Evidence map›Paper›PMID 30401534›Full record

ReviewBiochimica et biophysica acta. Molecular cell research2019

Dual-specificity MAP kinase phosphatases in health and disease.

Ole-Morten Seternes, Andrew M Kidger, Stephen M Keyse

Open access · hybridAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Molecular cell research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
4.5field-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

95 citing papers in PubMed, 141 citations in OpenAlex.

  1. Article
  2. DUSP4 promotes anti-tumor CD8Nature communications · 2026
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35 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

3 authors at 3 institutions in 2 countries.

Ole-Morten SeternesDepartment of Pharmacy, UiT The Arctic University of Norway, N-9037 Tromsø, Norway. Electronic address: ole-morten.seternes@uit.no.
Andrew M KidgerSignalling Programme, The Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, England, UK. Electronic address: andrew.kidger@babraham.ac.uk.
Stephen M KeyseStress Response Laboratory, Jacqui Wood Cancer Centre, James Arrot Drive, Ninewells Hospital & Medical School, Dundee DD1 9SY, UK. Electronic address: s.m.keyse@dundee.ac.uk.
Babraham Institute · GBNinewells Hospital · GBUiT The Arctic University of Norway · NO

Funding

Cancer Research UK 12053Medical Research Council MR/N020790/1Medical Research Council MR/NO20790/1
6 · The paper itself

Abstract

It is well established that a family of dual-specificity MAP kinase phosphatases (MKPs) play key roles in the regulated dephosphorylation and inactivation of MAP kinase isoforms in mammalian cells and tissues. MKPs provide a mechanism of spatiotemporal feedback control of these key signalling pathways, but can also mediate crosstalk between distinct MAP kinase cascades and facilitate interactions between MAP kinase pathways and other key signalling modules. As our knowledge of the regulation, substrate specificity and catalytic mechanisms of MKPs has matured, more recent work using genetic models has revealed key physiological functions for MKPs and also uncovered potentially important roles in regulating the pathophysiological outcome of signalling with relevance to human diseases. These include cancer, diabetes, inflammatory and neurodegenerative disorders. It is hoped that this understanding will reveal novel therapeutic targets and biomarkers for disease, thus contributing to more effective diagnosis and treatment for these debilitating and often fatal conditions.

Indexed as

AnimalsCatalysisCell NucleusCytoplasmDiabetes MellitusDual-Specificity PhosphatasesHumansMAP Kinase Signaling SystemMiceMitogen-Activated Protein Kinase PhosphatasesMitogen-Activated Protein KinasesNeuropathologyObesityPhosphoprotein PhosphatasesPhosphorylationProtein Tyrosine PhosphatasesDual-Specificity PhosphatasesMitogen-Activated Protein Kinase PhosphatasesMitogen-Activated Protein KinasesPhosphoprotein PhosphatasesProtein Tyrosine PhosphatasesDiabetesMAP kinaseMAP kinase phosphataseNeuropathologyObesityOncogenic signalling

Identifiers

PMID30401534
PMCPMC6227380
OpenAlexW2891486965

What OpenQuestion holds

Textmetadata
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.