About: Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation

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scientific journal article

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rdf:type	Item
description	artículu científicu espublizáu en 1994 (ast) vědecký článek publikovaný v roce 1994 (cs) 1994年學術文章 (zh) наукова стаття, опублікована в листопаді 1994 (uk) 1994 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած (hyw) 1994 թվականի նոյեմբերին հրատարակված գիտական հոդված (hy) научни чланак (објављен 1994/11/08) (sr) vedecký článok (publikovaný 1994/11/08) (sk) مقالة علمية (نشرت في 8-11-1994) (ar) article publié dans les Proceedings of the National Academy of Sciences of the United States of America (fr) scientific journal article (en) im November 1994 veröffentlichter wissenschaftlicher Artikel (de) wetenschappelijk artikel (gepubliceerd op 1994/11/08) (nl)
publication date	wds:Q28115072-43DC2C88-8BF2-43D4-83AC-26DE0AFE2686
publication date	1994-11-08 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28115072-FC0D0DA4-6FCC-4894-813C-2F8302F4A157
language of work or name	English
cites work	wds:Q28115072-037C959D-217F-48AE-B4B9-21D4C44F7203 wds:Q28115072-060BD773-E07F-4D80-9212-4BC068448831 wds:Q28115072-0A3C0B03-7C96-4A20-B703-811C183EB607 wds:Q28115072-14F288EF-7CF4-4B67-B0C2-32D83D8CADEE wds:Q28115072-1C2E1517-D2F8-46AD-AFC1-073D5916A099 wds:Q28115072-239232D7-3CD8-4155-8E44-02B3A025E4C1 wds:Q28115072-260A7C1E-03D9-49CC-BBB3-FA0ADD1108D2 wds:Q28115072-2E388156-93F7-44B0-8096-5D17114B1641 wds:Q28115072-2E96DF11-D8FF-4D24-9E27-5F55086FED71 wds:Q28115072-35A2EFC6-1EE2-41C8-9C6C-E6E591A9C130 wds:Q28115072-403322CE-4F7C-470D-B163-5C527541B025 wds:Q28115072-54C7DC02-8D3E-456E-BFAF-39407D476246 wds:Q28115072-5FA639B5-98E3-4B66-9B37-955F99BCDE7E wds:Q28115072-700D2BC9-EAE5-4F5A-B062-93F15C095D6C wds:Q28115072-72A7E1E8-A237-465F-937E-D35A23F281CD wds:Q28115072-74230583-73FB-422D-91B5-AD0FA647948E wds:Q28115072-78E24CCD-A86C-40C7-89D2-3F10F2087D27 wds:Q28115072-8B8D8692-55E3-4D54-8EFC-DCB6D5690461 wds:Q28115072-98C203CA-8B36-4F46-A522-37B031FAC177 wds:Q28115072-A30167E2-A746-4FA7-82FE-A97859203602 wds:Q28115072-BC1E1C87-F5C0-453A-B805-5E507AD73740 wds:Q28115072-C1D88F04-CDBF-4110-A530-91E5CA894C20 wds:Q28115072-C52D50A9-B321-4117-9413-8921E3E913F3 wds:Q28115072-CC2C2165-D04E-4CB0-AFBB-8CB25D2C2C29 wds:Q28115072-CD5D4002-8585-48AD-9273-67D183596C54 wds:Q28115072-CDEA11D1-8A87-4F31-9B81-CEC005CE607E wds:Q28115072-CE4D0837-B890-4BCB-B0A4-D7E5CEEE4000 wds:Q28115072-F590FCA9-8719-420D-B113-B87D925A07B2 wds:Q28115072-F5D2E36B-5EF8-49F5-84C2-2410342A3B46 wds:Q28115072-FD443E31-FC22-4AB8-991A-D2C94A500407
cites work	Fc epsilon RI-mediated tyrosine phosphorylation and activation of the 72-kDa protein-tyrosine kinase, PTK72, in RBL-2H3 rat tumor mast cells Protein-tyrosine kinase p72syk in high affinity IgE receptor signaling. Identification as a component of pp72 and association with the receptor gamma chain after receptor aggregation Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis Abolition of anaphylaxis by targeted disruption of the high affinity immunoglobulin E receptor alpha chain gene Structure and function of the B cell antigen receptor FcR gamma chain deletion results in pleiotrophic effector cell defects Multichain immune recognition receptors: similarities in structure and signaling pathways Signal transduction by Fc receptors: the Fc epsilon RI case Fc epsilon R1-mediated tyrosine phosphorylation of multiple proteins, including phospholipase C gamma 1 and the receptor beta