Cell-specific information processing in segregating populations of Eph receptor ephrin-expressing cells (Q28267574)

10

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David Wilkinson

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object named as

David G Wilkinson

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Rune Linding

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object named as

Rune Linding

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author name string

Claus Jørgensen

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Andrew Sherman

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Ginny I Chen

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Alexei Poliakov

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Marilyn Hsiung

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Brett Larsen

describes a project that uses

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language of work or name

English

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publication date

11 December 2009

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published in

Science

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volume

326

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page(s)

1502-9

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issue

5959

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HEK293-EPHB1

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HEK293-EPHB2

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cites work

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Beta-catenin and TCF mediate cell positioning in the intestinal epithelium by controlling the expression of EphB/ephrinB

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Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands

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Compartmentalized signaling by GPI-anchored ephrin-A5 requires the Fyn tyrosine kinase to regulate cellular adhesion

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The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif

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Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics

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Accurate quantitation of protein expression and site-specific phosphorylation

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Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules

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Immunoaffinity profiling of tyrosine phosphorylation in cancer cells

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STRING: a database of predicted functional associations between proteins

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Juxtamembrane tyrosine residues couple the Eph family receptor EphB2/Nuk to specific SH2 domain proteins in neuronal cells

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Growth factor-dependent phosphorylation of the actin-binding protein cortactin is mediated by the cytoplasmic tyrosine kinase FER

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Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation

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Eph receptor signalling casts a wide net on cell behaviour

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Reading protein modifications with interaction domains

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Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases

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The ins and outs of signalling

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Guidance from above: common cues direct distinct signaling outcomes in vascular and neural patterning

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Eph receptors and ephrins restrict cell intermingling and communication.

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Eph, a protein family coming of age: more confusion, insight, or complexity?

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Tyrosine phosphorylation of transmembrane ligands for Eph receptors

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A systems model of signaling identifies a molecular basis set for cytokine-induced apoptosis.

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Common effector processing mediates cell-specific responses to stimuli

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Regulation of EphB2 activation and cell repulsion by feedback control of the MAPK pathway

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Directional and quantitative phosphorylation networks

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Systematic Discovery of In Vivo Phosphorylation Networks

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Linear Motif Atlas for Phosphorylation-Dependent Signaling

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Eph receptors are negatively controlled by protein tyrosine phosphatase receptor type O.

21 January 2018

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Data-driven modelling of signal-transduction networks

21 January 2018

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Phosphorylation networks regulating JNK activity in diverse genetic backgrounds

21 January 2018

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Positive selection of tyrosine loss in metazoan evolution.

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21 January 2018

Identifiers

DOI

10.1126/SCIENCE.1176615

1 reference

Consolidated OpenCitations Corpus – April 2017

release_fihgmmmogjckzedfg3hxqf5f2y

2002474

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/fihgmmmogjckzedfg3hxqf5f2y

mapped directly with Wikidata item

24 November 2022

based on heuristic

2002474

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference