Ontology highlight
ABSTRACT:
SUBMITTER: Chen JJ
PROVIDER: S-EPMC5108364 | biostudies-literature | 2016 Oct
REPOSITORIES: biostudies-literature
Chen John J JJ Genereux Joseph C JC Suh Eul Hyun EH Vartabedian Vincent F VF Rius Bibiana B Qu Song S Dendle Maria T A MTA Kelly Jeffery W JW Wiseman R Luke RL
Cell chemical biology 20161006 10
Transthyretin (TTR) is a tetrameric serum protein associated with multiple systemic amyloid diseases. In these disorders, TTR aggregates in extracellular environments through a mechanism involving rate-limiting dissociation of the tetramer to monomers, which then misfold and aggregate into soluble oligomers and amyloid fibrils that induce toxicity in distal tissues. Using an assay established herein, we show that highly destabilized, aggregation-prone TTR variants are secreted as both native tet ...[more]