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1994 | 1 |
1995 | 2 |
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Phosphorylation of both phosphoacceptor sites in the HIV-1 Vpu cytoplasmic domain is essential for Vpu-mediated ER degradation of CD4.
Virology. 1997 May 26;232(1):207-16. doi: 10.1006/viro.1997.8541.
Virology. 1997.
PMID: 9185604
Free article.
The human immunodeficiency virus type 1 Vpu protein tethered to the CD4 extracellular domain is localized to the plasma membrane and is biologically active in the secretory pathway of mammalian cells: implications for the mechanisms of Vpu function.
Raja NU, Jabbar MA.
Raja NU, et al.
Virology. 1996 Jun 1;220(1):141-51. doi: 10.1006/viro.1996.0294.
Virology. 1996.
PMID: 8659106
Free article.
Item in Clipboard
Functional analysis of the phosphorylation sites on the human immunodeficiency virus type 1 Vpu protein.
Friborg J, Ladha A, Göttlinger H, Haseltine WA, Cohen EA.
Friborg J, et al.
J Acquir Immune Defic Syndr Hum Retrovirol. 1995 Jan 1;8(1):10-22.
J Acquir Immune Defic Syndr Hum Retrovirol. 1995.
PMID: 8548340
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Differential activities of the human immunodeficiency virus type 1-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartments.
Schubert U, Strebel K.
Schubert U, et al.
J Virol. 1994 Apr;68(4):2260-71. doi: 10.1128/JVI.68.4.2260-2271.1994.
J Virol. 1994.
PMID: 8139011
Free PMC article.
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The human immunodeficiency virus type 1 Vpu protein: a potential regulator of proteolysis and protein transport in the mammalian secretory pathway.
Vincent MJ, Abdul Jabbar M.
Vincent MJ, et al.
Virology. 1995 Nov 10;213(2):639-49. doi: 10.1006/viro.1995.0035.
Virology. 1995.
PMID: 7491787
Free article.
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