Structure-Based Identification and Neutralization Mechanism of Tyrosine Sulfate Mimetics That Inhibit HIV-1 Entry-Reference-Cited by-同舟云学术

Structure-Based Identification and Neutralization Mechanism of Tyrosine Sulfate Mimetics That Inhibit HIV-1 Entry

Published:2011-08-05 Issue:10 Volume:6 Page:1069-1077
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Acharya Priyamvada,Dogo-Isonagie Cajetan,LaLonde Judith M.¹,Lam Son N.,Leslie George J.²,Louder Mark K.,Frye Leah L.³,Debnath Asim K.⁴,Greenwood Jeremy R.³,Luongo Timothy S.,Martin Loïc⁵,Watts K. Shawn³,Hoxie James A.²,Mascola John R.,Bewley Carole A.,Kwong Peter D.

Affiliation:

1. Department of Chemistry, Bryn Mawr College, Bryn Mawr, Pennsylvania 19010, United States

2. Department of Medicine, Hematology-Oncology Division, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States

3. Schrödinger, LLC, Portland, Oregon 97204, United States

4. Laboratory of Molecular Modeling and Drug Design, Lindsley F. Kimball Research Institute, New York Blood Center, 310 E 67th Street, New York, New York 10021, United States

5. CEA, iBiTecS, Service d’Ingénierie Moléculaire des Protéines, Gif sur Yvette F-91191, France

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/cb200068b

Reference43 articles.

1. HIV entry inhibitors and their potential in HIV therapy

2. Structure of an unliganded simian immunodeficiency virus gp120 core

3. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody

4. A Conserved HIV gp120 Glycoprotein Structure Involved in Chemokine Receptor Binding

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