Related references
Note: Only part of the references are listed.α-Synuclein in Central Nervous System and from Erythrocytes, Mammalian Cells, and Escherichia coli Exists Predominantly as Disordered Monomer
Bruno Fauvet et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2012)
N-terminal acetylation is critical for forming a-helical oligomer of a-synuclein
Adam J. Trexler et al.
PROTEIN SCIENCE (2012)
C-13 Direct-Detection Biomolecular NMR Spectroscopy in Living Cells
Ivano Bertini et al.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2011)
Internal and Global Protein Motion Assessed with a Fusion Construct and In-Cell NMR Spectroscopy
Christopher O. Barnes et al.
CHEMBIOCHEM (2011)
Paramagnetic relaxation enhancement to improve sensitivity of fast NMR methods: application to intrinsically disordered proteins
Francois-Xavier Theillet et al.
JOURNAL OF BIOMOLECULAR NMR (2011)
α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
Tim Bartels et al.
NATURE (2011)
Intrinsic disorder in measles virus nucleocapsids
Malene Ringkjobing Jensen et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2011)
A soluble α-synuclein construct forms a dynamic tetramer
Wei Wang et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2011)
In-cell protein NMR and protein leakage
Christopher O. Barnes et al.
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2011)
Cellular structural biology
Yutaka Ito et al.
CURRENT OPINION IN STRUCTURAL BIOLOGY (2010)
A bioreactor for in-cell protein NMR
Naima G. Sharaf et al.
JOURNAL OF MAGNETIC RESONANCE (2010)
The rod-shaped conformation of Starmaker
Tomasz M. Kaplon et al.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS (2009)
Speeding Up 13C Direct Detection Biomolecular NMR Spectroscopy
Wolfgang Bermel et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2009)
Structural and mechanistic basis behind the inhibitory interaction of PcTS on α-synuclein amyloid fibril formation
Gonzalo R. Lamberto et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2009)
Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of α-synuclein
Katerina E. Paleologou et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
Differential dynamical effects of macromolecular crowding on an intrinsically disordered protein and a globular protein: Implications for in-cell NMR spectroscopy
Conggang Li et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2008)
Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain
Mark Wells et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2008)
Hydrogen exchange of monomeric α-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli
Robyn L. Croke et al.
PROTEIN SCIENCE (2008)
Structural characterization of the intrinsically unfolded protein β-synuclein, a natural negative regulator of α-synuclein aggregation
Carlos W. Bertoncini et al.
JOURNAL OF MOLECULAR BIOLOGY (2007)
Residual structure, backbone dynamics, and interactions within the synuclein family
Yoon-hui Sung et al.
JOURNAL OF MOLECULAR BIOLOGY (2007)
Looking into live cells with in-cell NMR spectroscopy
Philipp Selenko et al.
JOURNAL OF STRUCTURAL BIOLOGY (2007)
α-Synuclein tertiary contact dynamics
Jennifer C. Lee et al.
JOURNAL OF PHYSICAL CHEMISTRY B (2007)
The aggregation and fibrillation of α-synuclein
Anthony L. Fink
ACCOUNTS OF CHEMICAL RESEARCH (2006)
Interaction of α-synuclein with divalent metal ions reveals key differences:: A link between structure, binding specificity and fibrillation enhancement
Andres Binolfi et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2006)
Macromolecular crowding in the Escherichia coli periplasm maintains α-synuclein disorder
BC McNulty et al.
JOURNAL OF MOLECULAR BIOLOGY (2006)
SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds
P Schanda et al.
JOURNAL OF BIOMOLECULAR NMR (2005)
Tertiary contact formation in α-synuclein probed by electron transfer
JC Lee et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2005)
Gir2 is an intrinsically unstructured protein that is present in Saccharomyces cerevisiae as a group of heterogeneously electrophoretic migrating forms
VS Alves et al.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2005)
Helix periodicity, topology, and dynamics of membrane-associated α-Synuclein
R Bussell et al.
PROTEIN SCIENCE (2005)
Structure and dynamics of micelle-bound human α-synuclein
TS Ulmer et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein
CW Bertoncini et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2005)
Mapping long-range interactions in α-synuclein using spin-label NMR and ensemble molecular dynamics simulations
MM Dedmon et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2005)
Impact of the acidic C-terminal region comprising amino acids 109-140 on α-synuclein aggregation in vitro
W Hoyer et al.
BIOCHEMISTRY (2004)
Structure of membrane-bound α-synuclein studied by site-directed spin labeling
CC Jao et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2004)
NMR of α-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation
CO Fernández et al.
EMBO JOURNAL (2004)
Conformational constraints for amyloid fibrillation: the importance of being unfolded
VN Uversky et al.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS (2004)
The intracellular domain of the Drosophila cholinesterase-like neural adhesion protein, gliotactin, is natively unfolded
T Zeev-Ben-Mordehai et al.
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2003)
A protein-chameleon:: Conformational plasticity of α-synuclein, a disordered protein involved in neurodegenerative disorders
VN Uversky
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS (2003)
A structural and functional role for 11-mer repeats in α-synuclein and other exchangeable lipid binding proteins
R Bussell et al.
JOURNAL OF MOLECULAR BIOLOGY (2003)
Dependence of α-synuclein aggregate morphology on solution conditions
W Hoyer et al.
JOURNAL OF MOLECULAR BIOLOGY (2002)
Residual structure and dynamics in Parkinson's disease-associated mutants of α-synuclein
R Bussell et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2001)
Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein -: A possible molecular link between Parkinson's disease and heavy metal exposure
VN Uversky et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2001)
Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy
Z Serber et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2001)
Alpha-synuclein and neurodegenerative diseases
M Goedert
NATURE REVIEWS NEUROSCIENCE (2001)
Conformational properties of α-synuclein in its free and lipid-associated states
D Eliezer et al.
JOURNAL OF MOLECULAR BIOLOGY (2001)
Evidence for a partially folded intermediate in α-synuclein fibril formation
VN Uversky et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2001)
A hydrophobic stretch of 12 amino acid residues in the middle of α-synuclein is essential for filament assembly
BI Giasson et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2001)