Evidence map›Paper›PMID 42206738›Full record

ArticleFEBS letters2026

Modulation of Homer1 EVH1 domain internal dynamics by putative autism-associated mutations.

Fanni Farkas, Brigitta Maruzs, Zsófia E Kálmán, Tomas Klumpler, Gyula Batta, Bálint Péterfia, Zoltán Gáspári

Abstract read
In one paragraph

Article in FEBS letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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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

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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

7 authors.

Fanni FarkasFaculty of Information Technology and Bionics, Pázmány Péter Catholic University, Budapest, Hungary.
Brigitta MaruzsFaculty of Information Technology and Bionics, Pázmány Péter Catholic University, Budapest, Hungary.
Zsófia E KálmánFaculty of Information Technology and Bionics, Pázmány Péter Catholic University, Budapest, Hungary.ORCID https://orcid.org/0000-0003-4634-0433
Tomas KlumplerCEITEC, Masaryk University, Brno, Czech Republic.
Gyula BattaDepartment of Organic Chemistry, University of Debrecen, Debrecen, Hungary.
Bálint PéterfiaFaculty of Information Technology and Bionics, Pázmány Péter Catholic University, Budapest, Hungary.ORCID https://orcid.org/0000-0001-9090-9979
Zoltán GáspáriFaculty of Information Technology and Bionics, Pázmány Péter Catholic University, Budapest, Hungary.ORCID https://orcid.org/0000-0002-8692-740X

Funding

Debreceni Egyetem Scientific Research Bridging Fund (DETKA)European Regional Development Fund GINOP-2.3.2-15-2016-00008European Regional Development Fund GINOP-2.3.3-15-2016-00004Hungarian National Research, Development and Innovation Office (NKFIH) 2021-4.1.2-NEMZ_KI-2022-00027Hungarian National Research, Development and Innovation Office (NKFIH) OTKA K 137947Hungarian National Research, Development and Innovation Office (NKFIH) TKP2021-EGA-42
6 · The paper itself

Abstract

The EVH1 domain of the Homer1 scaffold protein interacts with the proline-rich region of Shank3, forming a key network within the postsynaptic density. While two mutations (M65I and S97L) in the EVH1 domain have been suggested to be associated with autism spectrum disorder, our results show that neither mutation has a substantial effect on the overall structure or the partner binding properties of Homer1. Compared to the S97L variant, the M65I mutant exhibits larger chemical shift perturbations both upon the mutation itself and during partner binding, while also showing signs of thermal destabilization. Finally, integration of computational and NMR data suggests that both mutations perturb the μs-ms timescale internal motions of the EVH1 domain.

Indexed as

Autistic DisorderCarrier ProteinsHomer Scaffolding ProteinsMutationHumansModels, MolecularNerve Tissue ProteinsProtein BindingProtein DomainsCarrier ProteinsHOMER1 protein, humanHomer Scaffolding ProteinsNerve Tissue Proteinschemical shift perturbationhinge residuesHOMER1postsynaptic density

Identifiers

PMID42206738
PMCPMC13502648

What OpenQuestion holds

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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.