About: Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases

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scientific journal article

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rdf:type	Item
description	artículu científicu espublizáu en 1996 (ast) vědecký článek publikovaný v roce 1996 (cs) 1996 թուականի Փետրուարին հրատարակուած գիտական յօդուած (hyw) 1996 թվականի փետրվարին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в лютому 1996 (uk) vedecký článok (publikovaný 1996/02/09) (sk) مقالة علمية (نشرت في 9-2-1996) (ar) wetenschappelijk artikel (gepubliceerd op 1996/02/09) (nl) article publié dans la revue scientifique Science (fr) scientific journal article (en) im Februar 1996 veröffentlichter wissenschaftlicher Artikel (de) научни чланак (објављен 1996/02/09) (sr)
publication date	wds:Q28118717-F45DE755-8679-446E-B2DB-4A225A6263DA
publication date	1996-02-09 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28118717-A64C1152-5DEB-41B6-A032-04381E0CF672
language of work or name	English
author name string	wds:Q28118717-3465E428-B9E8-4567-9C60-93EAF261EB19 wds:Q28118717-5C88DF9C-95DF-4043-B9E4-528656BD8324 wds:Q28118717-86E96F2E-EBCF-46B8-838F-E95C67383A96 wds:Q28118717-8A3DF605-8F06-4FCC-BE90-CDE804F338DD wds:Q28118717-C41E5276-D8DE-4B03-BA8B-1B291A33A5F1 wds:Q28118717-DD5490B9-191D-4EB3-A047-432245BC60DB wds:Q28118717-DEDC8381-09B5-40E6-BE92-B11627FE2773 wds:Q28118717-ED6F43AE-EEFA-4031-8652-6AF1071F10EF wds:Q28118717-FD161DC0-6275-4D9A-A168-ECC51ADE9DD6
author name string	H. Park S. Lin O. N. Witte A. M. Scharenberg J. P. Kinet D. J. Rawlings A. C. Fluckiger M. I. Wahl R. M. Kato
rdfs:label	Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases (en) Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases (nl) Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases (ast)
skos:prefLabel	Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases (en) Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases (nl) Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases (ast)
name	Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases (en) Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases (nl) Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases (ast)
title	wds:Q28118717-659DD37B-1D53-4692-862B-3B964E45B0BD
title	Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases (en)
page(s)	wds:Q28118717-123AE8CB-9158-46D0-95EA-7B88CC42803C
page(s)	822–825
instance of	wds:Q28118717-C98A5579-E614-4819-AD4C-6A82015CE5C9
instance of	scholarly article
main subject	wds:Q28118717-1FCEF295-782E-4062-9580-EA36FEA834A9 wds:Q28118717-5576C050-CD9A-4C37-B328-8DF2FF74204D wds:Q28118717-70DB273E-2882-4971-8947-F23FA878F535
main subject	phosphorylation wd:Q7660502 protein tyrosine kinase activity
PubMed ID	wds:Q28118717-80AD9E73-785B-4691-BE58-CDDA2614D5AA
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8629002
PubMed ID	8629002
published in	wds:Q28118717-0D7A2EBE-A9A2-494B-864C-7D0ECA49B21C
published in	Science
issue	wds:Q28118717-2F83DD3D-B7F5-42B7-9F81-819A045A96FB
volume	wds:Q28118717-A632DFC9-0E27-400F-860F-7DB95A7F575F
issue	5250
volume	271
DOI	wds:Q28118717-84971026-C24E-4A50-A7F2-433C8BF8DF1D
DOI	http://dx.doi.org/10.1126/SCIENCE.271.5250.822
DOI	10.1126/SCIENCE.271.5250.822
ResearchGate publication ID	wds:Q28118717-91ADD9A5-C250-4D9A-830E-C492AE965068
ResearchGate publication ID	14571563
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28118717
is cites work of	Tec kinases, actin, and cell adhesion The Tec29 tyrosine kinase is required during Drosophila embryogenesis and interacts with Src64 in ring canal development Different roles for non-receptor tyrosine kinases in arachidonate release induced by zymosan and Staphylococcus aureus in macrophages Ligand-independent signaling during early avian B cell development Distinct pathways regulate Syk protein activation downstream of immune tyrosine activation motif (ITAM) and hemITAM receptors in platelets PCI-32765: a novel Bruton's tyrosine kinase inhibitor for the treatment of lymphoid malignancies The dynamics of protein kinase B regulation during B cell antigen receptor engagement Structure of the PH domain and Btk motif from Bruton's tyrosine kinase: molecular explanations for X-linked agammaglobulinaemia Insights into immunoglobulin E receptor signaling from structurally defined ligands rlk/TXK encodes two forms of a novel cysteine string tyrosine kinase activated by Src family kinases Antigen receptor signalling in B cells A crucial role for the p110delta subunit of phosphatidylinositol 3-kinase in B cell development and activation BLNK mediates Syk-dependent Btk activation Truncation of C-mip (Tc-mip), a new proximal signaling protein, induces c-maf Th2 transcription factor and cytoskeleton reorganization syk kinase activation by a src kinase-initiated activation loop phosphorylation chain reaction The tyrosine kinase network regulating mast cell activation BAP-135, a target for Bruton's tyrosine kinase in response to B cell receptor engagement Regulation of Btk function by a major autophosphorylation site within the SH3 domain PKCbeta modulates antigen receptor signaling via regulation of Btk membrane localization Conformation of full-length Bruton tyrosine kinase (Btk) from synchrotron X-ray solution scattering. Tyrosyl phosphorylation of Shp2 is required for normal ERK activation in response to some, but not all, growth factors Signal-dependent membrane targeting by pleckstrin homology (PH) domains Drosophila actin-Capping Protein limits JNK activation by the Src proto-oncogene. The role of Tec protein-tyrosine kinase in T cell signaling Independent SH2-binding sites mediate interaction of Dok-related protein with RasGTPase-activating protein and Nck Targeting pathological B cell receptor signalling in lymphoid malignancies Neuropeptide-induced androgen independence in prostate cancer cells: roles of nonreceptor tyrosine kinases Etk/Bmx, Src, and focal adhesion kinase Etk, a Btk family tyrosine kinase, mediates cellular transformation by linking Src to STAT3 activation Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain

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