Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Characterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFβ and CRL5 E3 ubiquitin ligase components.

PloS one - 1 Jan 2012

Zhou Xiaohong, Evans Sean L, Han Xue, Liu Yayan, Yu Xiao-Fang

Abstract excerpt

Human immunodeficiency virus-1 (HIV-1) viral infectivity factor (Vif) is essential for viral replication because of its ability to eliminate the host's antiviral response to HIV-1 that is mediated by the APOBEC3 family of cellular cytidine deaminases. Vif targets these proteins, including APOBEC3G, for polyubiquitination and subsequent proteasome-mediated degradation via the formation of a...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cullin Proteins
Share to Gene Expression
Share to Multiprotein Complexes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Interaction Domains and Motifs

Share to Protein Stability

Share to Recombinant Fusion Proteins

Share to Solubility

Share to vif Gene Products, Human Immunodeficiency Virus

Source

Open in PubMed Open full text

Identifiers

PMID: 22479405
DOI: 10.1371/journal.pone.0033495
PMCID: PMC3316577

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFβ and CRL5 E3 ubiquitin ligase components.PMID 22479405Read ↗

Evolutionarily Conserved Requirement for Core Binding Factor Beta in the Assembly of the Human Immunodeficiency Virus/Simian Immunodeficiency Virus Vif-Cullin 5-RING E3 Ubiquitin LigaseSemantic proximity Read ↗

Advances in the Structural Understanding of Vif ProteinsSemantic proximity Read ↗

Structural basis of HIV-1 Vif-mediated E3 ligase targeting of host APOBEC3HSemantic proximity Read ↗

Interactions between HIV-1 Vif and human ElonginB-ElonginC are important for CBF-β binding to VifSemantic proximity Read ↗

Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly.Semantic proximity Read ↗

Inhibition of Vif-Mediated Degradation of APOBEC3G through Competitive Binding of Core-Binding Factor Beta.Semantic proximity Read ↗

Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex.Semantic proximity Read ↗

Multifaceted HIV‐1 Vif interactions with human E3 ubiquitin ligase and APOBEC3sSemantic proximity Read ↗

Structural basis for HIV-1 antagonism of host APOBEC3G via Cullin E3 ligaseSemantic proximity Read ↗

Distinct Determinants in HIV-1 Vif and Human APOBEC3 Proteins Are Required for the Suppression of Diverse Host Anti-Viral ProteinsSemantic proximity Read ↗

Small-Molecule Inhibition of Human Immunodeficiency Virus Type 1 Replication by Targeting the Interaction between Vif and ElonginCSemantic proximity Read ↗

Identification of an APOBEC3G Binding Site in Human Immunodeficiency Virus Type 1 Vif and Inhibitors of Vif-APOBEC3G BindingSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.