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Article

Determinants for the rhesus monkey TRIM5alpha-mediated block of the late phase of HIV-1 replication.

The Journal of biological chemistry - 5 Feb 2010

Sakuma Ryuta, Ohmine Seiga, Ikeda Yasuhiro

Abstract excerpt

Rhesus monkey TRIM5alpha (TRIM5alpharh) includes RING, B-box, coiled-coil, and B30.2(PRYSPRY) domains and blocks HIV-1 infection by targeting HIV-1 core through a B30.2(PRYSPRY) domain. Previously, we reported that TRIM5alpharh also blocks HIV-1 production in a B30.2(PRYSPRY)-independent manner. Efficient encapsidation of TRIM5alpharh, but not human TRIM5alpha (TRIM5alphahu), in HIV-1 virus-like particles...

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Source

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Identifiers

PMID: 19951947
DOI: 10.1074/jbc.M109.059063
PMCID: PMC2823520

Genes

TRIM21

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Determinants for the rhesus monkey TRIM5alpha-mediated block of the late phase of HIV-1 replication.PMID 19951947Read ↗

The contribution of RING and B-box 2 domains to retroviral restriction mediated by monkey TRIM5alpha.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 ↗

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

The Antiviral Spectra of TRIM5α Orthologues and Human TRIM Family Proteins against Lentiviral ProductionSemantic proximity Read ↗

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

Functional Replacement of the RING, B-Box 2, and Coiled-Coil Domains of Tripartite Motif 5α (TRIM5α) by Heterologous TRIM DomainsSemantic proximity Read ↗

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

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

Role of TRIM5α RING Domain E3 Ubiquitin Ligase Activity in Capsid Disassembly, Reverse Transcription Blockade, and Restriction of Simian Immunodeficiency VirusSemantic proximity Read ↗

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

Binding of the rhesus TRIM5α PRYSPRY domain to capsid is necessary but not sufficient for HIV-1 restrictionSemantic proximity Read ↗

Modulation of retroviral restriction and proteasome inhibitor-resistant turnover by changes in the TRIM5alpha B-box 2 domain.Semantic proximity Read ↗

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