The concept of a prion as an infectious self-propagating protein isoform was initially
proposed to explain certain mammalian diseases. It is now clear that yeast also has …

Due to their ultra-small size, nanoparticles (NPs) have distinct properties compared with the
bulk form of the same materials. These properties are rapidly revolutionizing many areas of …

Most vertebrate oocytes contain a Balbiani body, a large, non-membrane-bound
compartment packed with RNA, mitochondria, and other organelles. Little is known about …

Prions are proteins that convert between structurally and functionally distinct states, one or
more of which is transmissible. In yeast, this ability allows them to act as non-Mendelian …

Amyloid-β (Aβ) deposits are a relatively late consequence of Aβ aggregation in Alzheimer's
disease. When pathogenic Aβ seeds begin to form, propagate and spread is not known, nor …

Mutations in TARDBP, encoding TAR DNA-binding protein-43 (TDP-43), are associated with
TDP-43 proteinopathies, including amyotrophic lateral sclerosis (ALS) and frontotemporal …

Protein misfolding is intimately associated with devastating human neurodegenerative
diseases, including Alzheimer's, Huntington's, and Parkinson's. Although disparate in their …

Aggregates of the RNA-binding protein TDP-43 (TAR DNA-binding protein) are a hallmark of
the overlap** neurodegenerative disorders amyotrophic lateral sclerosis (ALS) and …

Expansion of a polyglutamine tract in the androgen receptor (AR) causes spinal and bulbar
muscular atrophy (SBMA). We previously showed that Akt-mediated phosphorylation of AR …

Amyloid aggregation is associated with numerous protein misfolding pathologies and
underlies the infectious properties of prions, which are conformationally self-templating …