The GlycosylatedgagProtein of MuLV Is a Determinant of Neuroinvasiveness: Analysis of Second Site Revertants of a Mutant MuLV Lacking Expression of This Protein
Author:
Publisher
Elsevier BV
Subject
Virology
Cited by 18 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Murine Leukemia Virus Glycosylated Gag Reduces Murine SERINC5 Protein Expression at Steady-State Levels via the Endosome/Lysosome Pathway to Counteract SERINC5 Antiretroviral Activity;Journal of Virology;2019-01-15
2. Full-Length Glycosylated Gag of Murine Leukemia Virus Can Associate with the Viral Envelope as a Type I Integral Membrane Protein;Journal of Virology;2018-03-15
3. Functional Interplay Between Murine Leukemia Virus Glycogag, Serinc5, and Surface Glycoprotein Governs Virus Entry, with Opposite Effects on Gammaretroviral and Ebolavirus Glycoproteins;mBio;2016-12-30
4. N-Linked Glycosylation Protects Gammaretroviruses against Deamination by APOBEC3 Proteins;Journal of Virology;2014-12-10
5. The Nef-Like Effect of Murine Leukemia Virus Glycosylated Gag on HIV-1 Infectivity Is Mediated by Its Cytoplasmic Domain and Depends on the AP-2 Adaptor Complex;Journal of Virology;2014-03-15
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