Equivalencies: 0 | Classes: 0 | Children: 0 | Explore

Appears in Networks 3

In-Edges 6

deg(p(HGNC:MAPT)) negativeCorrelation p(HGNC:AKT1) View Subject | View Object

Interestingly, it was recently found that reducing the levels of Akt, another client of the Hsp90/CHIP complex, facilitates tau degradation [123], suggesting a synchronized balance between competing Hsp90 substrates that may be driven, in part, by their relative abundance or susceptibility to Hsp90 binding PubMed:21882945

complex(p(FPLX:HSP90), p(HGNC:STUB1)) association p(HGNC:AKT1) View Subject | View Object

Interestingly, it was recently found that reducing the levels of Akt, another client of the Hsp90/CHIP complex, facilitates tau degradation [123], suggesting a synchronized balance between competing Hsp90 substrates that may be driven, in part, by their relative abundance or susceptibility to Hsp90 binding PubMed:21882945

complex(p(HGNC:CDC37), p(SFAM:"HSP90 Family")) positiveCorrelation act(p(HGNC:AKT1), ma(kin)) View Subject | View Object

This coordination of kinase triage decisions by Hsp90 requires the co-chaperone Cdc37 (cell division cycle protein 37). The Hsp90/Cdc37 machine is essential for the maturation of a number of kinases, including Akt PubMed:21367866

a(PUBCHEM:9832404) decreases p(HGNC:AKT1) View Subject | View Object

In female mice, Akt1 (above) and ionized calcium–binding adapter molecule 1 (Iba1), a marker of microglial activation that crosslinks actin (42), were markedly increased in the Adnp+/– mouse spleen and normalized by NAP treatment, suggesting a potential peripheral inflammation–linked biomarker PubMed:30106381

p(HGNC:ADNP, pmod(MESH:Haploinsufficiency)) increases p(HGNC:AKT1) View Subject | View Object

In female mice, Akt1 (above) and ionized calcium–binding adapter molecule 1 (Iba1), a marker of microglial activation that crosslinks actin (42), were markedly increased in the Adnp+/– mouse spleen and normalized by NAP treatment, suggesting a potential peripheral inflammation–linked biomarker PubMed:30106381

Out-Edges 4

p(HGNC:AKT1) association complex(p(FPLX:HSP90), p(HGNC:STUB1)) View Subject | View Object

Interestingly, it was recently found that reducing the levels of Akt, another client of the Hsp90/CHIP complex, facilitates tau degradation [123], suggesting a synchronized balance between competing Hsp90 substrates that may be driven, in part, by their relative abundance or susceptibility to Hsp90 binding PubMed:21882945

p(HGNC:AKT1) negativeCorrelation deg(p(HGNC:MAPT)) View Subject | View Object

Interestingly, it was recently found that reducing the levels of Akt, another client of the Hsp90/CHIP complex, facilitates tau degradation [123], suggesting a synchronized balance between competing Hsp90 substrates that may be driven, in part, by their relative abundance or susceptibility to Hsp90 binding PubMed:21882945

act(p(HGNC:AKT1), ma(kin)) positiveCorrelation complex(p(HGNC:CDC37), p(SFAM:"HSP90 Family")) View Subject | View Object

This coordination of kinase triage decisions by Hsp90 requires the co-chaperone Cdc37 (cell division cycle protein 37). The Hsp90/Cdc37 machine is essential for the maturation of a number of kinases, including Akt PubMed:21367866

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.