Evidence map›Paper›PMID 29439552›Full record

ReviewMolecules (Basel, Switzerland)2018

Proteinaceous Regulators and Inhibitors of Protein Tyrosine Phosphatases.

Wiljan Hendriks, Annika Bourgonje, William Leenders, Rafael Pulido

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

12 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Functions and therapeutic potential of protein phosphatase 1: Insights from mouse genetics.Biochimica et biophysica acta. Molecular cell research · 2019
    Review
  12. 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 2 institutions in 3 countries.

Wiljan HendriksDepartment of Cell Biology, Radboud University Medical Center, Geert Grooteplein 26, 6525 GA Nijmegen, The Netherlands. wiljanjaj.hendriks@radboudumc.nl.ORCID 0000-0001-9481-8281
Annika BourgonjeDepartment of Cell Biology, Radboud University Medical Center, Geert Grooteplein 26, 6525 GA Nijmegen, The Netherlands. annika.bourgonje@radboudumc.nl.
William LeendersDepartment of Biochemistry, Radboud University Medical Center, Geert Grooteplein 26, 6525 GA Nijmegen, The Netherlands. william.leenders@radboudumc.nl.
Rafael PulidoBiomarkers in Cancer Unit, Biocruces Health Research Institute, 48903 Barakaldo, Spain. rpulidomurillo@gmail.com.
Radboud University Nijmegen · NLIkerbasque · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proper control of the phosphotyrosine content in signal transduction proteins is essential for normal cell behavior and is lost in many pathologies. Attempts to normalize aberrant tyrosine phosphorylation levels in disease states currently involve either the application of small compounds that inhibit tyrosine kinases (TKs) or the addition of growth factors or their mimetics to boost receptor-type TK activity. Therapies that target the TK enzymatic counterparts, the multi-enzyme family of protein tyrosine phosphatases (PTPs), are still lacking despite their undisputed involvement in human diseases. Efforts to pharmacologically modulate PTP activity have been frustrated by the conserved structure of the PTP catalytic core, providing a daunting problem with respect to target specificity. Over the years, however, many different protein interaction-based regulatory mechanisms that control PTP activity have been uncovered, providing alternative possibilities to control PTPs individually. Here, we review these regulatory principles, discuss existing biologics and proteinaceous compounds that affect PTP activity, and mention future opportunities to drug PTPs via these regulatory concepts.

Indexed as

AnimalsAntibodies, MonoclonalBrain NeoplasmsCatalytic DomainEnzyme InhibitorsGene Expression Regulation, NeoplasticGlioblastomaHumansModels, MolecularPhosphotyrosineProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein-Tyrosine KinasesProtein Tyrosine PhosphatasesAntibodies, MonoclonalEnzyme InhibitorsPhosphotyrosineProtein-Tyrosine KinasesProtein Tyrosine PhosphatasesbiologicsPDZ domainprotein inhibitorsprotein–protein interactionprotein tyrosine kinasesregulation of activitysignal transduction

Identifiers

PMID29439552
PMCPMC6016963
OpenAlexW2791136845

What OpenQuestion holds

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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.