Exploring higher-order EGFR oligomerisation and phosphorylation—a combined experimental and theoretical approach†
Abstract
The epidermal growth factor receptor (EGFR) kinase is generally considered to be activated by either
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* Corresponding authors
a
Centre for Micro-Photonics, Faculty of Engineering and Industrial Sciences, Cell Biophysics Laboratory, Swinburne University of Technology, PO Box 218, Hawthorn, Victoria 3122, Australia
E-mail:
aclayton@swin.edu.au
Fax: +61-3-9214-5435
Tel: +61-3-9214-5719
b
Theoretical Biology and Biophysics Group, Theoretical Division & Center for Nonlinear Studies, Mail Stop K710, Los Alamos National Laboratory, Los Alamos, New Mexico 87545, USA
E-mail:
wish@lanl.gov
Fax: +1-505-665-2616
Tel: +1-505-665-1355
c
Ludwig Institute for Cancer Research, Melbourne-Parkville Branch, PO Box 2008, Royal Melbourne Hospital, Victoria 3050, Australia
E-mail:
tburgess@wehi.edu.au
d Department of Biochemistry, Monash University, Clayton, Victoria 3080, Australia
The epidermal growth factor receptor (EGFR) kinase is generally considered to be activated by either
N. Kozer, D. Barua, S. Orchard, E. C. Nice, A. W. Burgess, W. S. Hlavacek and A. H. A. Clayton, Mol. BioSyst., 2013, 9, 1849 DOI: 10.1039/C3MB70073A
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