Uracil DNA glycosylase interacts with the p32 subunit of the replication protein A complex to modulate HIV-1 reverse transcription for optimal virus dissemination
Cécile Hérate; Clarisse Vigne; Carolin A. Guenzel; Marie Lambelé; Marie-Christine Rouyez; Serge Bénichou · 2016 · Retrovirology
WASTE classifies this as Negative / Null Result Report · AI classification, approximate
The study found no significant effect — useful as a negative control or null benchmark for your own design.
Abstract
BACKGROUND: Through incorporation into virus particles, the HIV-1 Vpr protein participates in the early steps of the virus life cycle by influencing the reverse transcription process. We previously showed that this positive impact on reverse transcription was related to Vpr binding to the uracil DNA glycosylase 2 enzyme (UNG2), leading to enhancement of virus infectivity in established CD4-positive cell lines via a nonenzymatic mechanism. RESULTS: We report here that Vpr can form a trimolecular complex with UNG2 and the p32 subunit (RPA32) of the replication protein A (RPA) complex and we expl
Abstract by Cécile Hérate; Clarisse Vigne; Carolin A. Guenzel; Marie Lambelé; Marie-Christine Rouyez; Serge Bénichou, Retrovirology (2016) — licensed CC BY 4.0.
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Metadata source: OpenAlex · DOI 10.1186/s12977-016-0257-x
