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anti-Human TRIM5 Antikörper:
anti-Mouse (Murine) TRIM5 Antikörper:
anti-Rat (Rattus) TRIM5 Antikörper:
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Human Monoclonal TRIM5 Primary Antibody für IHC, ELISA - ABIN969443
Keckesova, Ylinen, Towers: The human and African green monkey TRIM5alpha genes encode Ref1 and Lv1 retroviral restriction factor activities. in Proceedings of the National Academy of Sciences of the United States of America 2004
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Human Polyclonal TRIM5 Primary Antibody für IHC, ELISA - ABIN1003380
Reymond, Meroni, Fantozzi, Merla, Cairo, Luzi, Riganelli, Zanaria, Messali, Cainarca, Guffanti, Minucci, Pelicci, Ballabio: The tripartite motif family identifies cell compartments. in The EMBO journal 2001
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Human Polyclonal TRIM5 Primary Antibody für IHC, ELISA - ABIN1003379
Xu, Yang, Moitra, Hashimoto, Rallabhandi, Kaul, Meroni, Jensen, Weissman, DArpa: BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. in Experimental cell research 2003
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Human Monoclonal TRIM5 Primary Antibody für IHC, WB - ABIN967208
Stremlau, Owens, Perron, Kiessling, Autissier, Sodroski: The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys. in Nature 2004
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Human Polyclonal TRIM5 Primary Antibody für FM, ELISA - ABIN1003377
Hatziioannou, Perez-Caballero, Yang, Cowan, Bieniasz: Retrovirus resistance factors Ref1 and Lv1 are species-specific variants of TRIM5alpha. in Proceedings of the National Academy of Sciences of the United States of America 2004
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Human Polyclonal TRIM5 Primary Antibody für ELISA, ICC - ABIN4362500
Li, Yeung, Fiegen, Sodroski: Determinants of the higher order association of the restriction factor TRIM5alpha and other tripartite motif (TRIM) proteins. in The Journal of biological chemistry 2011
Human Polyclonal TRIM5 Primary Antibody für IHC, IHC (p) - ABIN4362497
Sandler, Bosinger, Estes, Zhu, Tharp, Boritz, Levin, Wijeyesinghe, Makamdop, del Prete, Hill, Timmer, Reiss, Yarden, Darko, Contijoch, Todd, Silvestri, Nason, Norgren, Keele, Rao, Langer, Lifson et al.: Type I interferon responses in rhesus macaques prevent SIV infection and slow disease progression. ... in Nature 2014
The Sylvilagus TRIM5 alpha was 91% identical to the Oryctolagus protein.
TRIM5 and TRIM22 (zeige TRIM22 Antikörper) 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 (zeige CD209 Antikörper)+ 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 (zeige PML Antikörper) and also interacts with TRIM5alpha
TRIM5alpha variations influence transduction efficiency with lentiviral vectors in both human and rhesus CD34 (zeige CD34 Antikörper)(+) 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.
High resolution crystal structure of a Trim5Alpha dimeric Bbox (zeige BBOX1 Antikörper) domain.
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 (zeige SUMO1 Antikörper) and SUMO 2 (zeige SUMO2 Antikörper) 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.
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