Evidence map›Paper›PMID 21738220›Full record

ReviewEMBO reports2011

Protein kinase D: coupling extracellular stimuli to the regulation of cell physiology.

Ya Fu, Charles S Rubin

Open access · greenAbstract readReview
In one paragraph

Review in EMBO reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

81 citing papers in PubMed, 130 citations in OpenAlex.

  1. Mechanical forces stimulate Golgi export.The Journal of cell biology · 2026
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  5. Natural variation in protein kinase D modifies alcohol sensitivity inbioRxiv : the preprint server for biology · 2024
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21 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

2 authors at 1 institution in 1 country.

Ya FuDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, USA.
Charles S Rubin
Albert Einstein College of Medicine · US

Funding

Properties, Regulation and Functions of Diacylglycerol-Activated Protein Kinase DR01GM080615 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI RUBIN, CHARLES S · 2008 to 2011
$1.3M
NIGMS NIH HHS GM080615NIGMS NIH HHS R01 GM080615
6 · The paper itself

Abstract

Protein kinase D (PKD) mediates the actions of stimuli that promote diacylglycerol (DAG) biogenesis. By phosphorylating effectors that regulate transcription, fission and polarized transport of Golgi vesicles, as well as cell migration and survival after oxidative stress, PKDs substantially expand the range of physiological processes controlled by DAG. Dysregulated PKDs have been linked to pathologies including heart hypertrophy and cancer invasiveness. Our understanding of PKD regulation by trans- and autophosphorylation, as well as the subcellular dynamics of PKD substrate phosphorylation, have increased markedly. Selective PKD inhibitors provide new, powerful tools for elucidating the physiological roles of PKDs and potentially treating cardiac disease and cancer.

Indexed as

AnimalsBiological TransportCell Physiological PhenomenaDiglyceridesExtracellular SpaceHumansProtein Kinase CDiglyceridesProtein Kinase Cprotein kinase D

Identifiers

PMID21738220
PMCPMC3147268
OpenAlexW2116992704

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.