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- W2092277227 abstract "A family of mutant proteins related to calmodulin (CaM) has been produced using cDNA constructs in bacterial expression vectors. The new proteins contain amino acid substitutions in Ca2+-binding domains I, II, both I and II, or both II and IV. The calmodulin-like proteins have been characterized with respect to mobility on SDS-polyacrylamide gels, Ca2+-dependent enhancement of tyrosine fluorescence, and abilities to activate the CaM-dependent phosphatase calcineurin. These studies suggest that an intact Ca2+-binding domain II is minimally required for full activation of calcineurin." @default.
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- W2092277227 date "1988-09-26" @default.
- W2092277227 modified "2023-09-23" @default.
- W2092277227 title "Domain II of calmodulin is involved in activation of calcineurin" @default.
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- W2092277227 doi "https://doi.org/10.1016/0014-5793(88)80230-8" @default.
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