Evidence map›Paper›PMID 39723827›Full record

ArticleProtein science : a publication of the Protein Society2025

The structural influence of the oncogenic driver mutation N642H in the STAT5B SH2 domain.

Liam Haas-Neill, Deniz Meneksedag-Erol, Ayesha Chaudhry, Masha Novoselova, Qirat F Ashraf, Elvin D de Araujo, Derek J Wilson, Sarah Rauscher

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. The structural influence of the oncogenic driver mutation N642H in the STAT5B SH2 domain.Protein science : a publication of the Protein Society · 2025
    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

8 authors.

Liam Haas-NeillDepartment of Physics, University of Toronto, Toronto, Ontario, Canada.ORCID 0000-0003-3852-8786
Deniz Meneksedag-ErolDepartment of Chemical and Physical Sciences, University of Toronto Mississauga, Mississauga, Ontario, Canada.ORCID 0000-0002-7765-3304
Ayesha ChaudhryDepartment of Chemistry, York University, Toronto, Ontario, Canada.
Masha NovoselovaDepartment of Chemical and Physical Sciences, University of Toronto Mississauga, Mississauga, Ontario, Canada.ORCID 0009-0005-5043-6261
Qirat F AshrafDepartment of Chemical and Physical Sciences, University of Toronto Mississauga, Mississauga, Ontario, Canada.
Elvin D de AraujoDepartment of Chemical and Physical Sciences, University of Toronto Mississauga, Mississauga, Ontario, Canada.ORCID 0000-0003-0716-2830
Derek J WilsonDepartment of Chemistry, York University, Toronto, Ontario, Canada.ORCID 0000-0002-7012-6085
Sarah RauscherDepartment of Physics, University of Toronto, Toronto, Ontario, Canada.ORCID 0000-0001-9860-3237

Funding

Digital Research Alliance of CanadaNatural Sciences and Engineering Research Council of Canada CRDPJ-507056Natural Sciences and Engineering Research Council of Canada RGPIN-201806408Natural Sciences and Engineering Research Council of Canada RGPIN-480432
6 · The paper itself

Abstract

The point mutation N642H of the signal transducer and activator of transcription 5B (STAT5B) protein is associated with aggressive and drug-resistant forms of leukemia. This mutation is thought to promote cancer due to hyperactivation of STAT5B caused by increased stability of the active, parallel dimer state. However, the molecular mechanism leading to this stabilization is not well understood as there is currently no structure of the parallel dimer. To investigate the mutation's mechanism of action, we conducted extensive all-atom molecular dynamics simulations of multiple oligomeric forms of both STAT5B and STAT5B

Indexed as

Molecular Dynamics Simulationsrc Homology DomainsSTAT5 Transcription FactorHumansHydrogen BondingPoint MutationProtein MultimerizationSTAT5B protein, humanSTAT5 Transcription Factorintrinsically disordered regionsmolecular dynamics simulationsoncogenic mutationprotein dynamicsSH2 domainssignal transducer and activator of transcriptionSTAT proteins

Identifiers

PMID39723827
PMCPMC11670306

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.