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Biochemistry|May 18, 1976
A Ca2+-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscleW R Dayton, D E Goll, M G Zeece, et al.Journal of Animal Science|June 15, 2007
Effect of postmortem storage on activity of mu- and m-calpain in five bovine musclesJ P Camou, J A Marchello, V F Thompson, et al.The Journal of Cell Biology|November 4, 2000
Evidence that beta3 integrin-induced Rac activation involves the calpain-dependent formation of integrin clusters that are distinct from the focal complexes and focal adhesions that form as Rac and RhoA become activeK Bialkowska, S Kulkarni, X Du, et al.The Journal of Biological Chemistry|November 10, 1976
Some properties of purified skeletal muscle alpha-actininA Suzuki, D E Goll, I Singh, et al.Acta Neuropathologica|January 1, 1995
Immunohistochemical study of calpain and its endogenous inhibitor in the skeletal muscle of muscular dystrophyT Kumamoto, H Ueyama, S Watanabe, et al.The Anatomical Record|January 1, 1992
Localization of the Ca(2+)-dependent proteinases and their inhibitor in normal, fasted, and denervated rat skeletal muscleT Kumamoto, W C Kleese, J Y Cong, et al.Biochimica Et Biophysica Acta|October 19, 1989
Chicken skeletal muscle has three Ca2+-dependent proteinasesF H Wolfe, S K Sathe, D E Goll, et al.Journal of Animal Science|September 20, 2007
Isolation and characterization of mu-calpain, m-calpain, and calpastatin from postmortem muscle. I. Initial stepsJ P Camou, S W Mares, J A Marchello, et al.Journal of Animal Science|March 4, 2008
Effect of two dietary concentrate levels on tenderness, calpain and calpastatin activities, and carcass merit in Waguli and Brahman steersR M Ibrahim, D E Goll, J A Marchello, et al.Pageof 6