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Article

APOBEC3G is degraded by the proteasomal pathway in a Vif-dependent manner without being polyubiquitylated.

The Journal of biological chemistry - 9 May 2008

Dang Ying, Siew Lai Mun, Zheng Yong-Hui

Abstract excerpt

Although the covalent attachment of a polyubiquitin is the prevailing paradigm for entry into proteasomes, accumulating evidence suggests that poorly defined ubiquitin-free pathways also degrade proteins. The cytidine deaminase APOBEC3G (A3G) potently inhibits human immunodeficiency virus type 1 replication by disrupting viral reverse transcription. However, human immunodeficiency virus type 1 produces a viral...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 18326044
DOI: 10.1074/jbc.M708728200
PMCID: PMC2430655

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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APOBEC3G is degraded by the proteasomal pathway in a Vif-dependent manner without being polyubiquitylated.PMID 18326044Read ↗

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