the bladder transitional epithelium: a novel strategy for identifying metaplastic lesions. Cancer Res 1999; 59: 3003–9.
  • Celis JE, Rasmussen HH, Vorum H et al. Bladder squamous cell carcinomas express psoriasin and externalise it to the urine. J Urol 1996; 155: 2105–12.
  • Østergaard M, Wolf H, Orntoft TF, Celis JE. Psoriasin (S100A7): a putative urinary marker for the follow-up of patients with bladder squamous cell carcinomas. Electrophoresis 1999; 20: 349–54.
  • Celis A, Rasmussen HH, Celis P et al. Short-term culturing of low-grade superficial bladder transitional cell carcinomas leads to changes in the expression levels of several proteins involved in key cellular activities. Electrophoresis 1999; 20: 355–61.
  • Franzen B, Linder S, Uryu K et al. Expression of tropomyosin isoforms in benign and malignant human breast lesions. Br J Cancer 1996; 73: 909–13.
  • Franzen B, Auer G, Alaiya AA et al. Assessment of homogeneity in polypeptide expression in breast carcinomas shows widely variable expression in highly malignant tumours. Int J Cancer 1996; 69: 408–14.
  • Giometti CS, Williams K, Tollaksen SL. A two-dimensional electrophoresis database of human breast epithelial cell proteins. Electrophoresis 1997; 18: 573–81.
  • Alaiya AA, Franzen B, Fujioka K et al. Phenotypic analysis of ovarian carcinoma: polypeptide expression in benign, borderline and malignant tumors. Int J Cancer 1997; 73: 678–83.
  • Alaiya AA, Franzen B, Hagman A et al. Classification of human ovarian tumors using multivariate data analysis of polypeptide expression patterns. Int J Cancer 2000; 86: 731–6.
  • Alaiya AA, Roblick U, Egevad L et al. Polypeptide expression in prostate hyperplasia and prostate adenocarcinoma. Anal Cell Pathol 2000; 21: 1–9.
  • Alaiya AA, Oppermann M, Langridge J et al. Identification of proteins in human prostate tumor material by two-dimensional gel electrophoresis and mass spectrometry. Cell Mol Life Sci 2001; 58: 307–11.
  • Jungblut PR, Zimny-Arndt U, Zeindl-Eberhart E et al. Proteomics in human disease: cancer, heart and infectious diseases. Electrophoresis 1999; 20: 2100–10.
  • Hirano T, Fujioka K, Franzen B et al. Relationship between TAO1 and TAO2 polypeptides associated with lung adenocarcinoma and histocytological features. Br J Cancer 1997; 75: 978–85.
  • Chuman Y, Bergman A, Ueno T et al. A member of the aspartic protease family is abundantly expressed in normal lung and kidney tissue and is expressed in lung adenocarcinomas. FEBS Lett 1999; 26: 129–34.
  • Sarto C, Marocchi A, Sanchez J-C et al. Renal cell carcinoma and normal kidney protein expression. Electrophoresis 1997; 18: 599–604.
  • Marshall T, Williams J, Williams KM. Two-dimensional electrophoresis of human serum proteins following acute myocardial infarction. Electrophoresis 1989; 10: 584–8.
  • Knecht M, Regitz-Zagrosek V, Pleissner KP et al. Characterization of myocardial protein composition in dilated cardiomyopathy by two-dimensional gel electrophoresis. Eur Heart J 1994; 15: 37–44.
  • Corbett JM, Why HJ, Wheeler CH et al. Cardiac protein abnormalities in dilated cardiomyopathy detected by two-dimensional polyacrylamide gel electrophoresis. Electrophoresis 1998; 19: 2031–42.
  • Latif N, Taylor PM, Khan MA, Yacoub MH, Dunn MJ. The expression of heat shock protein 60 in patients with dilated cardiomyopathy. Basic Res Cardiol 1999; 94: 112–9.
  • Scheler C, Li XP, Salnikow J, Dunn MJ, Jungblut PR. Comparison of two-dimensional electrophoresis patterns of heat shock protein hsp27 species in normal and cardiomyopathic hearts. Electrophoresis 1999; 20: 3623–8.
