Large Changes in the CRAC Segment of gp41 of HIV Do Not Destroy Fusion Activity if the Segment Interacts with Cholesterol-Reference-Cited by-同舟云学术

Large Changes in the CRAC Segment of gp41 of HIV Do Not Destroy Fusion Activity if the Segment Interacts with Cholesterol

Published:2008-10-21 Issue:45 Volume:47 Page:11869-11876
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Vishwanathan Sundaram A.¹,Thomas Annick¹,Brasseur Robert¹,Epand Raquel F.¹,Hunter Eric¹,Epand Richard M.¹

Affiliation:

1. Emory Vaccine Research Center, Yerkes, Emory University, 954 Gatewood Road, Atlanta, Georgia 30329, Department of Biochemistry and Biomedical Sciences, McMaster University, 1200 Main Street West, Hamilton, Ontario L8N 3Z5, Canada, and Faculté Universitaire des Sciences Agronomiques de Gembloux Centre de Biophysique Moléculaire Numérique, Passage des Déportés, 2 5030 Gembloux, Belgium

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi8014828

Reference39 articles.

1. A Conserved Tryptophan-Rich Motif in the Membrane-Proximal Region of the Human Immunodeficiency Virus Type 1 gp41 Ectodomain Is Important for Env-Mediated Fusion and Virus Infectivity

2. Role of the Membrane-Proximal Domain in the Initial Stages of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein-Mediated Membrane Fusion

3. Role of the Fusion Peptide and Membrane-Proximal Domain in HIV-1 Envelope Glycoprotein-Mediated Membrane Fusion

4. The Broadly Neutralizing Anti-Human Immunodeficiency Virus Type 1 4E10 Monoclonal Antibody Is Better Adapted to Membrane-Bound Epitope Recognition and Blocking than 2F5

5. Interfacial pre-transmembrane domains in viral proteins promoting membrane fusion and fission

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