Domain V of m-calpain shows the potential to form an oblique-orientated α-helix, which may modulate the enzyme's activity via interactions with anionic lipid-Reference-Cited by-同舟云学术

Domain V of m-calpain shows the potential to form an oblique-orientated α-helix, which may modulate the enzyme's activity via interactions with anionic lipid

Published:2002-10-30 Issue:22 Volume:269 Page:5414-5422
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:

Author:

Brandenburg Klaus,Harris Frederick,Dennison Sarah,Seydel Ulrich,Phoenix David

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1432-1033.2002.03225.x/fullpdf

Reference57 articles.

1. The structure of calpain;Sorimachi;J. Biol. Chem.,2001

2. Structure and physiological function of calpains;Sorimachi;Biochem. J.,1997

3. Calpains: intact and active?;Johnson;Bioessays,1997

4. Characterization and expression of calpain 10. A novel ubiquitous calpain with nuclear localization;Ma;J. Biol. Chem.,2001

5. Calpain function in the modulation of signal transduction molecules;Sato;Biol. Chem.,2001

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