Evidence map›Paper›PMID 29513138›Full record

ReviewCritical reviews in biochemistry and molecular biology2018

Protein kinase C: perfectly balanced.

Alexandra C Newton

Open access · greenAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 182 papers.

0numbers the graph read from it
0cells of the map it votes in
182citing papers in PubMed
11.2field-weighted citation impact, top 1% 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

182 citing papers in PubMed, 341 citations in OpenAlex.

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  16. Protein Kinase C Regulates Meiosis in Mammalian Oocytes.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  17. Review
  18. Article
  19. Article
  20. Article

122 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

Alexandra C Newtona Department of Pharmacology , University of California at San Diego , La Jolla , CA , USA.
University of California San Diego · US

Funding

Molecular Mechanisms of Cell SignalingR35GM122523 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ALEXANDRA C. NEWTON · 2017 to 2026
$6.7M
NIGMS NIH HHS R35 GM122523
6 · The paper itself

Abstract

Protein kinase C (PKC) isozymes belong to a family of Ser/Thr kinases whose activity is governed by reversible release of an autoinhibitory pseudosubstrate. For conventional and novel isozymes, this is effected by binding the lipid second messenger, diacylglycerol, but for atypical PKC isozymes, this is effected by binding protein scaffolds. PKC shot into the limelight following the discovery in the 1980s that the diacylglycerol-sensitive isozymes are "receptors" for the potent tumor-promoting phorbol esters. This set in place a concept that PKC isozymes are oncoproteins. Yet three decades of cancer clinical trials targeting PKC with inhibitors failed and, in some cases, worsened patient outcome. Emerging evidence from cancer-associated mutations and protein expression levels provide a reason: PKC isozymes generally function as tumor suppressors and their activity should be restored, not inhibited, in cancer therapies. And whereas not enough activity is associated with cancer, variants with enhanced activity are associated with degenerative diseases such as Alzheimer's disease. This review describes the tightly controlled mechanisms that ensure PKC activity is perfectly balanced and what happens when these controls are deregulated. PKC isozymes serve as a paradigm for the wisdom of Confucius: "to go beyond is as wrong as to fall short."

Indexed as

Second Messenger SystemsAlzheimer DiseaseAnimalsHumansIsoenzymesMutationNeoplasmsOncogene ProteinsProtein Kinase CProtein Kinase InhibitorsTumor Suppressor ProteinsIsoenzymesOncogene ProteinsProtein Kinase CProtein Kinase InhibitorsTumor Suppressor ProteinsAlzheimer’s diseasecancerdiacylglycerolphorbol estersphosphorylationProtein kinase Cpseudosubstratetumor suppressor

Identifiers

PMID29513138
PMCPMC5901981
OpenAlexW2792970702

What OpenQuestion holds

Textmetadata
LicenceTDM
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.