The DOI matches its Crossref record; 138 of the 138 references it cites were found in a registry or an index.
The protein kinase C family
Abstract
Protein kinase C represents a structurally homologous group of proteins similar in size, structure and mechanism of activation. They can modulate the biological function of proteins in a rapid and reversible manner. Protein kinase C participates in one of the major signal transduction systems triggered by the external stimulation of cells by various ligands including hormones, neurotransmitters and growth factors. Hydrolysis of membrane inositol phospholipids by phospholipase C or of phosphatidylcholine, generates sn‐1,2‐diacylglycerol, considered the physiological activator of this kinase. Other agents, such as arachidonic acid, participate in the activation of some of these proteins. Activation of protein kinase C by phorbol esters and related compounds is not physiological and may be responsible, at least in part, for their tumor‐promoting activity. The cellular localization of the different calcium‐activated protein kinases, their substrate and activator specificity are dissimilar and thus their role in signal transduction is unlike. A better understanding of the exact cellular function of the different protein kinase C isoenzymes requires the identification and characterization of their physiological substrates.
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Cites
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Cited by
Phosphatidylcholine breakdown and signal transduction
Exton, J. H. (1994) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(94)90186-4 · Cited by 960
Exploitation of the tropical oil seed plant Jatropha curcas L.
Gübitz, G. (1999) · Bioresource Technology · doi:10.1016/s0960-8524(99)00069-3 · Cited by 698
Inhibition of Cyclin‐Dependent Kinases by Purine Analogues
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Vitamin and mineral status: effects on physical performance
Lukaski, H. C. (2004) · Nutrition · doi:10.1016/j.nut.2004.04.001 · Cited by 587
Synaptotagmins: C2-Domain Proteins That Regulate Membrane Traffic
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Metadata
- Authors
- AZZI, A., BOSCOBOINIK, D., & HENSEY, C.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1992-09
- Volume
- 208
- Issue
- 3
- Pages
- 547-557
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W1968162244
- Cited by
- 400
- References
- 138
- FWCI
- 15.01
- Type
- journal article
- Language
- en
- Open access
- closed
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