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Activation of protein kinase C alters p34(cdc2) phosphorylation state and kinase activity in early sea urchin embryos by abolishing intracellular Ca2+ transients.

The p34(cdc2) protein kinase, a universal regulator of mitosis, is controlled positively and negatively by phosphorylation, and by association with B-type mitotic cyclins. In addition, activation and inactivation of p34(cdc2) are induced by Ca(2+) and prevented by Ca(2+) chelators in permeabilized c...

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Bibliografiska uppgifter
Huvudupphovsmän: Suprynowicz, F A, Groigno, L, Whitaker, M, Miller, F J, Sluder, G, Sturrock, J, Whalley, T
Materialtyp: Artigo
Språk:Inglês
Publicerad: 2000
Ämnen:
Länkar:https://ncbi.nlm.nih.gov/pmc/articles/PMC1221172/
https://ncbi.nlm.nih.gov/pubmed/10880348
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