Helen R. Broom
Waterloo, ON N2L3G1, Canada
Last Updated: 09/26/2026
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Found 9 publications
Immature ALS-associated mutant superoxide dismutases form variable aggregate structures through distinct oligomerization processes.
Journal: Biophysical chemistry
Published: March 01, 2022
Probing the free energy landscapes of ALS disease mutants of SOD1 by NMR spectroscopy.
Journal: Proceedings of the National Academy of Sciences of the United States of America
Published: October 30, 2016
ALS-linked misfolded SOD1 species have divergent impacts on mitochondria.
Journal: Acta neuropathologica communications
Published: February 23, 2016
Concurrent Increases and Decreases in Local Stability and Conformational Heterogeneity in Cu, Zn Superoxide Dismutase Variants Revealed by Temperature-Dependence of Amide Chemical Shifts.
Journal: Biochemistry
Published: February 06, 2016
Combined Isothermal Titration and Differential Scanning Calorimetry Define Three-State Thermodynamics of fALS-Associated Mutant Apo SOD1 Dimers and an Increased Population of Folded Monomer.
Journal: Biochemistry
Published: December 30, 2015
Destabilization of the dimer interface is a common consequence of diverse ALS-associated mutations in metal free SOD1.
Journal: Protein science : a publication of the Protein Society
Published: July 15, 2015
Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways.
Journal: eLife
Published: March 03, 2015
Many roads lead to Rome? Multiple modes of Cu,Zn superoxide dismutase destabilization, misfolding and aggregation in amyotrophic lateral sclerosis.
Journal: Essays in biochemistry
Published: August 19, 2014
Energetics of oligomeric protein folding and association.
Journal: Archives of biochemistry and biophysics
Published: October 03, 2012
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Last Updated: 09/26/2026