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

Restriction of HIV-1 by rhesus TRIM5α is governed by alpha helices in the Linker2 region.

Journal of virology - 1 Aug 2014

Sastri Jaya, Johnsen Laura, Smolin Nikolai, Imam Sabrina, Mukherjee Santanu, Lukic Zana, Brandariz-Nuñez Alberto, Robia Seth L, Diaz-Griffero Felipe, Wiethoff Christopher, Campbell Edward M

Abstract excerpt

UNLABELLED: TRIM5α proteins are a potent barrier to the cross-species transmission of retroviruses. TRIM5α proteins exhibit an ability to self-associate at many levels, ultimately leading to the formation of protein assemblies with hexagonal symmetry in vitro and cytoplasmic assemblies when expressed in cells. However, the role of these assemblies in restriction, the determinants that mediate their formation, and...

Read the complete abstract on PubMed

Topics

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

Share to Carrier Proteins
Share to Chemokine CCL2

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytoplasm

Share to HEK293 Cells

Share to HeLa Cells

Share to Macaca mulatta

Share to Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 24872590
DOI: 10.1128/JVI.01134-14
PMCID: PMC4136267

Genes

CCL2

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

Restriction of HIV-1 by rhesus TRIM5α is governed by alpha helices in the Linker2 region.PMID 24872590Read ↗

Dynamic conformational changes in the rhesus TRIM5α dimer dictate the potency of HIV-1 restriction.Semantic proximity Read ↗

Identification of residues within the L2 region of rhesus TRIM5alpha that are required for retroviral restriction and cytoplasmic body localization.Semantic proximity Read ↗

Retroviral restriction factor TRIM5alpha is a trimer.Semantic proximity Read ↗

Characterization of TRIM5alpha trimerization and its contribution to human immunodeficiency virus capsid binding.Semantic proximity Read ↗

The Three-Fold Axis of the HIV-1 Capsid Lattice Is the Species-Specific Binding Interface for TRIM5α.Semantic proximity Read ↗

A B-box 2 surface patch important for TRIM5alpha self-association, capsid binding avidity, and retrovirus restriction.Semantic proximity Read ↗

Human TRIM5α: Autophagy Connects Cell-Intrinsic HIV-1 Restriction and Innate Immune Sensor FunctioningSemantic proximity Read ↗

RING domain mutations uncouple TRIM5α restriction of HIV-1 from inhibition of reverse transcription and acceleration of uncoating.Semantic proximity Read ↗

Human Tripartite Motif 5α Domains Responsible for Retrovirus Restriction Activity and SpecificitySemantic proximity Read ↗

TRIM5α selectively binds a restriction-sensitive retroviral capsidSemantic proximity Read ↗

A naturally occurring single amino acid substitution in human TRIM5α linker region affects its anti-HIV type 1 activity and susceptibility to HIV type 1 infection.Semantic proximity Read ↗

TRIM5α Restricts Flavivirus Replication by Targeting the Viral Protease for Proteasomal DegradationSemantic proximity Read ↗

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