Author

J. Boisbouvier

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 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 3 Assay:structural biology· 2 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Approach:deep learning· 1 Organism:human· 1 Assay:protein structure· 1

Frequent Co-Authors

A. Favier· 2 shared G. Schoehn· 2 shared P. Gans· 2 shared P. Macek· 2 shared A. C. Sivertsen· 1 shared A. Fournet· 1 shared A. Morato· 1 shared A. Urbanek· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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2 shared papersBiophysics

A. Favier

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Author profile →

4 papers

Recent·Most cited

Site-Specific Introduction of Alanines for the NMR Investigation of Low-Complexity Regions and Large Biomolecular Assemblies

C. A. Elena-Real, A. Urbanek, L. Imbert, A. Morato, A. Fournet, F. Allemand, N. Sibille, J. BOISBOUVIER, P. Bernado

This paper introduces a method to site-specifically incorporate isotopically labeled alanines into proteins for NMR studies, enabling structural analysis of large biomolecular assemblies and low-complexity regions.

bioRxiv · May 8, 2023 · PreprintBiochemistry

Visualizing the Transiently Populated Closed-State of Human HSP90 ATP Binding Domain

F. Henot, E. Rioual, A. Favier, P. Macek, E. Crublet, P. Josso, B. Brutscher, M. Frech, P. Gans, C. Loison, J. Boisbouvier

The paper identifies a metastable excited state in the HSP90 ATP binding domain using solution NMR and mutagenesis, showing it transiently samples a closed state distant from the ground state.

bioRxiv · Mar 16, 2022 · PreprintBiophysics

Structural Basis for the Inhibition of IAPP Fibril Formation by the Hsp60 Co-Chaperonin Prefoldin

R. Toerner, T. Kupreichyk, L. Gremer, E. Colas Debled, D. Fenel, P. Gans, D. Willbold, G. Schoehn, W. Hoyer, J. Boisbouvier

This study shows how prefoldin inhibits IAPP fibril formation by binding to the N-terminal segment of IAPP on fibril surfaces and ends, reducing aggregate size and number.

bioRxiv · Oct 20, 2021Biophysics

Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex

D. Gauto, L. Estrozi, C. Schwieters, G. Effantin, P. Macek, r. sounier, A. C. Sivertsen, E. Schmidt, R. Kerfah, G. Mas, J.-P. Colletier, P. Guntert, A. Favier, G. Schoehn, J. Boisbouvier, P. Schanda

The paper integrates NMR and cryo-EM to determine the atomic structure of a large enzyme complex, achieving high precision and accuracy beyond the limitations of each method individually.

bioRxiv · Dec 16, 2018Biophysics