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Specific binding of CAP-50 to calcyclin.
Minami H, Tokumitsu H, Mizutani A, Watanabe Y, Watanabe M, Hidaka H. Minami H, et al. Among authors: tokumitsu h. FEBS Lett. 1992 Jul 6;305(3):217-9. doi: 10.1016/0014-5793(92)80671-3. FEBS Lett. 1992. PMID: 1299619 Free article.
CAP-50, a calcyclin-associated protein with an apparent molecular mass of 50 kDa, was purified and proved to be a novel annexin [Tokumitsu, H. et al. (1992) J. Biol. Chem. 267, 8919-8924]. We examined the binding of CAP-50 to other Ca(2+)-binding proteins which have …
CAP-50, a calcyclin-associated protein with an apparent molecular mass of 50 kDa, was purified and proved to be a novel annexin [Tokumits …
Molecular cloning of rabbit CAP-50, a calcyclin-associated annexin protein.
Tokumitsu H, Mizutani A, Muramatsu M, Yokota T, Arai K, Hidaka H. Tokumitsu H, et al. Biochem Biophys Res Commun. 1992 Aug 14;186(3):1227-35. doi: 10.1016/s0006-291x(05)81537-2. Biochem Biophys Res Commun. 1992. PMID: 1380798
CAP-50 is a member of annexin family proteins which binds specifically to calcyclin in a Ca2+ dependent manner (Tokumitsu. H., Mizutani. A., Minami. H., Kobayashi. R., and Hidaka. H. (1992) J. Biol. Chem. 267,8919-8924). ...
CAP-50 is a member of annexin family proteins which binds specifically to calcyclin in a Ca2+ dependent manner (Tokumitsu. H., …
Site-directed mutation makes rabbit calcyclin dimer.
Ando Y, Watanabe M, Akatsuka H, Tokumitsu H, Hidaka H. Ando Y, et al. Among authors: tokumitsu h. FEBS Lett. 1992 Dec 14;314(2):109-13. doi: 10.1016/0014-5793(92)80953-e. FEBS Lett. 1992. PMID: 1459239 Free article.
139 results