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Article

Interaction of HIV-1 integrase with DNA repair protein hRad18.

The Journal of biological chemistry - 26 Jul 2002

Mulder Lubbertus C F, Chakrabarti Lisa A, Muesing Mark A

Abstract excerpt

We have previously shown that human immunodeficiency virus-1 (HIV-1) integrase is an unstable protein and a substrate for the N-end rule degradation pathway. This degradation pathway shares its ubiquitin-conjugating enzyme, Rad6, with the post-replication/translesion DNA repair pathway. Because DNA repair is thought to play an essential role in HIV-1 integration, we investigated whether other molecules of this...

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Identifiers

PMID: 12016221
DOI: 10.1074/jbc.M203061200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Interaction of HIV-1 integrase with DNA repair protein hRad18.PMID 12016221Read ↗

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The putative U94 integrase is dispensable for human herpesvirus 6 (HHV-6) chromosomal integrationSemantic proximity Read ↗

Physical interaction between the herpes simplex virus type 1 exonuclease, UL12, and the DNA double-strand break-sensing MRN complex.Semantic proximity Read ↗

The 26S proteasome negatively regulates the level of overall genomic nucleotide excision repair.Semantic proximity Read ↗

E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6.Semantic proximity Read ↗

Uracil DNA Glycosylase 2 negatively regulates HIV-1 LTR transcriptionSemantic proximity Read ↗

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