α-Synuclein misfolding and aggregation: Implications in Parkinson's disease pathogenesis
Abstract α-Synuclein (α-Syn) has been extensively studied for its structural and biophysical
properties owing to its pathophysiological role in Parkinson's disease (PD). Lewy bodies …
properties owing to its pathophysiological role in Parkinson's disease (PD). Lewy bodies …
Materials for fluorescence resonance energy transfer analysis: beyond traditional donor–acceptor combinations
KE Sapsford, L Berti, IL Medintz - … Chemie International Edition, 2006 - Wiley Online Library
Fluorescence resonance energy transfer (FRET) is a nonradiative process whereby an
excited state donor D (usually a fluorophore) transfers energy to a proximal ground state …
excited state donor D (usually a fluorophore) transfers energy to a proximal ground state …
Structure of the toxic core of α-synuclein from invisible crystals
The protein α-synuclein is the main component of Lewy bodies, the neuron-associated
aggregates seen in Parkinson disease and other neurodegenerative pathologies. An 11 …
aggregates seen in Parkinson disease and other neurodegenerative pathologies. An 11 …
α-Synuclein binds to TOM20 and inhibits mitochondrial protein import in Parkinson's disease
R Di Maio, PJ Barrett, EK Hoffman, CW Barrett… - Science translational …, 2016 - science.org
α-Synuclein accumulation and mitochondrial dysfunction have both been strongly implicated
in the pathogenesis of Parkinson's disease (PD), and the two appear to be related …
in the pathogenesis of Parkinson's disease (PD), and the two appear to be related …
Inhibition of mitochondrial fusion by α‐synuclein is rescued by PINK1, Parkin and DJ‐1
F Kamp, N Exner, AK Lutz, N Wender… - The EMBO …, 2010 - embopress.org
Aggregation of α‐synuclein (αS) is involved in the pathogenesis of Parkinson's disease (PD)
and a variety of related neurodegenerative disorders. The physiological function of αS is …
and a variety of related neurodegenerative disorders. The physiological function of αS is …
Interplay of α-synuclein binding and conformational switching probed by single-molecule fluorescence
We studied the coupled binding and folding of α-synuclein, an intrinsically disordered
protein linked with Parkinson's disease. Using single-molecule fluorescence resonance …
protein linked with Parkinson's disease. Using single-molecule fluorescence resonance …
Interaction of α-synuclein with divalent metal ions reveals key differences: A link between structure, binding specificity and fibrillation enhancement
The aggregation of α-synuclein (AS) is characteristic of Parkinson's disease and other
neurodegenerative synucleinopathies. Interactions with metal ions affect dramatically the …
neurodegenerative synucleinopathies. Interactions with metal ions affect dramatically the …
Biophysical characterization of intrinsically disordered proteins
D Eliezer - Current opinion in structural biology, 2009 - Elsevier
The challenges associated with the structural characterization of disordered proteins have
resulted in the application of a host of biophysical methods to such systems. NMR …
resulted in the application of a host of biophysical methods to such systems. NMR …
[HTML][HTML] Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins
LA Munishkina, AL Fink - Biochimica et Biophysica Acta (BBA) …, 2007 - Elsevier
Amyloidogenesis is a characteristic feature of the 40 or so known protein deposition
diseases, and accumulating evidence strongly suggests that self-association of misfolded …
diseases, and accumulating evidence strongly suggests that self-association of misfolded …
Differential phospholipid binding of α-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy
Three familial variants of the presynaptic protein α-synuclein (αS), A30P, E46K, and A53T,
correlate with rare inherited Parkinson's disease (PD), while wild-type αS is implicated in …
correlate with rare inherited Parkinson's disease (PD), while wild-type αS is implicated in …