  • Latif N, Khan MA, Birks E et al. Upregulation of the Bcl-2 family of proteins in end-stage heart failure. J Am Coll Cardiol 2000; 35: 1769–77.
  • Dunn MJ. Studying heart disease using the proteomic approach. Drug Discov Today 2000; 5: 76–84.
  • Emmert-Buck MR, Bonner RF, Smith PD et al. Laser capture microdissection. Science 1996: 274: 921–2.
  • Banks RE, Dunn MJ, Forbes MA et al. The potential use of laser capture microdissection to selectively obtain distinct populations of cells for proteomic analysis: preliminary findings. Electrophoresis 1999; 20: 689–700.
  • Emmert-Buck MR, Gillespie JW, Paweletz CP et al. An approach to proteomic analysis of human tumors. Mol Carcinog 2000; 27: 158–65.
  • Paweletz CP, Liotta LA, Petricoin EF. New technologies for biomarker analysis of prostate cancer progression: laser capture microdissection and tissue proteomics. Urology 2001; 57: 160–3.
  • Simone NL, Paweletz CP, Charboneau L, Petricoin EF, Liotta LA. Laser capture microdissection: beyond functional genomics to proteomics. Mol Diagn 2000; 5: 301–7.
  • Gillespie JW, Ahram M, Best CJ et al. The role of tissue microdissection in cancer research. Cancer J 2001; 7: 32–9.
  • Hochstrasser DF, Tissot J-D. Clinical application of high-resolution two-dimensional polyacrylamide gel electrophoresis. Adv Electrophor 1993; 6: 267–375.
  • Marshall T, Williams KM, Holmquist L, Carlson LA, Vesterberg O. Plasma apolipoprotein pattern in fish-eye disease examined by high-resolution two-dimensional electrophoresis. Clin Chem 1985; 31: 2032–5.
  • Latner AL, Marshall T, Gambie M. Microheterogeneity of serum myeloma immunoglobulins revealed by a technique of high-resolution two-dimensional electrophoresis. Electrophoresis 1980; 1: 82–9.
  • Marshall T, Williams KM. The simplified technique of high-resolution two-dimensional polyacrylamide gel electrophoresis: biomedical applications in health and disease. Electrophoresis 1991; 12: 461–71.
  • Liberatori S, Bini L, De Felice C et al. Acute-phase proteins in perinatal human plasma. Electrophoresis 1997; 18: 520–6.
  • Charrier J-P, Tournel C, Michel S et al. Differential diagnosis of prostate cancer and benign prostate hyperplasia using two-dimensional electrophoresis. Electrophoresis 2001; 22: 1861–6.
  • Gerner C, Steinkellner W, Holzmann K et al. Elevated plasma levels of crosslinked fibrinogen g-chain dimer indicate cancerrelated fibrin deposition and fibrinolysis. Thromb Haemost 2001; 85: 494–501.
  • Harrington MG, Merril CR, Torrey EF. Differences in cerebrospinal fluid proteins between patients with schizophrenia and normal persons. Clin Chem 1985; 31: 722–6.
  • Harrington MG, Merril CR, Asher DM, Gajdusek DC. Abnormal proteins in the cerebrospinal fluid of patients with Creutzfeldt-Jakob disease. N Engl J Med 1986; 315: 279–83.
  • Lee KH, Harrington MG. The assay development of a molecular marker for transmissable spongiform encephalopathies. Electrophoresis 1997; 18: 502–6.
  • Zerr I, Bodemer M, Gefeller O et al. Detection of 14–3-3 protein in the cerebrospinal fluid supports the diagnosis of Creutzfeldt-Jakob disease. Ann Neurol 1998; 43: 32–40.
  • Beaudry P, Cohen P, Brandel JP et al. 14–3-3 protein, neuronespecific enolase and S-100 protein in cerebrospinal fluid of patients with Creutzfeldt-Jakob disease. Dement Geriatr Cogn Disord 1999; 10: 40–6.
