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

Structural perspectives on HIV‐1 Vif and APOBEC3 restriction factor interactions

13 Sept 2019

Abstract excerpt

T cells, macrophages, and dendritic cells. The human apolipoprotein B mRNA- editing catalytic polypeptide 3 (APOBEC3 or A3) cytidine deaminases are a key class of intrinsic restriction factors that inhibit replication of HIV. When HIV-1 enters the cell, the immune system responds by inducing the activation of the A3 family proteins, which convert cytosines to uracils in single-stranded DNA replication...

Read the complete abstract on PubMed

Topics

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

Share to Hepatitis C virus research
Share to HIV/AIDS drug development and treatment
Share to HIV Research and Treatment

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 31518043
DOI: 10.1002/pro.3729

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural perspectives on HIV‐1 Vif and APOBEC3 restriction factor interactionsPMID 31518043Read ↗

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

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

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

Structural Features of Antiviral APOBEC3 Proteins are Linked to Their Functional ActivitiesSemantic proximity Read ↗

Multiple APOBEC3 Restriction Factors for HIV-1 and One Vif to Rule Them AllSemantic proximity Read ↗

Role of the single deaminase domain APOBEC3A in virus restriction, retrotransposition, DNA damage and cancerSemantic proximity Read ↗

The structural basis for HIV-1 Vif antagonism of human APOBEC3GSemantic proximity Read ↗

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

Identification of the HIV-1 Vif and Human APOBEC3G Protein InterfaceSemantic 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 ↗

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

Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction.Semantic proximity Read ↗

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