Eph receptors are negatively controlled by protein tyrosine phosphatase receptor type O. (Q42802380)

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20 January 2020

title

Eph receptors are negatively controlled by protein tyrosine phosphatase receptor type O (English)

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20 January 2020

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20 January 2020

author name string

Takafumi Shintani

1

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20 January 2020

Masaru Ihara

2

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20 January 2020

Hiraki Sakuta

3

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20 January 2020

Hiroo Takahashi

4

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20 January 2020

Ikuko Watakabe

5

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20 January 2020

language of work or name

English

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publication date

7 May 2006

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20 January 2020

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20 January 2020

volume

9

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20 January 2020

issue

6

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20 January 2020

page(s)

761-769

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https://scigraph.springernature.com/pub.10.1038/nn1697

20 January 2020

exact match

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cites work

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Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis

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Repelling class discrimination: ephrin-A5 binds to and activates EphB2 receptor signaling

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EphB forward signaling controls directional branch extension and arborization required for dorsal-ventral retinotopic mapping

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A genomic perspective on protein tyrosine phosphatases: gene structure, pseudogenes, and genetic disease linkage

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CRYP-2/cPTPRO is a neurite inhibitory repulsive guidance cue for retinal neurons in vitro

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Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases

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In vitro assay to test differential substrate affinities of growing axons and migratory cells

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Modulation of EphA receptor function by coexpressed ephrinA ligands on retinal ganglion cell axons.

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Reciprocal expression of the Eph receptor Cek5 and its ligand(s) in the early retina

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Expression and tyrosine phosphorylation of Eph receptors suggest multiple mechanisms in patterning of the visual system.

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Receptor protein tyrosine phosphatases in nervous system development

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Juxtamembrane autoinhibition in receptor tyrosine kinases.

21 January 2018

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Ephrin-A5 exerts positive or inhibitory effects on distinct subsets of EphA4-positive motor neurons.

21 January 2018

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Regulation of repulsion versus adhesion by different splice forms of an Eph receptor

21 January 2018

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6B4 proteoglycan/phosphacan, an extracellular variant of receptor-like protein-tyrosine phosphatase zeta/RPTPbeta, binds pleiotrophin/heparin-binding growth-associated molecule (HB-GAM)

21 January 2018

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Pleiotrophin signals increased tyrosine phosphorylation of beta beta-catenin through inactivation of the intrinsic catalytic activity of the receptor-type protein tyrosine phosphatase beta/zeta

21 January 2018

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Identification of GIT1/Cat-1 as a substrate molecule of protein tyrosine phosphatase zeta /beta by the yeast substrate-trapping system

21 January 2018

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A Receptor-like Protein-tyrosine Phosphatase PTP /RPTP Binds a Heparin-binding Growth Factor Midkine: INVOLVEMENT OF ARGININE 78 OF MIDKINE IN THE HIGH AFFINITY BINDING TO PTP

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Regulated cleavage of a contact-mediated axon repellent

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Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans

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Rac-dependent trans-endocytosis of ephrinBs regulates Eph-ephrin contact repulsion

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EphB-ephrinB bi-directional endocytosis terminates adhesion allowing contact mediated repulsion.

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Eph family transmembrane ligands can mediate repulsive guidance of trunk neural crest migration and motor axon outgrowth

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Axonal morphogenesis controlled by antagonistic roles of two CRMP subtypes in microtubule organization

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Visual projection map specified by topographic expression of transcription factors in the retina.

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Ventroptin: a BMP-4 antagonist expressed in a double-gradient pattern in the retina.

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CBF1 controls the retinotectal topographical map along the anteroposterior axis through multiple mechanisms.

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Unified Nomenclature for Eph Family Receptors and Their Ligands, the Ephrins

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