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Volumn 31, Issue 6, 2003, Pages 402-409

Preparing undergraduates to participate in the post-genome era: A capstone laboratory experience in proteomics

Author keywords

Biochemistry laboratory; Heat shock; Matrix assisted laser desorption ionization time of flight mass spectrometry; Molecular chaperones; Proteomics

Indexed keywords

BACTERIUM CULTURE; DATA BASE; DNA SEQUENCE; ESCHERICHIA COLI K 12; GENOME; LABORATORY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN PHOSPHORYLATION; PROTEOMICS; REVIEW; TWO DIMENSIONAL GEL ELECTROPHORESIS;

EID: 0347504895     PISSN: 14708175     EISSN: None     Source Type: Journal    
DOI: 10.1002/bmb.2003.494031060291     Document Type: Review
Times cited : (11)

References (30)
  • 6
    • 0027319272 scopus 로고
    • Regulation of the Escherichia coli heat-shock response
    • B. Bukau (1993) Regulation of the Escherichia coli heat-shock response, Mol. Microbiol. 9, 671-680.
    • (1993) Mol. Microbiol. , vol.9 , pp. 671-680
    • Bukau, B.1
  • 7
    • 0031873712 scopus 로고    scopus 로고
    • Regulation of heat-shock response in bacteria
    • G. Segal, E. Z. Ron (1998) Regulation of heat-shock response in bacteria, Ann. N. Y. Acad. Sci. 851, 147-150.
    • (1998) Ann. N. Y. Acad. Sci. , vol.851 , pp. 147-150
    • Segal, G.1    Ron, E.Z.2
  • 8
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • F. U. Hartl (1996) Molecular chaperones in cellular protein folding, Nature 381, 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 11
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)(7) chaperonin complex
    • Z. H. Xu, A. L. Horwich, P. B. Sigler (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP)(7) chaperonin complex, Nature 388, 741-750.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.H.1    Horwich, A.L.2    Sigler, P.B.3
  • 12
    • 0017950371 scopus 로고
    • Transient rates of synthesis of individual polypeptides in E. coli following temperature shifts
    • P. G. Lemaux, S. L. Herendeen, P. L. Bloch, F. C. Neidhardt (1978) Transient rates of synthesis of individual polypeptides in E. coli following temperature shifts, Cell 13, 427-434.
    • (1978) Cell , vol.13 , pp. 427-434
    • Lemaux, P.G.1    Herendeen, S.L.2    Bloch, P.L.3    Neidhardt, F.C.4
  • 13
    • 0018776963 scopus 로고
    • Levels of major proteins of Escherichia coli during growth at different temperatures
    • S. L. Herendeen, R. A. VanBogelen, F. C. Neidhardt (1979) Levels of major proteins of Escherichia coli during growth at different temperatures, J. Bacteriol. 139, 185-194.
    • (1979) J. Bacteriol. , vol.139 , pp. 185-194
    • Herendeen, S.L.1    VanBogelen, R.A.2    Neidhardt, F.C.3
  • 14
    • 0026519887 scopus 로고
    • Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation
    • M. Y. Sherman, A. L. Goldberg (1992) Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation, Nature 357, 167-169.
    • (1992) Nature , vol.357 , pp. 167-169
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 15
    • 0023240043 scopus 로고
    • The heat shock response of E. coli is regulated by changes in the concentration of sigma 32
    • D. B. Straus, W. A. Walter, C. A. Gross (1987) The heat shock response of E. coli is regulated by changes in the concentration of sigma 32, Nature 329, 348-351.
    • (1987) Nature , vol.329 , pp. 348-351
    • Straus, D.B.1    Walter, W.A.2    Gross, C.A.3
  • 16
    • 0025632973 scopus 로고
    • DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32
    • D. B. Straus, W. A. Walter, C. A. Gross (1990) DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32, Genes Dev. 4, 2202-2209.
    • (1990) Genes Dev. , vol.4 , pp. 2202-2209
    • Straus, D.B.1    Walter, W.A.2    Gross, C.A.3
  • 18
    • 0037317098 scopus 로고    scopus 로고
    • Identifying a protein by MALDI-TOF mass spectrometry: An experiment for the undergraduate laboratory
    • A. E. Counterman, M. S. Thompson, D. E. Clemmer (2003) Identifying a protein by MALDI-TOF mass spectrometry: An experiment for the undergraduate laboratory, J. Chem. Educ. 80, 177-180.
    • (2003) J. Chem. Educ. , vol.80 , pp. 177-180
    • Counterman, A.E.1    Thompson, M.S.2    Clemmer, D.E.3
  • 19
    • 84875463071 scopus 로고
    • Matrix-assisted laser desorption ionization mass-spectrometry of biopolymers
    • F. Hillenkamp, M. Karas, R. C. Beavis, B. T. Chait (1991) Matrix-assisted laser desorption ionization mass-spectrometry of biopolymers, Anal. Chem. 63, A1193-A1202.
    • (1991) Anal. Chem. , vol.63
    • Hillenkamp, F.1    Karas, M.2    Beavis, R.C.3    Chait, B.T.4
  • 23
    • 77957012032 scopus 로고
    • Spectrophotometric and turbdtimetric methods for measuring proteins
    • E. Layne (1957) Spectrophotometric and turbdtimetric methods for measuring proteins, Methods Enzymol. 3, 451-454.
    • (1957) Methods Enzymol. , vol.3 , pp. 451-454
    • Layne, E.1
  • 24
    • 0000745994 scopus 로고
    • Isolierung und Kristallisation des Garungsfermentes Enolase
    • O. Warburg, W. Christian (1941) Isolierung und Kristallisation des Garungsfermentes Enolase, Biochem. Z. 310, 384.
    • (1941) Biochem. Z. , vol.310 , pp. 384
    • Warburg, O.1    Christian, W.2
  • 28
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • D. J. C. Pappin, P. Hojrup, A. J. Bleasby (1993) Rapid identification of proteins by peptide-mass fingerprinting, Curr. Biol. 3, 327-332.
    • (1993) Curr. Biol. , vol.3 , pp. 327-332
    • Pappin, D.J.C.1    Hojrup, P.2    Bleasby, A.J.3
  • 29
    • 0027220168 scopus 로고
    • Heat shock of Escherichia coli increases binding of DnaK (the hsp 70 homolog) to polypeptides by promoting its phosphoyrlation
    • M. Y. Sherman, A. L. Goldberg (1993) Heat shock of Escherichia coli increases binding of DnaK (The hsp 70 homolog) to polypeptides by promoting its phosphoyrlation, Proc. Natl. Acad. Sci. U. S. A. 90, 8648-8652.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 8648-8652
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 30
    • 0037319895 scopus 로고    scopus 로고
    • Assembly of the 30S ribosomal subunit
    • G. M. Culver (2003) Assembly of the 30S ribosomal subunit, Biopolymers 68, 234-249.
    • (2003) Biopolymers , vol.68 , pp. 234-249
    • Culver, G.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.