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 …

Alpha-synuclein function and dysfunction on cellular membranes

D Snead, D Eliezer - Experimental neurobiology, 2014 - pmc.ncbi.nlm.nih.gov
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 …

Single-molecule studies of intrinsically disordered proteins

M Brucale, B Schuler, B Samorì - Chemical reviews, 2014 - ACS Publications
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 …

[HTML][HTML] Transient β-hairpin formation in α-synuclein monomer revealed by coarse-grained molecular dynamics simulation

H Yu, W Han, W Ma, K Schulten - The Journal of chemical physics, 2015 - pubs.aip.org
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 …

Effect of an amyloidogenic SARS-COV-2 protein fragment on α-synuclein monomers and fibrils

AK Jana, CW Lander, AD Chesney… - The Journal of …, 2022 - ACS Publications
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 …

Small molecule sequestration of the intrinsically disordered protein, p27Kip1, within soluble oligomers

LI Iconaru, S Das, A Nourse, AA Shelat, J Zuo… - Journal of molecular …, 2021 - Elsevier
Proteins that exhibit intrinsically disordered regions (IDRs) are prevalent in the human
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 …

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 …

Comparison of strategies for non-perturbing labeling of α-synuclein to study amyloidogenesis

CM Haney, RF Wissner, JB Warner, YJ Wang… - Organic & …, 2016 - pubs.rsc.org
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 …

Studies of protein folding and dynamics using single molecule fluorescence spectroscopy

S Basak, K Chattopadhyay - Physical chemistry chemical physics, 2014 - pubs.rsc.org
Single molecule fluorescence spectroscopy is emerging as an extremely powerful and
sensitive tool to study complex biological problems. Single molecule fluorescence …