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Appears in Networks 2

In-Edges 3

p(HGNC:HSPB1) directlyIncreases complex(p(HGNC:HSPB1), p(HGNC:MAPT, pmod(Ph))) View Subject | View Object

Hsp27 has emerged as a potential target for tau regulation based on early findings that it preferentially binds to phosphorylated and hyperphosphorylated tau and promotes their clearance [125,126] PubMed:21882945

p(HGNC:HSPB1) increases complex(p(HGNC:HSPB1), p(HGNC:MAPT, pmod(Ph))) View Subject | View Object

Here we show that heat shock protein 27 (Hsp27) preferentially binds pathological hyperphosphorylated tau and paired helical filaments tau directly but not non-phosphorylated tau. The formation of this complex altered the conformation of pathological hyperphosphorylated tau and reduced its concentration by facilitating its degradation and dephosphorylation. PubMed:14963027

Annotations
Uberon
temporal cortex

p(HGNC:MAPT, pmod(Ph)) increases complex(p(HGNC:HSPB1), p(HGNC:MAPT, pmod(Ph))) View Subject | View Object

Here we show that heat shock protein 27 (Hsp27) preferentially binds pathological hyperphosphorylated tau and paired helical filaments tau directly but not non-phosphorylated tau. The formation of this complex altered the conformation of pathological hyperphosphorylated tau and reduced its concentration by facilitating its degradation and dephosphorylation. PubMed:14963027

Annotations
Uberon
temporal cortex

Out-Edges 5

complex(p(HGNC:HSPB1), p(HGNC:MAPT, pmod(Ph))) increases deg(p(HGNC:MAPT, pmod(Ph))) View Subject | View Object

Hsp27 has emerged as a potential target for tau regulation based on early findings that it preferentially binds to phosphorylated and hyperphosphorylated tau and promotes their clearance [125,126] PubMed:21882945

complex(p(HGNC:HSPB1), p(HGNC:MAPT, pmod(Ph))) increases deg(p(HGNC:MAPT, pmod(Ph))) View Subject | View Object

Here we show that heat shock protein 27 (Hsp27) preferentially binds pathological hyperphosphorylated tau and paired helical filaments tau directly but not non-phosphorylated tau. The formation of this complex altered the conformation of pathological hyperphosphorylated tau and reduced its concentration by facilitating its degradation and dephosphorylation. PubMed:14963027

Annotations
Uberon
temporal cortex

complex(p(HGNC:HSPB1), p(HGNC:MAPT, pmod(Ph))) increases rxn(reactants(p(HGNC:MAPT, pmod(Ph))), products(a(CHEBI:"phosphate(3-)"), p(HGNC:MAPT))) View Subject | View Object

Here we show that heat shock protein 27 (Hsp27) preferentially binds pathological hyperphosphorylated tau and paired helical filaments tau directly but not non-phosphorylated tau. The formation of this complex altered the conformation of pathological hyperphosphorylated tau and reduced its concentration by facilitating its degradation and dephosphorylation. PubMed:14963027

Annotations
Uberon
temporal cortex

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.