- Abstract:
-
Deregulation of epidermal growth factor receptor (EGFR) signaling has been correlated with the development of a variety of human carcinomas. EGF-induced receptor dimerization and consequent trans- auto-phosphorylation are among the earliest events in signal transduction. Binding of EGF is thought to induce a conformational change that consequently unfolds an ectodomain loop required for dimerization indirectly. It may also induce important allosteric changes in the cytoplasmic domain. Despite...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's Version
- Files:
-
-
(html, 58.0KB)
-
- Publisher copy:
- 10.1016/j.bpj.2015.01.005
-
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- Publisher:
- Biophysical Society Publisher's website
- Journal:
- Biophysical Journal Journal website
- Volume:
- 108
- Issue:
- 5
- Pages:
- 1013-1026
- Publication date:
- 2015-03-10
- Acceptance date:
- 2015-01-07
- DOI:
- EISSN:
-
1542-0086
- ISSN:
-
0006-3495
- Pubs id:
-
pubs:514431
- URN:
-
uri:27500004-95db-459a-9e0f-0bc7afb438fa
- UUID:
-
uuid:27500004-95db-459a-9e0f-0bc7afb438fa
- Local pid:
- pubs:514431
- Language:
- English
- Keywords:
- Copyright holder:
- Coban et al.
- Copyright date:
- 2015
- Notes:
- Copyright © 2015 The Authors. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
Journal article
Effect of phosphorylation on EGFR dimer stability probed by single-molecule dynamics and FRET/FLIM
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