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Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
- P. Kwong, R. Wyatt, J. Robinson, R. Sweet, J. Sodroski, W. Hendrickson
- Biology, Medicine
- Nature
- 18 June 1998
The entry of human immunodeficiency virus (HIV) into cells requires the sequential interaction of the viral exterior envelope glycoprotein, gp120, with the CD4 glycoprotein and a chemokine receptor… Expand
Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1
- X. Wu, Zhi-yong Yang, +21 authors J. Mascola
- Biology, Medicine
- Science
- 13 August 2010
Designer Anti-HIV Developing a protective HIV vaccine remains a top global health priority. One strategy to identify potential vaccine candidates is to isolate broadly neutralizing antibodies from… Expand
Antibody neutralization and escape by HIV-1
Neutralizing antibodies (Nab) are a principal component of an effective human immune response to many pathogens, yet their role in HIV-1 infection is unclear. To gain a better understanding of this… Expand
Structure of a V3-Containing HIV-1 gp120 Core
- Chih-chin Huang, M. Tang, +9 authors P. Kwong
- Biology, Medicine
- Science
- 11 November 2005
The third variable region (V3) of the HIV-1 gp120 envelope glycoprotein is immunodominant and contains features essential for coreceptor binding. We determined the structure of V3 in the context of… Expand
Structural basis of cell-cell adhesion by cadherins
- L. Shapiro, A. Fannon, +7 authors W. Hendrickson
- Chemistry, Medicine
- Nature
- 23 March 1995
Crystal structures of the amino-terminal domain of N-cadherin provide a picture at the atomic level of a specific adhesive contact between cells. A repeated set of dimer interfaces is common to the… Expand
Broad and potent neutralization of HIV-1 by a gp41-specific human antibody
- J. Huang, G. Ofek, +17 authors M. Connors
- Biology, Medicine
- Nature
- 18 September 2012
Characterization of human monoclonal antibodies is providing considerable insight into mechanisms of broad HIV-1 neutralization. Here we report an HIV-1 gp41 membrane-proximal external region… Expand
Structural Basis for Broad and Potent Neutralization of HIV-1 by Antibody VRC01
- T. Zhou, I. Georgiev, +15 authors P. Kwong
- Biology, Medicine
- Science
- 13 August 2010
Designer Anti-HIV Developing a protective HIV vaccine remains a top global health priority. One strategy to identify potential vaccine candidates is to isolate broadly neutralizing antibodies from… Expand
Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
- J. Mclellan, M. Pancera, +44 authors P. Kwong
- Biology, Medicine
- Nature
- 23 November 2011
Variable regions 1 and 2 (V1/V2) of human immunodeficiency virus-1 (HIV-1) gp120 envelope glycoprotein are critical for viral evasion of antibody neutralization, and are themselves protected by… Expand
Structure and Mechanistic Analysis of the Anti-Human Immunodeficiency Virus Type 1 Antibody 2F5 in Complex with Its gp41 Epitope
ABSTRACT The membrane-proximal region of the ectodomain of the gp41 envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) is the target of three of the five broadly neutralizing… Expand
The antigenic structure of the HIV gp120 envelope glycoprotein
- R. Wyatt, P. Kwong, +4 authors J. Sodroski
- Biology, Medicine
- Nature
- 18 June 1998
The human immunodeficiency virus HIV-1 establishes persistent infections in humans which lead to acquired immunodeficiency syndrome (AIDS). The HIV-1 envelope glycoproteins, gp120 and gp41, are… Expand
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