Biologically active milli-calpain associated with caveolae is involved in a spatially compartmentalised signalling involving protein kinase C alpha and myristoylated alanine-rich C-kinase substrate (MARCKS)-Reference-Cited by-同舟云学术

Biologically active milli-calpain associated with caveolae is involved in a spatially compartmentalised signalling involving protein kinase C alpha and myristoylated alanine-rich C-kinase substrate (MARCKS)

Published:2005-09 Issue:9 Volume:37 Page:1900-1910
ISSN:1357-2725
Container-title:The International Journal of Biochemistry & Cell Biology
language:en
Short-container-title:The International Journal of Biochemistry & Cell Biology

Author:

Goudenege Sébastien,Poussard Sylvie,Dulong Sandrine,Cottin Patrick

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry

Reference48 articles.

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3. Calpain zymography with casein or fluorescein isothiocyanate casein;Arthur;Methods Mol. Biol.,2000

4. Betal integrins are distributed in adhesion structures with fibronectin and caveolin and in coated pits;Boyd;Biochem. Cell. Biol.,2003

5. Ca(2+)-dependent proteinases (calpains) and muscle cell differentiation;Cottin;Biochim. Biophys. Acta,1994

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4. ENaC activity is regulated by calpain-2 proteolysis of MARCKS proteins;American Journal of Physiology-Cell Physiology;2017-07-01

5. Oxidative Stress Induces Caveolin 1 Degradation and Impairs Caveolae Functions in Skeletal Muscle Cells;PLOS ONE;2015-03-23