About: In vitro phosphorylation of the epidermal growth factor receptor autophosphorylation domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites

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About: In vitro phosphorylation of the epidermal growth factor receptor autophosphorylation domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites Goto Sponge NotDistinct Permalink

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scientific journal article

Attributes	Values
rdf:type	Item
description	vědecký článek publikovaný v roce 1995 (cs) artículu científicu espublizáu en 1995 (ast) наукова стаття, опублікована в грудні 1995 (uk) 1995 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած (hyw) 1995 թվականի դեկտեմբերին հրատարակված գիտական հոդված (hy) vedecký článok (publikovaný 1995/12/19) (sk) مقالة علمية (نشرت في 19-12-1995) (ar) scientific journal article (en) im Dezember 1995 veröffentlicher wissenschaftlicher Artikel (de) wetenschappelijk artikel (gepubliceerd op 1995/12/19) (nl)
publication date	wds:Q28610011-F64D46F1-9A8D-422B-BBC1-F14DA5587192
publication date	1995-12-19 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28610011-72700E77-43FA-4326-995B-360128D12DC2
language of work or name	English
author name string	wds:Q28610011-3611FB1A-1372-4344-B6D2-7C32FCC177B8 wds:Q28610011-49F104A0-C212-47EB-8718-1788AD774EFB wds:Q28610011-DF3A02A4-5686-43EC-A012-39BD70C58625
author name string	C. R. Lombardo D. B. Kassel T. G. Consler
rdfs:label	In vitro phosphorylation of the epidermal growth factor receptor autophosphorylation domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites (en) In vitro phosphorylation of the epidermal growth factor receptor autophosphorylation domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites (nl) In vitro phosphorylation of the epidermal growth factor receptor autophosphorylation domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites (ast)
skos:prefLabel	In vitro phosphorylation of the epidermal growth factor receptor autophosphorylation domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites (en) In vitro phosphorylation of the epidermal growth factor receptor autophosphorylation domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites (nl) In vitro phosphorylation of the epidermal growth factor receptor autophosphorylation domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites (ast)
name	In vitro phosphorylation of the epidermal growth factor receptor autophosphorylation domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites (en) In vitro phosphorylation of the epidermal growth factor receptor autophosphorylation domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites (nl) In vitro phosphorylation of the epidermal growth factor receptor autophosphorylation domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites (ast)
title	wds:Q28610011-C27851D8-87B8-49D2-ADA8-9609CFD04DC8
title	In vitro phosphorylation of the epidermal growth factor receptor autophosphorylation domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites (en)
page(s)	wds:Q28610011-D90DCC33-CC32-4945-A67B-15DF7AE50142
page(s)	16456–16466
instance of	wds:Q28610011-CCFC235D-5144-4D4B-814E-06D2A7EF9871
instance of	scholarly article
main subject	wds:Q28610011-0C238E3D-4040-4564-90A5-1635DAA95444
main subject	phosphorylation
PubMed ID	wds:Q28610011-1CD29804-1E9A-4E52-8AA2-19623B76D4B9
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8845374
PubMed ID	8845374
published in	wds:Q28610011-E5832673-DF70-41CF-95C3-9FB215A3B0D3
published in	Biochemistry
issue	wds:Q28610011-C7A6A52A-D765-4A05-A0AD-E3BA5E3A2C88
volume	wds:Q28610011-BFB39BF3-C957-4AFF-B216-1F6A73AD460E
issue	50
volume	34
DOI	wds:Q28610011-DD09233D-9036-481A-959E-6103FEFF0C67
DOI	http://dx.doi.org/10.1021/BI00050A029
DOI	10.1021/BI00050A029
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28610011
