Evidence map›Paper›PMID 12461518›Full record

ReviewNature reviews. Drug discovery2002

Dual-specificity phosphatases as targets for antineoplastic agents.

Michael A Lyon, Alexander P Ducruet, Peter Wipf, John S Lazo

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Drug discovery, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

31 citing papers in PubMed, 140 citations in OpenAlex.

  1. Article
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  6. Deregulation of the protein phosphatase 2A, PP2A in cancer: complexity and therapeutic options.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
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  17. Review
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  20. Is Cdc25 a druggable target?Anti-cancer agents in medicinal chemistry · 2008
    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 1 country.

Michael A LyonDepartment of Chemistry, Chevron Science Center, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.
Alexander P Ducruet
Peter Wipf
John S Lazo
University of Pittsburgh · USChevron (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dual-specificity protein phosphatases are a subclass of protein tyrosine phosphatases that are uniquely able to hydrolyse the phosphate ester bond on both a tyrosine and a threonine or serine residue on the same protein. Dual-specificity phosphatases have a central role in the complex regulation of signalling pathways that are involved in cell stress responses, proliferation and death. Although this enzyme family is increasingly the target of drug discovery efforts in pharmaceutical companies, a summary of the salient developments in the biology and medicinal chemistry of dual-specificity phosphatases has been lacking. We hope that this comprehensive overview will stimulate further progress in the development of small-molecule inhibitors that could form the basis for a new class of target-directed therapeutic agents.

Indexed as

AnimalsAntineoplastic AgentsEnzyme InhibitorsHumansModels, BiologicalNeoplasmsProtein Tyrosine PhosphatasesAntineoplastic AgentsEnzyme InhibitorsProtein Tyrosine Phosphatases

Identifiers

PMID12461518
OpenAlexW2137586189

What OpenQuestion holds

Textmetadata
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.