Author

B. Wiseman

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· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:bacteria (other)· 2 Assay:structural biology· 2 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

M. Hogbom· 2 shared A. Boumendjel· 1 shared A. E. Carlson· 1 shared A. Gobet· 1 shared A. Kilburg· 1 shared A. Stsiapanava· 1 shared C. Emori· 1 shared C. Orelle· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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2 shared papersBiochemistry

M. Hogbom

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Architecture of the Vertebrate Egg Coat and Structural Basis of the ZP2 Block to Polyspermy

S. Nishio, C. Emori, B. Wiseman, D. Fahrenkamp, E. Dioguardi, S. Zamora-Caballero, M. Bokhove, L. Han, A. Stsiapanava, Y. Lu, M. Kodani, R. E. Bainbridge, K. M. Komondor, A. E. Carlson, M. Landreh, , L. Jovine

This study investigates how cleavage of ZP2 in the egg zona pellucida leads to oligomerization and structural changes that block polyspermy.

bioRxiv · Jun 21, 2023Biophysics

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

Conformational changes in Apolipoprotein N-acyltransferase (Lnt)

B. Wiseman, M. Hogbom

This paper reports two crystal structures of Apolipoprotein N-acyltransferase (Lnt) that reveal conformational changes associated with substrate binding and potential apolipoprotein docking.

bioRxiv · Dec 16, 2018Biochemistry