Subject/object roles reversed.

[johnbachman]

I'm attaching some sentences where REACH is extracting that "X regulates/phosphorylates/etc EGF", where EGF (epidermal growth factor) is incorrectly identified as the object of the relation.

This may be related to #250, #327, and #609.

For the following sentences, REACH extracts "EGFR activates EGF". Because EGF is the ligand and EGFR the cognate receptor that EGF activates, this extraction (which appears 172 times in our corpus) is pretty much guaranteed to be incorrect. Examples:

EGF endogenous and exogenous effects on papilla formation are mediated by EGFR.

Dacomitinib but not Cetuximab Inhibits EGF Stimulated EGFR Downstream Pathways.

Whereas specific inhibition of the EGFR kinase activity blocked EGF- but not GPCR agonist induced Met receptor transactivation, it was abrogated in the presence of a reducing agent or treatment of cells with a NADPH oxidase inhibitor.

We next explored whether SWNT functionalized with EGF targets EGFR on HNSCC cultures in vitro (XREF_FIG).

In conclusion, over-expression of GH induces the increase in EGFR expression but does not result in up-regulation of EGF signaling.

When EGFR is activated by its physiological ligands, transforming growth factor-alpha or EGF, various enabled G protein linked kinases affect the transcription and secretion of growth enhancing mediators.

However, forced overexpression of EGFR enables EGF to produce persistent MAPK activation and induce neurite outgrowth.

Similar to above, but with the opposite polarity, "EGFR inhibits EGF":

As XREF_FIG illustrates, addition of the EGFR tyrosine kinase inhibitor Iressa (10 muM) inhibits EGF stimulated migration in this assay, as do the direct myosin II inhibitor blebbistatin and an inhibitor of Rho kinase (ROCK; Y27632), which is an immediate upstream activator of myosin II.

The EGFR specific tyrosine kinase inhibitor C56 blocked the effect of excess EGF, indicating that the neurotoxicity was mediated through EGFR signaling.

This interaction, in turn, inhibits EGF stimulated ubiquitination and internalization of ErbB1, thus allowing prolonged activation of EGF mediated downstream signaling events (XREF_FIG).

Sentences yielding "ERK/MAPK activates EGF", also incorrect:

However, only p38 inhibition, and not inhibition of PI3K and AKT or MEK and ERK, blocked EGF mediated cell scattering.

Cytoprotective responses involve dominantly mitogen activated protein kinase (MAPK) through radiation induced activation of EGF receptors and may stimulate cell proliferation if radiation induced damage is successfully repaired.

The knockdown of ERK1/2 by siRNA significantly reduced both EGF- and IL-1beta-induced AP-1 activation in a dose dependent manner (P < 0.05 compared with control siRNA, independent sample t-test).

TGF-beta1 Reduces Cell Cycle and Cytochrome P450 Metabolism Pathways, While EGF Increases MAPK and PI3K-Akt Pathways.

Immunoblotting showed that inhibition of ERK and PI3K by the respective small-molecule inhibitors U0126 and LY294002 blocked the EGF induction of FOXC1, while JNK inhibition by SP600125 did not (XREF_FIG).

More available upon request. Thanks!

[MihaiSurdeanu]

Thanks @johnbachman!