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Volumn 19, Issue 22, 2000, Pages 5980-5988

Protein folding in the periplasm in the absence of primary oxidant DsbA: Modulation of redox potential in periplasmic space via OmpL porin

Author keywords

Disulfide bond formation; DsbA; DsbB; Outer membrane; Protein folding

Indexed keywords

ALKALINE PHOSPHATASE; DISULFIDE; DITHIOTHREITOL; DSBA PROTEIN; GENE PRODUCT; MUTANT PROTEIN; OUTER MEMBRANE PROTEIN; OXIDIZING AGENT; PORIN; PROTEIN OMPL; UNCLASSIFIED DRUG;

EID: 0034669205     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.22.5980     Document Type: Article
Times cited : (19)

References (31)
  • 7
    • 0034011364 scopus 로고    scopus 로고
    • Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm
    • (2000) Mol. Microbiol. , vol.35 , pp. 1099-1109
    • Chung, J.1    Chen, T.2    Missiakas, D.3
  • 10
    • 0026567097 scopus 로고
    • Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme
    • (1992) EMBO J. , vol.11 , pp. 57-62
    • Kamitani, S.1    Akiyama, Y.2    Ito, K.3
  • 24
    • 0025951604 scopus 로고
    • The Escherichia coli htrP gene product if essential for bacterial growth at high temperature: Mapping, cloning, sequencing and transcriptional regulation of htrP
    • (1991) J. Bacteriol. , vol.173 , pp. 5999-6008
    • Raina, S.1    Mabey, L.2    Georgopoulos, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.