Inhibition of protein kinase C by alcohols and anaesthetics
Article Abstract:
A lipid-dependent assay reveals that protein kinase C, a key component in signal transduction, is inhibited by anaesthetics. The assay also shows the possible role of lipids in the protein-site model. The lack of restriction in the isolated catalytic domain suggests that the site of inhibition is on the regulatory subunit, which is unique to protein kinase C.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338
Article Abstract:
The Ras proteins control many effectors such as members of the Raf family of protein kinases. It is shown that Pak3 protein kinases phosphorylates Raf-1 on serine 338. The Rho-family GTPases Rac and Cdc42 regulate the p21 activated protein kinases. The results indicated that signal transduction via Raf-1 relies on both Ras and the Pak pathway activation.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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Induction of vanilloid receptor channel activity by protein kinase C
Article Abstract:
Vanilloid receptor channel activity induction by protein kinase C is examined.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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