Author

Kevin W. Huynh

Pfizer (United States)ORCID 0000-0001-8116-563XUnclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biophysics· 1 Immunology· 1 Molecular Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:drug response / drug discovery· 1 Approach:mechanistic / dynamical model· 1 Organism:mouse· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

Huixian WuiD· 2 shared Kimberly F. FennelliD· 2 shared Alberto J. Gonzalez-HernandeziD· 1 shared Alexa StraussiD· 1 shared Alexander MuikiD· 1 shared Andrew P. McKeen· 1 shared Anisul ArefiniD· 1 shared Annaliesa S. AndersoniD· 1 shared

Activity by Year

2023-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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2 shared papersMolecular Biology

Huixian WuORCID

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3 papers

Recent·Most cited

Molecular BiologybioRxivPreprintFeb 12, 2026

Insight into the scaffolding function of USP18 from a high resolution cryo-EM structure of STAT2-USP18-ISG15 ternary complex

Kevin W. Huynh, Rachel Plumb, David R. Healy…·Masaya Yamaguchi

The paper determines the structure of the STAT2-USP18-ISG15 ternary complex using cryo-EM, revealing how USP18's scaffolding function suppresses IFN-I signaling by disrupting its enzymatic activity.

1 citation

protein structureexperimental assay

𝕏 PostBluesky

BiophysicsbioRxivPreprintFeb 3, 2025

Structural Diversity and Dynamics of Metabotropic Glutamate Receptor/Beta-Arrestin Coupling

Dagan C. Marx, Kevin W. Huynh, Alberto J. Gonzalez-Hernandez…·Joshua Levitz

This study investigates the structural and dynamic diversity of metabotropic glutamate receptor/beta-arrestin coupling using biophysical and structural methods, revealing new coupling stoichiometries and interaction mechanisms.

3 citations

structural biologybiophysical modeling

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ImmunologybioRxivNov 17, 2023

Preclinical Characterization of the Omicron XBB.1.5-Adapted BNT162b2 COVID-19 Vaccine

Kayvon Modjarrad, Ye Che, Wei Chen…·Kena A. Swanson

The monovalent Omicron XBB.1.5-adapted BNT162b2 mRNA vaccine elicits stronger neutralizing antibody responses against XBB.1.5 and related sublineages than the bivalent Wild Type + Omicron BA.4/5 vaccine.

DOI 10.1038/s41541-024-01013-9

mouseexperimental assay

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