Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Insights into Eph receptor tyrosine kinase activation from crystal structures of the EphA4 ectodomain and its complex with ephrin-A5.

Proceedings of the National Academy of Sciences of the United States of America - 3 Sept 2013

Xu Kai, Tzvetkova-Robev Dorothea, Xu Yan, Goldgur Yehuda, Chan Yee-Peng, Himanen Juha P, Nikolov Dimitar B

Abstract excerpt

Eph receptor tyrosine kinases and their ephrin ligands mediate cell signaling during normal and oncogenic development. Eph signaling is initiated in a multistep process leading to the assembly of higher-order Eph/ephrin clusters that set off bidirectional signaling in interacting cells. Eph and ephrins are divided in two subclasses based on their abilities to bind and activate each other and on sequence...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding Sites
Share to Blotting, Western

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Enzyme Activation

Share to HEK293 Cells

Share to Protein Conformation

Share to Protein Multimerization

Share to Protein Structure, Tertiary

Source

Open in PubMed Open full text

Identifiers

PMID: 23959867
DOI: 10.1073/pnas.1311000110
PMCID: PMC3767517

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Insights into Eph receptor tyrosine kinase activation from crystal structures of the EphA4 ectodomain and its complex with ephrin-A5.PMID 23959867Read ↗

Three distinct molecular surfaces in ephrin-A5 are essential for a functional interaction with EphA3.Semantic proximity Read ↗

Eph receptor signaling and ephrins.Semantic proximity Read ↗

Dancing with the dead: Eph receptors and their kinase-null partners.Semantic proximity Read ↗

Ephrin receptor A4 (EphA4) is a new Kaposi’s sarcoma-associated herpesvirus virus entry receptorSemantic proximity Read ↗

EPH Receptor Tyrosine Kinases Regulate Epithelial Morphogenesis and Phosphorylate the PAR-3 Scaffold Protein to Modulate Downstream Signaling NetworksSemantic proximity Read ↗

Autoregulation by the juxtamembrane region of the human ephrin receptor tyrosine kinase A3 (EphA3).Semantic proximity Read ↗

Phosphorylation of tyrosine residues in the kinase domain and juxtamembrane region regulates the biological and catalytic activities of Eph receptors.Semantic proximity Read ↗

The Sequence Basis for Selectivity of Ephrin-B2 Ligand for Eph Receptors and Pathogenic Henipavirus G GlycoproteinsSemantic proximity Read ↗

Eph Receptors and Ephrins: Therapeutic OpportunitiesSemantic proximity Read ↗

Molecular Characteristics and Prognostic Role of EPHA2 in Human Tumors via Pan-cancer AnalysisSemantic proximity Read ↗

EphA2 Receptor Tyrosine Kinase as a Promising Target for Cancer TherapeuticsSemantic proximity Read ↗

Notch-Jagged signaling complex defined by an interaction mosaic.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.