Nielsen, Alexander L. published the artcileMechanism-based inhibitors of SIRT2: structure-activity relationship, X-ray structures, target engagement, regulation of α-tubulin acetylation and inhibition of breast cancer cell migration, Quality Control of 42074-68-0, the publication is RSC Chemical Biology (2021), 2(2), 612-626, database is CAplus and MEDLINE.
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 biol. 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 chem. probes that are potent, selective, stable in serum, water-soluble, and inhibit SIRT2-mediated deacetylation and demyristoylation in cells. 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.
RSC Chemical Biology published new progress about 42074-68-0. 42074-68-0 belongs to chlorides-buliding-blocks, auxiliary class Chloride,Benzyl chloride,Benzene, name is 2-Chlorotrityl chloride, and the molecular formula is C19H14Cl2, Quality Control of 42074-68-0.
Referemce:
https://en.wikipedia.org/wiki/Chloride,
Chlorides – an overview | ScienceDirect Topics