Author

P.-E. Milhiet

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 3 Microbiology· 2

Signature Assays, Organisms & Methods

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Organism:human· 4 Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:host-pathogen & immune response· 2 Assay:imaging· 2 Approach:microscopy & imaging analysis· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2

Frequent Co-Authors

L. Costa· 4 shared P. Dosset· 2 shared A. Barducci· 1 shared A. Dolata· 1 shared A. Estana· 1 shared A. Fournet· 1 shared A. Le Gall· 1 shared A. Morato· 1 shared

Activity by Year

2018-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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4 shared papersBiophysics

L. Costa

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Author profile →

5 papers

Recent·Most cited

Phase separation and molecular ordering of the prion-like domain of the thermosensory protein EARLY FLOWERING 3

S. Hutin, J. R. Kumita, V. I. Strotmann, A. Dolata, W. L. Ling, N. Louafi, A. Popov, P.-E. Milhiet, M. Blackledge, M. H. Nanao, P. A. Wigge, Y. Stahl, L. Costa, M. D. Tully, C. Zubieta

The paper investigates the phase separation behavior of the prion-like domain of ELF3 in Arabidopsis, showing how polyQ length affects structural transitions and hydrogel formation.

bioRxiv · Mar 12, 2023Biophysics

The structure of pathogenic huntingtin exon-1 defines the bases of its aggregation propensity

C. A. Elena-Real, A. Sagar, A. Urbanek, M. Popovic, A. Morato, A. Estana, A. Fournet, X. L. Lund, Z.-D. Shi, L. Costa, A. Thureau, F. Allemand, R. E. Swenson, P.-E. Milhiet, A. Barducci, , P. Bernado

This study investigates how the structure of pathogenic huntingtin exon-1 with expanded poly-Q tracts influences its aggregation propensity and fibril formation.

bioRxiv · Oct 25, 2022Biophysics

Structure and mechanics of the human Nuclear Pore Complex basket

A. Vial, L. Costa, P. Dosset, P. Rosso, G. Boutieres, O. Faklaris, H. Haschke, P.-E. Milhiet, C. M. Doucet

The paper uses AFM and SMLM to show the human Nuclear Pore Complex basket is soft and conformationally flexible, enabling diverse cargo transport.

bioRxiv · Oct 20, 2022 · PreprintBiophysics

A tripartite complex HIV-1 Tat-cyclophilin A-capsid protein enables Tat encapsidation that is required for HIV-1 infectivity

M. Schatz, L. Marty, C. Ounadjela, P. B. V. Tong, I. Cardace, C. Mettling, P.-E. Milhiet, L. Costa, C. Godefroy, M. Pugniere, J.-F. Guichou, J.-M. Mesnard, M. Blaise, B. Beaumelle

This study identifies a Tat-CypA-CA tripartite complex that enables Tat encapsidation, which is essential for HIV-1 infectivity and viral production.

bioRxiv · Aug 7, 2022Microbiology

HIV-1 specifically traps CD9 and CD81 tetraspanins within viral buds and induces their membrane depletion

S. Dahmane, C. Doucet, A. Le Gall, C. Chamontin, P. Dosset, F. Murcy, L. Fernandez, D. Salas Pastene, E. Rubinstein, M. Mougel, M. Nollmann, P.-E. Milhiet

This study shows HIV-1 traps CD9 and CD81 tetraspanins in viral buds, depleting them from cellular membranes and inhibiting virus-induced fusion.

bioRxiv · May 17, 2018Microbiology