Author

H. Sosa

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 Cell Biology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:cryo-EM· 3 Research Focus:protein structure prediction· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Organism:Drosophila· 1 Research Focus:protein folding & dynamics· 1 Assay:structural biology· 1

Frequent Co-Authors

A. B. Asenjo· 3 shared M. P. M. H. Benoit· 3 shared A. A. Mohammed Khalid· 1 shared A. Asenjo· 1 shared A. El Marjou· 1 shared A. Houdusse· 1 shared B. H. Kwok· 1 shared B. Hunter· 1 shared

Activity by Year

2017-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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3 shared papersCell Biology

A. B. Asenjo

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Author profile →

4 papers

Recent·Most cited

Nucleotide-free structures of Kif20A illuminate the atypical allostery in this mitotic kinesin-6

F. M. Ranaivoson, V. Crozet, M. Benoit, A. A. Mohammed Khalid, C. Kikuti, H. Sirkia, A. El Marjou, A. Asenjo, H. Sosa, C. Schmidt, S. Rosenfeld, A. Houdusse

This paper presents the first high-resolution structure of Kif20A's motor domain, revealing structural features and allostery mechanisms that explain its atypical motility and ATPase activity.

bioRxiv · Nov 10, 2022 · PreprintBiochemistry

Kinesin-8-specific loop-2 controls the dual activities of the motor domain according to tubulin protofilament shape

B. Hunter, M. P. M. H. Benoit, A. B. Asenjo, C. Doubleday, D. Trofimova, H. Sosa, J. S. Allingham

This study defines the mechanism of kinesin-8 dual activity by showing how loop-2 regulates motor domain conformation based on tubulin protofilament shape.

bioRxiv · Feb 28, 2022Biochemistry

Structural basis of mechano-chemical coupling by the mitotic kinesin KIF14

M. P. M. H. Benoit, A. B. Asenjo, M. Paydar, S. Dhakal, B. H. Kwok, H. Sosa

This study determines cryo-EM structures of KIF14 bound to microtubules with nucleotide analogues, revealing conformational changes linked to ATP hydrolysis and motor function.

bioRxiv · Jun 1, 2020Cell Biology

Cryo-EM Reveals the Structural Basis of Microtubule Depolymerization by Kinesin-13s

M. P. M. H. Benoit, A. B. Asenjo, H. Sosa

The paper uses cryo-EM to determine the structure of Drosophila kinesin-13 KLP10A bound to tubulin, revealing how it induces microtubule depolymerization through conformational changes.

bioRxiv · Oct 19, 2017Cell Biology