Mutations in the feline immunodeficiency virus envelope glycoprotein confer resistance to a dominant–negative fragment of Tsg101 by enhancing infectivity and cell-to-cell virus transmission
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference94 articles.
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2. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress;Martin-Serrano;Nat. Med.,2001
3. Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding;Garrus;Cell,2001
4. Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag);VerPlank;Proc. Natl. Acad. Sci. U. S. A.,2001
5. Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function;Demirov;Proc. Natl. Acad. Sci. U. S. A.,2002
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1. Importance of Viral Late Domains in Budding and Release of Enveloped RNA Viruses;Viruses;2021-08-06
2. Alix-Mediated Rescue of Feline Immunodeficiency Virus Budding Differs from That Observed with Human Immunodeficiency Virus;Journal of Virology;2020-05-18
3. Mutations in the HIV-1 envelope glycoprotein can broadly rescue blocks at multiple steps in the virus replication cycle;Proceedings of the National Academy of Sciences;2019-04-11
4. HIV-1 adaptation studies reveal a novel Env-mediated homeostasis mechanism for evading lethal hypermutation by APOBEC3G;PLOS Pathogens;2018-04-20
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