Ontology highlight
ABSTRACT:
SUBMITTER: Shahmoradian SH
PROVIDER: S-EPMC3707056 | biostudies-literature | 2013 Jul
REPOSITORIES: biostudies-literature
Shahmoradian Sarah H SH Galaz-Montoya Jesus G JG Schmid Michael F MF Cong Yao Y Ma Boxue B Spiess Christoph C Frydman Judith J Ludtke Steven J SJ Chiu Wah W
eLife 20130709
In Huntington's disease, a mutated version of the huntingtin protein leads to cell death. Mutant huntingtin is known to aggregate, a process that can be inhibited by the eukaryotic chaperonin TRiC (TCP1-ring complex) in vitro and in vivo. A structural understanding of the genesis of aggregates and their modulation by cellular chaperones could facilitate the development of therapies but has been hindered by the heterogeneity of amyloid aggregates. Using cryo-electron microscopy (cryoEM) and singl ...[more]