Molecular mechanisms of amyloid formation in living systems
T Sinnige - Chemical Science, 2022 - pubs.rsc.org
Fibrillar protein aggregation is a hallmark of a variety of human diseases. Examples include
the deposition of amyloid-β and tau in Alzheimer's disease, and that of α-synuclein in …
the deposition of amyloid-β and tau in Alzheimer's disease, and that of α-synuclein in …
Novel targeted therapies for Parkinson's disease
T Ntetsika, PE Papathoma, I Markaki - Molecular Medicine, 2021 - Springer
Parkinson's disease (PD) is the second more common neurodegenerative disease with
increasing incidence worldwide associated to the population ageing. Despite increasing …
increasing incidence worldwide associated to the population ageing. Despite increasing …
Sequence grammar underlying the unfolding and phase separation of globular proteins
Aberrant phase separation of globular proteins is associated with many diseases. Here, we
use a model protein system to understand how the unfolded states of globular proteins drive …
use a model protein system to understand how the unfolded states of globular proteins drive …
Acute intermittent porphyria: an overview of therapy developments and future perspectives focusing on stabilisation of HMBS and proteostasis regulators
HJ Bustad, JP Kallio, M Vorland, V Fiorentino… - International Journal of …, 2021 - mdpi.com
Acute intermittent porphyria (AIP) is an autosomal dominant inherited disease with low
clinical penetrance, caused by mutations in the hydroxymethylbilane synthase (HMBS) …
clinical penetrance, caused by mutations in the hydroxymethylbilane synthase (HMBS) …
Structural basis of huntingtin fibril polymorphism revealed by cryogenic electron microscopy of exon 1 HTT fibrils
The lack of detailed insight into the structure of aggregates formed by the huntingtin protein
(HTT) has hampered the efforts to develop therapeutics and diagnostics targeting pathology …
(HTT) has hampered the efforts to develop therapeutics and diagnostics targeting pathology …
Capturing the conversion of the pathogenic alpha-1-antitrypsin fold by ATF6 enhanced proteostasis
Genetic variation in alpha-1 antitrypsin (AAT) causes AAT deficiency (AATD) through liver
aggregation-associated gain-of-toxic pathology and/or insufficient AAT activity in the lung …
aggregation-associated gain-of-toxic pathology and/or insufficient AAT activity in the lung …
Potential application of heat shock proteins as therapeutic targets in Parkinson's disease
H Guo, J Yi, F Wang, T Lei, H Du - Neurochemistry International, 2023 - Elsevier
Parkinson's disease (PD) is a common chronic neurodegenerative disease, and the heat
shock proteins (HSPs) are proved to be of great value for PD. In addition, HSPs can maintain …
shock proteins (HSPs) are proved to be of great value for PD. In addition, HSPs can maintain …
Therapeutic strategies to reduce the toxicity of misfolded protein oligomers
RP Kreiser, AK Wright, NR Block, JE Hollows… - International journal of …, 2020 - mdpi.com
The aberrant aggregation of proteins is implicated in the onset and pathogenesis of a wide
range of neurodegenerative disorders, including Alzheimer's and Parkinson's diseases …
range of neurodegenerative disorders, including Alzheimer's and Parkinson's diseases …
Supersaturation, a critical factor underlying proteostasis of amyloid fibril formation
From a physicochemical viewpoint, amyloid fibril formation is a phase transition from soluble
to crystal-like sates limited by supersaturation. It occurs only above solubility (ie, the …
to crystal-like sates limited by supersaturation. It occurs only above solubility (ie, the …
Extracellular chaperone networks and the export of J-domain proteins
JEA Braun - Journal of Biological Chemistry, 2023 - ASBMB
An extracellular network of molecular chaperones protects a diverse array of proteins that
reside in or pass through extracellular spaces. Proteins in the extracellular milieu face …
reside in or pass through extracellular spaces. Proteins in the extracellular milieu face …