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Appears in Networks 2

TAU and Interaction Partners v1.2.5

TAU Interactions Section of NESTOR

Tau Modifications v1.9.5

Tau Modifications Sections of NESTOR

In-Edges 6

a(CHEBI:"calcium(2+)") increases act(p(FPLX:CALM)) View Subject | View Object

These findings provide new insights into the regulation of microtubule assembly, since Ca2+/calmodulin inhibition of tubulin polymerization into microtubules could be mediated by the direct binding of calmodulin to tau, thus preventing the interaction of this latter protein with tubulin. PubMed:2123288

p(HBP:"tubulin-binding repeat 2") association p(FPLX:CALM) View Subject | View Object

The present studies show that the calcium-binding protein calmodulin interacts with a tubulin binding site on tau defined by the second repetitive sequence PubMed:2123288

p(HBP:"DAPK, basic loop (BL) motif") positiveCorrelation act(p(FPLX:CALM)) View Subject | View Object

Unexpectedly, impairment of the basic loop interaction site completely abolishes calcium/calmodulin binding and DAPK2 activity is reduced to a residual level, indicative of coupled binding to the two sites. PubMed:27133022

Appears in Networks:

Out-Edges 5

p(FPLX:CALM) association p(HBP:"tubulin-binding repeat 2") View Subject | View Object

The present studies show that the calcium-binding protein calmodulin interacts with a tubulin binding site on tau defined by the second repetitive sequence PubMed:2123288

act(p(FPLX:CALM)) increases complex(a(CHEBI:"calcium(2+)"), p(FPLX:CALM)) View Subject | View Object

These findings provide new insights into the regulation of microtubule assembly, since Ca2+/calmodulin inhibition of tubulin polymerization into microtubules could be mediated by the direct binding of calmodulin to tau, thus preventing the interaction of this latter protein with tubulin. PubMed:2123288

act(p(FPLX:CALM)) decreases bp(GO:"microtubule polymerization") View Subject | View Object

These findings provide new insights into the regulation of microtubule assembly, since Ca2+/calmodulin inhibition of tubulin polymerization into microtubules could be mediated by the direct binding of calmodulin to tau, thus preventing the interaction of this latter protein with tubulin. PubMed:2123288

act(p(FPLX:CALM)) positiveCorrelation p(HBP:"DAPK, basic loop (BL) motif") View Subject | View Object

Unexpectedly, impairment of the basic loop interaction site completely abolishes calcium/calmodulin binding and DAPK2 activity is reduced to a residual level, indicative of coupled binding to the two sites. PubMed:27133022

Appears in Networks:

act(p(FPLX:CALM)) increases act(p(HGNC:DAPK2)) View Subject | View Object

Unexpectedly, impairment of the basic loop interaction site completely abolishes calcium/calmodulin binding and DAPK2 activity is reduced to a residual level, indicative of coupled binding to the two sites. PubMed:27133022

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.