p(HBP:"Tau epitope, AT8") decreases act(p(HGNC:MAPT))

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PubMed:19459590

Because S199/S202/T205E, S396/S404E, 6-Phos and 7-Phos all demonstrated an AD-like shift in mobility as a result of phosphorylation-like changes, we conclude that they have the characteristics of hyperphosphorylated tau. These mutants will therefore be referred to as pseudo-hyperphosphorylated tau throughout the manuscript. On the basis of the observations that pseudohyperphosphorylated tau has decreased affinity for microtubules and reduced inducer-initiated rates of nucleation and polymerization, we propose that this combination could be the cause of the increased cytotoxicity of hyperphosphorylated tau in Alzheimer's disease and also explain the potentially beneficial role of tau polymerization and NFT formation.

Related Edges 10

• a(HBP:"Tau epitope, PHF1") decreases act(p(HGNC:MAPT))
• bp(GO:"microtubule polymerization") positiveCorrelation act(p(HGNC:MAPT))
• act(p(HGNC:MAPT)) negativeCorrelation p(HBP:"Tau epitope, AT8")
• act(p(HGNC:MAPT)) positiveCorrelation bp(GO:"microtubule polymerization")
• p(HBP:"Tau epitope, AT8") negativeCorrelation act(p(HGNC:MAPT))
• p(HBP:"Tau epitope, CP13") decreases act(p(HGNC:MAPT))
• act(p(HGNC:GSK3B), ma(kin)) increases p(HGNC:MAPT, pmod(Ph, Ser, 199))
• act(p(HGNC:GSK3B), ma(kin)) increases p(HGNC:MAPT, pmod(Ph, Ser, 396))
• act(p(HGNC:GSK3B), ma(kin)) increases p(HGNC:MAPT, pmod(Ph, Ser, 404))
• act(p(HGNC:GSK3B), ma(kin)) increases p(HBP:"Tau epitope, AT8")

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