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  3. complex(a(MESH:Proteins), p(HGNC:STUB1), p(INTERPRO:"Heat shock protein 70 family"))

complex(a(MESH:Proteins), p(HGNC:STUB1), p(INTERPRO:"Heat shock protein 70 family"))

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Components

Appears in Networks 1

Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies v1.0.0

In-Edges 1

complex(a(MESH:Proteins), p(INTERPRO:"Heat shock protein 70 family")) positiveCorrelation complex(a(MESH:Proteins), p(HGNC:STUB1), p(INTERPRO:"Heat shock protein 70 family")) View Subject | View Object

In this model,accumulation of an Hsp70–substrate complex (either via treatment with chemical inhibitors or because of intrinsic properties of the substrate) might allow enough time for a degradation factor (e.g., CHIP) to bind and facilitate polyubiquitination. PubMed:21882945

Appears in Networks:

Out-Edges 5

complex(a(MESH:Proteins), p(HGNC:STUB1), p(INTERPRO:"Heat shock protein 70 family")) hasComponent a(MESH:Proteins) View Subject | View Object

Appears in Networks:

complex(a(MESH:Proteins), p(HGNC:STUB1), p(INTERPRO:"Heat shock protein 70 family")) hasComponent p(HGNC:STUB1) View Subject | View Object

Appears in Networks:

complex(a(MESH:Proteins), p(HGNC:STUB1), p(INTERPRO:"Heat shock protein 70 family")) hasComponent p(INTERPRO:"Heat shock protein 70 family") View Subject | View Object

Appears in Networks:

complex(a(MESH:Proteins), p(HGNC:STUB1), p(INTERPRO:"Heat shock protein 70 family")) positiveCorrelation complex(a(MESH:Proteins), p(INTERPRO:"Heat shock protein 70 family")) View Subject | View Object

In this model,accumulation of an Hsp70–substrate complex (either via treatment with chemical inhibitors or because of intrinsic properties of the substrate) might allow enough time for a degradation factor (e.g., CHIP) to bind and facilitate polyubiquitination. PubMed:21882945

Appears in Networks:

complex(a(MESH:Proteins), p(HGNC:STUB1), p(INTERPRO:"Heat shock protein 70 family")) increases bp(GO:"protein polyubiquitination") View Subject | View Object

In this model,accumulation of an Hsp70–substrate complex (either via treatment with chemical inhibitors or because of intrinsic properties of the substrate) might allow enough time for a degradation factor (e.g., CHIP) to bind and facilitate polyubiquitination. PubMed:21882945

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.