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This Service

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.

This Project

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.

IndraLab

Statements

EGF phosphorylates PTK2 on Y397. 3 / 3

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"CD99CRIII3 inhibited EGF-induced phosphorylation of FAK at Y397."

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"XREF_BIBR - XREF_BIBR Here, we stress our new finding in this experiment that EGF caused tyrosine phosphorylation of FAK (Y397) and p130cas (Y410), and Fn caused general phosphorylation of ERK, which were neglected before."

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"Integrin stimulated FAK autophosphorylation at Tyr 397 and epidermal growth factor (EGF)-stimulated trans-phosphorylation of FAK at Tyr 397 creates a high-affinity binding site for the Src-homology 2 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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Our Sources:

INDRA allows us to combine the results from a multitude of sources. In particular, the INDRA Database draws on the following...