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Neuropathology : Official Journal of the Japanese Society of Neuropathology|April 17, 2001
Formation of advanced glycation end-product-modified superoxide dismutase-1 (SOD1) is one of the mechanisms responsible for inclusions common to familial amyotrophic lateral sclerosis patients with SOD1 gene mutation, and transgenic mice expressing human SOD1 gene mutationS Kato, K Nakashima, S Horiuchi, et al.Proceedings of the National Academy of Sciences of the United States of America|August 16, 1994
Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activityD R Borchelt, M K Lee, H S Slunt, et al.Neurology|October 1, 1996
Mechanisms of selective motor neuron death in transgenic mouse models of motor neuron diseaseD W Cleveland, L I Bruijn, P C Wong, et al.Ciba Foundation Symposium|January 1, 1996
Motor neuron disease and model systems: aetiologies, mechanisms and therapiesD L Price, V E Koliatsos, P C Wong, et al.Neuron|February 1, 1997
ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusionsL I Bruijn, M W Becher, M K Lee, et al.Neurobiology of Disease|August 14, 1998
Axonal transport of mutant superoxide dismutase 1 and focal axonal abnormalities in the proximal axons of transgenic miceD R Borchelt, P C Wong, M W Becher, et al.Science (New York, N.Y.)|October 4, 2003
Wild-type nonneuronal cells extend survival of SOD1 mutant motor neurons in ALS miceA M Clement, M D Nguyen, E A Roberts, et al.Chromosome Research : an International Journal on the Molecular, Supramolecular and Evolutionary Aspects of Chromosome Biology|April 13, 2013
Esperanto for histones: CENP-A, not CenH3, is the centromeric histone H3 variantW C Earnshaw, R C Allshire, B E Black, et al.Pageof 15