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 …
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) …
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 …
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 …
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 …
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
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 …
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 …
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 …
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 …
Huber,*[a] and Malte Drescher*[b] α-Synuclein (αS) is a 140-residue protein abundantly …
A broken α-helix in folded α-synuclein
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 …
11-residue repeats and a hydrophilic tail. α-Synuclein misfolding and dysfunction may …