Evidence map›Paper›PMID 42336880›Full record

ArticleScientific reports2026

The ITM2B-associated retinal dystrophy mutation modifies BRI23 peptide interactions in the human retina.

Tasnim Ben Yacoub, Andréa Amprou, Camille Letellier, Christelle Michiels, Julien Navarro, Said El Shamieh, Tual Monfort, Salvatore Azzollini, Juliette Wohlschlegel, Guillaume Chevreux and 7 more

Abstract read
In one paragraph

Article in Scientific reports, 2026. 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

17 authors.

Tasnim Ben YacoubSorbonne Université, INSERM, CNRS, Institut de la Vision, Paris, France. tasnim.inserm@gmail.com.
Andréa AmprouSorbonne Université, INSERM, CNRS, Institut de la Vision, Paris, France.
Camille LetellierSorbonne Université, INSERM, CNRS, Institut de la Vision, Paris, France.
Christelle MichielsSorbonne Université, INSERM, CNRS, Institut de la Vision, Paris, France.
Julien NavarroSorbonne Université, INSERM, CNRS, Institut de la Vision, Paris, France.
Said El ShamiehSorbonne Université, INSERM, CNRS, Institut de la Vision, Paris, France.
Tual MonfortSorbonne Université, INSERM, CNRS, Institut de la Vision, Paris, France.
Salvatore AzzolliniSorbonne Université, INSERM, CNRS, Institut de la Vision, Paris, France.
Juliette WohlschlegelSorbonne Université, INSERM, CNRS, Institut de la Vision, Paris, France.
Guillaume ChevreuxProteoSeine@IJM, Université de Paris, CNRS, Institut Jacques Monod, Paris, 75006, France.
Véronique LegrosProteoSeine@IJM, Université de Paris, CNRS, Institut Jacques Monod, Paris, 75006, France.
Morgane LemaoMitoLab Team, Université Angers, UMR CNRS 6015 - INSERM U1083, Institut MitoVasc, SFR ICAT, Angers, France.
Guy LenaersMitoLab Team, Université Angers, UMR CNRS 6015 - INSERM U1083, Institut MitoVasc, SFR ICAT, Angers, France.
Kate GrieveSorbonne Université, INSERM, CNRS, Institut de la Vision, Paris, France.
Manuela ArgentiniSorbonne Université, INSERM, CNRS, Institut de la Vision, Paris, France.
Christina ZeitzSorbonne Université, INSERM, CNRS, Institut de la Vision, Paris, France.
Isabelle AudoSorbonne Université, INSERM, CNRS, Institut de la Vision, Paris, France. isabelle.audo@inserm.fr.

Funding

Foundation Fighting Blindness C-CMM-0907-0428-INSERM04IHU FOReSIGHT ANR-18-IAHU-0001LABEX LIFESENSES ANR-10-LABX-65
6 · The paper itself

Abstract

BRI23, composed of the 23 last amino acids of the integral transmembrane protein 2B (ITM2B) C-terminus, is associated with several neurodegenerative diseases, including retinal dystrophy (RD) and familial dementia. Its role in the retina remains poorly understood. This study provides a comprehensive analysis of BRI23 interactome in the human retina. Using a peptide-bead coupling system, we identified 2302 proteins, primarily involved in mitochondrial processes, synaptic transmission and photoreceptor function. Our findings show that the BRI23-RD variant, associated with the ITM2B-related RD (IRRD), exhibits significantly altered protein interactions compared to the wild-type form. Notably, we observed an increased abundance of mitochondrial proteins and synaptic molecules, indicating a potential disruption of cellular pathways driven by the IRRD variant.

Indexed as

Membrane ProteinsMutationRetinaRetinal DystrophiesAdaptor Proteins, Signal TransducingHumansProtein BindingAdaptor Proteins, Signal TransducingITM2B protein, humanMembrane Proteins

Identifiers

PMID42336880
PMCPMC13575134

What Socratic 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 Socratic graph.