Structure and Plasticity of the Human Immunodeficiency Virus gp41 Fusion Domain in Lipid Micelles and Bilayers-Reference-Cited by-同舟云学术

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Structure and Plasticity of the Human Immunodeficiency Virus gp41 Fusion Domain in Lipid Micelles and Bilayers

Published:2007-08 Issue:3 Volume:93 Page:876-885
ISSN:0006-3495
Container-title:Biophysical Journal
language:en
Short-container-title:Biophysical Journal

Author:

Li Yinling,Tamm Lukas K.

Publisher

Elsevier BV

Subject

Biophysics

Reference38 articles.

1. Atomic structure of the ectodomain from HIV-1 gp41;Weissenhorn;Nature,1997

2. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody;Kwong;Nature,1998

3. Mechanisms of viral membrane fusion and its inhibition;Eckert;Annu. Rev. Biochem.,2001

4. Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus;Gallaher;Cell,1987

5. A leucine zipper-like sequence from the cytoplasmic tail of the HIV-1 envelope glycoprotein binds and perturbs lipid bilayers;Kliger;Biochemistry,1997

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2. Positive residues of the SARS-CoV-2 fusion domain are key contributors to the initiation of membrane fusion;Journal of Biological Chemistry;2024-08

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