Vpr expression abolishes the capacity of HIV-1 infected cells to repair uracilated DNA.
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The DDB1-DCAF1-Vpr-UNG2 crystal structure reveals how HIV-1 Vpr steers human UNG2 toward destructionUracil DNA glycosylase interacts with the p32 subunit of the replication protein A complex to modulate HIV-1 reverse transcription for optimal virus dissemination.HIV-1 and HIV-2 exhibit divergent interactions with HLTF and UNG2 DNA repair proteinsDiverse fates of uracilated HIV-1 DNA during infection of myeloid lineage cells.HIV-1 Vpr-a still "enigmatic multitasker".The ubiquitin-conjugating system: multiple roles in viral replication and infection.Virion-Associated Vpr Alleviates a Postintegration Block to HIV-1 Infection of Dendritic Cells.Structural alteration of DNA induced by viral protein R of HIV-1 triggers the DNA damage response.A highly sensitive strategy for base excision repair enzyme activity detection based on graphene oxide mediated fluorescence quenching and hybridization chain reaction.
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Vpr expression abolishes the capacity of HIV-1 infected cells to repair uracilated DNA.
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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 30 October 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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Vpr expression abolishes the capacity of HIV-1 infected cells to repair uracilated DNA.
@en
Vpr expression abolishes the capacity of HIV-1 infected cells to repair uracilated DNA.
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Vpr expression abolishes the capacity of HIV-1 infected cells to repair uracilated DNA.
@en
Vpr expression abolishes the capacity of HIV-1 infected cells to repair uracilated DNA.
@nl
prefLabel
Vpr expression abolishes the capacity of HIV-1 infected cells to repair uracilated DNA.
@en
Vpr expression abolishes the capacity of HIV-1 infected cells to repair uracilated DNA.
@nl
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P50
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P1476
Vpr expression abolishes the capacity of HIV-1 infected cells to repair uracilated DNA.
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Eric Bernard
Nathalie Chazal
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P304
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10.1093/NAR/GKT974
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P577
2013-10-30T00:00:00Z