Author

A. Gobet

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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Biochemistry· 2 Biophysics· 2

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 4 Approach:experimental assay· 2 Organism:bacteria (other)· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:deep learning· 1 Research Focus:host-pathogen & immune response· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

v. Chaptal· 4 shared C. Orelle· 2 shared J. Martin· 2 shared J.-M. Jault· 2 shared L. Moissonnier· 2 shared P. Falson· 2 shared S. Magnard· 2 shared V. Zampieri· 2 shared

Activity by Year

2020-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 40 mutual co-author links

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4 shared papersBiochemistry

v. Chaptal

Mutual co-authors in cluster

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4 papers

Recent·Most cited

R6G narrows BmrA conformational spectrum for a more efficient use of ATP

A. Gobet, L. Moissonnier, E. Zarkadas, S. Magnard, E. Bettler, J. Martin, R. Terreux, G. Schoehn, C. Orelle, J.-M. Jault, P. Falson, v. Chaptal

This study shows that Rhodamine6G binding to BmrA narrows its conformational spectrum, enhancing ATP-dependent transport efficiency.

bioRxiv · Mar 15, 2024 · PreprintBiochemistry

Conformational space exploration of cryo-EM structures by variability refinement

P. Afonine, A. Gobet, L. Moissonnier, B. Poon, v. Chaptal

This paper introduces a tool to refine ensembles of structures into maps from cryo-EM variability analysis, enabling identification of variable and static structural elements.

bioRxiv · Dec 23, 2022Biophysics

Drug-bound and -free outward-facing structures of a multidrug ABC exporter point to a swing mechanism

v. Chaptal, V. Zampieri, B. Wiseman, C. Orelle, J. Martin, K.-A. Nguyen, S. Magnard, A. Gobet, M. Di cesare, W. Javed, A. Kilburg, M. Peuchmaur, J. Marcoux, M. Hogbom, J.-M. Jault, , P. G. Falson

The paper resolves two ATP-Mg2+-bound outward-facing conformations of BmrA, revealing a swing mechanism for drug transport through structural and dynamic analyses.

bioRxiv · Mar 12, 2021 · PreprintBiochemistry

Nanodisc, amphipol or detergent belts in cryoEM reconstructions of membrane proteins are similar and correspond to a common ordered solvent layer

V. Zampieri, A. Gobet, X. Robert, P. Falson, v. Chaptal

The paper compares belt structures in cryo-EM reconstructions of membrane proteins solved in nanodiscs, amphipols, or detergents, finding they are similar and represent a common ordered solvent layer.

bioRxiv · Dec 10, 2020Biophysics