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

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

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6123813

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

About this item

Full title

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

Publisher

London: Nature Publishing Group UK

Journal title

Communications biology, 2018-02, Vol.1 (1), p.15-15, Article 15

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The EphA2 receptor tyrosine kinase is capable of activating multiple diverse signaling pathways with roles in processes such as tissue homeostasis and cancer. EphA2 is known to form activated oligomers in the presence of ephrin-A ligands. Here, we characterize the lateral interactions between full-length EphA2 molecules in the plasma membrane in th...

Alternative Titles

Full title

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

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6123813

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6123813

Other Identifiers

ISSN

2399-3642

E-ISSN

2399-3642

DOI

10.1038/s42003-018-0017-7

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