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Small-molecule covalent bond formation at tyrosine creates a binding site and inhibits activation of Ral GTPases [Biochemistry]
Proceedings of the National Academy of Sciences of the United States of America ( IF 9.4 ) Pub Date : 2020-03-31
Khuchtumur Bum-Erdene, Degang Liu, Giovanni Gonzalez-Gutierrez, Mona K. Ghozayel, David Xu, Samy O. Meroueh

Ral (Ras-like) GTPases are directly activated by oncogenic Ras GTPases. Mutant K-Ras (G12C) has enabled the development of covalent K-Ras inhibitors currently in clinical trials. However, Ral, and the overwhelming majority of mutant oncogenic K-Ras, are devoid of a druggable pocket and lack an accessible cysteine for the development of...

中文翻译:

酪氨酸上的小分子共价键形成会形成结合位点,并抑制Ral GTPases的激活[生物化学]

Ral(类Ras)GTPases由致癌性Ras GTPases直接激活。突变K-Ras(G12C)使目前临床试验中的共价K-Ras抑制剂得以开发。但是,Ral和绝大多数的致癌突变K-Ras缺乏可药用的口袋,并且缺乏可开发的半胱氨酸。
更新日期:2020-03-31
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