TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 271, No. 16, Issue of April 19, pp. 9185–9188, 1996 Communication Printed in U.S.A. derive from distinct genes, are capable of binding to the extra- STAT Activation by Epidermal cellular domain of the EGF receptor. These ligands include Growth Factor (EGF) and EGF, transforming growth factor-a, amphiregulin (AR), hepa- rin binding EGF-like growth factor, epiregulin, and betacellu- Amphiregulin lin (2). All of these growth factors contain a characteristic EGF-like domain, which is defined by 6 evenly spaced cysteine REQUIREMENT FOR THE EGF RECEPTOR KINASE residues that generate 3 loops through the formation of disul- BUT NOT FOR TYROSINE PHOSPHORYLATION fide bonds. In the case of AR it has been demonstrated that SITES OR JAK1* heparan sulfate proteoglycans are necessary for activation of the EGF receptor and a cellular response (3). Upon ligand (Received for publication, November 28, 1995, and in revised binding, the intrinsic tyrosine kinase activity of the EGF re- form, February 8, 1996) ceptor is augmented, resulting in autophosphorylation as well Michael David‡§, Lily Wong‡, Richard Flavell , as the phosphorylation of specific intracellular substrates (4). Stewart A. Thompson , Alan Wells**, Among the target proteins that become phosphorylated in re- 
TI - STAT Activation by Epidermal Growth Factor (EGF) and Amphiregulin
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.271.16.9185
DA - 1996-04-01
UR - https://www.deepdyve.com/lp/unpaywall/stat-activation-by-epidermal-growth-factor-egf-and-amphiregulin-3vbkfB9ToM
DP - DeepDyve
ER -