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Appears in Networks 2

In-Edges 1

act(p(FPLX:HSP90)) association a(CHEBI:celastrol) View Subject | View Object

More recently, there has also been interest in developing compounds, such as celastrol (Figure 1), that selectively disrupt association of co-chaperones with Hsp90 as an alternative way to control chaperone activity [93–96]. PubMed:21882945

Out-Edges 3

a(CHEBI:celastrol) association act(p(FPLX:HSP90)) View Subject | View Object

More recently, there has also been interest in developing compounds, such as celastrol (Figure 1), that selectively disrupt association of co-chaperones with Hsp90 as an alternative way to control chaperone activity [93–96]. PubMed:21882945

a(CHEBI:celastrol) decreases act(p(FPLX:HSP90)) View Subject | View Object

The Cdc37/Hsp90 inhibitors, Celasterol and Withaferin A (Zhang et al., 2008; Yu et al., 2010), reduce tau levels and a new compound, platycodin D has just been discovered (Li et al., 2017). Platycodin D does not affect the ATPase activity of Hsp90, but instead disrupts the interaction between Hsp90 and Cdc37 leading to client protein degradation without an increase in Hsp70 (Li et al., 2017). PubMed:29311797

a(CHEBI:celastrol) decreases p(HGNC:MAPT) View Subject | View Object

The Cdc37/Hsp90 inhibitors, Celasterol and Withaferin A (Zhang et al., 2008; Yu et al., 2010), reduce tau levels and a new compound, platycodin D has just been discovered (Li et al., 2017). Platycodin D does not affect the ATPase activity of Hsp90, but instead disrupts the interaction between Hsp90 and Cdc37 leading to client protein degradation without an increase in Hsp70 (Li et al., 2017). PubMed:29311797

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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.