is cites work of	Src family protein tyrosine kinases: cooperating with growth factor and adhesion signaling pathways S100A7-downregulation inhibits epidermal growth factor-induced signaling in breast cancer cells and blocks osteoclast formation Prognostic effect of activated EGFR expression in human colon carcinomas: comparison with EGFR status Phosphotyrosine interactome of the ErbB-receptor kinase family Tyrosine phosphorylation of nicotinic acetylcholine receptor mediates Grb2 binding Identification of in vitro phosphorylation sites in the growth cone protein SCG10. Effect Of phosphorylation site mutants on microtubule-destabilizing activity Met and c-Src cooperate to compensate for loss of epidermal growth factor receptor kinase activity in breast cancer cells Biasing the prostaglandin F2α receptor responses toward EGFR-dependent transactivation of MAPK. A quantitative study of the recruitment potential of all intracellular tyrosine residues on EGFR, FGFR1 and IGF1R. Loss of Hsp90 association up-regulates Src-dependent ErbB2 activity Macrophages stimulate gastric and colorectal cancer invasion through EGFR Y(1086), c-Src, Erk1/2 and Akt phosphorylation and smallGTPase activity Differential phosphoproteomics of fibroblast growth factor signaling: identification of Src family kinase-mediated phosphorylation events 20-HETE activates the Raf/MEK/ERK pathway in renal epithelial cells through an EGFR- and c-Src-dependent mechanism Phosphorylation of EGFR by SRC kinase SH2 Ligand-Like Effects of Second Cytosolic Domain of Na/K-ATPase α1 Subunit on Src Kinase Identification of protein kinase A phosphorylation sites on NBD1 and R domains of CFTR using electrospray mass spectrometry with selective phosphate ion monitoring MAPK scaffold IQGAP1 binds the EGF receptor and modulates its activation Extracellular region of epidermal growth factor receptor: a potential target for anti-EGFR drug discovery The proto-oncogene c-Src and its downstream signaling pathways are inhibited by the metastasis suppressor, NDRG1. Fully automated synthesis of (phospho)peptide arrays in microtiter plate wells provides efficient access to protein tyrosine kinase characterization Differences in phosphorylation of human and chicken stathmin by MAP kinase Therapeutic IMC-C225 antibody inhibits breast cancer cell invasiveness via Vav2-dependent activation of RhoA GTPase Ca2+/Calmodulin and Apo-Calmodulin Both Bind to and Enhance the Tyrosine Kinase Activity of c-Src Deep mutational analysis reveals functional trade-offs in the sequences of EGFR autophosphorylation sites Spleen tyrosine kinase activity regulates epidermal growth factor receptor signaling pathway in ovarian cancer In vitro significance of SOCS-3 and SOCS-4 and potential mechanistic links to wound healing. Performance comparison of three trypsin columns used in liquid chromatography.
is cites work of	wds:Q33322536-449D1861-CAD1-4831-B260-3664E0BD3A70 wds:Q33636419-3202CCCA-B1A8-47D0-83AC-26F5CB853E70 wds:Q37337330-5D628E17-EEBA-4ADC-A257-E4AB975690D1 wds:Q50297459-EF4AE98F-931F-4AE9-8127-AC0567133C43 wds:Q30470153-569D9EF6-F0A1-4D36-A9B6-F6725E1B0FF0 wds:Q35836087-51C2CA0B-2875-42A5-8F8D-DB7196832D41 wds:Q39156200-CD65259E-3161-47FF-AEAD-BF1A2D6505E2 wds:Q39728441-99D01038-2F07-4408-BD5A-26018EB2FB13 wds:Q90252710-67B071BA-C4F0-4A47-91E9-621545225BB7 wds:Q24294200-A58D3663-298E-4E33-BEC2-CBD074400CD2 wds:Q35658526-5803993A-3507-4D79-BB77-14EB148EC0AF wds:Q38989275-59614A6E-21E7-4E73-9530-CA301BCD69E4 wds:Q73420522-05D0D3A8-D941-4ECB-93EA-E73E66EC3C71 wds:Q35832242-D0D8AA18-EFB7-4E43-9C0A-135EFA78E874 wds:Q31792293-AFEDA1E9-AB83-46A9-9A5C-0BC6D7A56CC9 wds:Q41158794-4AF1BD30-CE52-45A8-A291-87563237BE99 wds:Q35641650-4CDDB114-0787-4F57-9711-C3254CEED96D wds:Q33872638-AA1E1877-D649-414A-B00C-FCAD191BD8EE wds:Q35151696-65D1640F-7B1A-4D7E-8F17-C416009261D6 wds:Q24792853-5A27E29B-63E8-47E8-8227-CD6D008AB509 wds:Q30415408-728CEA02-D700-4F1A-88E6-7976121C8914 wds:Q93159928-7EA06453-4924-4DEB-93E9-59733F1B5E95

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