Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders.

By E. Masliah, E. Rockenstein, I. Veinbergs, M. Mallory, M. Hashimoto, A. Takeda, Y. Sagara, A. Sisk, L. Mucke. Science, 2000

1,838 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Neurology

View Paper: https://www.semanticscholar.org/paper/dd60b4742e7b340603c83b8e9f1bb70fa8be36f4

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In Cellular and Molecular Neuroscience

In Neurology

Citations in the corpus

Non–cell autonomous toxicity in neurodegenerative disorders: ALS and beyond (2009, background): “A proportion of both dismutase-active and -inactive mutants, however, has been shown convincingly to be mitochondrially associated (Mattiazzi et al., 2002; Liu et al., 2004; Vijayvergiya et al., 2005; Vande Velde et al., 2008).”
Molecular pathophysiology of Parkinson's disease. (2005, background): “The notion of cytotoxic protofibrils is further supported by studies in one line of αsynuclein transgenic mice, whereby motoric impairment and loss of DA nerve terminals are observed in the presence of non-fibrillar α-synuclein inclusions (Masliah et al. 2000).”
Chronic systemic pesticide exposure reproduces features of Parkinson's disease (2000, background): “Transgenic mice expressing the pathogenic human α-synuclein mutation develop modest dopaminergic pathology (although the specificity of this degeneration is not detailed), and many neurons contain small cytoplasmic inclusions that are granular rather than fibrilla”
Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. (2002, background): “Third, transgenic mice and Drosophila expressing human wild-type (WT) a-synuclein or, in the flies, the mutants, are characterized by a-synuclein inclusions that resemble Lewy bodies.(7,8) In both models, the formation of these inclusions is correlated to the onset of disease phenotype.”
Different Species of α-Synuclein Oligomers Induce Calcium Influx and Seeding (2007, background): “…oligomers and protofibrils, rather than mature fibrils of -syn, are the pathogenic species (Conway et al., 2000; Goldberg and Lansbury, 2000; Masliah et al., 2000; Auluck et al., 2002; Bucciantini et al., 2002, 2004; Gosavi et al., 2002; Kayed et al., 2003, 2004; Park and Lansbury, 2003;…”
Expression of A53T Mutant But Not Wild-Type α-Synuclein in PC12 Cells Induces Alterations of the Ubiquitin-Dependent Degradation System, Loss of Dopamine Release, and Autophagic Cell Death (2001, background): “Phenotypic heterogeneity has also been observed in families with -synuclein mutations (Papadimitriou et al., 1999) and in transgenic mouse models overexpressing wild-type or mutant -synuclein (Masliah et al., 2000; Matsuoka et al., 2001; Rathke-Hartlieb et al., 2001).”
Secondary Structure of α-Synuclein Oligomers: Characterization by Raman and Atomic Force Microscopy (2006, background): “than the mature fibrils, could be pathogenic.(5,8,12) Thus, there are distinct steps in the aggregation process where intervention might be able to prevent or reverse the formation of oligomers and/or fibrils.”
Alpha-synuclein in Parkinson’s disease and other synucleinopathies: from overt neurodegeneration back to early synaptic dysfunction (2023, background): “Moreover, animal models’ data strongly agree that overexpression of α-syn leads to a direct insult to the dopaminergic system, reported as a decrease in tyrosine hydroxylase (TH) activity and expression within the striatum [36].”
Parkinson's disease: genetics and pathogenesis. (2011, background): “In mice, transgenic expression of wild-type human α-synuclein produces a reduction in striatal dopaminergic nerve terminals, concomitant decreased motor performance, and formation of α-synuclein-rich neuronal cytoplasmic and nuclear inclusions (129).”