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Volumn 290, Issue 1, 2002, Pages 427-430

A study on the C-terminal membrane anchoring of Escherichia coli penicillin-binding protein 5

Author keywords

C terminal helix; Conformational change; E. coli PBP5; Membrane

Indexed keywords

BACTERIAL PROTEIN; MEMBRANE LIPID; PENICILLIN BINDING PROTEIN; PENICILLIN BINDING PROTEIN 5; UNCLASSIFIED DRUG;

EID: 0036298545     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2001.6198     Document Type: Article
Times cited : (2)

References (19)
  • 7
    • 0025154988 scopus 로고
    • Investigation into structural features of the Escherichia coli penicillin-binding protein 5 C-terminal anchor
    • (1990) Biochem. Soc. Trans. , vol.18 , pp. 948-949
    • Phoenix, D.A.1
  • 9
    • 0023375156 scopus 로고
    • An 18 amino acid amphiphilic helix forms the membrane anchoring domain of the Escherichia coli penicillin binding protein 5
    • (1987) Mol. Microbiol. , vol.1 , pp. 23-28
    • Jackson, M.E.1    Pratt, J.M.2
  • 14
    • 0027309005 scopus 로고
    • Membrane interaction of Escherichia coli penicillin-binding protein 5 is modulated by the ectomembranous domain
    • (1993) FEBS Lett. , vol.322 , pp. 215-218
    • Phoenix, D.A.1    Pratt, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.