Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
The Sylvilagus TRIM5 alpha was 91% identical to the Oryctolagus protein.
TRIM5 and TRIM22 (show TRIM22 Proteins) single nucleotide polymorphisms are associated to increased odds of significant liver fibrosis and sustained virological response after pegIFNalpha/RBV therapy in human immunodeficiency virus/hepatitis C virus coinfected patients.
TRIM5alpha polymorphisms were associated with proviral loads, indicating that TRIM5alpha could be implicated in HTLV-1 replication.
TRIM5alpha potently restricts HIV-1 infection of Langerhans cells but not of subepithelial DC-SIGN (show CD209 Proteins)+ dendritic cells
Collectively, these results are consistent with observations that the turnover of TRIM5alpha 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.
This meta-analysis indicates that TRIM5alpha H43Y polymorphism is associated with a decreased risk of HIV-1 infection in the homozygote comparison and recessive model.
higher-order oligomerization of TRIM5alpha, which is promoted by the interaction with the retroviral capsid, enhances the E3 Ub ligase activity of TRIM5alpha and contributes to its antiretroviral function.
TRIM5alpha requires Ube2W to anchor Lys63-linked ubiquitin chains and restrict reverse transcription.
co-immunoprecipitation experiments demonstrate that IE1CORE binds via the coiled-coil domain to PML (show PML Proteins) and also interacts with TRIM5alpha
TRIM5alpha variations influence transduction efficiency with lentiviral vectors in both human and rhesus CD34 (show CD34 Proteins)(+) cells in vitro and in vivo.
TRIM5 acts as a selective autophagy receptor. Based on direct sequence-specific recognition, TRIM5 delivered its cognate cytosolic target, a viral capsid protein, for autophagic degradation. Thus, our study establishes that TRIMs can function both as regulators of autophagy and as autophagic cargo receptors, and reveals a basis for selective autophagy in mammalian cells.
L2 region of the TRIM5alpha dimer undergoes dynamic conformational changes, which results in the displacement of L2 regions by 25 angstroms relative to each other.
Mutations in gag and pol are associated with escape of HIV-1 from rhTrim5alpha.
These studies provide direct evidence that ubiquitin conjugation to rhTRIM5alpha-containing complexes is required for inhibition of HIV-1 Reverse Transcription and Capsid Destabilization.
These results confirm that the SUMO machinery is involved in TRIM5alpha-mediated retroviral restriction, and demonstrate that TRIM5alpha is a SUMO 1 (show SUMO1 Proteins) and SUMO 2 (show SUMO2 Proteins) substrate.
These data show that there could be some distinct HIV-1 capsid patterns to confer significant resistance to rhesus TRIM5-alpha.
Authors found that TRIM5alpha restriction significantly delayed disease progression and improved the survival rate of simian immunodeficiency virus-infected macaques.
Analysis of TRIM genotype revealed a potential role for TRIM in disease development in the central nervous system. 5 of 5 animals with the permissive TRIM5alpha genotype (TRIMQ/Q) progressed to Simian Immunodeficiency Virus Encephalitis. In contrast, 2 animals with the restrictive TRIM5alpha genotype (TRIMTFP/TFP) did not show neurologic signs, nor did they develop SIVE.
Rhesus TRIM5alpha acts as an autophagic receptor to restrict HIV-1 through autophagic degradation.
In conclusion, the TRIM5alpha sumoylation site appears to modulate the E3 ubiquitin ligase activities of the adjacent RING domain, promoting K63-linked ubiquitin chains at the expense of auto-ubiquitylation which is probably K48-linked.
The antiparallel organization of the NtD regions of Fv1 and Trim5alpha dimers correctly positions C-terminal specificity and N-terminal effector domains and facilitates stable binding to adjacent capsid hexamers in viral cores.
TRIM5alpha protein functionally resembled human TRIM5alpha, potently restricting infection by N-tropic murine leukemia virus (N-MLV) and moderately restricting human immunodeficiency virus type 1 (HIV-1) infection
SPRY domain of TRIM5alpha showed higher nonsynon/synonymous substitution ratios than the non-SPRY domain, indicating that the adaptive evolution of TRIM5alpha might be a strategy developed in defending retrovirus infection during primate evolution.
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.
tripartite motif-containing 5
, tripartite motif-containing 5 alpha
, tripartite motif-containing protein 5
, tri-partite motif protein 5
, ring finger protein 88
, tripartite motif containing 5 transcript variant iota
, tripartite motif containing 5 transcript variant kappa
, tripartite motif protein TRIM5
, tripartite motif-containing protein 5 isoform alpha
, TRIM5 alpha