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Human tau 0N4R isoform hyperphosphorylation LC-MS/MS

ABSTRACT: Soluble aggregates of the microtubule-associated protein tau have been challenging to assemble and characterize, despite their important role in the development of tauopathies. We found that sequential hyperphosphorylation by protein kinase A in conjugation with either glycogen synthase kinase 3betaor stress activated protein kinase 4 enabled recombinant wild-type tau of isoform 0N4R to spontaneously polymerize into small amorphous aggregates in vitro. We employed tandem mass spectrometry to determine the phosphorylation sites.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Jonathan Meng

LAB HEAD: David Klenerman

PROVIDER: PXD033127 | Pride | 2022-04-13

REPOSITORIES: pride

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			Action	DRS
	checksum.txt	Txt
	first_trial_g_tau.dat	Other
	first_trial_g_tau.raw	Raw
	first_trial_pka_tau.dat	Other
	first_trial_pka_tau.raw	Raw

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