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complex(a(CHEBI:ATP), p(FPLX:HSP90))

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Components

Appears in Networks 2

Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies v1.0.0

Molecular Chaperone Functions in Protein Folding and Proteostasis v1.0.0

In-Edges 1

p(FPLX:HSP90, pmod(Ac)) decreases complex(a(CHEBI:ATP), p(FPLX:HSP90)) View Subject | View Object

Acetylation of Hsp90 affects client protein interaction and also decreases binding of Hsp90 to ATP (Yu et al., 2002; Mollapour and Neckers, 2012). PubMed:29311797

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Out-Edges 3

complex(a(CHEBI:ATP), p(FPLX:HSP90)) hasComponent a(CHEBI:ATP) View Subject | View Object

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complex(a(CHEBI:ATP), p(FPLX:HSP90)) hasComponent p(FPLX:HSP90) View Subject | View Object

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complex(a(CHEBI:ATP), p(FPLX:HSP90)) regulates act(p(FPLX:HSP90)) View Subject | View Object

Inhibition of ATP binding and hydrolysis either by mutagenesis of the N domain or by specific inhibitors, such as geldanamycin and radicicol, demonstrated the functional requirement of the Hsp90 ATPase (81, 169). PubMed:23746257

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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.