The HIV1 protein Vpr acts to enhance constitutive DCAF1-dependent UNG2 turnover (Q21134793)

2

Laurieann

Casey Klockow

1 reference

17 August 2022

Michael Nekorchuk

3

Michael

Nekorchuk

1 reference

17 August 2022

Hamayun J Sharifi

4

Hamayun J

Sharifi

1 reference

17 August 2022

Carlos M C de Noronha

5

Carlos M C

Creative Commons Attribution 4.0 International

de Noronha

1 reference

17 August 2022

language of work or name

English

0 references

publication date

2012

0 references

published in

PLOS One

0 references

volume

7

0 references

issue

1

0 references

page(s)

e30939

0 references

copyright license

start time

24 January 2012

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

0 references

cites work

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DDB1 and Cul4A are required for human immunodeficiency virus type 1 Vpr-induced G2 arrest

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HIV1 Vpr arrests the cell cycle by recruiting DCAF1/VprBP, a receptor of the Cul4-DDB1 ubiquitin ligase

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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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Human immunodeficiency virus type 1 Vpr protein binds to the uracil DNA glycosylase DNA repair enzyme

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The human immunodeficiency virus type 1 vpr gene arrests infected T cells in the G2 + M phase of the cell cycle

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Lentiviral Vpx accessory factor targets VprBP/DCAF1 substrate adaptor for cullin 4 E3 ubiquitin ligase to enable macrophage infection

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VprBP targets Merlin to the Roc1-Cul4A-DDB1 E3 ligase complex for degradation

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The antiviral factor APOBEC3G enhances the recognition of HIV-infected primary T cells by natural killer cells.

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HIV-1 Vpr loads uracil DNA glycosylase-2 onto DCAF1, a substrate recognition subunit of a cullin 4A-ring E3 ubiquitin ligase for proteasome-dependent degradation

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HIV-1 Vpr up-regulates expression of ligands for the activating NKG2D receptor and promotes NK cell-mediated killing

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HIV-1 Vpr triggers natural killer cell-mediated lysis of infected cells through activation of the ATR-mediated DNA damage response

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Primate lentiviral Vpx commandeers DDB1 to counteract a macrophage restriction

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The HIV1 protein Vpr acts to promote G2 cell cycle arrest by engaging a DDB1 and Cullin4A-containing ubiquitin ligase complex using VprBP/DCAF1 as an adaptor

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The interaction of vpr with uracil DNA glycosylase modulates the human immunodeficiency virus type 1 In vivo mutation rate

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12 September 2017

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HIV-1 Vpr activates the G2 checkpoint through manipulation of the ubiquitin proteasome system

12 September 2017

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Activation of the ATR-mediated DNA damage response by the HIV-1 viral protein R.

27 September 2017

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

27 September 2017

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Protein stability influences human immunodeficiency virus type 2 Vpr virion incorporation and cell cycle effect

27 September 2017

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Biochemical mechanism of HIV-1 Vpr function. Oligomerization mediated by the N-terminal domain.

27 September 2017

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Epitope-tagging approach to determine the stoichiometry of the structural and nonstructural proteins in the virus particles: amount of Vpr in relation to Gag in HIV-1.

30 May 2018

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https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0030939

HIV-1-associated uracil DNA glycosylase activity controls dUTP misincorporation in viral DNA and is essential to the HIV-1 life cycle

21 January 2018

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Proteolytic degradation of the nuclear isoform of uracil-DNA glycosylase occurs during the S phase of the cell cycle

21 January 2018

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https://api.crossref.org/works/10.1371%2FJOURNAL.PONE.0030939

Diversity of HIV-1 Vpr interactions involves usage of the WXXF motif of host cell proteins

21 January 2018

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