N-terminal substitutions in HIV-1 gp41 reduce the expression of non-trimeric envelope glycoproteins on the virus
Author:
Publisher
Elsevier BV
Subject
Virology
Reference89 articles.
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3. Mutations in human immunodeficiency virus type 1 gp41 affect sensitivity to neutralization by gp120 antibodies;Back;J. Virol.,1993
4. A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure;Binley;J. Virol.,2000
5. Enhancing the proteolytic maturation of human immunodeficiency virus type 1 envelope glycoproteins;Binley;J. Virol.,2002
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1. Alterations in gp120 glycans or the gp41 fusion peptide-proximal region modulate the stability of the human immunodeficiency virus (HIV-1) envelope glycoprotein pretriggered conformation;Journal of Virology;2023-09-28
2. Impact of stabilizing mutations on the antigenic profile and glycosylation of membrane-expressed HIV-1 envelope glycoprotein;PLOS Pathogens;2023-08-07
3. Impact of Common Modifications on the Antigenic Profile and Glycosylation of Membrane-Expressed HIV-1 Envelope Glycoprotein;2023-06-05
4. Functional and Highly Cross-Linkable HIV-1 Envelope Glycoproteins Enriched in a Pretriggered Conformation;Journal of Virology;2022-04-27
5. Potent Induction of Envelope-Specific Antibody Responses by Virus-Like Particle Immunogens Based on HIV-1 Envelopes from Patients with Early Broadly Neutralizing Responses;Journal of Virology;2022-01-12
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