ReviewFrontiers in pharmacology2015
Mechanisms for redox-regulation of protein kinase C.
Review in Frontiers in pharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
57 citing papers in PubMed, 105 citations in OpenAlex.
- A quantitative redox proteome of the human muscle response to exercise.bioRxiv : the preprint server for biology · 2026Article
- CarboxymethylatedFood science & nutrition · 2026Article
- A new paradigm in Parkinson's disease: kidney-origin α-synuclein pathology driven by PKC signaling and aurothioglucose.Inflammopharmacology · 2026Review
- Neutrophil extracellular traps in cardiovascular disease: a bibliometric analysis (2005-2024).Naunyn-Schmiedeberg's archives of pharmacology · 2026Review
- Reactive oxygen species counteract zebrafish wound contraction and promote wound healing.Biophysical journal · 2025Article
- Protein Kinase C promotes peroxisome biogenesis and peroxisome-endoplasmic reticulum interaction.The Journal of cell biology · 2025Article
- Double alkylation with maleimide-PEG-biotin: An enrichment method for cysteine redox states.Analytical biochemistry · 2025Article
- Resveratrol Impairs Insulin Signaling in Hepatic Cells via Activation of PKC and PTP1B Pathways.International journal of molecular sciences · 2025Article
- IDH status dictates oHSV mediated metabolic reprogramming affecting anti-tumor immunity.Nature communications · 2025Article
- Mitochondrial stress disassembles nuclear architecture through proteolytic activation of PKCδ and Lamin B1 phosphorylation in neuronal cells: implications for pathogenesis of age-related neurodegenerative diseases.Frontiers in cellular neuroscience · 2025Article
- Nitroalkene inhibition of pro-inflammatory macrophage effector function via modulation of signaling metabolite levels.Frontiers in physiology · 2025Article
- Article
- Natural products for enhancing the sensitivity or decreasing the adverse effects of anticancer drugs through regulating the redox balance.Chinese medicine · 2024Review
- The Role of Vitamins in Mitigating the Effects of Various Stress Factors in Pigs Breeding.Animals : an open access journal from MDPI · 2024Review
- Activity-dependent mitochondrial ROS signaling regulates recruitment of glutamate receptors to synapses.eLife · 2024Article
- A Prognostic Activity of Glutaredoxin 1 Protein (Grx1) in Colon Cancer.International journal of molecular sciences · 2024Article
- Dysregulation of intracellular redox homeostasis by the SARS-CoV-2 ORF6 protein.Virology journal · 2023Article
- Review
- Review
- Oxidative Regulation of Vascular CaAntioxidants (Basel, Switzerland) · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Protein kinase C (PKC) is comprised of a family of signal-regulated enzymes that play pleiotropic roles in the control of many physiological and pathological responses. PKC isoforms are traditionally viewed as allosterically activated enzymes that are recruited to membranes by growth factor receptor-generated lipid cofactors. An inherent assumption of this conventional model of PKC isoform activation is that PKCs act exclusively at membrane-delimited substrates and that PKC catalytic activity is an inherent property of each enzyme that is not altered by the activation process. This traditional model of PKC activation does not adequately explain the many well-documented actions of PKC enzymes in mitochondrial, nuclear, and cardiac sarcomeric (non-sarcolemmal) subcellular compartments. Recent studies address this dilemma by identifying stimulus-specific differences in the mechanisms for PKC isoform activation during growth factor activation versus oxidative stress. This review discusses a number of non-canonical redox-triggered mechanisms that can alter the catalytic properties and subcellular compartmentation patterns of PKC enzymes. While some redox-activated mechanisms act at structural determinants that are common to all PKCs, the redox-dependent mechanism for PKCδ activation requires Src-dependent tyrosine phosphorylation of a unique phosphorylation motif on this enzyme and is isoform specific. Since oxidative stress contributes to pathogenesis of a wide range of clinical disorders, these stimulus-specific differences in the controls and consequences of PKC activation have important implications for the design and evaluation of PKC-targeted therapeutics.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.