메뉴 건너뛰기




Volumn 140, Issue , 2000, Pages 169-177

Folding Assays: Assessing the Native Conformation of Proteins

Author keywords

Folding Reaction; Guanidinium Hydrochloride; Rabbit Reticulocyte Lysate; Saran Wrap; Total Tubulin

Indexed keywords

ACTIN; BUFFER; CHAPERONIN; DYES, REAGENTS, INDICATORS, MARKERS AND BUFFERS; LUCIFERASE; MICROTUBULE ASSOCIATED PROTEIN; NUCLEAR PROTEIN; PPP1R11 PROTEIN, HUMAN; PROTEIN; PROTEINASE; SIGNAL PEPTIDE; SULFUR; T COMPLEX PROTEINS; TUBULIN;

EID: 0034570552     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1385/1-59259-061-6:169     Document Type: Chapter
Times cited : (11)

References (9)
  • 1
    • 0031614812 scopus 로고    scopus 로고
    • (LaRoss, R. A., ed), ed. R.A. LaRoss. Humana, Totowa, NJ
    • Thulasiraman, V. and Matts, R. L. (1998) Methods in Molecular Biology, vol. 102, (LaRoss, R. A., ed.), ed. R.A. LaRoss. Humana, Totowa, NJ, pp. 129–141.
    • (1998) Methods in Molecular Biology , vol.102 , pp. 129-141
    • Thulasiraman, V.1    Matts, R. L.2
  • 2
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide-chains in a high-molecular-mass assembly with molecular chaperones
    • Frydman, J., Nimmesgern, E., Ohtsuka, K., and Hartl, F. U. (1994) Folding of nascent polypeptide-chains in a high-molecular-mass assembly with molecular chaperones. Nature 370, 111–117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, F. U.4
  • 3
    • 0026776331 scopus 로고
    • A cytoplasmic chaperonin that catalyzes ß-Actin folding
    • Gao, Y., Thomas, J. O., Chow, R. L., Lee, G.-H., and Cowan, N. J. (1992) A cytoplasmic chaperonin that catalyzes ß-Actin folding. Cell 69, 1043–1050.
    • (1992) Cell , vol.69 , pp. 1043-1050
    • Gao, Y.1    Thomas, J. O.2    Chow, R. L.3    Lee, G.-H.4    Cowan, N. J.5
  • 4
    • 0029980091 scopus 로고    scopus 로고
    • Principles of chaperone-assisted protein-folding: differences between In-Vitro In-Vivo Mechanisms
    • Frydman, J. and Hartl, F. U. (1996) Principles of chaperone-assisted protein-folding: differences between In-Vitro In-Vivo Mechanisms. Science 272, 1497–1502.
    • (1996) Science , vol.272 , pp. 1497-1502
    • Frydman, J.1    Hartl, F. U.2
  • 5
    • 0026416043 scopus 로고
    • Chaperonin-mediated protein folding at the surface of GroEL through a “molten globule”-like intermediate
    • Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A. L., and Hartl, F. U. (1991) Chaperonin-mediated protein folding at the surface of GroEL through a “molten globule”-like intermediate. Nature 352, 36–42.
    • (1991) Nature , vol.352 , pp. 36-42
    • Martin, J.1    Langer, T.2    Boteva, R.3    Schramel, A.4    Horwich, A. L.5    Hartl, F. U.6
  • 6
    • 0029127242 scopus 로고
    • Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding
    • Hlodan, R., Tempst, P., and Hartl, F. U. (1995) Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding. Nature Struct. Biol. 2, 587–595.
    • (1995) Nature Struct. Biol , vol.2 , pp. 587-595
    • Hlodan, R.1    Tempst, P.2    Hartl, F. U.3
  • 7
    • 0028822679 scopus 로고
    • Quasi-native chaperonin-bound intermediates in facilitated protein-folding
    • 913
    • Tian, G. L., Vainberg, I. E., Tap, W. D., Lewis, S. A., and Cowan, N. J. (1995) Quasi-native chaperonin-bound intermediates in facilitated protein-folding. J. Biol. Chem. 270, 23,910–23,913.
    • (1995) J. Biol. Chem , vol.270 , Issue.23 , pp. 910-923
    • Tian, G. L.1    Vainberg, I. E.2    Tap, W. D.3    Lewis, S. A.4    Cowan, N. J.5
  • 8
    • 85152590823 scopus 로고    scopus 로고
    • Effect of geldanamycin on the kinetics of chaperone-mediated renaturation of firefly luciferase in rabbit reticulocyte lysate
    • 13,443–13,450
    • Thulasiraman, V. and Matts, R. L. (1996) Effect of geldanamycin on the kinetics of chaperone-mediated renaturation of firefly luciferase in rabbit reticulocyte lysate. Biochemistry 35, p. 13,443–13,450.
    • (1996) Biochemistry , vol.35
    • Thulasiraman, V.1    Matts, R. L.2
  • 9
    • 0023941956 scopus 로고
    • Expression of a human alpha-tubulin: properties of the isolated subunit
    • Yaffe, M. B., Levison, B. S., Szasz, J., and Sternlicht, H. (1988) Expression of a human alpha-tubulin: properties of the isolated subunit. Biochemistry 27, 1869–1880.
    • (1988) Biochemistry , vol.27 , pp. 1869-1880
    • Yaffe, M. B.1    Levison, B. S.2    Szasz, J.3    Sternlicht, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.