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α-synuclein in the pathophysiology of Alzheimer's disease
D Twohig, HM Nielsen - Molecular neurodegeneration, 2019 - Springer
The Alzheimer's disease (AD) afflicted brain is neuropathologically defined by extracellular
amyloid-β (Aβ) plaques and intraneuronal neurofibrillary tangles composed of …
amyloid-β (Aβ) plaques and intraneuronal neurofibrillary tangles composed of …
Alpha-synuclein function and dysfunction on cellular membranes
Alpha-synuclein is a small neuronal protein that is closely associated with the etiology of
Parkinson's disease. Mutations in and alterations in expression levels of alpha-synuclein …
Parkinson's disease. Mutations in and alterations in expression levels of alpha-synuclein …
Single-molecule studies of intrinsically disordered proteins
The last 15 years saw a dramatic increase in the number of published papers exposing
research related to the concept of protein disorder and a concomitant increase in the …
research related to the concept of protein disorder and a concomitant increase in the …
[HTML][HTML] Transient β-hairpin formation in α-synuclein monomer revealed by coarse-grained molecular dynamics simulation
Parkinson's disease, originating from the intrinsically disordered peptide α-synuclein, is a
common neurodegenerative disorder that affects more than 5% of the population above age …
common neurodegenerative disorder that affects more than 5% of the population above age …
Effect of an amyloidogenic SARS-COV-2 protein fragment on α-synuclein monomers and fibrils
Aggregates of α-synuclein are thought to be the disease-causing agent in Parkinson's
disease. Various case studies have hinted at a correlation between COVID-19 and the onset …
disease. Various case studies have hinted at a correlation between COVID-19 and the onset …
Small molecule sequestration of the intrinsically disordered protein, p27Kip1, within soluble oligomers
Proteins that exhibit intrinsically disordered regions (IDRs) are prevalent in the human
proteome and perform diverse biological functions, including signaling and regulation. Due …
proteome and perform diverse biological functions, including signaling and regulation. Due …
Quantitative biophysical characterization of intrinsically disordered proteins
EB Gibbs, SA Showalter - Biochemistry, 2015 - ACS Publications
Intrinsically disordered proteins (IDPs) are broadly defined as protein regions that do not
cooperatively fold into a spatially or temporally stable structure. Recent research strongly …
cooperatively fold into a spatially or temporally stable structure. Recent research strongly …
Distance-Dependent Tryptophan-Induced Quenching of Thioflavin T Defines the Amyloid Core Architecture
L Arora, D Bhowmik, H Sawdekar… - The Journal of …, 2024 - ACS Publications
Thioflavin T (ThT) is widely employed as a fluorogenic marker for amyloid formation. ThT
fluorescence is utilized to detect amyloid fibrils as well as to follow aggregation kinetics …
fluorescence is utilized to detect amyloid fibrils as well as to follow aggregation kinetics …
Comparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis
Characterization of the amyloidogenic Parkinson's disease protein α-synuclein (αS) has
proven difficult due to its structural plasticity. Here, we present a number of complementary …
proven difficult due to its structural plasticity. Here, we present a number of complementary …
Studies of protein folding and dynamics using single molecule fluorescence spectroscopy
Single molecule fluorescence spectroscopy is emerging as an extremely powerful and
sensitive tool to study complex biological problems. Single molecule fluorescence …
sensitive tool to study complex biological problems. Single molecule fluorescence …