与活化的TICAM-1特异性相互作用的蛋白质数据集。
The dataset of proteins specifically interacted with activated TICAM-1.
作者信息
Funami Kenji, Matsumoto Misako, Oshiumi Hiroyuki, Obuse Chikashi, Seya Tsukasa
机构信息
Department of Microbiology and Immunology, Graduate School of Medicine, Hokkaido University, Sapporo 060-8638, Japan.
Department of Microbiology and Immunology, Graduate School of Medicine, Hokkaido University, Sapporo 060-8638, Japan; Division of Molecular Life Science, Graduate School of Life Science, Hokkaido University, Sapporo 001-0021, Japan.
出版信息
Data Brief. 2016 Jun 28;8:697-9. doi: 10.1016/j.dib.2016.06.030. eCollection 2016 Sep.
The presented data are related with our paper entitled "14-3-3-zeta participates in TLR3-mediated TICAM-1 signal-platform formation" (Funami et al., 2016) [1]. These data show the proteins which specifically bind to the activated (oligomerized) TICAM-1. Fifty-three proteins were identified as specifically interacted with oligomerized TICAM-1. Mutant TICAM-1 cannot form the active oligomer, so the proteins interacted with mutant TICAM-1 are dispensable for TICAM-1-signaling. Among 53 proteins, 14-3-3-zeta specifically interacts with oligomerized TICAM-1 to corroborate TICAM-1 signalosome.
所呈现的数据与我们发表的题为《14-3-3-ζ参与Toll样受体3介导的TICAM-1信号平台形成》（舟见等人，2016年）[1]的论文相关。这些数据展示了与活化的（寡聚化的）TICAM-1特异性结合的蛋白质。53种蛋白质被鉴定为与寡聚化的TICAM-1特异性相互作用。突变型TICAM-1不能形成活性寡聚体，因此与突变型TICAM-1相互作用的蛋白质对于TICAM-1信号传导是可有可无的。在这53种蛋白质中，14-3-3-ζ与寡聚化的TICAM-1特异性相互作用，以证实TICAM-1信号体。
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