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Optogenetic control of Protein Kinase C-epsilon activity reveals its intrinsic signaling properties with spatiotemporal resolution

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Protein Kinase C

Journal of Cellular Physiology, 1986
The combined application of protein structural techniques, immunochemistry, and molecular biology has permitted an analysis of the differential expression of the genes for the three related protein kinases, C-alpha, -beta, and gamma. The evidence now suggests that the type of protein kinase C in a cell may govern the nature and mechanisms of functional
P J, Parker, A, Ullrich
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Protein kinase C

Pharmacology & Therapeutics, 1991
Based on the molecular structure of the individual members of the protein kinase C family, general properties and the mode of activation of this enzyme family are discussed. Examples are presented of how the investigation of protein kinase C function in vivo has been approached at the molecular level.
S, Stabel, P J, Parker
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Retinal protein kinase C

Neurochemistry International, 1997
The protein kinase C (PKC) family of serine/threonine kinase isoenzymes are universally expressed in vertebrate tissues where they control vital cellular functioning. PKC comprises twelve currently identified mammalian isoenzymes, described in three distinct groups according to their need for different effector stimulation.
J P, Wood, R J, McCord, N N, Osborne
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Nuclear protein kinase C

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2006
Protein kinase C (PKC) isozymes constitute a family of ubiquitous phosphotransferases which act as key transducers in many agonist-induced signaling cascades. To date, at least 11 different PKC isotypes have been identified and are believed to play distinct regulatory roles. PKC isoforms are physiologically activated by a number of lipid cofactors. PKC
MARTELLI, ALBERTO MARIA   +3 more
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