Ontology highlight
ABSTRACT:
SUBMITTER: Stothert AR
PROVIDER: S-EPMC5738387 | biostudies-literature | 2017 Dec
REPOSITORIES: biostudies-literature
Stothert Andrew R AR Suntharalingam Amirthaa A Tang Xiaolan X Crowley Vincent M VM Mishra Sanket J SJ Webster Jack M JM Nordhues Bryce A BA Huard Dustin J E DJE Passaglia Christopher L CL Lieberman Raquel L RL Blagg Brian S J BSJ Blair Laura J LJ Koren John J Dickey Chad A CA
Scientific reports 20171220 1
The heat shock protein 90 (Hsp90) family of molecular chaperones regulates protein homeostasis, folding, and degradation. The ER-resident Hsp90 isoform, glucose-regulated protein 94 (Grp94), promotes the aggregation of mutant forms of myocilin, a protein associated with primary open-angle glaucoma. While inhibition of Grp94 promotes the degradation of mutant myocilin in vitro, to date no Grp94-selective inhibitors have been investigated in vivo. Here, a Grp94-selective inhibitor facilitated muta ...[more]