当前位置: X-MOL 学术Adv. Sci. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Inflammatory Response: USP38 Couples Histone Ubiquitination and Methylation via KDM5B to Resolve Inflammation (Adv. Sci. 22/2020)
Advanced Science ( IF 14.3 ) Pub Date : 2020-11-19 , DOI: 10.1002/advs.202070122
Zhiyao Zhao , Zexiong Su , Puping Liang , Di Liu , Shuai Yang , Yaoxing Wu , Ling Ma , Junyan Feng , Xiya Zhang , Chenglei Wu , Junjiu Huang , Jun Cui

In article number 2002680, Jun Cui and co‐workers identify a new histone modifier‐USP38, that modulates histone ubiquitination and methylation to resolve inflammatory response. USP38 acts as a “Safety Machine” which shuts down the inflammation by de‐ubiquitinating histone H2B and stabilizes KDM5B to de‐methylate H3K4, which blocks the transcription of pro‐inflammatory genes. The USP38‐KDM5B complex might be a potential clinical target for therapy against inflammatory diseases.
image


中文翻译:

炎症反应:USP38通过KDM5B偶联组蛋白泛素化和甲基化以解决炎症(Adv。Sci。22/2020)

崔军及其同事在文章编号2002680中,确定了一种新的组蛋白修饰剂USP38,它可以调节组蛋白的泛素化和甲基化以解决炎症反应。USP38充当“安全机器”,通过去泛素化组蛋白H2B来关闭炎症,并使KDM5B稳定以使H3K4去甲基化,从而阻止促炎基因的转录。USP38-KDM5B复合物可能是抗炎性疾病的潜在临床靶标。
图片
更新日期:2020-11-19
down
wechat
bug