About: Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific journal article

Attributes	Values
rdf:type	Item
description	наукова стаття, опублікована в лютому 1990 (uk) 1990 թուականի Փետրուարին հրատարակուած գիտական յօդուած (hyw) artículu científicu espublizáu en 1990 (ast) vědecký článek publikovaný v roce 1990 (cs) 1990 թվականի փետրվարին հրատարակված գիտական հոդված (hy) vedecký článok (publikovaný 1990/02/01) (sk) مقالة علمية (نشرت في فبراير 1990) (ar) article scientifique publié en 1990 (fr) scientific journal article (en) wetenschappelijk artikel (gepubliceerd op 1990/02/01) (nl) im Februar 1990 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q28609951-38871AA4-B8A4-4206-90F4-7FE5F07A3C37
publication date	1990-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28609951-6CD1A453-2352-4914-91C0-017B282273D4
language of work or name	English
cites work	wds:Q28609951-02A9212F-0273-4B2F-9AEF-40BA0AAEF036 wds:Q28609951-05CC6F40-A7A9-44CB-B37D-099D186B9AA4 wds:Q28609951-07B3BDEA-7160-4DE8-B462-F162C6AF251B wds:Q28609951-1BDD68C9-7458-4B45-A379-B5E2565F0720 wds:Q28609951-1D32745A-4F4A-4F48-984A-87C573D46ECF wds:Q28609951-3660912D-057D-46DC-8F9D-E991EE6966B0 wds:Q28609951-47EC11EC-727A-4D1A-AA65-36AC584743C9 wds:Q28609951-54296602-E0CB-4E5D-846C-981845997B3A wds:Q28609951-60C5B5C7-B62B-4B1A-938A-59BA2F016BD8 wds:Q28609951-69C6C79E-FF93-4688-BAB5-E45DBC533DCC wds:Q28609951-6B5FDF8C-CCD6-4478-B3CD-0CABD4CB370F wds:Q28609951-76C13C81-7A9B-4842-B4B2-7A82E220DF76 wds:Q28609951-781881DE-AC42-4969-8510-FC071F087F71 wds:Q28609951-83674EB2-1DA8-425C-B8A2-052EB703E903 wds:Q28609951-872F3C1F-FDD7-455B-A5A5-626E180C0C66 wds:Q28609951-93653605-23E3-4EC5-9E76-D27E2C36156A wds:Q28609951-A3B20C69-4576-4D6C-9E0A-CAE76CFCB447 wds:Q28609951-A9A753B5-0B8F-4435-9C34-E9B7D8C3C045 wds:Q28609951-B0D1A9EC-D88D-4E7A-879A-92B45945A233 wds:Q28609951-BB2B6FCA-18FC-4492-BB72-BFD52ECAC534 wds:Q28609951-BF56710E-1641-4CCA-984B-7233C0725FB9 wds:Q28609951-CB8548D1-6703-484A-84D5-894E9957C999 wds:Q28609951-CF9ACECF-F02E-4C1A-B4E1-8B0FD9EEED4A wds:Q28609951-DAF31F3A-389A-4FDE-BD58-54957173889A wds:Q28609951-DDC77644-8F41-4B7C-A521-8B37DA95EE41 wds:Q28609951-DE039E4A-5DC1-4120-A037-A8F4FB5B5F1A wds:Q28609951-E581CD32-190D-493E-BFAD-576D361596E8 wds:Q28609951-E95CEC71-ADC6-4213-8631-A1790843D998 wds:Q28609951-EB6202B5-9EFC-471B-8A60-FF6158A87FC2 wds:Q28609951-F38F790B-2CBD-4785-BB56-248A580E010C wds:Q28609951-FD9F58FB-19C1-4B19-B1CD-6CEF3CBD20F2
cites work	Studies of inositol phospholipid-specific phospholipase C. Tyrosine phosphorylation of phospholipase C-II in vitro by the epidermal growth factor receptor. All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor Antiphosphotyrosine recovery of phospholipase C activity after EGF treatment of A-431 cells EGF induces tyrosine phosphorylation of phospholipase C-II: a potential mechanism for EGF receptor signaling Signal transduction by allosteric receptor oligomerization Phospholipase C-gamma, a substrate for PDGF receptor kinase, is not phosphorylated on tyrosine during the mitogenic response to CSF-1. C-kinase phosphorylates the epidermal growth factor receptor and reduces its epidermal growth factor-stimulated tyrosine protein kinase activity Epidermal growth factor and potent phorbol tumor promoters induce epidermal growth factor receptor phosphorylation in a similar but distinctively different manner in human epidermoid carcinoma A431 cells A mutant epidermal growth factor receptor with defective protein tyrosine kinase is unable to stimulate proto-oncogene expression and DNA synthesis Autophosphorylation sites on the epidermal growth factor receptor. Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routing Allosteric regulation of the epidermal growth factor receptor kinase Evidence that autophosphorylation of solubilized receptors for epidermal growth factor is mediated by intermolecular cross-phosphorylation Kinetic parameters of the protein tyrosine kinase activity of EGF-receptor mutants with individually altered autophosphorylation sites Direct activation of the serine/threonine kinase activity of Raf-1 through tyrosine phosphorylation by the PDGF beta-receptor Phospholipase C-gamma is a substrate for the PDGF and EGF receptor protein-tyrosine kinases in vivo and in vitro Epidermal growth factor stimulates tyrosine phosphorylation of phospholipase C-II independently of receptor internalization and extracellular calcium Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity. Resolution of high and low affinity epidermal growth factor receptors. Inhibition of high affinity component by low temperature, cycloheximide, and phorbol esters Monoclonal antibodies to three phospholipase C isozymes from bovine brain Biologically active phorbol esters specifically alter affinity of epidermal growth factor membrane receptors Demonstration of epidermal growth factor-induced receptor dimerization in living cells using a chemical covalent cross-linking agent Reconstitution of human epidermal growth factor receptors and its deletion mutants in cultured hamster cells Regulation of epidermal growth factor-stimulated formation of inositol phosphates in A-431 cells by calcium and protein kinase C Epidermal growth factor stimulates the production of phosphatidylinositol monophosphate and the breakdown of polyphosphoinositides in A431 cells Phosphoinositide metabolism and the control of cell proliferation Biological activities of EGF-receptor mutants with individually altered autophosphorylation sites A point mutation at the ATP-binding site of the EGF-receptor abolishes signal transduction The kinetics of tyrosine phosphorylation by the purified epidermal growth factor receptor kinase of A-431 cells An insertional mutant of epidermal growth factor receptor allows dissection of diverse receptor functions
author name string	wds:Q28609951-21B3E967-A2E1-4D24-A9C0-6049B02D8B6D wds:Q28609951-8EE37B70-07B6-42A2-B1DD-CCE59E64E156 wds:Q28609951-90071305-6209-4A3E-85BA-DB35DEE22AEC wds:Q28609951-B4E98B5E-2F09-4039-B496-C85627FC2A35 wds:Q28609951-BED7ECCC-A268-4651-9DE4-1252F89D0A65 wds:Q28609951-E3CC0573-EB6E-4245-BE60-B051DE4FE146
OpenCitations bibliographic resource ID	wds:Q28609951-FB5E7518-C065-4596-AE5D-7A5271D364D1
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/4204177
author name string	B. Margolis J. Schlessinger A. Ullrich A. M. Honegger A. Zilberstein F. Bellot
OpenCitations bibliographic resource ID	4204177
rdfs:label	Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor (en) Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor (nl) Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor (ast)
skos:prefLabel	Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor (en) Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor (nl) Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor (ast)
name	Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor (en)

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 196 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software