The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …

Despite advances in machine learning-based protein structure prediction, we are still far
from fully understanding how proteins fold into their native conformation. The conventional …

Hsp70 chaperones are central hubs of the protein quality control network and collaborate
with co-chaperones having a J-domain (an∼ 70-residue–long helical hairpin with a flexible …

The toxic accumulation of misfolded proteins as inclusions, fibrils, or aggregates is a
hallmark of many neurodegenerative diseases. However, how molecular chaperones, such …

Protein aggregation is a complex process resulting in the formation of heterogeneous
mixtures of aggregate populations that are closely linked to neurodegenerative conditions …

Protein misfolding and aggregation are characteristic of a wide range of neurodegenerative
disorders, including Alzheimer and Parkinson diseases. A hallmark of these diseases is the …

Soluble aggregates of the microtubule-associated protein tau have been challenging to
assemble and characterize, despite their important role in the development of tauopathies …

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

The conversion of native peptides and proteins into amyloid aggregates is a hallmark of over
50 human disorders, including Alzheimer's and Parkinson's diseases. Increasing evidence …

Protein aggregation is a hallmark of major neurodegenerative disorders. Increasing data
suggest that smaller aggregates cause higher toxic response than filamentous aggregates …