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Phosphorylation of calmodulin on Tyr99 selectively attenuates the action of calmodulin antagonists on type-I cyclic nucleotide phosphodiesterase activity.
Tyr99 phosphorylation of calmodulin appears to induce a distinct conformational change as is evident from the profound attenuation of the Ca(2+)-induced enhancement of calmodulin's mobility seen during SDS/PAGE. The effect of this conformational change appears to be localized, in that both calm...
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| Hlavní autoři: | , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
1994
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1138100/ https://ncbi.nlm.nih.gov/pubmed/8192677 |
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