ReviewPhysiological reviews2008
Structural basis of protein kinase C isoform function.
Review in Physiological reviews, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 466 papers, 3 of them syntheses that pooled it.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
466 citing papers in PubMed, 3 syntheses or guidelines pooled it, 866 citations in OpenAlex.
- Macrophage-associated kinase signaling in atherosclerosis - a systematic review.Cell communication and signaling : CCS · 2026Pooled it
- Pharmacological insights intoFrontiers in pharmacology · 2025Pooled it
- Genetic variants associated with longitudinal changes in brain structure across the lifespan.Nature neuroscience · 2022Pooled it
- High levels of nitric oxide and peroxynitrite with protein nitration: a new therapeutic target for gliomas.Medical gas research · 2027Review
- PKC inhibitors reveal PKC isoforms involved in HIV latency reversal and immunomodulation.Journal of virology · 2026Article
- A new paradigm in Parkinson's disease: kidney-origin α-synuclein pathology driven by PKC signaling and aurothioglucose.Inflammopharmacology · 2026Review
- Psoriasis and chronic kidney disease: insights into mechanisms and novel therapeutic outlooks.International urology and nephrology · 2026Review
- Serum proteomic signatures and an immune-calcium signaling cascade associated with antipsychotic-related erectile dysfunction in schizophrenia.Scientific reports · 2026Article
- Molecular basis of allosteric regulation and pharmaceutical targeting of protein kinase Cβ.Nature communications · 2026Article
- Article
- Protein Kinase C-Delta (PKCδ) inhibition stabilizes endothelium and suppresses triple-negative breast cancer (TNBC) intravasation in a microfluidic hypoxic tumor model.Bioengineering & translational medicine · 2026Article
- ALOX15-Derived Oxylipins Attenuate Macrophage Inflammatory Signaling Via a GαFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Ablation of PKCα Phosphorylation by CRISPR-Cas9 Base Editing Rescues Heart Failure.Circulation research · 2026Article
- Marine medaka PKCα promotes red-spotted grouper nervous necrosis virus entry by orchestrating MYL3-mediated macropinocytosis and cofilin-dependent actin remodeling.Journal of virology · 2026Article
- Opposite Effects of Diacylglycerol and Phosphatidic Acid in the Modulation of the Plasma Membrane CaBiomedicines · 2026Article
- Article
- Protein Kinase C Regulates Meiosis in Mammalian Oocytes.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Unlocking New Treatment Horizons for Celiac Disease: PRKCD Revealed as a Promising Target through Mendelian RandomizationEndocrine, metabolic & immune disorders drug targets · 2026Article
- The C2 Domain of PKC‑δ as a Dominant-Negative Modulator of Breast Cancer Cell Survival and Chemosensitivity.ACS omega · 2025Article
- AAK1 activation-mediated iron trafficking drives ferroptotic cell death.Nature communications · 2025Article
406 more citing papers are in PubMed but not listed here.
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) isoforms comprise a family of lipid-activated enzymes that have been implicated in a wide range of cellular functions. PKCs are modular enzymes comprised of a regulatory domain (that contains the membrane-targeting motifs that respond to lipid cofactors, and in the case of some PKCs calcium) and a relatively conserved catalytic domain that binds ATP and substrates. These enzymes are coexpressed and respond to similar stimulatory agonists in many cell types. However, there is growing evidence that individual PKC isoforms subserve unique (and in some cases opposing) functions in cells, at least in part as a result of isoform-specific subcellular compartmentalization patterns, protein-protein interactions, and posttranslational modifications that influence catalytic function. This review focuses on the structural basis for differences in lipid cofactor responsiveness for individual PKC isoforms, the regulatory phosphorylations that control the normal maturation, activation, signaling function, and downregulation of these enzymes, and the intra-/intermolecular interactions that control PKC isoform activation and subcellular targeting in cells. A detailed understanding of the unique molecular features that underlie isoform-specific posttranslational modification patterns, protein-protein interactions, and subcellular targeting (i.e., that impart functional specificity) should provide the basis for the design of novel PKC isoform-specific activator or inhibitor compounds that can achieve therapeutically useful changes in PKC signaling in cells.
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What OpenQuestion holds
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.