gamma 2 complex, in RBL-2H3 rat basophilic leukemia cells Tyrosine phosphorylation coupled to IgE receptor-mediated signal transduction and histamine release Phosphorylation and dephosphorylation of the high-affinity receptor for immunoglobulin E immediately after receptor engagement and disengagement Complete structure and expression in transfected cells of high affinity IgE receptor Differential control of the tyrosine kinases Lyn and Syk by the two signaling chains of the high affinity immunoglobulin E receptor 3 Determination of phosphoamino acid composition by acid hydrolysis of protein blotted to immobilon Interaction of aggregated native and mutant IgE receptors with the cellular skeleton Aggregation of the high-affinity IgE receptor and enhanced activity of p53/56lyn protein-tyrosine kinase IgE-induced histamine release from rat basophilic leukemia cell lines: isolation of releasing and nonreleasing clones Phospholipids stabilize the interaction between the .alpha. and .beta. subunits of the solubilized receptor for immunoglobulin E Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases Protein-tyrosine phosphorylation: an essential component of Fc epsilon RI signaling. Transmembrane signaling by the high-affinity IgE receptor on membrane preparations Antigen- and ionophore-induced signal transduction in rat basophilic leukemia cells involves protein tyrosine phosphorylation Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinases in vivo and in vitro. Dynamics of signal transduction after aggregation of cell-surface receptors: studies on the type I receptor for IgE. A synthetic peptide derived from p34cdc2 is a specific and efficient substrate of src-family tyrosine kinases Dissociation of the receptor for immunoglobulin E in mild detergents Structural basis of specific and efficient phosphorylation of peptides derived from p34cdc2 by a pp60src-related protein tyrosine kinase High-affinity IgE receptor-mediated stimulation of rat basophilic leukemia (RBL-2H3) cells induces early and late protein-tyrosine phosphorylations Phosphorylation/dephosphorylation of high-affinity IgE receptors: a mechanism for coupling/uncoupling a large signaling complex Signal transduction by the cytoplasmic domains of Fc epsilon RI-gamma and TCR-zeta in rat basophilic leukemia cells
author name string	wds:Q28115072-3B7A45D9-E755-4521-A0C7-99AF72F88829 wds:Q28115072-57E5D9FC-C0CB-43CB-B812-44895106EEA3 wds:Q28115072-790C9940-7DAF-4A5A-BC2F-9A8E682AF812
author name string	H. Metzger V. S. Pribluda C. Pribluda
rdfs:label	Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation (en) Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation (nl) Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation (ast)
skos:prefLabel	Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation (en) Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation (nl) Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation (ast)
name	Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation (en) Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation (nl) Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation (ast)
title	wds:Q28115072-1E11E666-47C0-471E-8B7D-DD2A9230CACB
title	Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation (en)
page(s)	wds:Q28115072-4EE864C7-CCFE-477F-92A4-4635F874110D
page(s)	11246–11250
instance of	wds:Q28115072-F8C13BAB-1505-44D3-99F8-FD4A0C44DADE
instance of	scholarly article
main subject	wds:Q28115072-294FAB1E-494F-4B2F-8655-43AC299069DA

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