Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors

Beyond homotypic receptor interactions that are required for Eph signaling, ligand-independent association and crosstalk between members of the EphA and -B subclasses determine cell signaling outcomes.

Bibliographic Details
Main Authors:	Janes, Peter W., Griesshaber, Bettina, Atapattu, Lakmali, Nievergall, Eva, Hii, Linda L., Mensinga, Anneloes, Chheang, Chanly, Day, Bryan W., Boyd, Andrew W., Bastiaens, Philippe I., Jørgensen, Claus, Pawson, Tony, Lackmann, Martin
Format:	Online
Language:	English
Published:	The Rockefeller University Press 2011
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3241718/

id	pubmed-3241718
recordtype	oai_dc
spelling	pubmed-32417182012-06-12 Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors Janes, Peter W. Griesshaber, Bettina Atapattu, Lakmali Nievergall, Eva Hii, Linda L. Mensinga, Anneloes Chheang, Chanly Day, Bryan W. Boyd, Andrew W. Bastiaens, Philippe I. Jørgensen, Claus Pawson, Tony Lackmann, Martin Research Articles Beyond homotypic receptor interactions that are required for Eph signaling, ligand-independent association and crosstalk between members of the EphA and -B subclasses determine cell signaling outcomes. The Rockefeller University Press 2011-12-12 /pmc/articles/PMC3241718/ /pubmed/22144690 http://dx.doi.org/10.1083/jcb.201104037 Text en © 2011 Janes et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Janes, Peter W. Griesshaber, Bettina Atapattu, Lakmali Nievergall, Eva Hii, Linda L. Mensinga, Anneloes Chheang, Chanly Day, Bryan W. Boyd, Andrew W. Bastiaens, Philippe I. Jørgensen, Claus Pawson, Tony Lackmann, Martin
spellingShingle	Janes, Peter W. Griesshaber, Bettina Atapattu, Lakmali Nievergall, Eva Hii, Linda L. Mensinga, Anneloes Chheang, Chanly Day, Bryan W. Boyd, Andrew W. Bastiaens, Philippe I. Jørgensen, Claus Pawson, Tony Lackmann, Martin Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors
author_facet	Janes, Peter W. Griesshaber, Bettina Atapattu, Lakmali Nievergall, Eva Hii, Linda L. Mensinga, Anneloes Chheang, Chanly Day, Bryan W. Boyd, Andrew W. Bastiaens, Philippe I. Jørgensen, Claus Pawson, Tony Lackmann, Martin
author_sort	Janes, Peter W.
title	Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors
title_short	Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors
title_full	Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors
title_fullStr	Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors
title_full_unstemmed	Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors
title_sort	eph receptor function is modulated by heterooligomerization of a and b type eph receptors
description	Beyond homotypic receptor interactions that are required for Eph signaling, ligand-independent association and crosstalk between members of the EphA and -B subclasses determine cell signaling outcomes.
publisher	The Rockefeller University Press
publishDate	2011
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3241718/
_version_	1611495625841442816

Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors

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