Evidence map›Paper›PMID 25399557›Full record

ReviewBiochemical Society transactions2014

Tuning the signalling output of protein kinase C.

Corina E Antal, Alexandra C Newton

Abstract readReview
In one paragraph

Review in Biochemical Society transactions, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.3field-weighted citation impact, top 7% of its field
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

39 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. PKCα Is Recruited toFrontiers in immunology · 2021
    Article
  16. Article
  17. Article
  18. Review
  19. A real-time, click chemistry imaging approach reveals stimulus-specific subcellular locations of phospholipase D activity.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. Review
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

2 authors at 1 institution in 1 country.

Corina E Antal
Alexandra C Newton*Department of Pharmacology, University of California at San Diego, La Jolla, CA 92093, U.S.A.
University of California, San Diego · US

Funding

GRADUATE TRAINING IN CELLULAR &MOLECULAR PHARMACOLOGYT32GM007752 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BROWN, JOAN HELLER, HANDEL, TRACY M · 1985 to 2023
$13.5M
Structure, Function and Regulation of Protein Kinase CR37GM043154 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI NEWTON, ALEXANDRA C. · 2003 to 2012
$4.0M
STRUCTURE/FUNCTION AND REGULATION OF PROTEIN KINASE CR01GM043154 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI NEWTON, ALEXANDRA C. · 1990 to 2016
$2.5M
NIGMS NIH HHS GM43154NIGMS NIH HHS R01 GM043154NIGMS NIH HHS R37 GM043154NIGMS NIH HHS T32 GM007752
6 · The paper itself

Abstract

Precise control of the amplitude of protein kinase C (PKC) signalling is essential for cellular homoeostasis, and disruption of this control leads to pathophysiological states such as cancer, neurodegeneration and diabetes. For conventional and novel PKC, this amplitude is meticulously tuned by multiple inputs that regulate the amount of enzyme in the cell, its ability to sense its allosteric activator diacylglycerol, and protein scaffolds that co-ordinate access to substrates. Key to regulation of the signalling output of most PKC isoenzymes is the ability of cytosolic enzyme to respond to the membrane-embedded lipid second messenger, diacylglycerol, in a dynamic range that prevents signalling in the absence of agonists but allows efficient activation in response to small changes in diacylglycerol levels. The present review discusses the regulatory inputs that control the spatiotemporal dynamics of PKC signalling, with a focus on conventional and novel PKC isoenzymes.

Indexed as

Signal TransductionAllosteric RegulationHumansProtein ConformationProtein Kinase CSecond Messenger SystemsProtein Kinase C

Identifiers

PMID25399557
PMCPMC5783555
OpenAlexW2315582586

What OpenQuestion holds

Textmetadata
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Read underepoch 390

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.