EGFR oligomerization organizes kinase-active dimers into competent signalling platforms
Epidermal growth factor receptors have been shown to oligomerise upon binding to their cognate ligands. Here, the authors use biochemical, biophysical and cell biology techniques to analyse the structures of these oligomers, and argue that these formations are required for signalling.
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Nature Portfolio
2016
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Acceso en línea: | https://doaj.org/article/4106f1db16d64a39ab5d782e227f6e6e |
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oai:doaj.org-article:4106f1db16d64a39ab5d782e227f6e6e2021-12-02T16:57:02ZEGFR oligomerization organizes kinase-active dimers into competent signalling platforms10.1038/ncomms133072041-1723https://doaj.org/article/4106f1db16d64a39ab5d782e227f6e6e2016-10-01T00:00:00Zhttps://doi.org/10.1038/ncomms13307https://doaj.org/toc/2041-1723Epidermal growth factor receptors have been shown to oligomerise upon binding to their cognate ligands. Here, the authors use biochemical, biophysical and cell biology techniques to analyse the structures of these oligomers, and argue that these formations are required for signalling.Sarah R. NeedhamSelene K. RobertsAnton ArkhipovVenkatesh P. MysoreChristopher J. TynanLaura C. Zanetti-DominguesEric T. KimValeria LosassoDimitrios KorovesisMichael HirschDaniel J. RolfeDavid T. ClarkeMartyn D. WinnAlireza LajevardipourAndrew H. A. ClaytonLinda J. PikeMichela PeraniPeter J. ParkerYibing ShanDavid E. ShawMarisa L. Martin-FernandezNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-14 (2016) |
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Science Q |
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Science Q Sarah R. Needham Selene K. Roberts Anton Arkhipov Venkatesh P. Mysore Christopher J. Tynan Laura C. Zanetti-Domingues Eric T. Kim Valeria Losasso Dimitrios Korovesis Michael Hirsch Daniel J. Rolfe David T. Clarke Martyn D. Winn Alireza Lajevardipour Andrew H. A. Clayton Linda J. Pike Michela Perani Peter J. Parker Yibing Shan David E. Shaw Marisa L. Martin-Fernandez EGFR oligomerization organizes kinase-active dimers into competent signalling platforms |
description |
Epidermal growth factor receptors have been shown to oligomerise upon binding to their cognate ligands. Here, the authors use biochemical, biophysical and cell biology techniques to analyse the structures of these oligomers, and argue that these formations are required for signalling. |
format |
article |
author |
Sarah R. Needham Selene K. Roberts Anton Arkhipov Venkatesh P. Mysore Christopher J. Tynan Laura C. Zanetti-Domingues Eric T. Kim Valeria Losasso Dimitrios Korovesis Michael Hirsch Daniel J. Rolfe David T. Clarke Martyn D. Winn Alireza Lajevardipour Andrew H. A. Clayton Linda J. Pike Michela Perani Peter J. Parker Yibing Shan David E. Shaw Marisa L. Martin-Fernandez |
author_facet |
Sarah R. Needham Selene K. Roberts Anton Arkhipov Venkatesh P. Mysore Christopher J. Tynan Laura C. Zanetti-Domingues Eric T. Kim Valeria Losasso Dimitrios Korovesis Michael Hirsch Daniel J. Rolfe David T. Clarke Martyn D. Winn Alireza Lajevardipour Andrew H. A. Clayton Linda J. Pike Michela Perani Peter J. Parker Yibing Shan David E. Shaw Marisa L. Martin-Fernandez |
author_sort |
Sarah R. Needham |
title |
EGFR oligomerization organizes kinase-active dimers into competent signalling platforms |
title_short |
EGFR oligomerization organizes kinase-active dimers into competent signalling platforms |
title_full |
EGFR oligomerization organizes kinase-active dimers into competent signalling platforms |
title_fullStr |
EGFR oligomerization organizes kinase-active dimers into competent signalling platforms |
title_full_unstemmed |
EGFR oligomerization organizes kinase-active dimers into competent signalling platforms |
title_sort |
egfr oligomerization organizes kinase-active dimers into competent signalling platforms |
publisher |
Nature Portfolio |
publishDate |
2016 |
url |
https://doaj.org/article/4106f1db16d64a39ab5d782e227f6e6e |
work_keys_str_mv |
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