Richard T. Wyatt

发表

Proof of principle for epitope-focused vaccine design

David Baker, Eric Stevens, Man Chen, 2014, Nature.

Structure of HIV-1 gp120 with gp41-Interactive Region: Layered Architecture and Basis of Conformational Mobility

Young Do Kwon, Tongqing Zhou, Lei Chen, 2009 .

Mechanism of Human Immunodeficiency Virus Type 1 Resistance to Monoclonal Antibody b12 That Effectively Targets the Site of CD4 Attachment

Tongqing Zhou, Peter D. Kwong, Richard T. Wyatt, 2009, Journal of Virology.

Mechanism of Neutralization by the Broadly Neutralizing HIV-1 Monoclonal Antibody VRC01

Barney S. Graham, Richard T. Wyatt, John R. Mascola, 2011, Journal of Virology.

Breadth of Human Immunodeficiency Virus-Specific Neutralizing Activity in Sera: Clustering Analysis and Association with Clinical Variables

Richard T. Wyatt, Bette T. Korber, John R. Mascola, 2009, Journal of Virology.

Vaccine-elicited primate antibodies use a distinct approach to the HIV-1 primary receptor binding site informing vaccine redesign

Richard Wilson, Richard T. Wyatt, Robyn L. Stanfield, 2014, Proceedings of the National Academy of Sciences.

Structure-Based Stabilization of HIV-1 gp120 Enhances Humoral Immune Responses to the Induced Co-Receptor Binding Site

Tongqing Zhou, Gary J. Nabel, Peter D. Kwong, 2009, PLoS pathogens.

Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-120 interface

Gwo-Yu Chuang, Peter D. Kwong, Richard T. Wyatt, 2014, Nature.

Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1

Mario Roederer, Tongqing Zhou, Gary J. Nabel, 2010, Science.

Access of Antibody Molecules to the Conserved Coreceptor Binding Site on Glycoprotein gp120 Is Sterically Restricted on Primary Human Immunodeficiency Virus Type 1

Christoph Grundner, Christos J. Petropoulos, Terri Wrin, 2003, Journal of Virology.

Broad diversity of neutralizing antibodies isolated from memory B cells in HIV-infected individuals

Richard T. Wyatt, Michael S. Seaman, John R. Mascola, 2009, Nature.

PGV04, an HIV-1 gp120 CD4 Binding Site Antibody, Is Broad and Potent in Neutralization but Does Not Induce Conformational Changes Characteristic of CD4

Tongqing Zhou, Terri Wrin, Peter D. Kwong, 2012, Journal of Virology.

Particulate Array of Well‐Ordered HIV Clade C Env Trimers Elicits Neutralizing Antibodies that Display a Unique V2 Cap Approach

Richard T. Wyatt, John R. Mascola, J. Mascola, 2017, Immunity.

Selection Pressure on HIV-1 Envelope by Broadly Neutralizing Antibodies to the Conserved CD4-Binding Site

Richard T. Wyatt, John R. Mascola, Mark Connors, 2012, Journal of Virology.