Using X-ray crystallography of the Asp55Asn mutant of the phosphatidylcholine-preferring phospholipase C from Bacillus cereus to support the mechanistic role of Asp55 as the general base-Reference-Cited by-同舟云学术

Using X-ray crystallography of the Asp55Asn mutant of the phosphatidylcholine-preferring phospholipase C from Bacillus cereus to support the mechanistic role of Asp55 as the general base

Published:2003-09 Issue:1 Volume:417 Page:81-86
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Antikainen Nina M,Monzingo Arthur F,Franklin Christopher L,Robertus Jon D,Martin Stephen F

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference39 articles.

1. Cell Signalling Through Guanine-Nucleotide-Binding Regulatory Proteins (G Proteins) and Phospholipases

2. Phosphatidylcholine-Preferring Phospholipase C from B. cereus. Function, Structure, and Mechanism

3. Apparent phosphate retrieval system in Bacillus cereus

4. High-resolution (1.5 Å) crystal structure of phospholipase C from Bacillus cereus

5. Antibodies prepared to Bacillus cereus phospholipase C crossreact with a phosphatidylcholine preferring phosoholipase C in mammalian cells

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