Related references
Note: Only part of the references are listed.Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways
Ashok Sekhar et al.
ELIFE (2015)
Disulfide Scrambling Describes the Oligomer Formation of Superoxide Dismutase (SOD1) Proteins in the Familial Form of Amyotrophic Lateral Sclerosis
Keisuke Toichi et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2013)
New developments in the ATSAS program package for small-angle scattering data analysis
Maxim V. Petoukhov et al.
JOURNAL OF APPLIED CRYSTALLOGRAPHY (2012)
Copper and Zinc Metallation Status of Copper-Zinc Superoxide Dismutase from Amyotrophic Lateral Sclerosis Transgenic Mice
Herman L. Lelie et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2011)
NMR Characterization of a Fibril-Ready State of Demetalated Wild-Type Superoxide Diemutase
Lucia Banci et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2011)
Quality control of protein standards for molecular mass determinations by small-angle X-ray scattering
Shuji Akiyama
JOURNAL OF APPLIED CRYSTALLOGRAPHY (2010)
Disulfide-Reduced ALS Variants of Cu, Zn Superoxide Dismutase Exhibit Increased Populations of Unfolded Species
Can Kayatekin et al.
JOURNAL OF MOLECULAR BIOLOGY (2010)
Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization
Kaare Teilum et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2009)
Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis
Yoshiaki Furukawa et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
Oxidative modification to cysteine sulfonic acid of Cys111 in human copper-zinc superoxide dismutase
Noriko Fujiwara et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2007)
Structural characterization of flexible proteins using small-angle X-ray scattering
Pau Bernado et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2007)
Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein
Soshanna Zittin Potter et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2007)
Motor neuron disease in mice expressing the wild type-like D90A mutant superoxide dismutase-1
P. Andreas Jonsson et al.
JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY (2006)
Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry
Bryan Francis Shaw et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Disulphide-reduced superoxide dismutase-1 in CNS of transgenic amyotrophic lateral sclerosis models
PA Jonsson et al.
BRAIN (2006)
Human SOD1 before harboring the catalytic metal - Solution structure of copper-depleted, disulfide-reduced form
L Banci et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Using circular dichroism spectra to estimate protein secondary structure
Norma J. Greenfield
NATURE PROTOCOLS (2006)
How to study proteins by circular dichroism
SM Kelly et al.
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS (2005)
Global rigid body modeling of macromolecular complexes against small-angle scattering data
MV Petoukhov et al.
BIOPHYSICAL JOURNAL (2005)
Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the Apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation
Y Furukawa et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant - Insights into the molecular basis for dimer stability
PA Doucette et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS
Y Furukawa et al.
EMBO JOURNAL (2004)
The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status
F Arnesano et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2004)
Folding of human superoxide dismutase: Disulfide reduction prevents dimerization and produces marginally stable monomers
MJ Lindberg et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2004)
Unraveling the mechanisms involved in motor neuron degeneration in ALS
LI Bruijn et al.
ANNUAL REVIEW OF NEUROSCIENCE (2004)
PRIMUS:: a Windows PC-based system for small-angle scattering data analysis
PV Konarev et al.
JOURNAL OF APPLIED CRYSTALLOGRAPHY (2003)
Solution structure of apo Cu,Zn superoxide dismutase: Role of metal ions in protein folding
L Banci et al.
BIOCHEMISTRY (2003)
Uniqueness of ab initio shape determination in small-angle scattering
VV Volkov et al.
JOURNAL OF APPLIED CRYSTALLOGRAPHY (2003)
Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS
JS Elam et al.
NATURE STRUCTURAL BIOLOGY (2003)
The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis
RW Strange et al.
JOURNAL OF MOLECULAR BIOLOGY (2003)
Familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase are susceptible to disulfide reduction
A Tiwari et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
Structure and dynamics of copper-free SOD: The protein before binding copper
L Banci et al.
PROTEIN SCIENCE (2002)
Oxidation-induced misfolding and agagaregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis
R Rakhit et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site
J Wang et al.
NEUROBIOLOGY OF DISEASE (2002)
Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis
LJ Hayward et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase
JA Rodriguez et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues
M Watanabe et al.
NEUROBIOLOGY OF DISEASE (2001)
Modeling tricks and fitting techniques for multiresolution structures
W Wriggers et al.
STRUCTURE (2001)
Determination of domain structure of proteins from X-ray solution scattering
DI Svergun et al.
BIOPHYSICAL JOURNAL (2001)
Mechanisms of tryptophan fluorescence shifts in proteins
JT Vivian et al.
BIOPHYSICAL JOURNAL (2001)
New consensus research on neuropathological aspects of familial amyotrophic lateral sclerosis with superoxide dismutase 1 (SOD1) gene mutations: Inclusions containing SOD1 in neurons and astrocytes
S Kato et al.
AMYOTROPHIC LATERAL SCLEROSIS (2000)
Share Paper
