Q-Rich Yeast Prion [PSI⁺] Accelerates Aggregation of Transthyretin, a Non-Q-Rich Human Protein.

ABSTRACT: Interactions amongst different amyloid proteins have been proposed as a probable mechanism of aggregation and thus an important risk factor for the onset as well as progression of various neurodegenerative disorders including Alzheimer's, Parkinson's, Huntington's, and Amyotrophic Lateral Sclerosis. Evidences suggest that transthyretin (TTR), a plasma protein associated with transthyretin amyloidosis or familial polyneuropathy (FAP) interacts with heterologous amyloid proteins including amyloid beta and islet amyloid polypeptide. In addition, recent clinical studies have revealed the presence of systemic polyneuropathy associated with FAP mutations in patients with spinocerebral ataxia, amyotrophic lateral sclerosis, and new familial systematic prion disease. Hence, it is important to inve

SUBMITTER: Verma M 

PROVIDER: S-EPMC5859028 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature