p(HBP:"Tau isoform F (441 aa)", var("p.Arg406Tyr"))

Entity

Name

Tau isoform F (441 aa)

Namespace

HBP

Namespace Version

20181119

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/90e1cb9e5e882703380c9db8d4915ac6f3cba137/export/hbp-names.belns

TAU Interactions Section of NESTOR

The quantification of all immunoreactive bands revealed that the R406W mutation exhibits a decreased phosphorylation at T205, T212, and the PHF1 epitope (S396/S404; reductions of 40–65%) as compared with wt tau, whereas other sites were not affected or only slightly affected (T181, S199, S214, and S262). PubMed:21339331

The quantification of all immunoreactive bands revealed that the R406W mutation exhibits a decreased phosphorylation at T205, T212, and the PHF1 epitope (S396/S404; reductions of 40–65%) as compared with wt tau, whereas other sites were not affected or only slightly affected (T181, S199, S214, and S262). PubMed:21339331

The quantification of all immunoreactive bands revealed that the R406W mutation exhibits a decreased phosphorylation at T205, T212, and the PHF1 epitope (S396/S404; reductions of 40–65%) as compared with wt tau, whereas other sites were not affected or only slightly affected (T181, S199, S214, and S262). PubMed:21339331

The quantification of all immunoreactive bands revealed that the R406W mutation exhibits a decreased phosphorylation at T205, T212, and the PHF1 epitope (S396/S404; reductions of 40–65%) as compared with wt tau, whereas other sites were not affected or only slightly affected (T181, S199, S214, and S262). PubMed:21339331

The data suggest that tau’s membrane association causes retention of tau in the tip of neurites, which is compromised by the R406W mutation. Also, after BAPTA treatment, the difference in the retention of wt tau and R406W tau was abolished (Fig. 9 D), which again suggests that tau trapping is caused by an interaction with AnxA2 at the membrane. PubMed:21339331