  • Burkhard PR, Sanchez J-C, Landis T, Hochstrasser DF. CSF detection of the 14–3-3 protein in unselected patients with dementia. Neurology 2001; 56: 1528–33.
  • Green AJ, Thompson EJ, Stewart GE et al. Use of 14–3-3 and other brain-specific proteins in CSF in the diagnosis of variant Creutzfeldt-Jakob disease. J Neurol Neurosurg Psychiatry 2001; 70: 744–8.
  • Rohlff C. Proteomics in molecular medicine: applications in central nervous systems disorders. Electrophoresis 2000; 21: 1227–34.
  • Rohlff C. Proteomics in neuropsychiatric disorders. Int J Neuropsychopharmacol 2001; 4: 93–102.
  • Marshall T, Williams KM. Clinical analysis of human urinary proteins using high- resolution electrophoretic methods. Electrophoresis 1998; 9: 1752–70.
  • Hampel DJ, Sansome C, Sha M, Brodsky S, Lawson WE, Goligorsky MS. Toward proteomics in uroscopy: urinary protein profiles after radiocontrast medium administration. J Am Soc Nephrol 2001; 12: 1026–35.
  • Marshall T, Williams KM. Electrophoretic analysis of Bence-Jones proteinuria. Electrophoresis 1999; 20: 1307–24.
  • Thiede B, Siejak F, Dimmler C, Jungblut PR, Rudel T. A two-dimensional electrophoresis database of a human Jurkat T-cell line. Electrophoresis 2000; 21: 2713–20.
  • Marcus K, Immler D, Sternberger J, Meyer HE. Identification of platelet proteins separated by two-dimensional gel electrophoresis and analyzed by matrix-assisted laser desorption/ionization-time of flight-mass spectrometry and detection of tyrosine-phosphorylated proteins. Electrophoresis 2000; 21: 2622–36.
  • Steiner S, Witzmann FA. Proteomics: applications and opportunities in preclinical drug development. Electrophoresis 2000; 21: 2099–104.
  • Steiner S, Anderson NL. Expression profiling in toxicology: potentials and limitations. Toxicol Lett 2000; 112–113: 467–71.
  • Cutler P, Birrell H, Haran M et al. Proteomics in pharmaceutical research and development. Biochem Soc Trans 1999; 27: 555–9.
  • Anderson NL, Esquer-Blasco R, Hofmann JP, Anderson NG. A two-dimensional gel database of rat liver proteins useful in gene regulation and drug effects studies. Electrophoresis 1991; 12: 907–30
  • Steiner S, Gatlin CL, Lennon JJ et al. Proteomics to display lovastatin-induced protein and pathway regulation in rat liver. Electrophoresis 2000; 21: 2129–37.
  • Steiner S, Gatlin CL, Lennon JJ et al. Cholesterol biosynthesis regulation and protein changes in rat liver following treatment with fluvastatin. Toxicol Lett 2001; 120: 369–77.
  • Anderson L, Steele VK, Kelloff GJ, Sharma S. Effects of oltipraz and related chemoprevention compounds on gene expression in rat liver. J Cell Biochem Suppl 1995; 22: 108–16.
  • Steiner S, Wahl D, Mangold BL et al. Induction of the adipose differentiation-related protein in liver of etomoxir-treated rats. Biochem Biophys Res Commun 1996; 218: 777–82.
  • Arce A, Aicher L, Wahl D et al. Changes in the liver protein pattern of female Wistar rats treated with the hypoglycemic agent SDZ PGU 693. Life Sci 1998; 63: 2243–50.
  • Anderson NL, Esquer-Blasco R, Richardson F, Foxworthy P, Eacho P. The effects of peroxisome proliferators on protein abundancies in mouse liver. Toxicol Appl Pharmacol 1996; 137: 75–89.
  • Giometti CS, Tollaksen SL, Liang X, Cunningham ML. A comparison of liver protein changes in mice and hamsters treated with the peroxisome proliferator Wy-14,643. Electrophoresis 1998; 19: 2498–505.
