Evidence map›Paper›PMID 24510065›Full record

ReviewPflugers Archiv : European journal of physiology2014

Heart failure-specific changes in protein kinase signalling.

Kristina Lorenz, Konstantina Stathopoulou, Evelyn Schmid, Petra Eder, Friederike Cuello

Abstract readReview
PubMed Publisher
In one paragraph

Review in Pflugers Archiv : European journal of physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  8. Review
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  12. Astragalus Granule Prevents CaEvidence-based complementary and alternative medicine : eCAM · 2017
    Article
  13. Article
  14. Insulin Signaling and Heart Failure.Circulation research · 2016
    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

5 authors at 3 institutions in 1 country.

Kristina LorenzInstitute of Pharmacology and Toxicology, University of Würzburg, Versbacher Strasse 9, 97078, Würzburg, Germany, Lorenz@toxi.uni-wuerzburg.de.
Konstantina Stathopoulou
Evelyn Schmid
Petra Eder
Friederike Cuello
University Medical Center Hamburg-Eppendorf · DEUniversity of Würzburg · DEUniversitätsklinikum Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Among the myriad of molecular alterations occurring in heart failure development, aggravation of the disease is often attributed to global or local changes in protein kinase activity, thus making protein kinases attractive targets for therapeutic intervention. Since protein kinases do not only have maladaptive roles, but also contribute to the physiological integrity of cells, it is a challenging task to circumvent undesired inhibition of protein kinase activity. Identification of posttranslational modifications and/or protein-protein interactions that are exclusively apparent under pathophysiological conditions provides exciting information for alternative non-kinase inhibitory treatment strategies that eliminate maladaptive functions of a protein kinase, but preserve the beneficial ones. Here, we focus on the disease-specific regulation of a number of protein kinases, namely, Ca(2+)/calmodulin-dependent protein kinase II isoform δ (CaMKIIδ), G protein-coupled receptor kinase 2 (GRK2), extracellular signal-regulated kinase 1 and 2 (ERK1/2), protein kinase D (PKD) and protein kinase C isoform β2 (PKCβ2), which are embedded in complex signal transduction pathways implicated in heart failure development, and discuss potential avenues for novel treatment strategies to combat heart disease.

Indexed as

MAP Kinase Signaling SystemAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Extracellular Signal-Regulated MAP KinasesG-Protein-Coupled Receptor Kinase 2Heart FailureHumansProtein Kinase CCalcium-Calmodulin-Dependent Protein Kinase Type 2Extracellular Signal-Regulated MAP KinasesG-Protein-Coupled Receptor Kinase 2Protein Kinase Cprotein kinase D

Identifiers

PMID24510065
OpenAlexW2081174218

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.