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A database built with INDRA combining content from numerous readers and databases. This page allows you to curate the loaded statements. For more information please see the manual.

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INDRA is developed by indralabs, a part of the Harvard Medical School Laboratory of Systems Pharmacology.

This project, indra_db, is also developed by the indralab team. For more information on how we procure our sources, you can go here. This work was funded by ARO grant W911NF‐15‐1‐0544 under the DARPA Communicating with Computers program.

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IRS1 binds mutated PIK3CA. 3 / 3

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"Interaction between the helical domain mutant p110alpha and IRS1 does not require p85 or IRS1 phosphorylation."

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"In support of earlier results, it was also notable that the stapled mutant peptide did slightly reduce the protein levels of p110alpha, but did not affect levels of p85 and IRS1 (XREF_FIG and XREF_SUPPLEMENTARY), providing further evidence that the protein interaction between mutant p110alpha and IRS1 stabilizes p110alpha."

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"We then tested if peptides corresponding to only one of the two alpha-helical motifs could inhibit interactions between the mutant p110alpha and IRS1."

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IRS1 binds mutated PIK3CA. 3 / 3

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