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a(HBP:"Tau Protein Secondary Structure, Turn")

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Entity

Name
Tau Protein Secondary Structure, Turn
Namespace
HBP
Namespace Version
20190207
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/cf4d8bb88754f036b943b4d94ad96e103dcb7149/export/hbp-names.belns

Appears in Networks 2

Identification of the Tau phosphorylation pattern that drives its aggregation v1.0.0

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

In-Edges 3

p(HGNC:MAPT, pmod(Ph, Ser, 202), pmod(Ph, Thr, 205)) increases a(HBP:"Tau Protein Secondary Structure, Turn") View Subject | View Object

When combined with ERK2 catalyzed phosphorylation, the turn-like disrupting G207V mutation in TauF8 hence leads to fast aggregation that already occurs during the phosphorylation reaction. PubMed:28784767

Appears in Networks:

p(HGNC:MAPT, pmod(Ph, Ser, 208)) decreases a(HBP:"Tau Protein Secondary Structure, Turn") View Subject | View Object

Indeed, Tau phosphorylation at the three positions, Ser202/Thr205/Ser208, while not at Ser262, is sufficient to induce aggregation without the addition of any exogenous aggregation inducer. PubMed:28784767

Appears in Networks:

p(HGNC:MAPT, var("p.Gly207Val")) decreases a(HBP:"Tau Protein Secondary Structure, Turn") View Subject | View Object

When combined with ERK2 catalyzed phosphorylation, the turn-like disrupting G207V mutation in TauF8 hence leads to fast aggregation that already occurs during the phosphorylation reaction. PubMed:28784767

Appears in Networks:

Out-Edges 4

a(HBP:"Tau Protein Secondary Structure, Turn") decreases a(HBP:"Tau aggregates") View Subject | View Object

Our finding that the resulting Tau species with phosphorylation at Ser202/Th205, but with a disrupted turn-like structure, forms abundant fibers detectable by thioflavin fluorescence or electron microscopy (Figs. 2 and 4) suggests the initial turn-like structure induced by the phosphorylation of only Ser202 and Thr205 is protective against aggregation. PubMed:28784767

Appears in Networks:

a(HBP:"Tau Protein Secondary Structure, Turn") decreases a(HBP:"Tau aggregates") View Subject | View Object

Indeed, Tau phosphorylation at the three positions, Ser202/Thr205/Ser208, while not at Ser262, is sufficient to induce aggregation without the addition of any exogenous aggregation inducer. PubMed:28784767

Appears in Networks:

a(HBP:"Tau Protein Secondary Structure, Turn") decreases bp(HBP:"Tau aggregates") View Subject | View Object

Our finding that the resulting Tau species with phosphorylation at Ser202/Th205, but with a disrupted turn-like structure, forms abundant fibers detectable by thioflavin fluorescence or electron microscopy (Figs. 2 and 4) suggests the initial turn-like structure induced by the phosphorylation of only Ser202 and Thr205 is protective against aggregation. PubMed:28784767

Appears in Networks:

a(HBP:"Tau Protein Secondary Structure, Turn") decreases bp(HBP:"Tau aggregates") View Subject | View Object

Indeed, Tau phosphorylation at the three positions, Ser202/Thr205/Ser208, while not at Ser262, is sufficient to induce aggregation without the addition of any exogenous aggregation inducer. PubMed:28784767

Appears in Networks:

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

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.