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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao https://doi.org/10.1...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
https://doi.org/10.1016/b978-0...
Part of book or chapter of book . 1982 . Peer-reviewed
License: Elsevier TDM
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Casein Kinases—Multipotential Protein Kinases

Authors: Gary M. Hathaway; Jolinda A. Traugh;

Casein Kinases—Multipotential Protein Kinases

Abstract

Publisher Summary Casein kinase I and casein kinase II are unique protein kinases that have been described in a number of mammalian and avian cells; an enzyme with properties similar to those of casein kinase I has been described in yeast and plants. The casein kinases prefer acidic substrates and appear to differ from the enzyme endogenous to the mammary gland. Casein kinases I and II are multipotential in the sense that a number of endogenous substrates have been identified for them. Other multipotential protein kinases include the cAMP-dependent and cGMP-dependent protein kinases and phosphorylase kinase. No physiological regulator for casein kinase I has been identified, but the enzyme requires Mg2+ for activity and is stimulated by monovalent cations; the cation requirement is similar for casein kinase II.

Related Organizations
Keywords

2,3-Diphosphoglycerate, Chromosomal Proteins, Non-Histone, Caseins, Membrane Proteins, Diphosphoglyceric Acids, Phosphoproteins, Substrate Specificity, Phosvitin, Adenosine Triphosphate, Glycogen Synthase, Mammary Glands, Animal, Peptide Initiation Factors, Animals, Female, Amino Acid Sequence, Phosphorylation, Casein Kinases, Protein Kinase Inhibitors, Protein Kinases

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    citations
    This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
    544
    popularity
    This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
    Top 10%
    influence
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    impulse
    This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
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Powered by OpenAIRE graph
Found an issue? Give us feedback
citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
544
Top 10%
Top 0.1%
Top 1%
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