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Evidence for ProT alpha-TLR4/MD-2 binding: molecular dynamics and gravimetric assay studies

机译:ProT alpha-TLR4 / MD-2结合的证据:分子动力学和重量分析研究

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Objective: During preconditioning, lipopolysaccharide (LPS) selectively activates TLR4/MD-2/Toll/IL-1 receptor-domain-containing adaptor inducing IFN-beta (TRIF) pathway instead of pro-inflammatory myeloid differentiation protein-88 (MyD88)/MyD88-adaptor-like protein (MAL) pathway. Extracellular prothymosin alpha (ProT alpha) is also known to selectively activate the TLR4/MD2/TRIF-IRF3 pathway in certain diseased conditions. In the current study, biophysical evidence for ProT alpha/TLR4/MD-2 complex formation and its interaction dynamics have been studied.
机译:目的:在预处理过程中,脂多糖(LPS)选择性激活包含TLR4 / MD-2 / Toll / IL-1受体域的衔接子,从而诱导IFN-β(TRIF)途径,而不是促炎性髓样分化蛋白88(MyD88)/ MyD88适配器样蛋白(MAL)途径。还已知细胞外胸腺肽α(ProT alpha)在某些疾病条件下选择性激活TLR4 / MD2 / TRIF-IRF3途径。在当前的研究中,已经研究了ProT alpha / TLR4 / MD-2复合物形成及其相互作用动力学的生物物理证据。

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