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HIV-1 and HIV-2 exhibit divergent interactions with HLTF and UNG2 DNA repair proteins

HIV-1 and HIV-2 exhibit divergent interactions with HLTF and UNG2 DNA repair proteins

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The DDB1-DCAF1-Vpr-UNG2 crystal structure reveals how HIV-1 Vpr steers human UNG2 toward destruction Activation of the DNA Damage Response Is a Conserved Function of HIV-1 and HIV-2 Vpr That Is Independent of SLX4 Recruitment Temporal proteomic analysis of HIV infection reveals remodelling of the host phosphoproteome by lentiviral Vif variants Inhibition of Vpx-Mediated SAMHD1 and Vpr-Mediated Host Helicase Transcription Factor Degradation by Selective Disruption of Viral CRL4 (DCAF1) E3 Ubiquitin Ligase Assembly Quantitative Temporal Viromics of an Inducible HIV-1 Model Yields Insight to Global Host Targets and Phospho-Dynamics Associated with Protein Vpr.The HIV-1 Vpr Protein: A Multifaceted Target for Therapeutic Intervention.A Role for the Host DNA Damage Response in Hepatitis B Virus cccDNA Formation-and Beyond?Virion-Associated Vpr Alleviates a Postintegration Block to HIV-1 Infection of Dendritic Cells.Dual role of the chromatin-binding factor PHF13 in the pre- and post-integration phases of HIV-1 replication.HIV-1 Vif's capacity to manipulate the cell cycle is species-specific.Regulation of CD4 Receptor and HIV-1 Entry by MicroRNAs-221 and -222 during Differentiation of THP-1 Cells.HIV-1 Vpr protein directly loads helicase-like transcription factor (HLTF) onto the CRL4-DCAF1 E3 ubiquitin ligase.HIV-1 Vpr hijacks EDD-DYRK2-DDB1DCAF1 to disrupt centrosome homeostasis.Global phosphoproteomics of CCR5-tropic HIV-1 signaling reveals reprogramming of cellular protein production pathways and identifies p70-S6K1 and MK2 as HIV-responsive kinases required for optimal infection of CD4+ T cells.High-Definition Analysis of Host Protein Stability during Human Cytomegalovirus Infection Reveals Antiviral Factors and Viral Evasion Mechanisms Alternative splicing of helicase-like transcription factor (Hltf): Intron retention-dependent activation of immune tolerance at the feto-maternal interface HIV-1 Vpr Reprograms CLR4 E3 Ubiquitin Ligase to Antagonize Exonuclease 1-Mediated Restriction of HIV-1 Infection

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HIV-1 and HIV-2 exhibit divergent interactions with HLTF and UNG2 DNA repair proteins

http://www.wikidata.org/entity/Q37086412

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 22 June 2016

@en

vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

HIV-1 and HIV-2 exhibit divergent interactions with HLTF and UNG2 DNA repair proteins

@en

HIV-1 and HIV-2 exhibit divergent interactions with HLTF and UNG2 DNA repair proteins.

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HIV-1 and HIV-2 exhibit divergent interactions with HLTF and UNG2 DNA repair proteins

@en

HIV-1 and HIV-2 exhibit divergent interactions with HLTF and UNG2 DNA repair proteins.

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HIV-1 and HIV-2 exhibit divergent interactions with HLTF and UNG2 DNA repair proteins

@en

HIV-1 and HIV-2 exhibit divergent interactions with HLTF and UNG2 DNA repair proteins.

@nl

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PNAS.1605023113

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Proceedings of the National Academy of Sciences of the United States of America

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HIV-1 and HIV-2 exhibit divergent interactions with HLTF and UNG2 DNA repair proteins

@en

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Caili Hao

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Jacek Skowronski

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Kasia Hrecka

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Ming-Chieh Shun

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Sarabpreet Kaur

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Selene K Swanson

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P2860

Origin of HIV-1 in the chimpanzee Pan troglodytes troglodytes

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

Premature activation of the SLX4 complex by Vpr promotes G2/M arrest and escape from innate immune sensing

Chromatin association of human origin recognition complex, cdc6, and minichromosome maintenance proteins during the cell cycle: assembly of prereplication complexes in late mitosis

Evolution and horizontal transfer of dUTPase-encoding genes in viruses and their hosts

Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases

SAMHD1 is the dendritic- and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx

SAMHD1 restricts the replication of human immunodeficiency virus type 1 by depleting the intracellular pool of deoxynucleoside triphosphates

Vpx relieves inhibition of HIV-1 infection of macrophages mediated by the SAMHD1 protein

Uracil DNA glycosylase specifically interacts with Vpr of both human immunodeficiency virus type 1 and simian immunodeficiency virus of sooty mangabeys, but binding does not correlate with cell cycle arrest

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E3921-30

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scholarly article

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10.1073/PNAS.1605023113

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27

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113

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Laurence Florens

Michael P. Washburn

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2016-06-22T00:00:00Z

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27335459

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