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Volumn 284, Issue 23, 2009, Pages 15607-15618

Modulation of Bacillus thuringiensis phosphatidylinositolspecific phospholipase C activity by mutations in the putative dimerization interface

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ASSAY SYSTEM; BACILLUS THURINGIENSIS; CATALYTIC ACTIVITY; CRYSTALLOGRAPHIC ANALYSIS; DIMER INTERFACE; ENZYMATIC ACTIVITIES; ENZYME BINDING; ENZYME FUNCTIONS; KINETIC ASSAY; LIPID BINDING; MEMBRANE BINDING; MUTANT PROTEINS; MYO-INOSITOL; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLINOSITOL; PHOSPHOLIPASE; PHOSPHOLIPASE C; PHOSPHOLIPID BINDING; PROTEIN DIMERIZATION; TYROSINE RESIDUES;

EID: 67650123206     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M901601200     Document Type: Article
Times cited : (17)

References (45)
  • 20
    • 0002310525 scopus 로고
    • Grant, D. M, ed, pp, John Wiley & Sons, Inc, New York
    • Woessner, D. E. (1995) in Encyclopedia of NMR (Grant, D. M., ed.) pp. 1068-1083, John Wiley & Sons, Inc., New York
    • (1995) Encyclopedia of NMR , pp. 1068-1083
    • Woessner, D.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.