Rahimi, Marwa N. published the artcileProtein-protein inhibitor designed de novo to target the MEEVD region on the C-terminus of Hsp90 and block co-chaperone activity, Quality Control of 42074-68-0, the publication is Chemical Communications (Cambridge, United Kingdom) (2019), 55(6), 846-849, database is CAplus and MEDLINE.
Protein-protein interactions control all cellular functions. Presented is the 1st de novo designed protein-protein interaction inhibitor that targets the C-terminus of heat shock protein 90 (Hsp90) and blocks co-chaperones from binding. Compound LB76, which was created from an Hsp90 co-chaperone, selectively pulls down Hsp90 from cell lysates, binds to Hsp90’s C-terminal domain, and blocks the interactions between Hsp90 and TPR-containing co-chaperones. Through these interactions, LB76 inhibits the protein-folding function of Hsp90. Blocking these protein-protein interactions between Hsp90 and C-terminal co-chaperones regulate the cell’s entire protein-folding machinery.
Chemical Communications (Cambridge, United Kingdom) 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.
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Chlorides – an overview | ScienceDirect Topics