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The Journal of Biological Chemistry|May 5, 1995
Calpains are activated in necrotic fibers from mdx dystrophic miceM J Spencer, D E Croall, J G TidballThe Biochemical Journal|April 1, 1986
Fractionation and quantification of calcium-dependent proteinase activity from small tissue samplesA F Clark, G N DeMartino, D E CroallExperimental Cell Research|May 1, 1994
Proteolytic cleavage of the integrin beta 4 subunitA J Potts, D E Croall, M E HemlerThe Journal of Biological Chemistry|October 25, 1988
The calmodulin-binding site in alpha-fodrin is near the calcium-dependent protease-I cleavage siteA S Harris, D E Croall, J S MorrowThe Journal of Biological Chemistry|October 15, 1989
Calmodulin regulates fodrin susceptibility to cleavage by calcium-dependent protease IA S Harris, D E Croall, J S MorrowThe Journal of Biological Chemistry|September 15, 1986
Autoproteolysis of the small subunit of calcium-dependent protease II activates and regulates protease activityG N DeMartino, C A Huff, D E CroallArchives of Biochemistry and Biophysics|April 1, 1988
ATP-stimulated proteolysis in soluble extracts of BHK 21/C13 cells. Evidence for multiple pathways and a role for an enzyme related to the high-molecular-weight protease, macropainM J McGuire, D E Croall, G N DeMartinoBiochimica Et Biophysica Acta|July 16, 1986
Limited proteolysis of the erythrocyte membrane skeleton by calcium-dependent proteinasesD E Croall, J S Morrow, G N DeMartinoBiochemical and Biophysical Research Communications|October 29, 1993
The insulin receptor substrate (IRS-1) is a PEST protein that is susceptible to calpain degradation in vitroL K Smith, M Bradshaw, D E Croall, et al.Archives of Biochemistry and Biophysics|April 1, 1988
Proteolysis of the protein inhibitor of calcium-dependent proteases produces lower molecular weight fragments that retain inhibitory activityG N DeMartino, R Wachendorfer, M J McGuire, et al.Pageof 4