Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors - Wikidata - awgldk - TriplyDB

Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors

Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors

http://www.wikidata.org/entity/Q35621005

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Eph-ephrin signaling in nervous system development Eph/ephrin recognition and the role of Eph/ephrin clusters in signaling initiation A mathematical model for eph/ephrin-directed segregation of intermingled cells Structurally encoded intraclass differences in EphA clusters drive distinct cell responses Insights into Eph receptor tyrosine kinase activation from crystal structures of the EphA4 ectodomain and its complex with ephrin-A5 Axon guidance in the auditory system: multiple functions of Eph receptors.Eph/Ephrin signalling maintains eye field segregation from adjacent neural plate territories during forebrain morphogenesis.Size-based chromatography of signaling clusters in a living cell membrane Embryonic expression of EphA receptor genes in mice supports their candidacy for involvement in cleft lip and palate.Homotypic receptor-receptor interactions regulating Eph signaling.Eph receptor and ephrin function in breast, gut, and skin epithelia.Investigation of the interactions between the EphB2 receptor and SNEW peptide variants.Profiling Eph receptor expression in cells and tissues: a targeted mass spectrometry approach The multifaceted roles of Eph/ephrin signaling in breast cancer.Receptor Crosslinking: A General Method to Trigger Internalization and Lysosomal Targeting of Therapeutic Receptor:Ligand Complexes.Antibodies binding the ADAM10 substrate recognition domain inhibit Eph function DNA-mediated assembly of protein heterodimers on membrane surfaces.Eph receptor signaling and ephrins An activated form of ADAM10 is tumor selective and regulates cancer stem-like cells and tumor growth.EPH/ephrin profile and EPHB2 expression predicts patient survival in breast cancer Tie2 and Eph receptor tyrosine kinase activation and signaling.Deletion of the EphA2 receptor exacerbates myocardial injury and the progression of ischemic cardiomyopathy Therapeutic targeting of EPH receptors and their ligands.Eph- and ephrin-dependent mechanisms in tumor and stem cell dynamics.EphA3 biology and cancer.Attractive and repulsive factors act through multi-subunit receptor complexes to regulate nerve fiber growth.A role of the SAM domain in EphA2 receptor activation.Identification and characterization of a proteolytically primed form of the murine coronavirus spike proteins after fusion with the target cell.Ligand binding induces a conformational change in epidermal growth factor receptor dimers.Reelin induces EphB activation.Molecular Mechanoneurobiology: An Emerging Angle to Explore Neural Synaptic Functions.Ephrin-Eph signaling as a potential therapeutic target for the treatment of myocardial infarction.Optogenetic activation of EphB2 receptor in dendrites induced actin polymerization by activating Arg kinase.Pioneer of Eph biology and therapeutics: Martin Lackmann (1956-2014).Getting direction(s): The Eph/ephrin signaling system in cell positioning.The Neural Cell Adhesion Molecule (NCAM) Promotes Clustering and Activation of EphA3 Receptors in GABAergic Interneurons to Induce Ras Homolog Gene Family, Member A (RhoA)/Rho-associated protein kinase (ROCK)-mediated Growth Cone Collapse.Role of IGF-I and Efn-Eph Signaling in Skeletal Metabolism.

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Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors

http://www.wikidata.org/entity/Q35621005

description

2011 nî lūn-bûn

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2011年の論文

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2011年論文

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2011年論文

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2011年论文

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2011年论文

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2011年论文

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name

Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors

@ast

Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors

@en

type

label

Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors

@ast

Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors

@en

prefLabel

Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors

@ast

Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors

@en

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P1433

Journal of Cell Biology

P1476

Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors

@en

P2093

Andrew W Boyd

http://www.w3.org/2001/XMLSchema#string

Anneloes Mensinga

http://www.w3.org/2001/XMLSchema#string

Bettina Griesshaber

http://www.w3.org/2001/XMLSchema#string

Bryan W Day

http://www.w3.org/2001/XMLSchema#string

Chanly Chheang

http://www.w3.org/2001/XMLSchema#string

Claus Jørgensen

http://www.w3.org/2001/XMLSchema#string

Eva Nievergall

http://www.w3.org/2001/XMLSchema#string

Lakmali Atapattu

http://www.w3.org/2001/XMLSchema#string

Linda L Hii

http://www.w3.org/2001/XMLSchema#string

Martin Lackmann

http://www.w3.org/2001/XMLSchema#string

P2860

The EphA8 receptor regulates integrin activity through p110gamma phosphatidylinositol-3 kinase in a tyrosine kinase activity-independent manner

Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-expressing 293T and melanoma cells by CrkII and Rho-mediated signalling

PTP1B regulates Eph receptor function and trafficking

Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses

Targeting quantum dots to surface proteins in living cells with biotin ligase.

Somatic mutations affect key pathways in lung adenocarcinoma

Roles of Eph receptors and ephrins in segmental patterning

Cytoplasmic relaxation of active Eph controls ephrin shedding by ADAM10

Structural basis for autoinhibition of the Ephb2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region

An extracellular steric seeding mechanism for Eph-ephrin signaling platform assembly.

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1033-1045

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scholarly article

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10.1083/JCB.201104037

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P433

6

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195

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2011-12-05T00:00:00Z

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51855691

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22144690

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3241718

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