in α-synuclein deposits ~90%: in cytosolic α-synuclein 4 % of the protein is phosphorylated
||Theillet FX et al., Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs). Chem Rev. 2014 Jul 9 114(13):6661-714. doi: 10.1021/cr400695p p.6686 right column bottom paragraphPubMed ID24901537
|| Anderson JP et al., Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease. J Biol Chem. 2006 Oct 6 281(40):29739-52 DOI: 10.1074/jbc.M600933200  Fujiwara H et al., alpha-Synuclein is phosphorylated in synucleinopathy lesions. Nat Cell Biol. 2002 Feb4(2):160-4 DOI: 10.1038/ncb748  Takahashi M et al., Phosphorylation of alpha-synuclein characteristic of synucleinopathy lesions is recapitulated in alpha-synuclein transgenic Drosophila. Neurosci Lett. 2003 Jan 23 336(3):155-8PubMed ID16847063, 11813001, 12505616
||Primary source  abstract: "A comprehensive, unbiased inventory of synuclein forms present in Lewy bodies from patients with dementia with Lewy bodies was carried out using two-dimensional immunoblot analysis, novel sandwich enzyme-linked immunosorbent assays with modification-specific synuclein antibodies, and mass spectroscopy. The predominant modification of alpha-synuclein in Lewy bodies is a single phosphorylation at Ser-129." Primary source  abstract: "Here, [investigators] show by mass spectrometry analysis and studies with an antibody that specifically recognizes phospho-Ser 129 of alpha-synuclein, that this residue is selectively and extensively phosphorylated in synucleinopathy lesions." Primary source  abstract: "Here [investigators] studied by immunohistochemistry the accumulation of alpha-synuclein in transgenic (TG) Drosophila overexpressing wild-type (WT) or familial PD-linked mutant (i.e. A30P and A53T) alpha-synuclein in neurons, with special reference to the phosphorylation at Ser129, that is characteristic of human synucleinopathy lesions." In primary source  "human α-synuclein in pET21d vectors were transformed into the BL21(DE3) strain of Escherichia coli". Primary source  investigated human tissue. Primary source  studied α-synuclein overexpressed pan-neuronally in Drosophila.
||P.6686 right column bottom paragraph: "Early analyses of α-synuclein deposits in PD patients’ brains showed that ∼90% of the protein is phosphorylated at Ser129, whereas only 4% of cytosolic α-synuclein is modified (primary sources)."