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・ Triethylamine
・ Triethylammonium acetate
・ Triethylborane
・ Triethylcholine
・ Triethylene glycol
・ Triethylene glycol dimethyl ether
・ Triethylene glycol dinitrate
・ Triethylenemelamine
・ Triethylenetetramine
・ Triethylgallium
・ Triethyloxonium tetrafluoroborate
・ Triethylsilane
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TRIF
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TRIF : ウィキペディア英語版
TRIF

TIR-domain-containing adapter-inducing interferon-β (TRIF) is an adapter in responding to activation of toll-like receptors (TLRs). It mediates the rather delayed cascade of two TLR-associated signaling cascades, where the other one is dependent upon a MyD88 adapter.〔Palsson-McDermott, Eva and Luke A J O’Neill (2004) Immunology. 113(2) 153-162〕
Toll-like receptors (TLRs) recognize specific components of microbial invaders and activate an immune response to these pathogens. After these receptors recognize highly-conserved pathogenic patterns, a downstream signaling cascade is activated in order to stimulate the release of inflammatory cytokines and chemokines as well as to upregulate the expression of immune cells. All TLRs have a TIR domain that initiates the signaling cascade through TIR adapters. Adapters are platforms that organize downstream signaling cascades leading to a specific cellular response after exposure to a given pathogen.
== Structure ==
TRIF is primarily active in the spleen and is often regulated when MyD88 is deficient in the liver, indicating organ-specific regulation of signaling pathways. Curiously, there is a lack of redundancy within the TLR4 signaling pathway that leads to microbial evasion of immune response in the host after mutations occur within intermediates of the pathway.〔Palsson-McDermott, Eva and Luke A J O’Neill (2004) Immunology. 113(2) 153-162〕 Three TRAF-binding motifs present in the amino terminal region of TRIF are necessary for association with TRAF6. Destruction of these motifs reduced the activation of NF-κβ, a transcription factor that is also activated by the carboxy-terminal domain of TRIF in the upregulation of cytokines and co-stimulatory immune molecules. This domain recruits receptor-interacting protein (RIP1) and RIP3 through the RIP homotypic interaction motif. Cells deficient for RIP1 gene display attenuated TLR3 activation of NF-κβ, indicating the use of the RIP1 gene in downstream TRIF activation, in contrast to other TLRs that use IRAK protein for the activation of NF-κβ.〔Kawai, Taro and Shizuo Akira. (2004). Arthritis Res. Ter. 7(1) 12-19〕


抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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