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Volumn 183, Issue 22, 2001, Pages 6499-6508

A 12-amino-acid segment, present in type s2 but not type s1 Helicobacter pylori VacA proteins, abolishes cytotoxin activity and alters membrane channel formation

Author keywords

[No Author keywords available]

Indexed keywords

ANION CHANNEL; BACTERIAL TOXIN; UNCLASSIFIED DRUG; VACUOLATING TOXIN;

EID: 0034750730     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.183.22.6499-6508.2001     Document Type: Article
Times cited : (103)

References (64)
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    • (1997) J. Bacteriol. , vol.179 , pp. 2852-2856
    • Cao, P.1    Cover, T.L.2
  • 28
    • 0034043635 scopus 로고    scopus 로고
    • Natural diversity in the N terminus of the mature vacuolating cytotoxin of Helicobacter pylori determines cytotoxin activity
    • (2000) J. Bacteriol. , vol.182 , pp. 3278-3280
    • Letley, D.P.1    Atherton, J.C.2
  • 48
    • 0028365481 scopus 로고
    • Genetic analysis of the Helicobacter pylori vacuolating cytotoxin: Structural similarities with the IgA protease type of exported protein
    • (1994) Mol. Microbiol. , vol.12 , pp. 307-319
    • Schmitt, W.1    Haas, R.2
  • 63
    • 0033942982 scopus 로고    scopus 로고
    • Mutational analysis of the Helicobacter pylori vacuolating toxin amino terminus: Identification of amino acids essential for cellular vacuolation
    • (2000) Infect. Immun. , vol.68 , pp. 4354-4357
    • Ye, D.1    Blanke, S.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.