Full atomistic model of prion structure and conversion
Prions are unusual protein assemblies that propagate their conformationally-encoded
information in absence of nucleic acids. The first prion identified, the scrapie isoform (PrPSc) …
information in absence of nucleic acids. The first prion identified, the scrapie isoform (PrPSc) …
General principles underpinning amyloid structure
AIP Taylor, RA Staniforth - Frontiers in Neuroscience, 2022 - frontiersin.org
Amyloid fibrils are a pathologically and functionally relevant state of protein folding, which is
generally accessible to polypeptide chains and differs fundamentally from the globular state …
generally accessible to polypeptide chains and differs fundamentally from the globular state …
Protein nanofibrils and their use as building blocks of sustainable materials
The development towards a sustainable society requires a radical change of many of the
materials we currently use. Besides the replacement of plastics, derived from petrochemical …
materials we currently use. Besides the replacement of plastics, derived from petrochemical …
Structures of brain-derived 42-residue amyloid-β fibril polymorphs with unusual molecular conformations and intermolecular interactions
M Lee, WM Yau, JM Louis… - Proceedings of the …, 2023 - National Acad Sciences
Fibrils formed by the 42-residue amyloid-β peptide (Aβ42), a main component of amyloid
deposits in Alzheimer's disease (AD), are known to be polymorphic, ie, to contain multiple …
deposits in Alzheimer's disease (AD), are known to be polymorphic, ie, to contain multiple …
Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases
DJ Rinauro, F Chiti, M Vendruscolo… - Molecular …, 2024 - Springer
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 …
50 human disorders, including Alzheimer's and Parkinson's diseases. Increasing evidence …
Amyloid β 42 fibril structure based on small-angle scattering
Amyloid fibrils are associated with a number of neurodegenerative diseases, including fibrils
of amyloid β42 peptide (Aβ42) in Alzheimer's disease. These fibrils are a source of toxicity to …
of amyloid β42 peptide (Aβ42) in Alzheimer's disease. These fibrils are a source of toxicity to …
Structure-based inhibitors of amyloid beta core suggest a common interface with tau
Alzheimer's disease (AD) pathology is characterized by plaques of amyloid beta (Aβ) and
neurofibrillary tangles of tau. Aβ aggregation is thought to occur at early stages of the …
neurofibrillary tangles of tau. Aβ aggregation is thought to occur at early stages of the …
Amyloid fibril polymorphism: a challenge for molecular imaging and therapy
M Fändrich, S Nyström, KPR Nilsson… - Journal of Internal …, 2018 - Wiley Online Library
The accumulation of misfolded proteins (MP s), both unique and common, for different
diseases is central for many chronic degenerative diseases. In certain patients, MP …
diseases is central for many chronic degenerative diseases. In certain patients, MP …
Green Tea Extracts EGCG and EGC Display Distinct Mechanisms in Disrupting Aβ42 Protofibril
The amyloid beta (Aβ) fibrillar aggregate is the hallmark of Alzheimer's disease (AD).
Disassembling preformed fibril or inhibiting Aβ aggregation is considered as a therapeutic …
Disassembling preformed fibril or inhibiting Aβ aggregation is considered as a therapeutic …
Zinc ion rapidly induces toxic, off-pathway amyloid-β oligomers distinct from amyloid-β derived diffusible ligands in Alzheimer's disease
Alzheimer's disease (AD) is the most prevalent neurodegenerative disease in the elderly.
Zinc (Zn) ion interacts with the pathogenic hallmark, amyloid-β (Aβ), and is enriched in …
Zinc (Zn) ion interacts with the pathogenic hallmark, amyloid-β (Aβ), and is enriched in …