The extra C-terminal tail is involved in the conformation, stability changes and the N/C-domain interactions of the calmodulin-like protein from pearl oyster Pinctada fucata-Reference-Cited by-同舟云学术

The extra C-terminal tail is involved in the conformation, stability changes and the N/C-domain interactions of the calmodulin-like protein from pearl oyster Pinctada fucata

Published:2008-11 Issue:11 Volume:1784 Page:1514-1523
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Wang Qin,Li Shuo,Li Changzhong,Liang Jian,Fang Zi,Xie Liping,Zhang Rongqing

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference42 articles.

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3. Novel aspects of calmodulin target recognition and activation;Vetter;Eur. J. Biochem.,2003

4. Molecular and structural basis of target recognition by calmodulin;Crivici;Annu. Rev. Biophys. Biomol. Struct.,1995

5. Calmodulin-binding domains: just two faced or multi-faceted?;James;Trends. Biochem. Sci.,1995

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