https://www.selleckchem.com/products/jq1.html
We observed that phosphorylation at all five tyrosine residues, multiple N-terminal tyrosine residues (Tyr-18, -29, and -197) or specific phosphorylation only at residue Tyr-310 abolishes Tau aggregation and inhibits its microtubule- and lipid-binding properties. NMR experiments indicated that these effects are mediated by a local decrease in β-sheet propensity of Tau's PHF6 domain. Our findings underscore that although it previously has been overlooked despite its prominent location in Tau, Tyr-310 phosphorylation has unique role in the re
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