Author

L. Eshun-Wilson

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· 2 Immunology· 2

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 4 Approach:experimental assay· 3 Organism:human· 2 Research Focus:protein structure prediction· 2 Research Focus:cell signaling & trafficking· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

A. B. Ward· 2 shared E. Nogales· 2 shared A. Chumbe· 1 shared A. Jack· 1 shared A. Torrents de la Pena· 1 shared A. Yildiz· 1 shared D. Portran· 1 shared D. Toso· 1 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersImmunology

A. B. Ward

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Author profile →

4 papers

Recent·Most cited

Structural basis of epitope selectivity and potent protection from malaria by PfCSP antibody L9

G. Martin, M. L. Fernandez Quintero, W.-H. Lee, T. Pholcharee, L. Eshun-Wilson, K. R. Liedl, M. Pancera, R. A. Seder, I. A. Wilson, A. B. Ward

The paper determines the cryo-EM structure of the anti-PfCSP antibody L9, revealing its multivalent binding to NPNV repeats and the role of the light chain in affinity and protective efficacy.

bioRxiv · Oct 7, 2022 · PreprintImmunology

Structure of the hepatitis C virus E1E2 glycoprotein complex

A. Torrents de la Pena, K. Sliepen, L. Eshun-Wilson, M. Newby, J. D. Allen, S. Koekkoek, I. Zon, A. Chumbe, M. Crispin, J. Schinkel, G. C. Lander, R. W. Sanders, A. B. Ward

The paper presents the cryo-EM structure of the HCV E1E2 glycoprotein complex with antibodies, revealing the E1-E2 interface and its stabilization mechanisms.

bioRxiv · Dec 16, 2021 · PreprintImmunology

The mechanism of motor inhibition by microtubule-associated proteins

L. S. Ferro, L. Eshun-Wilson, M. Golcuk, J. Fernandes, T. Huijben, E. Gerber, A. Jack, K. Costa, M. Gur, Q. Feng, E. Nogales, A. Yildiz

This study investigates how microtubule-associated proteins (MAPs) regulate motor protein interactions, finding that MAPs inhibit motors without blocking their binding sites and that motors must interact with MAPs to move on MAP-coated microtubules.

bioRxiv · Oct 22, 2020 · PreprintBiophysics

Effects of α-tubulin acetylation on microtubule structure and stability

L. Eshun-Wilson, R. Zhang, D. Portran, M. Nachury, D. Toso, T. Lohr, M. Vendruscolo, M. Bonomi, J. Fraser, E. Nogales

This study uses cryo-EM and molecular dynamics to show that α-tubulin acetylation at K40 reduces loop disorder and may affect microtubule stability.

bioRxiv · Jan 9, 2019Biophysics