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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Tripartite motif containing 5

TRIM5alpha, TRIM5
The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein forms homo-oligomers via the coilel-coil region and localizes to cytoplasmic bodies. It appears to function as a E3 ubiquitin-ligase and ubiqutinates itself to regulate its subcellular localization. It may play a role in retroviral restriction. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene. [provided by RefSeq, Dec 2009] (from NCBI)
Top mentioned proteins: CAN, Trim, Peptidylprolyl Isomerase, ACID, APOBEC3G
Papers on TRIM5alpha
TRIM5α degradation via autophagy is not required for retroviral restriction.
Campbell et al., Maywood, United States. In J Virol, Feb 2016
Collectively, these results are consistent with observations that the turnover of TRIM5α proteins is sensitive to autophagy inhibition; however the data presented here do not support observations that the inhibition of autophagy abrogates retroviral restriction by TRIM5 proteins.
TRIM5alpha-mediated ubiquitin chain conjugation is required for inhibition of HIV-1 reverse transcription and capsid destabilization.
Bouamr et al., Maywood, United States. In J Virol, Jan 2016
UNASSIGNED: Rhesus macaque TRIM5α (rhTRIM5α) is a retroviral restriction factor, which inhibits HIV-1 infection.
Tripartite Motif (TRIM) 12c, a Mouse Homolog of TRIM5, Is a Ubiquitin Ligase That Stimulates Type I IFN and NF-κB Pathways along with TNFR-Associated Factor 6.
Ozato et al., Bethesda, United States. In J Immunol, Jan 2016
Tripartite motif (TRIM) protein TRIM5 of the primate species restricts replication of HIV and other retroviruses.
Increased expression and dysregulated association of restriction factors and type I interferon in HIV, HCV mono- and co-infected patients.
Zheng et al., Kunming, China. In J Med Virol, Dec 2015
The results showed that HCV, HIV mono- and co-infection differentially increased TRIM22, APOBEC3G and IFN-α, -β mRNA expression while the mRNA expression of TRIM5 was upregulated only by HCV-mono infection.
The innate immune roles of host factors TRIM5α and Cyclophilin A on HIV-1 replication.
Zheng et al., Kaifeng, China. In Med Microbiol Immunol, Oct 2015
Interestingly, Cyclophilin A is retrotransposed into the critical host gene, TRIM5, locus via LINE-1 element in some primate species including New World monkeys and Old World monkeys.
An overview of the lagomorph immune system and its genetic diversity.
Esteves et al., Porto, Portugal. In Immunogenetics, Oct 2015
Regarding innate immunity, we review the most recent advances in identifying interleukins, chemokines and chemokine receptors, Toll-like receptors, antiviral proteins (RIG-I and Trim5), and the genes encoding fucosyltransferases that are utilized by rabbit hemorrhagic disease virus as a portal for invading host respiratory and gut epithelial cells.
Impact of TRIM5α in vivo.
Shioda et al., Ōsaka, Japan. In Aids, Oct 2015
Genetic manipulation of the human TRIM5 gene could establish human cells totally resistant to HIV-1, which may lead to a cure for HIV-1 infection in the future.
HIV suppression by host restriction factors and viral immune evasion.
Xiong et al., New Haven, United States. In Curr Opin Struct Biol, Apr 2015
Here we review the recent developments towards establishing the structural and biochemical bases of HIV inhibition by, and viral countermeasures of, the restriction factors TRIM5, MxB, APOBEC3, SAMHD1, and BST2/tetherin.
TRIM5 Retroviral Restriction Activity Correlates with the Ability To Induce Innate Immune Signaling.
Luban et al., Genève, Switzerland. In J Virol, 2014
UNLABELLED: Host restriction factor TRIM5 inhibits retroviral transduction in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed.
Trans-species polymorphism in humans and the great apes is generally maintained by balancing selection that modulates the host immune response.
Cooper et al., Porto, Portugal. In Hum Genomics, 2014
To date, putative TSPs between humans and other primate species have been identified for the highly polymorphic major histocompatibility complex (MHC), the histo-blood ABO group, two antiviral genes (ZC3HAV1 and TRIM5), an autoimmunity-related gene LAD1 and several non-coding genomic segments with a putative regulatory role.
Human MX2 is an interferon-induced post-entry inhibitor of HIV-1 infection.
Malim et al., London, United Kingdom. In Nature, 2013
For the pathogenic retrovirus human immunodeficiency virus type 1 (HIV-1), these include widely expressed restriction factors, such as APOBEC3 proteins, TRIM5-α, BST2 (refs 4, 5) and SAMHD1 (refs 6, 7), as well as additional factors that are stimulated by type 1 interferon (IFN).
Intrinsic cellular defenses against human immunodeficiency viruses.
Bieniasz et al., New York City, United States. In Immunity, 2012
Among these are several classes of proteins (APOBEC3, TRIM5, Tetherin, and SAMHD1) that inhibit the replication of human and simian immunodeficiency viruses.
TRIM5 structure, HIV-1 capsid recognition, and innate immune signaling.
Luban et al., Zürich, Switzerland. In Curr Opin Virol, 2012
TRIM5 is a restriction factor that blocks retrovirus infection soon after the virion core enters the cell cytoplasm. Restriction activity is targeted to the virion core via recognition of the capsid protein lattice that encases the viral genomic RNA.[Review]
Gag cytotoxic T lymphocyte escape mutations can increase sensitivity of HIV-1 to human TRIM5alpha, linking intrinsic and acquired immunity.
Hance et al., Paris, France. In J Virol, 2011
findings suggest that Gag cytotoxic T lymphocyte mutations may influence HIV-1 replication by modifying both viral infectivity and sensitivity to TRIM5alpha
TRIM5 acts as more than a retroviral restriction factor.
Wu et al., Columbus, United States. In Viruses, 2011
Findings have defined a novel function for TRIM5 as a pattern recognition receptor in innate immune recognition and provided valuable mechanistic insight into its role as a retroviral restriction factor.
Caging the beast: TRIM5α binding to the HIV-1 core.
Diaz-Griffero, United States. In Viruses, 2011
TRIM5alpha "cages" the HIV-1 core by forming an hexagonal array on the surface of the viral capsid.
TRIM5 is an innate immune sensor for the retrovirus capsid lattice.
Luban et al., Genève, Switzerland. In Nature, 2011
the retroviral restriction factor TRIM5 has two additional activities that are linked to restriction: it constitutively promotes innate immune signalling and it acts as a pattern recognition receptor specific for the retrovirus capsid lattice
TRIM5α associates with proteasomal subunits in cells while in complex with HIV-1 virions.
Campbell et al., Maywood, United States. In Retrovirology, 2010
Proteasomal subunits are present in rhTRIM5alpha assemblies containing HIV-1 virions.
Restriction of an extinct retrovirus by the human TRIM5alpha antiviral protein.
Emerman et al., Seattle, United States. In Science, 2007
TRIM5 alpha may have protected early humans from invasion by Pan troglodytes endogenous retrovirus
Rhesus monkey TRIM5alpha restricts HIV-1 production through rapid degradation of viral Gag polyproteins.
Ikeda et al., Rochester, United States. In Nat Med, 2007
Tripartite motif-containing 5 isoform-alpha (TRIM5alpha) protein from rhesus monkey (TRIM5alpharh) restricts human immunodeficiency virus type 1 (HIV-1) infection at a postentry, preintegration stage in the viral life cycle, by recognizing the incoming capsid and promoting its premature disassembly.
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