Evidence map›Paper›PMID 34203203›Full record

ReviewInternational journal of molecular sciences2021

The Roles of Pseudophosphatases in Disease.

Andrew M Mattei, Jonathan D Smailys, Emma Marie Wilber Hepworth, Shantá D Hinton

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

14 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. TheGenes & diseases · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Emerging functions of pseudoenzymes.The Biochemical journal · 2023
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. The progress of research into pseudophosphatases.Frontiers in public health · 2022
    Review
  14. Pseudophosphatases as Regulators of MAPK Signaling.International journal of molecular sciences · 2021
    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

4 authors at 1 institution in 1 country.

Andrew M MatteiIntegrated Science Center, Department of Biology, College of William and Mary, Williamsburg, VA 23185, USA.
Jonathan D SmailysIntegrated Science Center, Department of Biology, College of William and Mary, Williamsburg, VA 23185, USA.
Emma Marie Wilber HepworthIntegrated Science Center, Department of Biology, College of William and Mary, Williamsburg, VA 23185, USA.
Shantá D HintonIntegrated Science Center, Department of Biology, College of William and Mary, Williamsburg, VA 23185, USA.
William & Mary · US

Funding

Pseudophosphatase MK-STYX: A Signaling Molecule for DifferentiationR15NS115074 · NINDS · COLLEGE OF WILLIAM AND MARY · PI HINTON, SHANTA' D · 2020 to 2022
$500k
National Science Foundation; National Institutes of Health NSF MCB 1909316; NIH 1 R15 NS115074-10NINDS NIH HHS R15 NS115074
6 · The paper itself

Abstract

The pseudophosphatases, atypical members of the protein tyrosine phosphatase family, have emerged as bona fide signaling regulators within the past two decades. Their roles as regulators have led to a renaissance of the pseudophosphatase and pseudoenyme fields, catapulting interest from a mere curiosity to intriguing and relevant proteins to investigate. Pseudophosphatases make up approximately fourteen percent of the phosphatase family, and are conserved throughout evolution. Pseudophosphatases, along with pseudokinases, are important players in physiology and pathophysiology. These atypical members of the protein tyrosine phosphatase and protein tyrosine kinase superfamily, respectively, are rendered catalytically inactive through mutations within their catalytic active signature motif and/or other important domains required for catalysis. This new interest in the pursuit of the relevant functions of these proteins has resulted in an elucidation of their roles in signaling cascades and diseases. There is a rapid accumulation of knowledge of diseases linked to their dysregulation, such as neuropathies and various cancers. This review analyzes the involvement of pseudophosphatases in diseases, highlighting the function of various role(s) of pseudophosphatases involvement in pathologies, and thus providing a platform to strongly consider them as key therapeutic drug targets.

Indexed as

AnimalsDual-Specificity PhosphatasesHumansProtein Tyrosine PhosphatasesSignal TransductionTensinsDual-Specificity PhosphatasesProtein Tyrosine PhosphatasesTensinsdiseasedual specificity phosphatases (DUSPs)MK-STYX (MAPK (mitogen-activated protein kinase) phosphoserine/threonine/tyrosine-binding protein)myotubularin phosphatases (MTMs)protein tyrosine phosphatases (PTPs)pseudoenzymespseudophosphatasesSTYX (phosphoserine/threonine/tyrosine-interacting protein)tensin

Identifiers

PMID34203203
PMCPMC8269279
OpenAlexW3175560554

What OpenQuestion holds

Textmetadata
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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.