Evidence map›Paper›PMID 31467668›Full record

ReviewCell & bioscience2019

DUSP8 phosphatase: structure, functions, expression regulation and the role in human diseases.

Tao Ding, Ya Zhou, Runying Long, Chao Chen, Juanjuan Zhao, Panpan Cui, Mengmeng Guo, Guiyou Liang, Lin Xu

Open access · goldAbstract readReview
In one paragraph

Review in Cell & bioscience, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. MAP kinase phosphatases in metabolic diseases.Trends in endocrinology and metabolism: TEM · 2026
    Review
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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

9 authors at 3 institutions in 1 country.

Tao DingSpecial Key Laboratory of Gene Detection and Therapy of Guizhou Province, Zunyi, 563000 Guizhou China.
Ya Zhou3Department of Medical Physics, Zunyi Medical University, Zunyi, 563000 Guizhou China.
Runying LongSpecial Key Laboratory of Gene Detection and Therapy of Guizhou Province, Zunyi, 563000 Guizhou China.
Chao ChenSpecial Key Laboratory of Gene Detection and Therapy of Guizhou Province, Zunyi, 563000 Guizhou China.
Juanjuan ZhaoSpecial Key Laboratory of Gene Detection and Therapy of Guizhou Province, Zunyi, 563000 Guizhou China.
Panpan CuiSpecial Key Laboratory of Gene Detection and Therapy of Guizhou Province, Zunyi, 563000 Guizhou China.
Mengmeng GuoSpecial Key Laboratory of Gene Detection and Therapy of Guizhou Province, Zunyi, 563000 Guizhou China.
Guiyou Liang4Department of Cardiovascular Surgery, Affiliated Hospital of Guizhou Medical University, Guiyang, 550004 Guizhou China.
Lin XuSpecial Key Laboratory of Gene Detection and Therapy of Guizhou Province, Zunyi, 563000 Guizhou China.
Guizhou Provincial Education Department · CNZunyi Medical University · CNGuiyang Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dual-specificity phosphatases (DUSPs) are a subset of protein tyrosine phosphatases (PTPs), many of which dephosphorylate the residues of phosphor-serine/threonine and phosphor-tyrosine on mitogen-activated protein kinases (MAPKs), and hence are also referred to as MAPK phosphatases (MKPs). Homologue of Vaccinia virus H1 phosphatase gene clone 5 (HVH-5), also known as DUSP8, is a unique member of the DUSPs family of phosphatases. Accumulating evidence has shown that DUSP8 plays an important role in phosphorylation-mediated signal transduction of MAPK signaling ranging from cell oxidative stress response, cell apoptosis and various human diseases. It is generally believed that DUSP8 exhibits significant dephosphorylation activity against JNK, however, with the deepening of research, plenty of new literature reports that DUSP8 also has effective dephosphorylation activity on p38 MAPK and ERKs, successfully affects the transduction of MAPKs pathway, indicating that DUSP8 presents a unknown diversity of DUSPs family on distinct corresponding dephosphorylated substrates in different biological events. Therefore, the in-depth study of DUSP8 not only throws a new light on the multi-biological function of DUSPs, but also is much valuable for the reveal of complex pathobiology of clinical diseases. In this review, we provide a detail overview of DUSP8 phosphatase structure, biological function and expression regulation, as well as its role in related clinical human diseases, which might be help for the understanding of biological function of DUSP8 and the development of prevention, diagnosis and therapeutics in related human diseases.

Indexed as

DephosphorylationDiseasesDUSP8MAPKRegulation

Identifiers

PMID31467668
PMCPMC6712826
OpenAlexW2971122722

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.