e-ISSN: Pending
Negative / Null Result ReportOpen accessImmunology and Microbiology· cited by 14

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.

About to run something similar?

Run an AI Precheck on your own design to catch failure modes like this one before you spend the time. Your first desk check is free.

WASTE indexes this work — it does not host or republish it. Failure-type classification is automated and approximate.

Metadata source: OpenAlex · DOI 10.1186/s12977-016-0257-x