Evidence map›Paper›PMID 40555575›Full record

ReviewTrends in endocrinology and metabolism: TEM2026

MAP kinase phosphatases in metabolic diseases.

Ananya Hota, Anton M Bennett

Abstract readReview
In one paragraph

Review in Trends in endocrinology and metabolism: TEM, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. 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

2 authors.

Ananya HotaDepartment of Biology, Howard University, Washington, DC, USA.
Anton M BennettDepartment of Pharmacology, Yale University School of Medicine, New Haven, CT, USA; Yale Center for Molecular and Systems Metabolism, Yale University School of Medicine, New Haven, CT, USA. Electronic address: anton.bennett@yale.edu.

Funding

Dual-specificity phosphatase action in muscle diseaseR01AR080152 · NIAMS · YALE UNIVERSITY · PI Anton M Bennett · 2022 to 2026
$2.5M
MKP5 allostery in MAPK regulation and signaling in the heartR01HL158876 · NHLBI · YALE UNIVERSITY · PI BENNETT, ANTON M, LOLIS, ELIAS · 2022 to 2025
$2.4M
NHLBI NIH HHS R01 HL158876NIAMS NIH HHS R01 AR080152
6 · The paper itself

Abstract

Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are essential regulators of MAPK signaling pathways. MKPs perform critical roles in various cellular responses by dephosphorylating the regulatory residues and thereby inactivating MAPKs. Many studies have highlighted the role of MKPs in metabolic diseases, including obesity, diabetes, and cardiovascular disorders. These metabolic diseases disrupt key pathways such as insulin signaling, glucose homeostasis, lipid metabolism, and other inflammatory processes. Here, we provide a comprehensive overview of the current understanding of the role played by MKPs in metabolism and highlight their roles in metabolic diseases and potential as therapeutic targets.

Indexed as

Metabolic DiseasesMitogen-Activated Protein Kinase PhosphatasesAnimalsHumansMAP Kinase Signaling SystemMitogen-Activated Protein Kinase Phosphatasesinflammationinsulin resistanceMAPK phosphatasesmetabolic diseasesmetabolismmitogen-activated protein kinasesobesitytype 2 diabetes

Identifiers

PMID40555575
PMCPMC13271833

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.