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

Different subcellular localisations of TRIM22 suggest species-specific function

11 Feb 2009

Abstract excerpt

The B30.2/SPRY domain is present in many proteins, including various members of the tripartite motif (TRIM) protein family such as TRIM5alpha, which mediates innate intracellular resistance to retroviruses in several primate species. This resistance is dependent on the integrity of the B30.2 domain that evolves rapidly in primates and exhibits species-specific anti-viral activity. TRIM22 is another positively...

Read the complete abstract on PubMed

Topics

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

Share to Herpesvirus Infections and Treatments
Share to HIV Research and Treatment
Share to interferon and immune responses

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 19212762
DOI: 10.1007/s00251-009-0357-z

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Different subcellular localisations of TRIM22 suggest species-specific functionPMID 19212762Read ↗

The B30.2(SPRY) domain of the retroviral restriction factor TRIM5alpha exhibits lineage-specific length and sequence variation in primates.Semantic proximity Read ↗

TRIM22: A Diverse and Dynamic Antiviral ProteinSemantic proximity Read ↗

Discordant Evolution of the Adjacent Antiretroviral Genes TRIM22 and TRIM5 in MammalsSemantic proximity Read ↗

All three variable regions of the TRIM5alpha B30.2 domain can contribute to the specificity of retrovirus restriction.Semantic proximity Read ↗

Evolution of a cytoplasmic tripartite motif (TRIM) protein in cows that restricts retroviral infection.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 ↗

Genomic analysis of the TRIM family reveals two groups of genes with distinct evolutionary propertiesSemantic proximity Read ↗

Ancient and recent adaptive evolution in the antiviral TRIM22 gene: identification of a single-nucleotide polymorphism that impacts TRIM22 function.Semantic proximity Read ↗

Unique features of TRIM5α among closely related human TRIM family membersSemantic proximity Read ↗

Relationship between SPRY and B30.2 protein domains. Evolution of a component of immune defence?Semantic proximity Read ↗

Retroviral restriction factor TRIM5alpha is a trimer.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 ↗

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