Skip to main content
Yaoxing Huang on Muck Rack

Yaoxing Huang

As seen in: Nature, Journal of Translational Medicine, BioRxiv, Cell Press, Cell Stem Cell, Pharma Focus Asia
Is this you? As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work. Claim your profile

Get in touch with Yaoxing

Contact Yaoxing, search articles and posts on X, monitor coverage, and track replies from one place.

Learn more about Muck Rack

Actions

Share this page

Is this you?

As a journalist, you can create a free Muck Rack account to customize your profile, list your contact preferences, and upload a portfolio of your best work.
Claim your profile

Articles

Bispecific 10E8.4/iMab broadly neutralizing antibody in people with or without HIV-1: a partially randomized phase 1 trial

|
By Deborah Theodore, Bryan Mayer, Charlotte-Paige Rolle, Edwin DeJesus, Margaret E Ackerman, Michael S. Seaman, Joshua Weiner, Hiroshi Mohri, Yaoxing Huang, Brett Gray, Jennifer Chang Verified, Monica Gerber, Jian Yu, Yang Luo, Neal N. Padte, Michael T. Yin, Burc Barin, Steven Palmer, Jorge Benitez, Chanc Orzell, David Ho, Ollivier Hyrien, Magdalena E. Sobieszczyk, Rusty Greene, Ariana Pazmino, Carlie Dorr, Meredith McNairy, James DiRenzo
| Nature Verified
Abstract Broadly neutralizing antibodies (bnAbs) are a promising tool for HIV prevention and treatment. Here we conducted a first-in-human, phase 1 trial of the bispecific 10E8.4/iMab antibody, which consists of a 10E8.4 arm binding the HIV-1 envelope glycoprotein membrane-proximal external region and an ibalizumab (iMab) arm binding the human CD4 molecule. 10E8.4/iMab was administered intravenously (IV) or subcutaneously (SC).
Open in Who Shared Issue with article?

Prefusion structure, evasion and neutralization of HSV-1 glycoprotein B - Nature Microbiology

|
By Andrea Biju, Yicheng Guo, Hsiang Hong, Li Ou, Yosef Sabo, Anum A. Glasgow, David Ho, Yaoxing Huang, Reda Rawi, Tongqing Zhou, Lawrence Shapiro, Mehin Suleiman
| Nature Verified
Abstract Glycoprotein B (gB) refolds between prefusion and postfusion conformations to facilitate herpesvirus entry into host cells. However, the isolation of prefusion-specific neutralizing antibodies, effective against other viral entry machines, has been challenging.
Open in Who Shared Issue with article?

Optimizing a human monoclonal antibody for better neutralization of SARS-CoV-2 - Nature Communications

|
By Yicheng Guo, Manoj Nair, Chih-Chen Tzang, Yaoxing Huang, Hsiang Hong
| Nature Verified
Abstract SARS-CoV-2 has largely evolved to resist antibody pressure, with each successive viral variant becoming more and more resistant to serum antibodies in the population. This evolution renders all previously authorized anti-spike therapeutic monoclonal antibodies inactive, and it threatens the remaining pipelines against COVID-19.
Open in Who Shared Issue with article?
See all 14 articles