Evidence map›Paper›PMID 19033211›Full record

ReviewJournal of lipid research2009

Lipid activation of protein kinases.

Alexandra C Newton

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of lipid research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

92 citing papers in PubMed, 161 citations in OpenAlex.

  1. Trial
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  17. Review
  18. Role of Protein Kinase CK2 in Aberrant Lipid Metabolism in Cancer.Pharmaceuticals (Basel, Switzerland) · 2020
    Review
  19. Review
  20. Article

32 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 NewtonDepartment of Pharmacology, University of California at San Diego, La Jolla, CA 92093-0721, USA. anewton@ucsd.edu
University of California, San Diego · US

Funding

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 GM43154
6 · The paper itself

Abstract

Lipids acutely control the amplitude, duration, and subcellular location of signaling by lipid second messenger-responsive kinases. Typically, this activation is controlled by membrane-targeting modules that allosterically control the function of kinase domains within the same polypeptide. Protein kinase C (PKC) has served as the archetypal lipid-regulated kinase, providing a prototype for lipid-controlled kinase activation that is followed by kinases throughout the kinome, including its close cousin, Akt (protein kinase B). This review addresses the molecular mechanisms by which PKC and Akt transduce signals propagated by the two major lipid second messenger pathways in cells, those of diacylglycerol signaling and phosphatidylinositol-3,4,5-trisphosphate (PIP3) signaling, respectively.

Indexed as

Lipid MetabolismAnimalsCell MembraneEnzyme ActivationProtein KinasesSignal TransductionProtein Kinases

Identifiers

PMID19033211
PMCPMC2674703
OpenAlexW1969250154

What OpenQuestion holds

Textmetadata
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.