Structural Plasticity of Eph Receptor A4 Facilitates Cross-Class Ephrin Signaling (Q27657815)

Thomas A Bowden

1

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Joanne E. Nettleship

Joanne E Nettleship

3

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David Ian Stuart

David I Stuart

7

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Yvonne Jones

8

E Yvonne Jones

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author name string

A Radu Aricescu

2

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Nahid Rahman-Huq

5

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Raymond J Owens

Ligand recognition by A-class Eph receptors: crystal structures of the EphA2 ligand-binding domain and the EphA2/ephrin-A1 complex

6

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publication date

14 October 2009

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published in

Structure

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volume

17

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issue

10

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page(s)

1386-97

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cites work

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Cdk5 regulates EphA4-mediated dendritic spine retraction through an ephexin1-dependent mechanism

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Eph tyrosine kinase receptor EphA4 is required for the topographic mapping of the corticospinal tract

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

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29 September 2017

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Structure and thermodynamic characterization of the EphB4/Ephrin-B2 antagonist peptide complex reveals the determinants for receptor specificity

2 June 2018

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27 November 2018

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Crystal structure of the ephrin-B1 ectodomain: implications for receptor recognition and signaling

27 November 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/19836338

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Processing of X-ray diffraction data collected in oscillation mode

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/19836338

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1016/J.STR.2009.07.018

1 reference

release_f2jwudlgkzc6ndtninqw7a3o3e

2793762

Fatcat ID

0 references

2793762

1 reference

1 reference

1 reference