Author

A. Thureau

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· 4 Biochemistry· 2 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:protein folding & dynamics· 4 Assay:protein structure· 4 Research Focus:chromatin & epigenetic regulation· 2 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Approach:statistical model· 2 Organism:bacteria (other)· 1

Frequent Co-Authors

A. Fournet· 2 shared A. Sagar· 2 shared F. Allemand· 2 shared N. Sibille· 2 shared P. Bernado· 2 shared A. Barducci· 1 shared A. Cepauskas· 1 shared A. Estana· 1 shared

Activity by Year

2021-2024 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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2 shared papersBiophysics

A. Fournet

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

A versatile bacterial innate immunity protein directly senses two disparate phage proteins

T. Zhang, A. Cepauskas, A. Nadieina, A. Thureau, K. Coppieters 't Wallant, C. Martens, D. C. Lim, A. Garcia-Pino, M. T. Laub

This study shows that the bacterial immunity protein CapRelSJ46 can sense two distinct phage proteins using the same domain, highlighting its versatility in anti-phage defense.

bioRxiv · May 10, 2024 · PreprintMicrobiology

Phosphorylation motif dictates GPCR C-terminal domain conformation and arrestin interaction

M. Guillien, A. Mouhand, A. Sagar, A. Fournet, F. Allemand, G. A. N. Pereira, A. Thureau, P. Bernado, J.-L. Baneres, N. Sibille

The paper investigates how phosphorylation of GPCR C-terminal domains affects their conformation and arrestin interaction, revealing phosphorylation-dependent structural changes that influence signaling outcomes.

Structure · Nov 1, 2023Peer-reviewedBiophysics

Disordered regions and folded modules in CAF-1 promote histone deposition in S. pombe

F. Ouasti, M. Audin, K. Freon, J.-P. Quivy, M. Tachekort, E. Cesard, A. Thureau, V. Ropars, P. F. Varela, G. Moal, I. Soumana-Amadou, A. Uryga, P. Legrand, J. Andreani, R. Guerois, , F. Ochsenbein

This study identifies how disordered regions and folded modules in SpCAF-1 from S. pombe enable histone deposition by mediating interactions with histones and PCNA during DNA replication.

bioRxiv · Jun 2, 2023Biochemistry

Structural transitions in TCTP tumor protein upon Mcl-1 binding

F. Malard, C. Sizun, A. Thureau, L. Carlier, E. Lescop

This study investigates the structural changes in TCTP upon binding to Mcl-1, revealing conformational plasticity and the role of specific residues in complex stability.

bioRxiv · Nov 5, 2022 · PreprintBiochemistry

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

Oligomerization processes limit photoactivation and recovery of the Orange Carotenoid Protein.

E. A. Andreeva, S. Nizinski, A. Wilson, M. Levantino, E. De Zitter, R. Munro, F. Muzzopappa, A. Thureau, N. Zala, G. Burdzinski, M. Sliwa, D. Kirilovsky, G. Schiro, J.-P. Colletier

This study investigates the role of oligomerization in the photoactivation and recovery of the Orange Carotenoid Protein (OCP) using X-ray scattering and optical spectroscopy, revealing that oligomerization regulates its photocycle and slows thermal recovery.

bioRxiv · Feb 4, 2022Biophysics

A large disordered region confers a wide spanning volume to vertebrate Suppressor of Fused as shown in a trans-species solution study.

S. Makamte, A. Jabrani, A. Paquelin, A. Plessis, M. Sanial, A. Thureau, O. Roudenko, F. Oteri, M. Baaden, V. Biou

The paper compares the solution structures of SuFu from drosophila, zebrafish, and human, showing that vertebrate SuFu's IDR2 spans a large volume, enabling functional interactions and post-translational modifications.

bioRxiv · Jun 14, 2021Biophysics