Evidence map›Paper›PMID 34353440›Full record

ReviewAdvances in cancer research2021

Protein Tyrosine Phosphatases: A new paradigm in an old signaling system?

Colin L Welsh, Preeti Pandey, Lalima G Ahuja

Open access · greenAbstract readReview
In one paragraph

Review in Advances in cancer research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
8.9field-weighted citation impact, top 2% 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

11 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Adenoviral E3/49K: CD45-targeted immune evasion and therapeutic potential.Frontiers in cellular and infection microbiology · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Prostaglandin DLife (Basel, Switzerland) · 2023
    Article
  10. Review
  11. Article
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 2 institutions in 1 country.

Colin L WelshDepartment of Cell and Molecular Pharmacology & Experimental Therapeutics, College of Medicine, Medical University of South Carolina, Charleston, SC, United States.
Preeti PandeyDepartment of Cell and Molecular Pharmacology & Experimental Therapeutics, College of Medicine, Medical University of South Carolina, Charleston, SC, United States.
Lalima G AhujaDepartment of Cell and Molecular Pharmacology & Experimental Therapeutics, College of Medicine, Medical University of South Carolina, Charleston, SC, United States; Hollings Cancer Center, Medical University of South Carolina, Charleston, SC, United States. Electronic address: ahujal@musc.edu.
Medical University of South Carolina · USMUSC Hollings Cancer Center · US

Funding

SOUTH CAROLINA COBRE IN OXIDANTS, REDOX BALANCE AND STRESS SIGNALINGP20GM103542 · NIGMS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI TEW, KENNETH D. · 2012 to 2020
$20.2M
South Carolina COBRE in Oxidants, Redox Balance and Stress SignalingP30GM140964 · NIGMS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI EBLEN, SCOTT T · 2021 to 2025
$6.4M
NIGMS NIH HHS P20 GM103542NIGMS NIH HHS P30 GM140964
6 · The paper itself

Abstract

Protein Tyrosine Phosphatases reverse cellular signals initiated by growth factors receptors and other tyrosine kinases by dephosphorylating phosphotyrosine on target proteins. The activity of these enzymes is crucial for maintaining cell homeostasis, yet these enzymes have been often dismissed as humble house-keeping proteins. Understandably, mutations and changes in expression patterns of Protein Tyrosine Phosphatases are implicated in tumorigenesis and various carcinomas. The conserved nature of their catalytic domains makes drug discovery a challenging pursuit. In this review, we focus on describing the various classes of Protein Tyrosine Phosphatases and their catalytic domains. We also summarize their role in cancer and neurodegenerative diseases using specific members as the model system. Finally, we explain the dichotomy in the biological role of catalytically active vs the pseudoenzyme forms of Protein Tyrosine Phosphatases in the context of their membrane bound receptor forms. This chapter aims to provide a current understanding of these proteins, in the background of their foundational past research.

Indexed as

NeoplasmsHumansPhosphorylationProtein-Tyrosine KinasesProtein Tyrosine PhosphatasesSignal TransductionProtein-Tyrosine KinasesProtein Tyrosine PhosphatasesDouble-domain PTPsLARPhosphotyrosineProtein phosphorylationProtein Tyrosine PhosphatasesPTP1BReceptor phosphatases

Identifiers

PMID34353440
PMCPMC10544742
OpenAlexW3191395344

What OpenQuestion 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 OpenQuestion graph.