Author

Ahmad Elbahnsi

Centre National de la Recherche ScientifiqueORCID 0000-0002-5356-2440Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Molecular Biology· 2 Bioinformatics· 1

Signature Assays, Organisms & Methods

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Organism:human· 3 Approach:statistical model· 3 Assay:protein structure· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

Isabelle CallebautiD· 3 shared Jean‐Paul Mornon· 2 shared Aleksander EdelmaniD· 1 shared Alexandre HinzpeteriD· 1 shared B. ChevalieriD· 1 shared Chandran KaiD· 1 shared Gérald Le GaciD· 1 shared Isabelle Sermet‐GaudelusiD· 1 shared

Activity by Year

2021-2025 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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3 shared papersMolecular Biology

Isabelle CallebautORCID

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3 papers

Recent·Most cited

BioinformaticsbioRxivPreprintNov 23, 2025

Mechanistic insights into CFTR function from molecular dynamics analysis of electrostatic interactions

Ahmad Elbahnsi, Jean‐Paul Mornon, Isabelle Callebaut

This study uses molecular dynamics simulations to analyze electrostatic interactions in CFTR, revealing their role in stabilizing structure and enabling ion conduction.

DOI 10.1101/2025.11.23.690003

humanstatistical model

Molecular BiologyThe FASEB JournalPeer-reviewedJul 3, 2024

Insights into the role of glycerophospholipids on the iron export function of SLC40A1 and the molecular mechanisms of ferroportin disease.

Rim Debbiche, Ahmad Elbahnsi, Kévin Uguen…·Gérald Le Gac

The paper investigates how glycerophospholipids influence SLC40A1 conformational changes and identifies key residues linked to ferroportin disease.

6 citations

humanstatistical model

Molecular BiologybioRxivPreprintMay 4, 2021

CFTR corrector efficacy is associated with occupancy of distinct binding sites

Nesrine Baatallah, Ahmad Elbahnsi, Jean‐Paul Mornon…·Alexandre Hinzpeter

The paper identifies two distinct VX-809 binding sites on CFTR that are critical for corrector efficacy, showing different sensitivity to mutations and allostery.

1 citation

humanprotein structure