α-Synuclein misfolding and aggregation: Implications in Parkinson's disease pathogenesis

S Mehra, S Sahay, SK Maji - Biochimica et Biophysica Acta (BBA)-Proteins …, 2019 - Elsevier
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 …

Cell biology and pathophysiology of α-synuclein

J Burré, M Sharma, TC Südhof - Cold Spring …, 2018 - perspectivesinmedicine.cshlp.org
α-Synuclein is an abundant neuronal protein that is highly enriched in presynaptic nerve
terminals. Genetics and neuropathology studies link α-synuclein to Parkinson's disease (PD) …

Alpha-synuclein aggregation pathway in Parkinson's disease: current status and novel therapeutic approaches

M Vidović, MG Rikalovic - Cells, 2022 - mdpi.com
Following Alzheimer's, Parkinson's disease (PD) is the second-most common
neurodegenerative disorder, sharing an unclear pathophysiology, a multifactorial profile …

The synaptic function of α-synuclein

J Burré - Journal of Parkinson's disease, 2015 - content.iospress.com
Abstract α-Synuclein is an abundant neuronal protein which localizes predominantly to
presynaptic terminals, and is strongly linked genetically and pathologically to Parkinson's …

A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity

M Perni, C Galvagnion, A Maltsev… - Proceedings of the …, 2017 - National Acad Sciences
The self-assembly of α-synuclein is closely associated with Parkinson's disease and related
syndromes. We show that squalamine, a natural product with known anticancer and antiviral …

Implication of alpha-synuclein phosphorylation at S129 in synucleinopathies: what have we learned in the last decade?

A Oueslati - Journal of Parkinson's disease, 2016 - content.iospress.com
Abnormal accumulation of proteinaceous intraneuronal inclusions called Lewy bodies (LBs)
is the neurpathological hallmark of Parkinson's disease (PD) and related synucleinopathies …

Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)

FX Theillet, A Binolfi, T Frembgen-Kesner… - Chemical …, 2014 - ACS Publications
It has long been axiomatic that a protein's structure determines its function. Intrinsically
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …

[HTML][HTML] α-Synuclein misfolding and Parkinson's disease

L Breydo, JW Wu, VN Uversky - … et Biophysica Acta (BBA)-Molecular Basis …, 2012 - Elsevier
Substantial evidence links α-synuclein, a small highly conserved presynaptic protein with
unknown function, to both familial and sporadic Parkinson's disease (PD). α-Synuclein has …

Protein misfolding, functional amyloid, and human disease

F Chiti, CM Dobson - Annu. Rev. Biochem., 2006 - annualreviews.org
Peptides or proteins convert under some conditions from their soluble forms into highly
ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging …

α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer

B Fauvet, MK Mbefo, MB Fares, C Desobry… - Journal of Biological …, 2012 - ASBMB
Since the discovery and isolation of α-synuclein (α-syn) from human brains, it has been
widely accepted that it exists as an intrinsically disordered monomeric protein. Two recent …