Hsp104 is a hexameric AAA+ ATPase and protein disaggregase found in yeast, which
couples ATP hydrolysis to the dissolution of diverse polypeptides trapped in toxic …

Numerous ATPases associated with diverse cellular activities (AAA+) proteins form
hexameric, ring-shaped complexes that function via ATPase-coupled translocation of …

Protein misfolding and aggregation underpin several fatal neurodegenerative diseases,
including Parkinson's disease (PD), amyotrophic lateral sclerosis (ALS), and frontotemporal …

Protein aggregation, once believed to be a harbinger and/or consequence of stress, age,
and pathological conditions, is emerging as a novel concept in cellular regulation. Normal …

In recent years, application of serine integrases for genomic engineering has increased in
popularity. The factor-independence and unidirectionality of these large serine …

Proteins have to be folded to their native structures to be functionally expressed. Misfolded
proteins are proteotoxic and negatively impact on cellular fitness. To maintain the proteome …

It is widely known that α-synuclein (aSyn) is an amyloidogenic protein prone to aggregation.
This protein is found in specific inclusions named Lewy bodies in the surviving neurons of …