Activation of protein phosphatase-2A1 by HIV-1 Vpr Cell death causing peptide in intact CD4+ T cells and in vitro
Author:
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference40 articles.
1. A C-terminal domain of HIV-1 accessory protein Vpr is involved in penetration, mitochondrial dysfunction and apoptosis of human CD4+ lymphocytes
2. Could Nef and Vpr Proteins Contribute to Disease Progression by Promoting Depletion of Bystander Cells and Prolonged Survival of HIV-Infected Cells?
3. Interaction between the cell-cycle-control proteins p34cdc2 and p9CKShs2. Evidence for two cooperative binding domains in p9CKShs2
4. Pathogenesis of HIV-1-protease inhibitor-associated peripheral lipodystrophy, hyperlipidaemia, and insulin resistance
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1. Hyperactivation of mammalian target of rapamycin complex 1 by HIV‐1 is necessary for virion production and latent viral reactivation;The FASEB Journal;2016-10-04
2. The Host-Pathogen interaction of human cyclophilin A and HIV-1 Vpr requires specific N-terminal and novel C-terminal domains;BMC Structural Biology;2011-12
3. PP2A1 Binding, Cell Transducing and Apoptotic Properties of Vpr77–92: A New Functional Domain of HIV-1 Vpr Proteins;PLoS ONE;2010-11-01
4. Protein phosphatase-2A is activated in pig brain following cardiac arrest and resuscitation;Metabolic Brain Disease;2008-01-16
5. HIV-1 Vpr Potently Induces Programmed Cell Death in the CNSin Vivo;DNA and Cell Biology;2007-02
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