Studies with GFP-Vpr fusion proteins: induction of apoptosis but ablation of cell-cycle arrest despite nuclear membrane or nuclear localization (Q73890416)

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scientific article published on 01 August 2003

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English	Studies with GFP-Vpr fusion proteins: induction of apoptosis but ablation of cell-cycle arrest despite nuclear membrane or nuclear localization	scientific article published on 01 August 2003

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scholarly article

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7 November 2019

Studies with GFP-Vpr fusion proteins: induction of apoptosis but ablation of cell-cycle arrest despite nuclear membrane or nuclear localization (English)

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7 November 2019

apoptotic process

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author name string

Megan G Waldhuber

1

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7 November 2019

Michael Bateson

2

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7 November 2019

Judith Tan

3

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7 November 2019

Alison L Greenway

4

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7 November 2019

Dale A McPhee

5

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7 November 2019

publication date

1 August 2003

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7 November 2019

313

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7 November 2019

91-104

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7 November 2019

1

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7 November 2019

The human immunodeficiency virus type 1 Vpr transactivator: cooperation with promoter-bound activator domains and binding to TFIIB

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Biological characterization of human immunodeficiency virus type 1 and type 2 mutants in human peripheral blood mononuclear cells

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Distinct effects in primary macrophages and lymphocytes of the human immunodeficiency virus type 1 accessory genes vpr, vpu, and nef: mutational analysis of a primary HIV-1 isolate

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Comparison of fixation protocols for adherent cultured cells applied to a GFP fusion protein of the epidermal growth factor receptor

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Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes

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The HIV-1 vpr protein acts as a negative regulator of apoptosis in a human lymphoblastoid T cell line: possible implications for the pathogenesis of AIDS

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Functions of the auxiliary gene products of the human immunodeficiency virus type 1.

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The HIV-1 Vpr displays strong anti-apoptotic activity

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HIV-1 Vpr increases viral expression by manipulation of the cell cycle: a mechanism for selection of Vpr in vivo

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A time to kill: viral manipulation of the cell death program

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The Vpr protein of human immunodeficiency virus type 1 influences nuclear localization of viral nucleic acids in nondividing host cells

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The HIV-1 viral protein R induces apoptosis via a direct effect on the mitochondrial permeability transition pore

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Characterization of HIV-1 vpr nuclear import: analysis of signals and pathways

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Cytoskeletal plasticity in cells expressing neuronal microtubule-associated proteins

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A peptide derived from the N-terminal region of HIV-1 Vpr promotes nuclear import in permeabilized cells: elucidation of the NLS region of the Vpr.

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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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Functional analysis of HIV-1 Vpr: identification of determinants essential for subcellular localization.

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Induction of apoptosis by the Vpr protein of human immunodeficiency virus type 1 occurs independently of G(2) arrest of the cell cycle

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Human immunodeficiency virus type 1 Vpr induces apoptosis in human neuronal cells

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Cell cycle arrest by Vpr in HIV-1 virions and insensitivity to antiretroviral agents.

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Viral protein R regulates docking of the HIV-1 preintegration complex to the nuclear pore complex

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Evidence for direct association of Vpr and matrix protein p17 within the HIV-1 virion

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Transdominant activity of human immunodeficiency virus type 1 Vpr with a mutation at residue R73.

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NMR structure of the (52-96) C-terminal domain of the HIV-1 regulatory protein Vpr: molecular insights into its biological functions

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Nucleocytoplasmic shuttling by human immunodeficiency virus type 1 Vpr.

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Roles of p53 and caspases in the induction of cell cycle arrest and apoptosis by HIV-1 vpr

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Green fluorescent protein. The green revolution

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Lentiviral delivery of HIV-1 Vpr protein induces apoptosis in transformed cells

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Human immunodeficiency virus type 1 vpr induces apoptosis through caspase activation

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Human immunodeficiency virus type 1 Vpr localization: nuclear transport of a viral protein modulated by a putative amphipathic helical structure and its relevance to biological activity

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HIV-1 Vpr transactivates LTR-directed expression through sequences present within -278 to -176 and increases virus replication in vitro.

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HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection

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Human immunodeficiency virus vpr gene encodes a virion-associated protein

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Cell cycle inhibitory effects of HIV and SIV Vpr and Vpx in the yeast Schizosaccharomyces pombe

1 reference

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Arginine residues in the C-terminus of HIV-1 Vpr are important for nuclear localization and cell cycle arrest

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Comparison of cell cycle arrest, transactivation, and apoptosis induced by the simian immunodeficiency virus SIVagm and human immunodeficiency virus type 1 vpr genes.

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

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7 January 2021

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

1 reference

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Vpr-induced cell cycle arrest is conserved among primate lentiviruses.

1 reference

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Effect of human immunodeficiency virus type 1 protein R (vpr) gene expression on basic cellular function of fission yeast Schizosaccharomyces pombe.

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Identifiers

10.1016/S0042-6822(03)00258-7

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7 November 2019

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