alpha-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

941 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/afed4135289b8f317074ebd1288320e3678c9af3

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Citations in the corpus

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).”
Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death (2011, unknown): “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).”
Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells (2009, background): “To further confirm that transduced -Syn PFFs are intracellular and to determine whether the resulting seeded-inclusions recapitulate posttranslational modifications found in human LBs, we next asked whether -Syn within inclusions inside transduced cells underwent hyperphosphorylation (18) and ubiqui”
Α-synuclein misfolding and Parkinson's disease. (2012, background): “This data shows that Ser-129 phosphorylation promotes aggregation of α-synuclein.”
Pathological α-Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice (2012, unknown): “Thus, propagation of LBs/LNs is connectivitydependent, and this provides an explanation for the nonuniform distribution of LBs/LNs observed in a-Syn PFF-seeded animals.”
Multi-organ distribution of phosphorylated α-synuclein histopathology in subjects with Lewy body disorders (2010, unknown): “In addition, the use of a method that is specific and sensitive for phosphorylated a-synuclein, which is detected only in pathological structures [34] effectively eliminates the”
Structures of α-Synuclein Filaments from Multiple System Atrophy (2020, background): “Most sarkosyl-insoluble α-synuclein phosphorylated at S129 was soluble in SDS.”