α-Synuclein is phosphorylated in synucleinopathy lesions

By Hideo Fujiwara, M. Hasegawa, N. Dohmae, A. Kawashima, E. Masliah, M. Goldberg, Jie Shen, K. Takio, T. Iwatsubo. Nature Cell Biology, 2002

1,871 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Neurology

View Paper: https://www.semanticscholar.org/paper/d2d4f599c7dec4bb02221ca22d6c9769a18b5254

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In Cellular and Molecular Neuroscience

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Citations in the corpus

Transneuronal Propagation of Pathologic α-Synuclein from the Gut to the Brain Models Parkinson's Disease. (2019, background): “Themajority of a-syn in fibrils and in LBs is phosphorylated on serine 129 (pSer129-a-syn) (Anderson et al., 2006; Fujiwara et al., 2002).”
Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice (2012, background): “1 F), a marker of pathological Syn (Fujiwara et al., 2002; Waxman and Giasson, 2008).”
Prion-like spreading of pathological α-synuclein in brain (2013, background): “In these so-called -synucleinopathies, -synuclein is deposited in a hyperphosphorylated form with b-sheet-rich, fibrillar structure (Spillantini et al., 1997, 1998; Baba et al., 1998; Wakabayashi et al., 1998; Fujiwara et al., 2002).”
Multi-organ distribution of phosphorylated α-synuclein histopathology in subjects with Lewy body disorders (2010, methodology): “In addition, the use of a method that is specific and sensitive for phosphorylated α-synuclein, which is detected only in pathological structures [34] effectively eliminates the ambiguity of staining results derived using antibodies that recognize normal α-synuclein.”
Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences (2012, neutral): “The acidic C-terminal domain contains several phosphorylation sites and inﬂuences the aggregation behaviour of a -synuclein (Okochi et al , 2000; Fujiwara et al , 2002; Tofaris et al , 2006). a -Synuclein is an intrinsically disordered protein in aqueous solution, however, depending on the…”
Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death (2011, positive): “…in Tx-100, but cells incubated with α-synhWT pffs showed Tx-100-insoluble aggregates (Figure 1A). α-Syn recruited into pathologic inclusions undergoes extensive phosphorylation at Ser129 (pSer129), thus antibodies against pSer129 selectively recognize α-syn pathology (Fujiwara et al., 2002).”