Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and -independent mechanisms
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A. Hill | I. Mackenzie | S. Plotkin | B. J. Turner | N. Cashman | J. Kumita | J. Yerbury | Bradley M. Coleman | A. Yanai | W. Guest | M. A. O’Neill | J. Silverman | L. Grad | Edward Pokrishevsky | Rafaa Zeineddine | Lisa Corcoran | L. Luheshi | M. Yousefi | L. I. Grad | Leslie I. Grad
[1] N. Nukina,et al. Intracellular seeded aggregation of mutant Cu,Zn‐superoxide dismutase associated with amyotrophic lateral sclerosis , 2013, FEBS letters.
[2] F. Brodsky,et al. Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds , 2013, Proceedings of the National Academy of Sciences.
[3] A. Walker,et al. Extracellular wildtype and mutant SOD1 induces ER–Golgi pathology characteristic of amyotrophic lateral sclerosis in neuronal cells , 2013, Cellular and Molecular Life Sciences.
[4] Wim Robberecht,et al. The changing scene of amyotrophic lateral sclerosis , 2013, Nature Reviews Neuroscience.
[5] I. Campbell,et al. Extracellular aggregated Cu/Zn superoxide dismutase activates microglia to give a cytotoxic phenotype , 2013, Glia.
[6] S. Prusiner,et al. A Unifying Role for Prions in Neurodegenerative Diseases , 2012, Science.
[7] I. Mackenzie,et al. Aberrant Localization of FUS and TDP43 Is Associated with Misfolding of SOD1 in Amyotrophic Lateral Sclerosis , 2012, PloS one.
[8] Andrew F. Hill,et al. Exosomes: Vehicles for the Transfer of Toxic Proteins Associated with Neurodegenerative Diseases? , 2012, Front. Physio..
[9] Matthew C. Kiernan,et al. Clinical diagnosis and management of amyotrophic lateral sclerosis , 2011, Nature Reviews Neurology.
[10] N. Cashman,et al. Generalization of the Prion Hypothesis to Other Neurodegenerative Diseases: An Imperfect Fit , 2011, Journal of toxicology and environmental health. Part A.
[11] D. Cleveland,et al. The Seeds of Neurodegeneration: Prion-like Spreading in ALS , 2011, Cell.
[12] Bruce L. Miller,et al. Expanded GGGGCC Hexanucleotide Repeat in Noncoding Region of C9ORF72 Causes Chromosome 9p-Linked FTD and ALS , 2011, Neuron.
[13] David Heckerman,et al. A Hexanucleotide Repeat Expansion in C9ORF72 Is the Cause of Chromosome 9p21-Linked ALS-FTD , 2011, Neuron.
[14] David S Wishart,et al. Intermolecular transmission of superoxide dismutase 1 misfolding in living cells , 2011, Proceedings of the National Academy of Sciences.
[15] Christian Münch,et al. Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells , 2011, Proceedings of the National Academy of Sciences.
[16] G. Krishnamoorthy,et al. Selective transfer of exosomes from oligodendrocytes to microglia by macropinocytosis , 2011, Journal of Cell Science.
[17] Jeffery N Agar,et al. Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS , 2010, Nature Neuroscience.
[18] John Q. Trojanowski,et al. Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS , 2010, Nature.
[19] Johan Jacobsson,et al. Novel Antibodies Reveal Inclusions Containing Non-Native SOD1 in Sporadic ALS Patients , 2010, PloS one.
[20] J. Julien,et al. Intracerebroventricular infusion of monoclonal antibody or its derived Fab fragment against misfolded forms of SOD1 mutant delays mortality in a mouse model of ALS , 2010, Journal of neurochemistry.
[21] J. Collinge,et al. Superoxide Dismutase 1 and tgSOD1G93A Mouse Spinal Cord Seed Fibrils, Suggesting a Propagative Cell Death Mechanism in Amyotrophic Lateral Sclerosis , 2010, PloS one.
[22] Ronald Melki,et al. Prion-like transmission of protein aggregates in neurodegenerative diseases , 2010, Nature Reviews Molecular Cell Biology.
[23] A. L. La Spada,et al. ALS motor phenotype heterogeneity, focality, and spread , 2009, Neurology.
[24] C. Théry,et al. Membrane vesicles as conveyors of immune responses , 2009, Nature Reviews Immunology.
[25] J. Trojanowski,et al. Establishment of a cell model of ALS disease: Golgi apparatus disruption occurs independently from apoptosis , 2008, Biotechnology Letters.
[26] D. Cleveland,et al. Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria , 2008, Proceedings of the National Academy of Sciences.
[27] A. Hill,et al. The role of exosomes in the processing of proteins associated with neurodegenerative diseases , 2008, European Biophysics Journal.
[28] P. Altevogt,et al. Evidence for secretion of Cu,Zn superoxide dismutase via exosomes from a cell model of amyotrophic lateral sclerosis , 2007, Neuroscience Letters.
[29] C. Armon. Sports and trauma in amyotrophic lateral sclerosis revisited , 2007, Journal of the Neurological Sciences.
[30] A. Chakrabartty,et al. An immunological epitope selective for pathological monomer-misfolded SOD1 in ALS , 2007, Nature Medicine.
[31] T. Siddique,et al. Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice. , 2006, Proceedings of the National Academy of Sciences of the United States of America.
[32] R. Morimoto,et al. Structural properties and neuronal toxicity of amyotrophic lateral sclerosis–associated Cu/Zn superoxide dismutase 1 aggregates , 2005, The Journal of cell biology.
[33] Y. Yedidia,et al. Heparan Sulfate Is a Cellular Receptor for Purified Infectious Prions* , 2005, Journal of Biological Chemistry.
[34] A. Hill,et al. Impaired Extracellular Secretion of Mutant Superoxide Dismutase 1 Associates with Neurotoxicity in Familial Amyotrophic Lateral Sclerosis , 2005, The Journal of Neuroscience.
[35] T. Tabira,et al. Neuroblastoma × spinal cord (NSC) hybrid cell lines resemble developing motor neurons , 1992, Developmental dynamics : an official publication of the American Association of Anatomists.
[36] P. Andersen,et al. Expression of wild-type human superoxide dismutase-1 in mice causes amyotrophic lateral sclerosis. , 2013, Human molecular genetics.