메뉴 건너뛰기




Volumn 297, Issue 3, 2000, Pages 809-818

Cyclophilin-promoted folding of mouse dihydrofolate reductase does not include the slow conversion of the late-folding intermediate to the active enzyme

Author keywords

Cyclophilin; Mouse DHFR; Prolyl isomerization; Protein folding

Indexed keywords

CYCLOPHILIN; DIHYDROFOLATE REDUCTASE; PROLINE;

EID: 0034737317     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3574     Document Type: Article
Times cited : (12)

References (43)
  • 5
    • 0033613814 scopus 로고    scopus 로고
    • Native Escherichia coli and murine dihydrofolate reductases contain late-folding non-native structures
    • (1999) J. Mol. Biol. , vol.285 , pp. 1765-1776
    • Clark, A.C.1    Frieden, C.2
  • 6
    • 0033613819 scopus 로고    scopus 로고
    • The chaperonin GroEL binds to late-folding non-native conformations present in native Escherichia coli and murine dihydrofolate reductases
    • (1999) J. Mol. Biol. , vol.285 , pp. 1777-1788
    • Clark, A.C.1    Frieden, C.2
  • 12
    • 0022515029 scopus 로고
    • Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
    • (1986) Nature , vol.322 , pp. 228-232
    • Eilers, M.1    Schatz, G.2
  • 15
    • 0000230763 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis/trans isomerases
    • Molecular Chaperones and Folding Catalysts (Bukau, B., ed.), Harwood Academic Publishers, Amsterdam
    • (1999) , pp. 461-489
    • Fischer, G.1    Schmid, F.X.2
  • 21
    • 0032559238 scopus 로고    scopus 로고
    • Prolyl isomerases and nuclear function
    • (1998) Cell , vol.92 , pp. 141-143
    • Hunter, T.1
  • 32
  • 37
    • 0000926770 scopus 로고
    • System for high-level production in Escherichia coli and rapid purification of recombinant proteins: Application to epitope mapping, preparation of antibodies, and structure-function analysis
    • Immunological Methods (Lefkovits, I. and Pernis, B., eds), Academic Press, Orlando, FL
    • (1992) , pp. 121-152
    • Stuber, D.1    Matile, H.2    Garotta, G.3
  • 43
    • 0030837026 scopus 로고    scopus 로고
    • The chaperonin cycle cannot substitute for prolyl isomerase activity, but GroEL alone promotes productive folding of a cyclophilin-sensitive substrate to a cyclophilin-resistant form
    • (1997) EMBO J. , vol.16 , pp. 4568-4578
    • Von Ahsen, O.1    Tropschug, M.2    Pfanner, N.3    Rassow, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.