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Effect of phosphorylation on EGFR dimer stability probed by single-molecule dynamics and FRET/FLIM

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...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's Version

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Publisher copy:
10.1016/j.bpj.2015.01.005

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Role:
Author
ORCID:
0000-0002-8394-8395
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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:

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