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Backbone and side-chain chemical shift assignments of a cellular FLICE-inhibitory protein (c-FLIPS).
Biomolecular NMR Assignments ( IF 0.9 ) Pub Date : 2020-06-06 , DOI: 10.1007/s12104-020-09953-8
Zhi-Qiang Bai 1, 2, 3 , Bin Liu 1, 3 , Xiaofang Ma 2 , Kaifeng Hu 1, 2
Affiliation  

Cellular FLICE-inhibitory protein (c-FLIP), which is involved in regulating the apoptosis of the extrinsic cell death pathway contains two death effector domains (DED). There are several splicing variants including short-form (c-FLIPS) and long-form (c-FLIPL). The death-inducing signaling complex (DISC) initiates apoptosis and programmed necrosis, DISC assembly and activation are regulated by c-FLIP. Here we report the NMR chemical shift assignments of c-FLIPs, which pave the way for investigating the molecular basis of the anti-apoptotic function of c-FLIPS.

中文翻译:

细胞 FLICE 抑制蛋白 (c-FLIPS) 的骨架和侧链化学位移分配。

参与调节外源性细胞死亡途径的细胞凋亡的细胞 FLICE 抑制蛋白 (c-FLIP) 包含两个死亡效应结构域 (DED)。有几种剪接变体,包括短形式 (c-FLIP S ) 和长形式 (c-FLIP L )。死亡诱导信号复合物 (DISC) 启动细胞凋亡和程序性坏死,DISC 组装和激活受 c-FLIP 调节。在这里,我们报告了 c-FLIPs 的 NMR 化学位移分配,这为研究 c-FLIP S抗凋亡功能的分子基础铺平了道路。
更新日期:2020-06-06
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