Structural insights on physiological functions and pathological effects of±‐synuclein

M Bisaglia, S Mammi, L Bubacco - The FASEB Journal, 2009 - Wiley Online Library
α‐Synuclein is an intrinsically unfolded protein that can adopt a partially helical structure
when it interacts with different lipid membranes. Its pathological relevance is linked to its …

[HTML][HTML] Dynamic structural flexibility of α-synuclein

DE Mor, SE Ugras, MJ Daniels, H Ischiropoulos - Neurobiology of disease, 2016 - Elsevier
Abstract α-Synuclein is a conserved, abundantly expressed protein that is partially localized
in pre-synaptic terminals in the central nervous system. The precise biological function (s) …

α-synuclein misfolding and neurodegenerative diseases

VN Uversky - Current protein and peptide science, 2008 - ingentaconnect.com
α-Synuclein is an abundant presynaptic brain protein, misfolding, aggregation and
fibrillation of which are implicated as critical factors in several neurodegenerative diseases …

Physiological and pathological properties of α-synuclein

GK Tofaris, MG Spillantini - Cellular and molecular life sciences, 2007 - Springer
α-Synuclein belongs to a small group of natively unfolded proteins that can transiently bind
to lipid membranes and acquire a partial α-helical conformation. Under certain pathogenic …

Residual structure, backbone dynamics, and interactions within the synuclein family

Y Sung, D Eliezer - Journal of molecular biology, 2007 - Elsevier
The human synuclein protein family includes α-synuclein, which has been linked to both
familial and sporadic Parkinson's disease, and the highly homologous β and γ-synuclein …

Order and disorder in the physiological membrane binding of α-synuclein

G Fusco, M Sanz-Hernandez, A De Simone - Current opinion in structural …, 2018 - Elsevier
Highlights•αS is a protein whose aggregation is strongly connected to Parkinson's
disease.•αS is partitioned between a disordered solution state and a helical membrane …

A protein-chameleon: conformational plasticity of α-synuclein, a disordered protein involved in neurodegenerative disorders

VN Uversky - Journal of Biomolecular Structure and Dynamics, 2003 - Taylor & Francis
Under the physiological conditions in vitro, α-synuclein, a conservative presynaptic protein,
the aggregation and fibrillation of which is assumed to be involved into the pathogenesis of …

Rationally Designed Variants of α-Synuclein Illuminate Its in vivo Structural Properties in Health and Disease

U Dettmer - Frontiers in Neuroscience, 2018 - frontiersin.org
α-Synuclein (αS) is a conserved and abundant neuronal protein with unusual structural
properties. It appears to partition between folded and unstructured states as well as between …

Direct evidence of coexisting horseshoe and extended helix conformations of membrane‐bound alpha‐synuclein

M Robotta, P Braun, B van Rooijen… - …, 2011 - Wiley Online Library
Marta Robotta,[b] Patrick Braun,[b] Bart van Rooijen,[c] Vinod Subramaniam,*[c] Martina
Huber,*[a] and Malte Drescher*[b] α-Synuclein (αS) is a 140-residue protein abundantly …

A broken α-helix in folded α-synuclein

S Chandra, X Chen, J Rizo, R Jahn… - Journal of Biological …, 2003 - ASBMB
α-Synuclein is a small cytosolic protein of presynaptic nerve terminals composed of seven
11-residue repeats and a hydrophilic tail. α-Synuclein misfolding and dysfunction may …