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UCSC Genome Browser Gene Interaction Graph
Gene interactions and pathways from curated databases and text-mining

◀ Back to MAPK3

MAPK3 — SMAD6

Text-mined interactions from Literome

Wrana et al., Science's STKE : signal transduction knowledge environment 2000 : In the cytosol, Smad translocation might be inhibited by mitogen activated protein kinase dependent phosphorylation, whereas in the nucleus Smads interact with a number of transcription factors that themselves are primary targets of other signaling pathways
Lee et al., Int J Oncol 2004 (Stomach Neoplasms) : In this study, we examined effects of cell adhesion status on the TGF-beta1 mediated Erk1/2 regulation, and roles of Smad proteins on the cell adhesion mediated effects, using a gastric carcinoma cell variant
Zhao et al., Mol Cell Biochem 2008 (Fibrosis...) : Additionally, the inhibition of MAPK signaling had no effect on Smad activation elicited by chymase
Schievenbusch et al., Biochem Biophys Res Commun 2009 (Fibrosis) : As previously shown, Erk1/2 phosphorylation results in Smad-linker phosphorylation, thereby antagonizing cellular signals induced by TGFbeta
Zhu et al., Prostate 2010 (MAP Kinase Signaling System) : These findings suggest a dual role for PHB as a downstream determinant of the cellular response to TGF-beta via Smad dependent pathway ( apoptosis ) and MAPK intracellular signaling ( survival )
Rodrigues Díez et al., PloS one 2010 (Fibrosis) : In cultured rat VSMCs, direct AngII/Smad pathway activation was mediated by p38 MAPK and ROCK activation
Ungefroren et al., Int J Oncol 2011 (Carcinoma, Pancreatic Ductal...) : Biochemically, dnSrc inhibition failed to block TGF-ß1/ALK5 induced activation of Smad2 and Smad3, but partially inhibited transcriptional activation of TGF-ß/Smad-responsive reporter genes, and effectively blocked basal and TGF-ß1 induced activation of p38 MAPK