Author

W. Hubbell

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· 1 Immunology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 2 Research Focus:protein structure prediction· 2 Assay:structural biology· 2 Organism:human· 1 Organism:non-human primate· 1

Frequent Co-Authors

K.-M. A. Dam· 2 shared M. Bridges· 2 shared A. Escolano· 1 shared A. F. Kintzer· 1 shared A. Herschhorn· 1 shared A. Kossiakoff· 1 shared A. T. DeLaitsch· 1 shared D. Deneka· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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2 shared papersMicrobiology

K.-M. A. Dam

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Conformational flexibility of HIV-1 envelope glycoproteins modulates transmitted / founder sensitivity to broadly neutralizing antibodies

D. Parthasarathy, K. R. Pothula, K.-M. A. Dam, S. Ratnapriya, H. C. Benet, R. Parsons, X. Huang, S. Sammour, K. Janowska, M. Harris, S. Sacco, J. Sodroski, M. Bridges, W. Hubbell, P. Acharya, A. Herschhorn

This paper shows that some HIV-1 transmitted/founder Envs are incompletely closed, making them sensitive to antibodies targeting open conformations, and highlights the importance of Env conformational flexibility for bnAb neutralization.

bioRxiv · Sep 13, 2023Microbiology

Neutralizing antibodies induced in immunized macaques recognize the CD4-binding site on an occluded-open HIV-1 envelope trimer

Z. Yang, K.-M. A. Dam, M. D. Bridges, M. A. G. Hoffmann, A. T. DeLaitsch, H. B. Gristick, A. Escolano, R. Gautam, M. A. Martin, M. Nussenzweig, W. Hubbell, P. J. Bjorkman

This study identifies two antibodies from immunized macaques that neutralize HIV-1 by targeting the CD4-binding site on an occluded-open Env trimer conformation.

bioRxiv · Nov 2, 2021Immunology

The structural basis for activation of voltage sensor domains in an ion channel TPC1

A. F. Kintzer, E. Green, P. Dominik, M. Bridges, J.-p. Armache, D. Deneka, S. Kim, W. Hubbell, A. Kossiakoff, Y. Cheng, R. Stroud

The paper presents four structures of the TPC1 ion channel's voltage sensor domain, revealing how activation occurs through conformational changes and Ca2+ binding.

bioRxiv · Jul 29, 2018Biophysics