  • Giometti CS, Liang X, Tollaksen SL et al. Mouse liver selenium-binding protein decreased in abundance by peroxisome proliferators. Electrophoresis 2000; 21: 2162–9.
  • Fountoulakis M, Berndt P, Boelsterli UA et al. Two-dimensional database of mouse liver proteins: changes in hepatic protein levels following treatment with acetaminophen or its non-toxic regioisomer 3-acetamidophenol. Electrophoresis 2000; 21: 2148–61.
  • Myers TG, Anderson NL, Waltham M et al. A protein expression database for the molecular pharmacology of cancer. Electrophoresis 1997; 18: 647–53.
  • Kovarova H, Hajduch M, Korinkova G et al. Proteomics approach in classifying the biochemical basis of the anticancer activity of the new olomoucine-derived synthetic cyclin-dependent kinase inhibitor bohemine. Electrophoresis 2000; 21: 3757–64.
  • Moller A, Soldan M, Volker U, Maser E. Two-dimensional gel electrophoresis: a powerful method to elucidate cellular responses to toxic compounds. Toxicology 2001; 160: 129–38.
  • Myers TG, Dietz EC, Anderson NL, Khairallah EA, Cohen SD, Nelson SD. A comparative study of mouse liver proteins arylated by reactive metabolites of acetaminophen and its nonhepatotoxic regioisomer 3’-hydroxyacetanilide. Chem Res Toxicol 1995; 8: 403–13.
  • Storm SM, Khawaja XZ. Probing for drug-induced multiplex signal transduction pathways using high-resolution two-dimensional gel electrophoresis: application to b-adrenoceptor stimulation in the rat C6 glioma cell. Brain Res Mol Brain Res 1999; 71: 50–60.
  • Blunk T, Hochstrasser DF, Sanchez J-C, Muller BW, Muller RH. Colloidal carriers for intravenous drug targeting: plasma protein adsorption patterns on surface-modified latex particles evaluated by two-dimensional polyacrylamide gel electrophoresis. Electrophoresis 1993; 14: 1382–7.
  • Luck M, Schroder W, Paulke BR, Blunk T, Muller RH. Complement activation by model drug carriers for intravenous application: determination by two-dimensional electrophoresis. Biomaterials 1999; 20: 2063–8.
  • Marshall T, Vesterberg O. Effects of chemical exposure on rat serum proteins revealed by a modified technique of two-dimensional gel electrophoresis. Electrophoresis 1983; 4: 363–6.
  • Marshall T, Williams KM, Vesterberg O. A comparison of two-dimensional gel electrophoresis methods for analysis of rat serum proteins following dimethylformamide exposure. Electrophoresis 1985; 6: 392–8.
  • Miller I, Haynes P, Eberini I, Gemeiner M, Aebersold R, Gianazza E. Proteins of rat serum: III. Gender-related differences in protein concentration under baseline conditions and upon experimental inflammation as evaluated by two-dimensional electrophoresis. Electrophoresis 1999; 20: 836–45.
  • Eberini I, Miller I, Zancan V et al. Proteins of rat serum: IV. Time course of acute-phase protein expression and its modulation by indomethacine. Electrophoresis 1999; 20: 846–53.
  • Eberini I, Agnello D, Miller I et al. Proteins of rat serum: V. Adjuvant arthritis and its modulation by non-steroidal anti-inflammatory drugs. Electrophoresis 2000; 21: 2170–9.
  • Marshall T, Williams KM, Vesterberg O. Unconcentrated human urinary proteins analysed by high-resolution two-dimensional electrophoresis with narrow pH gradients: preliminary findings after occupational exposure to cadmium. Electrophoresis 1985; 6: 47–52.
  • Myrick JE, Caudill SP, Robinson MK, Hubert IL. Quantitative two-dimensional electrophoretic detection of possible urinary protein biomarkers of occupational exposure to cadmium. Appl Theor Electrophor 1993; 3: 137–46.
