The discoidin domain receptor tyrosine kinases are activated by collagen (Q24313329)

Discoidin domain receptor tyrosine kinase 1

GOA release 2020-03-11

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protein tyrosine kinase collagen receptor activity

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

W Vogel

1

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G D Gish

2

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F Alves

3

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T Pawson

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

4

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language of work or name

English

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publication date

December 1997

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published in

Molecular Cell

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volume

1

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issue

1

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page(s)

13-23

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cites work

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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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A receptor tyrosine kinase found in breast carcinoma cells has an extracellular discoidin I-like domain

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PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine

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SH2 signaling in a lower eukaryote: a STAT protein that regulates stalk cell differentiation in dictyostelium.

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10 Posttranslational enzymes in the biosynthesis of collagen: Intracellular enzymes

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Developmentally Regulated, Carbohydrate-Binding Protein in Dictyostelium discoideum

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Radiation induction of the receptor tyrosine kinase gene Ptk-3 in normal rat astrocytes.

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Localization of an epithelial-specific receptor kinase (EDDR1) to chromosome 6q16

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An orphan receptor tyrosine kinase family whose members serve as nonintegrin collagen receptors

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Discoidin I is implicated in cell-substratum attachment and ordered cell migration of Dictyostelium discoideum and resembles fibronectin

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Integrin–collagen binding

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Assignment of the NTRK4 (trkE) gene to chromosome 6p21

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Identification of residues that control specific binding of the Shc phosphotyrosine-binding domain to phosphotyrosine sites

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The adaptor protein Shc couples a class of integrins to the control of cell cycle progression

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Interaction of the adaptor protein Shc and the adhesion molecule cadherin

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Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

1566203

1566203

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference