Ontology highlight
ABSTRACT:
SUBMITTER: Young LM
PROVIDER: S-EPMC4280571 | biostudies-literature | 2015 Jan
REPOSITORIES: biostudies-literature
Young Lydia M LM Saunders Janet C JC Mahood Rachel A RA Revill Charlotte H CH Foster Richard J RJ Tu Ling-Hsien LH Raleigh Daniel P DP Radford Sheena E SE Ashcroft Alison E AE
Nature chemistry 20141208 1
The search for therapeutic agents that bind specifically to precursor protein conformations and inhibit amyloid assembly is an important challenge. Identifying such inhibitors is difficult because many protein precursors of aggregation are partially folded or intrinsically disordered, which rules out structure-based design. Furthermore, inhibitors can act by a variety of mechanisms, including specific or nonspecific binding, as well as colloidal inhibition. Here we report a high-throughput metho ...[more]