Protein kinase C signaling and oxidative stress.
By R. Gopalakrishna, S. Jaken. Free Radical Biology & Medicine, 2000
686 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/1ac3047b70120bf28bda056455d06ba70fb8f615
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Citations in the corpus
- Chemopreventive and therapeutic effects of curcumin. (2005, background): “Furthermore, TPA- induced PKC is abolished by curcumin in NIH 3T3 mouse fibroblast cells [53].”
- Free radicals and antioxidants in normal physiological functions and human disease. (2007, background): “PKC contains several cysteine rich regions both in the zinc finger of the regulatory domain and in the catalytic site which can be modified by various oxidants (Gopalakrishna & Jaken, 2000).”
- Molecular events associated with reactive oxygen species and cell cycle progression in mammalian cells. (2004, background): “Various studies have established that oxygen free radicals can cause the phosphorylation and activation of numerous signaling proteins (Finkel and Holbrook, 2000), including Receptor Tyrosine Kinases (RTK) (Gamou and Shimizu, 1995; González-Rubio et al., 1996), PKC (Gopalakrishna and Jaken, 2000), ”
- Structural Basis of Protein Kinase C Isoform Function (2008, background): “While the focus of most studies in the literature has been on the effects of oxidative stress to activate Src family kinases and alter PKC signaling mechanisms through PKC tyrosine phosphorylation, PKCs are also direct targets for redox modifications (69).”
- The importance of antioxidants which play the role in cellular response against oxidative/nitrosative stress: current state (2015, neutral): “tion of the protein [129].”
- Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease (2015, positive): “Activation of PKC isoenzymes by ROS may entail phosphorylation of certain tyrosine residues that lie adjacent to the regulatory domain by non-receptor-type kinases [214], possibly by c-Abl [190], but it may also occur via oxidation of Cys residues in its regulatory or catalytic domains [215].”
- Antioxidant responses and cellular adjustments to oxidative stress (2015, background): “Protein kinase C (PKC) contains a cysteine rich domain susceptible to oxidation, while oxidation of Cys-245 and Cys-487 in the kinase domain of the nonreceptor tyrosine kinase Src results in the activation of the protein [210].”
- Cellular response to oxidative stress: Signaling for suicide and survival * (2002, background): “PKC represents a family of phospholipid-dependent serine-threonine kinases involved in signaling pathways that regulate cell growth, cell death, and stress responsiveness (reviewed in Gopalakrishna and Jaken, 2000).”