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

The Binding Interface between Human APOBEC3F and HIV-1 Vif Elucidated by Genetic and Computational Approaches

25 Nov 2015

Abstract excerpt

APOBEC3 family DNA cytosine deaminases provide overlapping defenses against pathogen infections. However, most viruses have elaborate evasion mechanisms such as the HIV-1 Vif protein, which subverts cellular CBF-β and a polyubiquitin ligase complex to neutralize these enzymes. Despite advances in APOBEC3 and Vif biology, a full understanding of this direct host-pathogen conflict has been elusive. We combine virus...

Read the complete abstract on PubMed

Topics

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

Share to HIV/AIDS drug development and treatment
Share to HIV/AIDS Research and Interventions
Share to HIV Research and Treatment

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 26628363
DOI: 10.1016/j.celrep.2015.10.067

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Binding Interface between Human APOBEC3F and HIV-1 Vif Elucidated by Genetic and Computational ApproachesPMID 26628363Read ↗

HIV-1 Vif gained breadth in APOBEC3G specificity after cross-species transmission of its precursorsSemantic proximity Read ↗

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

The Structural Interface between HIV-1 Vif and Human APOBEC3HSemantic proximity Read ↗

HIV-1 Vif Gained Breadth in APOBEC3G Specificity after Cross-Species Transmission of Its Precursors.Semantic proximity Read ↗

Structural perspectives on HIV‐1 Vif and APOBEC3 restriction factor interactionsSemantic proximity Read ↗

Strain-specific epistasis shapes fitness landscapes of APOBEC3G antagonism by HIV-1 Vif proteins.Semantic proximity Read ↗

Strain-Specific Epistasis Shapes Fitness Landscapes of APOBEC3G Antagonism By HIV-1 Vif ProteinsSemantic proximity Read ↗

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

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

A single amino acid in human APOBEC3F alters susceptibility to HIV-1 Vif.Semantic proximity Read ↗

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

A computational analysis of the structural determinants of APOBEC3’s catalytic activity and vulnerability to HIV-1 VifSemantic proximity Read ↗

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