Evidence map›Paper›PMID 26214365›Full record

ReviewBiochemistry2015

Dynamics and Membrane Interactions of Protein Kinase C.

Tatyana I Igumenova

Abstract readReview
In one paragraph

Review in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

52 citing papers in PubMed.

  1. Endosomal MrGPRX1 signaling sensitizes TRPV1 to enhance itch.Frontiers in molecular neuroscience · 2026
    Article
  2. Article
  3. Endosomal MrGPRX1 signaling sensitizes TRPV1 to enhance itch.bioRxiv : the preprint server for biology · 2025
    Article
  4. CaThe journal of physical chemistry. B · 2025
    Article
  5. Review
  6. Mitochondrial Biogenesis in Skeletal Muscle.Advances in experimental medicine and biology · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Inhibition of protein kinase C-α and activation of ezrin byAmerican journal of physiology. Endocrinology and metabolism · 2023
    Article
  12. Article
  13. Article
  14. IiScience · 2022
    Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author.

Tatyana I Igumenova

Funding

Structural and Functional Studies of Protein Kinase C RegulationR01GM108998 · NIGMS · TEXAS A&M AGRILIFE RESEARCH · PI Tatyana I. Igumenova · 2014 to 2026
$3.3M
NIGMS NIH HHS R01 GM108998
6 · The paper itself

Abstract

Protein kinase C (PKC) is a family of Ser/Thr kinases that regulate a multitude of cellular processes through participation in the phosphoinositide signaling pathway. Significant research efforts have been directed at understanding the structure, function, and regulatory modes of the enzyme since its discovery and identification as the first receptor for tumor-promoting phorbol esters. The activation of PKC involves a transition from the cytosolic autoinhibited latent form to the membrane-associated active form. The membrane recruitment step is accompanied by the conformational rearrangement of the enzyme, which relieves autoinhibitory interactions and thereby allows PKC to phosphorylate its targets. The multidomain structure and intrinsic flexibility of PKC present remarkable challenges and opportunities for the biophysical and structural biology studies of this class of enzymes and their interactions with membranes, the major focus of this Current Topic. I will highlight the recent advances in the field, outline the current challenges, and identify areas where biophysics and structural biology approaches can provide insight into the isoenzyme-specific regulation of PKC activity.

Indexed as

Amino Acid SequenceAnimalsBiophysical PhenomenaEnzyme ActivationHumansIsoenzymesModels, BiologicalModels, MolecularMolecular Dynamics SimulationMolecular Sequence DataProtein Kinase CProtein MultimerizationProtein Structure, TertiarySequence Homology, Amino AcidSignal TransductionIsoenzymesProtein Kinase C

Identifiers

PMID26214365
PMCPMC4979571

What OpenQuestion holds

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Registered trials

None linked

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.