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Nhan đề : Mechanism-based inhibitors of SIRT2: structure–activity relationship, Xray structures, target engagement, egulation of a-tubulin acetylation and inhibition of breast cancer cell migration†
Tác giả : Nielsen, Alexander L.
Từ khoá : Sirtuin; SIRT2; Cấu trúc tinh thể; Posttranslational modification; Inhibitor; Crystal structure
Năm xuất bản : 2020
Tóm tắt : Sirtuin 2 (SIRT2) is a protein deacylase enzyme that removes acetyl groups and longer chain acyl groups from post-translationally modified lysine residues. It affects diverse biological functions in the cell and has been considered a drug target in relation to both neurodegenerative diseases and cancer. Therefore, access to well-characterized and robust tool compounds is essential for the continued investigation of the complex functions of this enzyme. Here, we report a collection of probes that are potent, selective, stable in serum, water-soluble, amenable to cell culture experiments, and inhibit both SIRT2 deacetylation and demyristoylation. Compared to the current landscape of SIRT2 inhibitors, this is a unique ensemble of features built into a single compound. We expect the developed chemotypes to find broad application in the interrogation of SIRT2 functions in both healthy and diseased cells, and to provide a foundation for the development of future therapeutics.
URI: http://dlib.hust.edu.vn/handle/HUST/23976
Liên kết tài liệu gốc: https://www.biorxiv.org/content/10.1101/2020.03.20.000380v2
Trong bộ sưu tập: OER - Kỹ thuật hóa học; Công nghệ sinh học - Thực phẩm; Công nghệ môi trường
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