Gene interactions and pathways from curated databases and text-mining

◀ Back to AHSA1

AHSA1 — EGF

Text-mined interactions from Literome

Rebsamen et al., J Mol Cell Cardiol 2000 (Cardiomegaly) : The results further show that EGF activates Stat5, that this response requires p38 MAPK stimulation, and it is negatively modulated by p42/44 MAPK
Stoll et al., Wound Repair Regen 2003 (MAP Kinase Signaling System) : These data also indicate that autocrine heparin binding epidermal growth factor expression is not regulated by p38
Cooper et al., Toxicol Appl Pharmacol 2004 : In contrast, p38 activation was independent of EGF receptor or Src-family kinase activity
Guo et al., World J Gastroenterol 2005 : The data suggest that TPA and EGF induced p38 phosphorylation is through an autophosphorylation dependent mechanism ... Since p38 phosphorylation induced by TGF-beta1 plays an important role in caspase activation and apoptosis, TPA and EGF induced p38 phosphorylation may not be requisite for their anti-apoptotic function
Singh et al., Mol Cancer Ther 2006 (MAP Kinase Signaling System) : Silibinin treatment under similar conditions also strongly inhibited EGF induced ERK1/2, JNK1/2, and p38K as well as Akt phosphorylation, and also suppressed EGF induced AP-1 and NF-kappaB activation
Wang et al., Invest Ophthalmol Vis Sci 2006 : EGF induced changes in Erk1/2 and p38 phosphorylation status are dependent on PP-mediated crosstalk
Browne et al., Biochem Biophys Res Commun 2008 : ERK5 activation by either TGF-beta or epidermal growth factor (EGF) was also inhibited by the p38 MAP kinase inhibitor, SB-202190
Lofgren et al., Breast Cancer Res 2011 (Breast Neoplasms...) : Brk dependent signaling to p38 MAPK was recapitulated by Brk overexpression in the HC11 murine mammary epithelial cell (MEC) line and human MEC, while Brk knock-down in breast cancer cells blocked EGF stimulated p38 signaling
Hazzalin et al., Mol Cell Biol 1998 : These data show that anisomycin behaves like a true signalling agonist and suggest that the anisomycin desensitized signalling component ( s ) is not involved in JNK/SAPK or p38/RK activation by EGF , bFGF, TNF-alpha, or TPA but may play a significant role in UV- and hyperosmolarity stimulated responses
Chan-Hui et al., Biochem J 1998 : Kinase-inactive DeltaMAPKKK4 partly inhibited the activation of p38alpha , JNK1/2 and ERK2 induced by stress, tumour necrosis factor alpha or epidermal growth factor , suggesting that MAPKKK4 might be physiologically involved in all three MAPK cascades