F
Françoise Guerlesquin
Researcher at Aix-Marseille University
Publications - 115
Citations - 2711
Françoise Guerlesquin is an academic researcher from Aix-Marseille University. The author has contributed to research in topics: Cytochrome & Desulfovibrio vulgaris. The author has an hindex of 31, co-authored 113 publications receiving 2542 citations. Previous affiliations of Françoise Guerlesquin include University of Provence & Centre national de la recherche scientifique.
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Protein protein interaction inhibition (2P2I) combining high throughput and virtual screening: Application to the HIV-1 Nef protein.
Stephane Betzi,Audrey Restouin,Audrey Restouin,Sandrine Opi,Sandrine Opi,Stefan T. Arold,Isabelle Parrot,Françoise Guerlesquin,Xavier Morelli,Yves Collette,Yves Collette +10 more
TL;DR: The results identify the first set of drug-like compounds that functionally target the HIV-1 Nef SH3 binding surface and provide the basis for a powerful discovery process that should help to speed up 2P2I strategies and open avenues for new class of antiviral molecules.
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TRF2 promotes, remodels and protects telomeric Holliday junctions.
Anaïs Poulet,Rémi Buisson,Cendrine Faivre-Moskalenko,Melanie Koelblen,Simon Amiard,Fabien Montel,Santiago Cuesta-Lopez,Olivier Bornet,Françoise Guerlesquin,Thomas Godet,Julien Moukhtar,Françoise Argoul,Anne-Cécile Déclais,David M.J. Lilley,Stephen C.Y. Ip,Stephen C. West,Eric Gilson,Marie-Josèphe Giraud-Panis +17 more
TL;DR: It is proposed that TRF2 contributes to t‐loop stabilisation by stimulating HJ formation and by preventing resolvase cleavage, and this findings provide novel insights into the interplay between telomere protection and homologous recombination.
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Crystal structure of cytochrome c3 from Desulfovibrio desulfuricans Norway at 1.7 A resolution.
TL;DR: The crystal structure of cytochrome c3 from Desulfovibrio desulfuricans (118 residues, four heme groups) has been crystallographically refined to 1.7 A resolution using a simulated annealing method, based on the structure-model at 2.5 A resolution.
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Model of a complex between the tetrahemic cytochrome c3 and the ferredoxin I from Desulfovibrio desulfuricans (Norway strain).
TL;DR: A three‐dimensional model of an electron‐transfer complex between the tetrahemic cytochrome c3 and the ferredoxin I from the sulfatereducing bacterium Desulfovibrio desulfuricans (Norway strain) has been generated through computer graphics methods.
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Solution structure of the E.coli TolA C-terminal domain reveals conformational changes upon binding to the phage g3p N-terminal domain.
Christophe Deprez,Roland Lloubès,Marthe Gavioli,Dominique Marion,Françoise Guerlesquin,Laurence Blanchard +5 more
TL;DR: Free TolAIII, which interacts also in vivo with Pal and TolB, is able to adapt its conformation upon binding to various partners, and shift of secondary structures does occur, which is mainly identical to that of g3pN1-bound TolA III.