Evidence map›Paper›PMID 31151270›Full record

ReviewInternational journal of molecular sciences2019

Regulation of Dual-Specificity Phosphatase (DUSP) Ubiquitination and Protein Stability.

Hsueh-Fen Chen, Huai-Chia Chuang, Tse-Hua Tan

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed
5.9field-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

124 citing papers in PubMed, 198 citations in OpenAlex.

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  5. ERK autoinhibition mechanism informs a drug combination strategy.Protein science : a publication of the Protein Society · 2026
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64 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 1 institution in 1 country.

Hsueh-Fen ChenImmunology Research Center, National Health Research Institutes, Zhunan 35053, Taiwan. 061013@nhri.edu.tw.
Huai-Chia ChuangImmunology Research Center, National Health Research Institutes, Zhunan 35053, Taiwan. cinth@nhri.edu.tw.
Tse-Hua TanImmunology Research Center, National Health Research Institutes, Zhunan 35053, Taiwan. ttan@nhri.edu.tw.ORCID 0000-0003-4969-3170
National Health Research Institutes · TW

Funding

Ministry of Science and Technology, Taiwan 107-2314-B-400-027Ministry of Science and Technology, Taiwan 107-2321-B-400-013National Health Research Institutes, Taiwan IM-107-PP-01National Health Research Institutes, Taiwan IM-107-SP-01
6 · The paper itself

Abstract

Mitogen-activated protein kinases (MAPKs) are key regulators of signal transduction and cell responses. Abnormalities in MAPKs are associated with multiple diseases. Dual-specificity phosphatases (DUSPs) dephosphorylate many key signaling molecules, including MAPKs, leading to the regulation of duration, magnitude, or spatiotemporal profiles of MAPK activities. Hence, DUSPs need to be properly controlled. Protein post-translational modifications, such as ubiquitination, phosphorylation, methylation, and acetylation, play important roles in the regulation of protein stability and activity. Ubiquitination is critical for controlling protein degradation, activation, and interaction. For DUSPs, ubiquitination induces degradation of eight DUSPs, namely, DUSP1, DUSP4, DUSP5, DUSP6, DUSP7, DUSP8, DUSP9, and DUSP16. In addition, protein stability of DUSP2 and DUSP10 is enhanced by phosphorylation. Methylation-induced ubiquitination of DUSP14 stimulates its phosphatase activity. In this review, we summarize the knowledge of the regulation of DUSP stability and ubiquitination through post-translational modifications.

Indexed as

UbiquitinationAnimalsDisease SusceptibilityDual-Specificity PhosphatasesHumansIsoenzymesLysineMultigene FamilyProteasome Endopeptidase ComplexProtein Processing, Post-TranslationalProtein StabilityProteolysisDual-Specificity PhosphatasesIsoenzymesLysineProteasome Endopeptidase Complexdual-specificity phosphatasemitogen-activated protein kinaseprotein stabilityubiquitination

Identifiers

PMID31151270
PMCPMC6600639
OpenAlexW2947459970

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.