Hsp70 chaperone machineries have pivotal roles in an array of fundamental biological
processes through their facilitation of protein folding, disaggregation, and remodeling. The …

Aberrant accumulation of misfolded proteins into amyloid deposits is a hallmark in many age-
related neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's …

Protein phase separation is implicated in formation of membraneless organelles, signaling
puncta and the nuclear pore. Multivalent interactions of modular binding domains and their …

Expanded CAG repeats lead to debilitating neurodegenerative disorders characterized by
aggregation of proteins with expanded polyglutamine (polyQ) tracts. The mechanism of …

Although Huntington's disease (HD) is a well studied Mendelian genetic disorder, less is
known about its associated epigenetic changes. Here, we characterize DNA methylation …

Maintenance of protein homeostasis is vitally important in post-mitotic cells, particularly
neurons. Neurodegenerative diseases such as polyglutamine expansion disorders—like …

The Hsp70 family of chaperones works with its co-chaperones, the nucleotide exchange
factors and J-domain proteins, to facilitate a multitude of cellular functions. Central players in …

Detailed understanding of the mechanism by which Hsp70 chaperones protect cells against
protein aggregation is hampered by the lack of a comprehensive characterization of the …

The most common inherited cause of two genetically and clinico-pathologically overlap**
neurodegenerative diseases, amyotrophic lateral sclerosis (ALS) and frontotemporal …

Protein aggregation is a hallmark of neurodegeneration. Here, we find that Huntington's
disease-related HTT-polyQ aggregation induces a cellular proteotoxic stress response …