Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology
Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …
considered only as pathological aggregates implicated in human neurodegenerative …
Towards an understanding of amyloid-β oligomers: characterization, toxicity mechanisms, and inhibitors
Alzheimer's disease (AD) is characterized by an imbalance between production and
clearance of amyloid-β (Aβ) species. Aβ peptides can transform structurally from monomers …
clearance of amyloid-β (Aβ) species. Aβ peptides can transform structurally from monomers …
A hairpin motif in the amyloid-β peptide is important for formation of disease-related oligomers
The amyloid-β (Aβ) peptide is associated with the development of Alzheimer's disease and
is known to form highly neurotoxic prefibrillar oligomeric aggregates, which are difficult to …
is known to form highly neurotoxic prefibrillar oligomeric aggregates, which are difficult to …
[HTML][HTML] Melatonin regulates Aβ production/clearance balance and Aβ neurotoxicity: A potential therapeutic molecule for Alzheimer's disease
Y Li, J Zhang, J Wan, A Liu, J Sun - Biomedicine & Pharmacotherapy, 2020 - Elsevier
Alzheimer's disease (AD) is an age-related neurodegenerative disease with multiple
predisposing factors and complicated pathogenesis. Aβ peptide is one of the most important …
predisposing factors and complicated pathogenesis. Aβ peptide is one of the most important …
Liquid-liquid phase separation of α-synuclein: a new mechanistic insight for α-synuclein aggregation associated with Parkinson's disease pathogenesis
Aberrant aggregation of the misfolded presynaptic protein, α-Synuclein (α-Syn) into Lewy
body (LB) and Lewy neuritis (LN) is a major pathological hallmark of Parkinson's disease …
body (LB) and Lewy neuritis (LN) is a major pathological hallmark of Parkinson's disease …
Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation
SW Chen, S Drakulic, E Deas… - Proceedings of the …, 2015 - National Acad Sciences
We describe the isolation and detailed structural characterization of stable toxic oligomers of
α-synuclein that have accumulated during the process of amyloid formation. Our approach …
α-synuclein that have accumulated during the process of amyloid formation. Our approach …
[HTML][HTML] Effects of oligomer toxicity, fibril toxicity and fibril spreading in synucleinopathies
Protein misfolding is a general hallmark of protein deposition diseases, such as Alzheimer's
disease or Parkinson's disease, in which different types of aggregated species (oligomers …
disease or Parkinson's disease, in which different types of aggregated species (oligomers …
Cofactor-free oxidase-mimetic nanomaterials from self-assembled histidine-rich peptides
Natural oxidases mainly rely on cofactors and well-arranged amino acid residues for
catalysing electron-transfer reactions but suffer from non-recovery of their activity upon …
catalysing electron-transfer reactions but suffer from non-recovery of their activity upon …
[HTML][HTML] ATR-FTIR: A “rejuvenated” tool to investigate amyloid proteins
R Sarroukh, E Goormaghtigh, JM Ruysschaert… - … et Biophysica Acta (BBA …, 2013 - Elsevier
Amyloid refers to insoluble protein aggregates that are responsible for amyloid diseases but
are also implicated in important physiological functions (functional amyloids). The …
are also implicated in important physiological functions (functional amyloids). The …
Differences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease
The association of the amyloid-β (Aβ) peptide with cellular membranes is hypothesized to be
the underlying phenomenon of neurotoxicity in Alzheimer's disease. Misfolding of proteins …
the underlying phenomenon of neurotoxicity in Alzheimer's disease. Misfolding of proteins …