Evidence map›Paper›PMID 26617522›Full record

ReviewFrontiers in pharmacology2015

Counteracting Protein Kinase Activity in the Heart: The Multiple Roles of Protein Phosphatases.

Silvio Weber, Stefanie Meyer-Roxlau, Michael Wagner, Dobromir Dobrev, Ali El-Armouche

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in pharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
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  5. A Missense Variation inInternational journal of molecular sciences · 2023
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  6. Article
  7. Review
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  9. Regulation of Cardiac PKA Signaling by cAMP and Oxidants.Antioxidants (Basel, Switzerland) · 2021
    Review
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  13. Article
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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 2 institutions in 1 country.

Silvio WeberDepartment of Pharmacology and Toxicology, Dresden University of Technology , Dresden, Germany.
Stefanie Meyer-RoxlauDepartment of Pharmacology and Toxicology, Dresden University of Technology , Dresden, Germany.
Michael WagnerDepartment of Pharmacology and Toxicology, Dresden University of Technology , Dresden, Germany.
Dobromir DobrevInstitute of Pharmacology, Faculty of Medicine, West German Heart and Vascular Center , Essen, Germany.
Ali El-ArmoucheDepartment of Pharmacology and Toxicology, Dresden University of Technology , Dresden, Germany.
TU Dresden · DEWest German Heart and Vascular Center Essen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Decades of cardiovascular research have shown that variable and flexible levels of protein phosphorylation are necessary to maintain cardiac function. A delicate balance between phosphorylated and dephosphorylated states of proteins is guaranteed by a complex interplay of protein kinases (PKs) and phosphatases. Serine/threonine phosphatases, in particular members of the protein phosphatase (PP) family govern dephosphorylation of the majority of these cardiac proteins. Recent findings have however shown that PPs do not only dephosphorylate previously phosphorylated proteins as a passive control mechanism but are capable to actively control PK activity via different direct and indirect signaling pathways. These control mechanisms can take place on (epi-)genetic, (post-)transcriptional, and (post-)translational levels. In addition PPs themselves are targets of a plethora of proteinaceous interaction partner regulating their endogenous activity, thus adding another level of complexity and feedback control toward this system. Finally, novel approaches are underway to achieve spatiotemporal pharmacologic control of PPs which in turn can be used to fine-tune misleaded PK activity in heart disease. Taken together, this review comprehensively summarizes the major aspects of PP-mediated PK regulation and discusses the subsequent consequences of deregulated PP activity for cardiovascular diseases in depth.

Indexed as

calcineurinPIPPP1PP2Aprotein phosphatase inhibitor-1 (I-1)

Identifiers

PMID26617522
PMCPMC4643138
OpenAlexW2172749683

What OpenQuestion holds

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LicenceCC BY
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.