Author

I. Li de la Sierra-Gallay

Centre National de la Recherche ScientifiqueORCID 0000-0003-2770-7439Unclaimed ORCID profile · follow to get notified of new preprints

Additional preprints under this name without ORCID

I. Li de la Sierra-Gallay2 papers

Biology Disciplines

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Biochemistry· 1 Microbiology· 1 Molecular Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:bacteria (other)· 1 Organism:C. elegans· 1 Organism:plant (other)· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1 Assay:structural biology· 1

Frequent Co-Authors

Noureddine LazariD· 2 shared Christiane DietrichiD· 1 shared Claire CargemeliD· 1 shared Dominique Guianvarc’hiD· 1 shared Dominique UrbaniD· 1 shared Émilie LesuriD· 1 shared Florence Constantinesco· 1 shared Gilles DoisneauiD· 1 shared

Activity by Year

2023-2025 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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2 shared papersMicrobiology

Noureddine LazarORCID

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3 papers

Recent·Most cited

MicrobiologyJournal of Biological ChemistryPeer-reviewedJan 27, 2025

Synthetic mycolates derivatives as molecular tools to decipher protein mycoloylation, a unique post-translational modification in bacteria.

Émilie Lesur, Yijie Zhang, Nathalie Dautin…·Nicolas Bayan

The paper identifies MytC as the mycoloyltransferase responsible for protein mycoloylation in Corynebacterium glutamicum and demonstrates its specificity for mycolate donors.

7 citations

C. elegansexperimental assay

𝕏 PostBluesky

BiochemistryActa Crystallographica Section D Structural BiologyPeer-reviewedDec 28, 2024

Structural characterization of the ACDC domain from ApiAP2 proteins of the malaria parasite

Marine Le Berre, Thibault Tubiana, Philippa Reuterswärd…·Sylvie Nessler

The paper determines the crystal structure of the ACDC domain from ApiAP2 proteins in malaria parasites and identifies a potential inhibitor targeting this domain.

4 citations

plant (other)structural biology

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Molecular BiologyActa Crystallographica Section D Structural BiologyPeer-reviewedJan 19, 2023

The LH-DH module of the bacterial replicative helicases is the common binding site for DciA and other helicase loaders

Claire Cargemel, Stéphanie Marsin, Magali Noiray…·Sophie Quevillon‐Chéruel

The paper identifies a conserved binding site on bacterial replicative helicases that is targeted by both DciA and DnaC loaders, showing functional interchangeability between these loaders.

11 citations

bacteria (other)protein structure

𝕏 PostBluesky