HIV-1 Vpr-chloramphenicol acetyltransferase fusion proteins: sequence requirement for virion incorporation and analysis of antiviral effect (Q40928419)

24 September 2017

HIV-1 Vpr-chloramphenicol acetyltransferase fusion proteins: sequence requirement for virion incorporation and analysis of antiviral effect (English)

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24 September 2017

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Yao XJ

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24 September 2017

Kobinger G

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24 September 2017

Dandache S

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24 September 2017

Rougeau N

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24 September 2017

Cohen E

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1 September 1999

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1590-1599

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https://scigraph.springernature.com/pub.10.1038/sj.gt.3300988

24 September 2017

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Human immunodeficiency virus type 1 Vpr is a positive regulator of viral transcription and infectivity in primary human macrophages

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The zinc fingers of HIV nucleocapsid protein NCp7 direct interactions with the viral regulatory protein Vpr.

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Human immunodeficiency virus type 1 viral protein R (Vpr) arrests cells in the G2 phase of the cell cycle by inhibiting p34cdc2 activity

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7 January 2021

Human immunodeficiency virus type 1 Vpr arrests the cell cycle in G2 by inhibiting the activation of p34cdc2-cyclin B

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Incorporation of Vpr into human immunodeficiency virus type 1 virions: requirement for the p6 region of gag and mutational analysis.

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Human immunodeficiency virus type 1 viral protein R localization in infected cells and virions

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Inhibition of human and simian immunodeficiency virus protease function by targeting Vpx-protease-mutant fusion protein into viral particles

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Virion-targeted viral inactivation of human immunodeficiency virus type 1 by using Vpr fusion proteins.

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Nuclear import, virion incorporation, and cell cycle arrest/differentiation are mediated by distinct functional domains of human immunodeficiency virus type 1 Vpr.

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HIV-1 protease specificity of peptide cleavage is sufficient for processing of gag and pol polyproteins

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Sensitive reverse transcriptase assay to detect and quantitate human immunodeficiency virus.

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Identifiers

DOI

10.1038/SJ.GT.3300988

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Dimensions Publication ID

24 September 2017

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