The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures

Publication Date:
2018-03-06
Publisher:
Springer Nature
Electronic ISSN:
2399-3642
Topics:
Biology
Published by:
https://www.springernature.com/
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autor Deo R. Singh; Pranjali Kanvinde; Christopher King; Elena B. Pasquale; Kalina Hristova
beschreibung The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures, Published online: 22 February 2018; doi:10.1038/s42003-018-0017-7 Deo Singh et al. use Fully Quantified Spectral Imaging-FRET to show that the EphA2 receptor forms dimers or higher order oligomers depending on the type of ligand, and that different ligands stabilize EphA2 dimers through distinct interfaces. These findings may explain how EphA2 activates diverse signaling pathways.
citation_standardnr 6182449
datenlieferant ipn_articles
feed_id 314547
feed_publisher Springer Nature
feed_publisher_url https://www.springernature.com/
insertion_date 2018-03-06
journaleissn 2399-3642
publikationsjahr_anzeige 2018
publikationsjahr_facette 2018
publikationsjahr_intervall 7984:2015-2019
publikationsjahr_sort 2018
publisher Springer Nature
quelle Communications Biology
relation http://feeds.nature.com/~r/commsbio/rss/current/~3/lf-FhUTtQuo/s42003-018-0017-7
search_space articles
shingle_author_1 Deo R. Singh; Pranjali Kanvinde; Christopher King; Elena B. Pasquale; Kalina Hristova
shingle_author_2 Deo R. Singh; Pranjali Kanvinde; Christopher King; Elena B. Pasquale; Kalina Hristova
shingle_author_3 Deo R. Singh; Pranjali Kanvinde; Christopher King; Elena B. Pasquale; Kalina Hristova
shingle_author_4 Deo R. Singh; Pranjali Kanvinde; Christopher King; Elena B. Pasquale; Kalina Hristova
shingle_catch_all_1 The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures
The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures, Published online: 22 February 2018; doi:10.1038/s42003-018-0017-7 Deo Singh et al. use Fully Quantified Spectral Imaging-FRET to show that the EphA2 receptor forms dimers or higher order oligomers depending on the type of ligand, and that different ligands stabilize EphA2 dimers through distinct interfaces. These findings may explain how EphA2 activates diverse signaling pathways.
Deo R. Singh; Pranjali Kanvinde; Christopher King; Elena B. Pasquale; Kalina Hristova
Springer Nature
2399-3642
23993642
shingle_catch_all_2 The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures
The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures, Published online: 22 February 2018; doi:10.1038/s42003-018-0017-7 Deo Singh et al. use Fully Quantified Spectral Imaging-FRET to show that the EphA2 receptor forms dimers or higher order oligomers depending on the type of ligand, and that different ligands stabilize EphA2 dimers through distinct interfaces. These findings may explain how EphA2 activates diverse signaling pathways.
Deo R. Singh; Pranjali Kanvinde; Christopher King; Elena B. Pasquale; Kalina Hristova
Springer Nature
2399-3642
23993642
shingle_catch_all_3 The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures
The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures, Published online: 22 February 2018; doi:10.1038/s42003-018-0017-7 Deo Singh et al. use Fully Quantified Spectral Imaging-FRET to show that the EphA2 receptor forms dimers or higher order oligomers depending on the type of ligand, and that different ligands stabilize EphA2 dimers through distinct interfaces. These findings may explain how EphA2 activates diverse signaling pathways.
Deo R. Singh; Pranjali Kanvinde; Christopher King; Elena B. Pasquale; Kalina Hristova
Springer Nature
2399-3642
23993642
shingle_catch_all_4 The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures
The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures, Published online: 22 February 2018; doi:10.1038/s42003-018-0017-7 Deo Singh et al. use Fully Quantified Spectral Imaging-FRET to show that the EphA2 receptor forms dimers or higher order oligomers depending on the type of ligand, and that different ligands stabilize EphA2 dimers through distinct interfaces. These findings may explain how EphA2 activates diverse signaling pathways.
Deo R. Singh; Pranjali Kanvinde; Christopher King; Elena B. Pasquale; Kalina Hristova
Springer Nature
2399-3642
23993642
shingle_title_1 The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures
shingle_title_2 The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures
shingle_title_3 The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures
shingle_title_4 The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures
timestamp 2025-07-31T23:42:42.736Z
titel The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures
titel_suche The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures
topic W
uid ipn_articles_6182449