메뉴 건너뛰기




Volumn 312, Issue 2, 2001, Pages 359-369

The role in flagellar rod assembly of the N-terminal domain of Salmonella FlgJ, a flagellum-specific Muramidase

Author keywords

Flagellar morphogenesis; L ring; P ring; Peptidoglycan; Type III protein export

Indexed keywords

BACTERIAL ENZYME; LYSOZYME; PEPTIDOGLYCAN;

EID: 0035860359     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4963     Document Type: Article
Times cited : (82)

References (40)
  • 2
    • 0029901224 scopus 로고    scopus 로고
    • Physiological and biochemical analyses of FlgH, a lipoprotein forming the outer membrane L ring of the flagellar basal body of Salmonella typhimurium
    • (1996) J. Bacteriol. , vol.178 , pp. 4200-4207
    • Schoenhals, G.J.1    Macnab, R.M.2
  • 15
    • 0027942085 scopus 로고
    • Information essential for cell-cycle-dependent secretion of the 591-residue Caulobacter hook protein is confined to a 21-amino-acid sequence near the N terminus
    • (1994) Mol. Microbiol. , vol.14 , pp. 73-85
    • Kornacker, M.G.1    Newton, A.2
  • 35
    • 0034111320 scopus 로고    scopus 로고
    • The Salmonella FlgA protein, a putative periplasmic chaperone essential for flagellar P ring formation
    • (2000) Microbiology , vol.146 , pp. 1171-1178
    • Nambu, T.1    Kutsukake, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.