Altered Thiol Chemistry in Human Amyotrophic Lateral Sclerosis-linked Mutants of Superoxide Dismutase 1

S-Glutathionylation of Cryptic Cysteines Enhances Titin Elasticity by Blocking Protein Folding

(2014) Jorge Alegre-Cebollada et al.   CELL

Mechanical Probes of SOD1 Predict Systematic Trends in Metal and Dimer Affinity of ALS-Associated Mutants

(2013) Atanu Das et al.   JOURNAL OF MOLECULAR BIOLOGY

Force dependency of biochemical reactions measured by single-molecule force-clamp spectroscopy

(2013) Ionel Popa et al.   Nature Protocols

The changing scene of amyotrophic lateral sclerosis

(2013) Wim Robberecht et al.   NATURE REVIEWS NEUROSCIENCE

Misfolded SOD1 and ALS: Zeroing in on mitochondria

(2012) Sarah Pickles et al.   Amyotrophic Lateral Sclerosis

Redox properties of the disulfide bond of human Cu,Zn superoxide dismutase and the effects of human glutaredoxin 1

(2012) Samantha D. Bouldin et al.   BIOCHEMICAL JOURNAL

Protein Folding Drives Disulfide Formation

(2012) Pallav Kosuri et al.   CELL

Disulfide Scrambling Describes the Oligomer Formation of Superoxide Dismutase (SOD1) Proteins in the Familial Form of Amyotrophic Lateral Sclerosis

(2012) Keisuke Toichi et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

A novel variant of human superoxide dismutase 1 harboring amyotrophic lateral sclerosis-associated and experimental mutations in metal-binding residues and free cysteines lacks toxicity in vivo

(2012) Mercedes Prudencio et al.   JOURNAL OF NEUROCHEMISTRY

Role of Disulfide Cross-Linking of Mutant SOD1 in the Formation of Inclusion-Body-Like Structures

(2012) Brittany L. T. Roberts et al.   PLoS One

Glutathionylation at Cys-111 Induces Dissociation of Wild Type and FALS Mutant SOD1 Dimers

(2011) Rachel L. Redler et al.   BIOCHEMISTRY

Direct observation of disulfide isomerization in a single protein

(2011) Jorge Alegre-Cebollada et al.   Nature Chemistry

Clinical genetics of amyotrophic lateral sclerosis: what do we really know?

(2011) Peter M. Andersen et al.   Nature Reviews Neurology

Characterization of a Covalent Polysulfane Bridge in Copper−Zinc Superoxide Dismutase,

(2010) Zheng You et al.   BIOCHEMISTRY

Isopeptide Bonds Block the Mechanical Extension of Pili in PathogenicStreptococcus pyogenes

(2010) Jorge Alegre-Cebollada et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Disulfide-Reduced ALS Variants of Cu, Zn Superoxide Dismutase Exhibit Increased Populations of Unfolded Species

(2010) Can Kayatekin et al.   JOURNAL OF MOLECULAR BIOLOGY

Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS

(2010) Daryl A Bosco et al.   NATURE NEUROSCIENCE

Thiol-based, site-specific and covalent immobilization of biomolecules for single-molecule experiments

(2010) Julia L Zimmermann et al.   Nature Protocols

Mechanochemistry: One Bond at a Time

(2009) Jian Liang et al.   ACS Nano

Aggregation of Copper–Zinc Superoxide Dismutase in Familial and Sporadic ALS

(2009) Madhuri Chattopadhyay et al.   ANTIOXIDANTS & REDOX SIGNALING

Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A

(2009) Ahmad Galaleldeen et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

Modifications of Superoxide Dismutase (SOD1) in Human Erythrocytes

(2009) Kyle C. Wilcox et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Metal Deficiency Increases Aberrant Hydrophobicity of Mutant Superoxide Dismutases That Cause Amyotrophic Lateral Sclerosis

(2009) Ashutosh Tiwari et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Loss of Metal Ions, Disulfide Reduction and Mutations Related to Familial ALS Promote Formation of Amyloid-Like Aggregates from Superoxide Dismutase

(2009) Zeynep A. Oztug Durer et al.   PLoS One

Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS

(2009) C. M. Karch et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Different regulation of wild-type and mutant Cu,Zn superoxide dismutase localization in mammalian mitochondria

(2008) Hibiki Kawamata et al.   HUMAN MOLECULAR GENETICS

A Limited Role for Disulfide Cross-linking in the Aggregation of Mutant SOD1 Linked to Familial Amyotrophic Lateral Sclerosis

(2008) Celeste M. Karch et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Complete Loss of Post-translational Modifications Triggers Fibrillar Aggregation of SOD1 in the Familial Form of Amyotrophic Lateral Sclerosis

(2008) Yoshiaki Furukawa et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Dynamical roles of metal ions and the disulfide bond in Cu, Zn superoxide dismutase folding and aggregation

(2008) F. Ding et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA