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HIV-I Vpr activates the G2 checkpoint through manipulation of the ubiquitin proteasome system
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HIV-1 Vpr function is mediated by interaction with the damage-specific DNA-binding protein DDB1
Baerbel Schroefelbauer et al.
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HIV1 Vpr arrests the cell cycle by recruiting DCAF1/VprBP, a receptor of the Cul4-DDB1 ubiquitin ligase
Erwann Le Rouzic et al.
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SIVSM/HIV-2 Vpx proteins promote retroviral escape from a proteasome-dependent restriction pathway present in human dendritic cells
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A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1
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Proteasome inhibitors uncouple rhesus TRIM5α restriction of HIV-1 reverse transcription and infection
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Specific recognition and accelerated uncoating of retroviral capsids by the TRIM5α restriction factor
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Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases
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Nef proteins from diverse groups of primate lentiviruses downmodulate CXCR4 to inhibit migration to the chemokine stromal derived factor 1
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Human immunodeficiency virus type 1 Vpr protein is incorporated into the virion in significantly smaller amounts than Gag and is phosphorylated in infected cells
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