Evidence map›Paper›PMID 25921264›Full record

ReviewBioorganic & medicinal chemistry2015

Perspective: Tyrosine phosphatases as novel targets for antiplatelet therapy.

Lutz Tautz, Yotis A Senis, Cécile Oury, Souad Rahmouni

Open access · greenAbstract readReview
In one paragraph

Review in Bioorganic & medicinal chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

9 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. A Network Pharmacology to Explore the Mechanism ofBioMed research international · 2021
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. 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

4 authors at 3 institutions in 3 countries.

Lutz TautzNCI-Designated Cancer Center, Sanford-Burnham Medical Research Institute, 10901 N Torrey Pines Rd, La Jolla, CA 92037, USA. Electronic address: tautz@sanfordburnham.org.
Yotis A SenisCentre for Cardiovascular Sciences, Institute of Biomedical Research, School of Clinical and Experimental Medicine, College of Medical and Dental Sciences, University of Birmingham, Edgbaston, Birmingham, UK.
Cécile OuryLaboratory of Thrombosis and Haemostasis, GIGA-Cardiovascular Sciences, University of Liège, Liège, Belgium.
Souad RahmouniImmunology and Infectious Diseases Unit, GIGA-Signal Transduction, University of Liège, Liège, Belgium.
University of Liège · BESanford Burnham Prebys Medical Discovery Institute · USUniversity of Birmingham · GB

Funding

Sanford-Burnham Center for Chemical GenomicsU54HG005033 · NHGRI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI JACKSON, MICHAEL · 2008 to 2012
$72.5M
Novel Delivery Technology for Potential Drugs for Cervical CancerR21CA132121 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI TAUTZ, LUTZ · 2008 to 2009
$473k
Small-Molecule Inhibitors of Vaccinia-H1-Related Phosphatase VHRR03MH084230 · NIMH · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI TAUTZ, LUTZ · 2008 to 2008
$25k
British Heart Foundation FS/13/1/29894NCI NIH HHS R21 CA132121NHGRI NIH HHS U54 HG005033NIMH NIH HHS R03 MH084230
6 · The paper itself

Abstract

Arterial thrombosis is the primary cause of most cases of myocardial infarction and stroke, the leading causes of death in the developed world. Platelets, highly specialized cells of the circulatory system, are key contributors to thrombotic events. Antiplatelet drugs, which prevent platelets from aggregating, have been very effective in reducing the mortality and morbidity of these conditions. However, approved antiplatelet therapies have adverse side effects, most notably the increased risk of bleeding. Moreover, there remains a considerable incidence of arterial thrombosis in a subset of patients receiving currently available drugs. Thus, there is a pressing medical need for novel antiplatelet agents with a more favorable safety profile and less patient resistance. The discovery of novel antiplatelet targets is the matter of intense ongoing research. Recent findings demonstrate the potential of targeting key signaling molecules, including kinases and phosphatases, to prevent platelet activation and aggregation. Here, we offer perspectives to targeting members of the protein tyrosine phosphatase (PTP) superfamily, a major class of enzymes in signal transduction. We give an overview of previously identified PTPs in platelet signaling, and discuss their potential as antiplatelet drug targets. We also introduce VHR (DUSP3), a PTP that we recently identified as a major player in platelet biology and thrombosis. We review our data on genetic deletion as well as pharmacological inhibition of VHR, providing proof-of-principle for a novel and potentially safer VHR-based antiplatelet therapy.

Indexed as

Drug DiscoveryAnimalsBlood PlateletsHumansModels, MolecularMolecular Targeted TherapyPlatelet ActivationPlatelet Aggregation InhibitorsProtein Tyrosine PhosphatasesSignal TransductionThrombosisPlatelet Aggregation InhibitorsProtein Tyrosine PhosphatasesAntiplateletAntithromboticCD148CLEC-2DrugDUSP3GPVIInhibitorPlateletsProtein tyrosine phosphatasesPTPPTP1BSHP1SHP2TherapyThrombosisVHR

Identifiers

PMID25921264
PMCPMC4451376
OpenAlexW2056525663

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.