  • Witzmann FA, Fultz CD, Grant RA, Wright LS, Kornguth SE, Siegel FL. Regional protein alterations in rat kidneys induced by lead exposure. Electrophoresis 1999; 20: 943–51.
  • Kanitz MH, Witzmann FA, Zhu H et al. Alterations in rabbit kidney protein expression following lead exposure as analyzed by two-dimensional electrophoresis. Electrophoresis 1999; 20: 2977–85.
  • Witzmann FA, Bauer MD, Fieno AM et al. Proteomic analysis of the renal effects of simulated occupational jet fuel exposure. Electrophoresis 2000; 21: 976–84.
  • Witzmann FA, Carpenter RL, Ritchie GD, Wilson CL, Nordholm AF, Rossi J. Toxicity of chemical mixtures: proteomic analysis of persisting liver and kidney protein alterations induced by repeated exposure of rats to JP-8 jet fuel vapour. Electrophoresis 2000; 21: 2138–47.
  • Cutler P, Bell DJ, Birrell HC et al. An integrated proteomic approach to studying glomerular nephrotoxicity. Electrophoresis 1999; 20: 3647–58.
  • Steiner S, Aicher L, Raymackers J et al. Cyclosporine A decreases the protein level of the calcium-binding protein calbindin-D 28kDa in rat kidney. Biochem Pharmacol 1996; 51: 253–8.
  • Aicher L, Wahl D, Arce A, Grenet O, Steiner S. New insights into cyclosporine A nephrotoxicity by proteome analysis. Electrophoresis 1998; 19: 1998–2003.
  • Celis JE, Gromov P. 2D protein electrophoresis: can it be perfected? Curr Opin Biotechnol 1999; 10: 16–21.
  • Haynes PA, Yates JR. Proteome profiling – pitfalls and progress. Yeast 2000; 17: 81–7.
  • Righetti PG, Bossi A. Isoelectric focusing in immobilised pH gradients: an update. J Chromatogr B Biomed Sci Appl 1997; 699: 77–89.
  • Marshall T, Williams KM, Vesterberg O. Two-dimensional electrophoresis of proteins in human serum: improved resolution by use of narrow pH gradients and prolonged electrophoresis. Clin Chem 1984; 30: 2008–13.
  • Righetti PG, Bossi A. Isoelectric focusing in immobilised pH gradients: recent analytical and preparative developments. Anal Biochem 1997; 247: 1–10.
  • Jenkins RE, Pennington SR. Arrays for protein expression profiling: towards a viable alternative to two-dimensional gel electrophoresis? Proteomics 2001; 1: 13–29.
  • Cahill DJ. Protein and antibody arrays and their medical applications. J Immunol Methods 2001; 250: 81–91.
  • Link AJ, Eng J, Schieltz DM et al. Direct analysis of protein complexes using mass spectrometry. Nature Biotechnol 1999; 17: 676–82.
  • Packer NH, Harrison MJ. Glycobiology and proteomics: is mass spectrometry the Holy Grail? Electrophoresis 1998; 19: 1872–82.
  • Harvey DJ. Identification of protein-bound carbohydrates by mass spectrometry. Proteomics 2001; 1: 311–28.
  • Küster B, Krogh TN, Mørtz E, Harvey DJ. Glycosylation analysis of gel-separated proteins. Proteomics 2001; 1: 350–61.
  • Rudert F. Genomics and proteomics tools for the clinic. Curr Opin Mol Ther 2000; 2: 633–42.
  • Fung ET, Wright GL, Dalmasso EA. Proteomic strategies for biomarker identification: progress and challenges. Curr Opin Mol Ther 2000; 2: 643–50.
  • Bienvenut WV, Sanchez J-C, Karmime A et al. Toward a clinical molecular scanner for proteome research: parallel protein chemical processing before and during Western blot. Anal Chem 1999;7 1: 4800–7.
  • Binz PA, Muller M, Walther D et al. A molecular scanner to automate proteomic research and display proteome images. Anal Chem 1999; 71: 4981–8.
  • Figeys D, Pinto D. Proteomics on a chip: promising developments. Electrophoresis 2001; 22: 208–16.

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