Evidence map›Paper›PMID 41463297›Full record

ArticleBiomolecules2025

Definition and Discovery of Tandem SH3-Binding Motifs Interacting with Members of the p47

Zsofia E Kalman, Tamas Lazar, Laszlo Dobson, Rita Pancsa

Abstract read
In one paragraph

Article in Biomolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Zsofia E KalmanFaculty of Information Technology and Bionics, Pázmány Péter Catholic University, 1088 Budapest, Hungary.ORCID 0000-0003-4634-0433
Tamas LazarStructural Biology Brussels (SBB), Department of Bioengineering Sciences, Vrije Universiteit Brussel (VUB), 1050 Brussels, Belgium.ORCID 0000-0001-7496-6711
Laszlo DobsonDepartment of Bioinformatics, Semmelweis University, Tűzoltó u. 7, 1094 Budapest, Hungary.ORCID 0000-0003-2765-3872
Rita PancsaInstitute of Molecular Life Sciences, HUN-REN Research Centre for Natural Sciences, 1117 Budapest, Hungary.ORCID 0000-0003-0849-9312

Funding

FEBS ST Fellowship 2025Flanders Innovation & Entrepreneurship Agency HBC.2022.0194HUN-REN Research Centre for Natural Sciences HU-19426268János Bolyai Research Fellowship of the Hungarian Academy of Sciences BO/00174/22National Research, Development and Innovation Fund of the Ministry of Culture and Innovation FK-142285National Research, Development and Innovation Fund of the Ministry of Culture and Innovation PD-146564University Research Scholarship Programme 2024 EKÖP-24-4-II-PPKE-98
6 · The paper itself

Abstract

SH3 domains are widespread protein modules that mostly bind to proline-rich short linear motifs (SLiMs). Most known SH3 domain-motif interactions and canonical or non-canonical recognition specificities are described for individual SH3 domains. Although cooperation and coordinated motif binding between tandem SH3 domains has already been described for members of the p47

Indexed as

NADPH Oxidasessrc Homology DomainsAmino Acid MotifsAmino Acid SequenceBinding SitesHumansProtein BindingNADPH OxidasesAlphaFold interaction predictiondomain-motif interactionseukaryotic linear motifsevolutionary conservationintrinsically disordered proteinsprotein–protein interactionshort linear motifs

Identifiers

PMID41463297
PMCPMC12730246

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Registered trials

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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.