Research Topics
Genomes and GenesSpecies | Cynthia M J HigginsSummaryAffiliation: University of Massachusetts Medical School Country: USA Publications
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Publications
ALS-associated mutant SOD1G93A causes mitochondrial vacuolation by expansion of the intermembrane space and by involvement of SOD1 aggregation and peroxisomesCynthia M J Higgins
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation St, Worcester, MA 01655, USA
BMC Neurosci 4:16. 2003..To determine which of these possibilities are true, we examined the vacuolar patterns in detail in transgenic mice expressing mutant SOD1G93A...
Mitochondrial electron transport chain complex dysfunction in a transgenic mouse model for amyotrophic lateral sclerosisCheolwha Jung
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA
J Neurochem 83:535-45. 2002..These results demonstrate a functional defect in mitochondria in the ventral horn region and support the view that mitochondrial damage plays a role in mutant SOD1-induced motoneuron degeneration pathway...
Mutant Cu, Zn superoxide dismutase that causes motoneuron degeneration is present in mitochondria in the CNSCynthia M J Higgins
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA
J Neurosci 22:RC215. 2002..By immunoelectron microscopy, we show that SOD1 is present within mitochondria at similar concentrations as in the cytoplasm. Thus SOD1, in addition to being a cytosolic enzyme, is present inside mitochondria in the CNS...
Inhibition of chaperone activity is a shared property of several Cu,Zn-superoxide dismutase mutants that cause amyotrophic lateral sclerosisHemachand Tummala
Department of Biochemistry and Molecular Pharmacology, Neurology, and Cell Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA
J Biol Chem 280:17725-31. 2005..Thus, mutant SOD1 proteins may impair chaperone function independent of gene expression in vivo, and this inhibition may be a shared property of ALS-linked mutant SOD1 proteins...
A quantitative histochemical assay for activities of mitochondrial electron transport chain complexes in mouse spinal cord sectionsCheolwha Jung
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA
J Neurosci Methods 114:165-72. 2002....
