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Updated: Jun 10, 2025

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结构导向的符合性限制导致高亲和度,选择性和细胞活性四化诺胺基非共价Keap1-Nrf2抑制剂

Yuting Qin1, Cecilie Poulsen2, Dilip Narayanan1

  • 1Department of Drug Design and Pharmacology, Faculty of Health and Medical Sciences, University of Copenhagen, Universitetsparken 2, DK-2100 Copenhagen, Denmark.

Journal of medicinal chemistry
|October 17, 2024
PubMed
概括

研究人员开发了新的基于四化类昆的化合物,可以强烈抑制Keap1-Nrf2相互作用,为治疗氧化应激疾病提供了有前途的策略.

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Regulation of the Unfolded Protein Response01:31

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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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