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

Vpr14-88-Apobec3G fusion protein is efficiently incorporated into Vif-positive HIV-1 particles and inhibits viral infection.

PloS one - 16 Apr 2008

Ao Zhujun, Yu Zhe, Wang Lina, Zheng Yingfeng, Yao Xiaojian

Abstract excerpt

BACKGROUND: APOBEC3G (A3G), a deoxycytidine deaminase, is a potent host antiviral factor that can restrict HIV-1 infection. During Vif-negative HIV-1 replication, A3G is incorporated into HIV-1 particles, induces mutations in reverse transcribed viral DNA and inhibits reverse transcription. However, HIV-1 Vif counteracts A3G's activities by inducing its degradation and by blocking its incorporation into HIV-1...

Read the complete abstract on PubMed

Topics

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

Share to APOBEC-3G Deaminase
Share to CD4-Positive T-Lymphocytes

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cytidine Deaminase

Share to Gene Products, vif

Share to HeLa Cells

Share to Leukocytes, Mononuclear

Share to Recombinant Fusion Proteins

Share to vpr Gene Products, Human Immunodeficiency Virus

Source

Open in PubMed Open full text

Identifiers

PMID: 18414671
DOI: 10.1371/journal.pone.0001995
PMCID: PMC2288674

Genes

CCR5

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Vpr14-88-Apobec3G fusion protein is efficiently incorporated into Vif-positive HIV-1 particles and inhibits viral infection.PMID 18414671Read ↗

Inhibition of HIV-1 infection and replication by enhancing viral incorporation of innate anti-HIV-1 protein A3G: a non-pathogenic Nef mutant-based anti-HIV strategy.Semantic proximity Read ↗

Various strategies for developing APOBEC3G protectors to circumvent human immunodeficiency virus type 1.Semantic proximity Read ↗

Multifaceted counter-APOBEC3G mechanisms employed by HIV-1 Vif.Semantic proximity Read ↗

Differential anti-APOBEC3G activity of HIV-1 Vif proteins derived from different subtypes.Semantic proximity Read ↗

APOBEC3G targets human T-cell leukemia virus type 1.Semantic 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 ↗

Interactions of host APOBEC3 restriction factors with HIV-1 in vivo: implications for therapeuticsSemantic proximity Read ↗

Cytidine Deaminases as a Weapon Against Retroviruses and a New Target for Antiviral TherapySemantic proximity Read ↗

Vpr.A3A Chimera Inhibits HIV ReplicationSemantic proximity Read ↗

HIV-1 Vif Blocks the Antiviral Activity of APOBEC3G by Impairing Both Its Translation and Intracellular StabilitySemantic proximity Read ↗

Antiviral Mechanism and Biochemical Basis of the Human APOBEC3 FamilySemantic proximity Read ↗

Distinct Domains within APOBEC3G and APOBEC3F Interact with Separate Regions of Human Immunodeficiency Virus Type 1 VifSemantic proximity Read ↗

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