Author

A. B. Asenjo

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 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Assay:cryo-EM· 4 Research Focus:cell signaling & trafficking· 2 Research Focus:protein structure prediction· 2 Research Focus:chromatin & epigenetic regulation· 1 Organism:Drosophila· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

M. P. M. H. Benoit· 4 shared H. Sosa· 3 shared H. J. Sosa· 2 shared A. Gennerich· 1 shared B. H. Kwok· 1 shared B. Hunter· 1 shared C. Doubleday· 1 shared D. F. J. Arginteanu· 1 shared

Activity by Year

2017-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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4 shared papersBiochemistry

M. P. M. H. Benoit

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5 papers

Recent·Most cited

Cryo-EM Unveils the Processivity Mechanism of Kinesin KIF1A and the Impact of its Pathogenic Variant P305L

M. P. M. H. Benoit, L. Rao, A. B. Asenjo, A. Gennerich, H. J. Sosa

The paper presents high-resolution cryo-EM structures of KIF1A-microtubule complexes, revealing the mechanism of processivity and the impact of the P305L mutation on microtubule binding.

bioRxiv · Feb 2, 2023 · 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

Kinesin-5 promotes microtubule nucleation and assembly by stabilizing a lattice-competent conformation of tubulin

G.-Y. Chen, A. B. Asenjo, Y. Chen, J. Mascaro, D. F. J. Arginteanu, H. J. Sosa, W. O. Hancock

This study identifies Eg5 as a microtubule polymerase that promotes microtubule growth by inducing a curved-to-straight transition in tubulin.

bioRxiv · Jan 14, 2019Biophysics

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