p(HGNC:MAPT, pmod(Ph, Ser, 235))
The reaction with the diagnostic antibodies (Fig. 4) is similar to the examples shown previously for cdk2 (Fig. 2), MAP kinase [8], or GSK-3 [26], indicating the phosphorylation of the SP motifs for which these antibodies are sensitive (serines 199, 202, 235, 396, 404; see Fig. 1) PubMed:8282104
The reaction with the diagnostic antibodies (Fig. 4) is similar to the examples shown previously for cdk2 (Fig. 2), MAP kinase [8], or GSK-3 [26], indicating the phosphorylation of the SP motifs for which these antibodies are sensitive (serines 199, 202, 235, 396, 404; see Fig. 1) PubMed:8282104
The reaction with the diagnostic antibodies (Fig. 4) is similar to the examples shown previously for cdk2 (Fig. 2), MAP kinase [8], or GSK-3 [26], indicating the phosphorylation of the SP motifs for which these antibodies are sensitive (serines 199, 202, 235, 396, 404; see Fig. 1) PubMed:8282104
The diagnostic antibodies AT8, TAU-1, SM131, SM134, and SM133 react to phosphorylation similarly as with MAPK and GSK-3, indicating that SP motifs before the repeat region (S199 and/or S202, S235) and after the repeats (S396, S404) become phosphorylated (Fig. 2,-2,); note that AT8, SMUl, and SM134 react with PHFs where the epitopes containing SP motifs are phosphorylated, while TAU-1 and SM133 react with normal tau where the epitopes are not phosphorylated PubMed:8282104
The reaction with the diagnostic antibodies (Fig. 4) is similar to the examples shown previously for cdk2 (Fig. 2), MAP kinase [8], or GSK-3 [26], indicating the phosphorylation of the SP motifs for which these antibodies are sensitive (serines 199, 202, 235, 396, 404; see Fig. 1) PubMed:8282104
In this study, we address the structural impact of phosphorylation of the Tau protein by Nuclear Magnetic Resonance (NMR) spectroscopy on a functional fragment of Tau (Tau[Ser208-Ser324] = TauF4). TauF4 was phosphorylated by the proline-directed CDK2/CycA3 kinase on Thr231 (generating the AT180 epitope), Ser235, and equally on Thr212 and Thr217 in the Proline-rich region (Tau[Ser208-Gln244] or PRR). These modifications strongly decrease the capacity of TauF4 to polymerize tubulin into microtubules. While all the NMR parameters are consistent with a globally disordered Tau protein fragment, local clusters of structuration can be defined. The most salient result of our NMR analysis is that phosphorylation in the PRR stabilizes a short α-helix that runs from pSer235 till the very beginning of the microtubule-binding region (Tau[Thr245-Ser324] or MTBR of TauF4). PubMed:22072628
We find that phosphorylated (p-) SER235-PRO, but not pTHR231-PRO, is exclusively catalyzed by full-length Pin1 and isolated PPIase domain. PubMed:26996941
We find that phosphorylated (p-) SER235-PRO, but not pTHR231-PRO, is exclusively catalyzed by full-length Pin1 and isolated PPIase domain. PubMed:26996941
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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.