The deposition of highly ordered fibrillar-type aggregates into inclusion bodies is a hallmark
of neurodegenerative diseases such as Parkinson's disease. The high stability of such …

Molecular chaperones contribute to the maintenance of cellular protein homoeostasis
through assisting de novo protein folding and preventing amyloid formation. Chaperones of …

Neurodegeneration in patients with Parkinson's disease is correlated with the occurrence of
Lewy bodies—intracellular inclusions that contain aggregates of the intrinsically disordered …

Intracellular amyloid fibrils linked to neurodegenerative disease typically accumulate in an
age-related manner, suggesting inherent cellular capacity for counteracting amyloid …

The ubiquitous heat shock protein 70 (HSP70) family consists of ATP-dependent molecular
chaperones, which perform numerous cellular functions that affect almost all aspects of the …

Intracellular aggregation of the human amyloid protein α-synuclein is causally linked to
Parkinson's disease. While the isolated protein is intrinsically disordered, its native structure …

Protein aggregation plays a crucial role in neurodegenerative diseases. A key feature of
protein aggregates is their ubiquitous modification by phosphorylation. Little is known …

Disaggregation of amyloid fibrils is a fundamental biological process required for amyloid
propagation. However, due to the lack of experimental systems, the molecular mechanism of …

The accumulation of misfolded proteins in intracellular amyloid inclusions, typical of many
neurodegenerative disorders including Huntington's and prion disease, is thought to occur …

The human molecular chaperone protein DNAJB6 was recently found to inhibit the formation
of amyloid fibrils from polyglutamine peptides associated with neurodegenerative disorders …