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p(SFAM:"CAMK2 Family")

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Entity

Name
CAMK2 Family
Namespace
SFAM
Namespace Version
20170725
Namespace URL
https://arty.scai.fraunhofer.de/artifactory/bel/namespace/selventa-protein-families/selventa-protein-families-20170725.belns

Appears in Networks 1

TAU and Interaction Partners v1.2.5

TAU Interactions Section of NESTOR

In-Edges 2

complex(p(HGNC:MAPT), p(HGNC:S100B)) decreases act(p(SFAM:"CAMK2 Family")) View Subject | View Object

We here confirmed the interaction of SlOOb with tau through affinity chromatography and crosslinking and demonstrated that such an interaction also inhibited mode I phosphorylation by a Ca2+/CaM-dependent kinase. Increasing Ca2+c oncentration to the 100 μM range potentiated the SlOOb effect. Therefore, although Ca2+-independent interactions may occur between SlOOb and protein tau, it is the Ca2+ form of SlOOb that has significant affinity for protein tau. In any case, Znz+ and Ca2+ both appear to be capabble of inducing a conformation in SlOOb that promotes its binding to target proteinins, including tau. PubMed:2833519

Appears in Networks:

act(p(HGNC:S100B)) decreases act(p(SFAM:"CAMK2 Family")) View Subject | View Object

We here confirmed the interaction of SlOOb with tau through affinity chromatography and crosslinking and demonstrated that such an interaction also inhibited mode I phosphorylation by a Ca2+/CaM-dependent kinase. Increasing Ca2+c oncentration to the 100 μM range potentiated the SlOOb effect. Therefore, although Ca2+-independent interactions may occur between SlOOb and protein tau, it is the Ca2+ form of SlOOb that has significant affinity for protein tau. In any case, Znz+ and Ca2+ both appear to be capabble of inducing a conformation in SlOOb that promotes its binding to target proteinins, including tau. PubMed:2833519

Appears in Networks:

Out-Edges 1

act(p(SFAM:"CAMK2 Family")) increases p(HGNC:MAPT, pmod(Ph)) View Subject | View Object

We here confirmed the interaction of SlOOb with tau through affinity chromatography and crosslinking and demonstrated that such an interaction also inhibited mode I phosphorylation by a Ca2+/CaM-dependent kinase. Increasing Ca2+c oncentration to the 100 μM range potentiated the SlOOb effect. Therefore, although Ca2+-independent interactions may occur between SlOOb and protein tau, it is the Ca2+ form of SlOOb that has significant affinity for protein tau. In any case, Znz+ and Ca2+ both appear to be capabble of inducing a conformation in SlOOb that promotes its binding to target proteinins, including tau. PubMed:2833519

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.