About: Identification of Residues within the SHC Phosphotyrosine Binding/Phosphotyrosine Interaction Domain Crucial for Phosphopeptide Interaction

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About: Identification of Residues within the SHC Phosphotyrosine Binding/Phosphotyrosine Interaction Domain Crucial for Phosphopeptide Interaction Goto Sponge NotDistinct Permalink

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scientific article published in Journal of Biological Chemistry

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rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 1996 (uk) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im Januar 1996 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Journal of Biological Chemistry (en)
publication date	wds:Q56918626-027E35C6-2B15-4C26-ABB1-81946BE5957B
publication date	1996-01-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q56918626-138739C3-44F7-46BA-B0BC-E333004AB874
language of work or name	English
cites work	wds:Q56918626-0E8EE87F-EB44-4887-93A4-D07F4DDAFAF6 wds:Q56918626-21F2F644-D366-4108-A787-919BBAE7FF0B wds:Q56918626-2243752D-C338-469D-BB79-52FE56090C27 wds:Q56918626-2F68F71B-8564-4BD1-908B-E76AA7211B82 wds:Q56918626-3B231602-B049-4E75-8210-32A1ED1192EC wds:Q56918626-3DBDC517-9E92-4F2F-9786-A4B6D98B4818 wds:Q56918626-49062827-F62A-4757-9E45-AEAB85DF1F59 wds:Q56918626-698C1D3D-421B-4D59-AE58-80134B8ADAA2 wds:Q56918626-A440954E-F641-42E2-9C46-A28C65C80511 wds:Q56918626-A77276E5-069E-465E-8395-5D5C2AD46181 wds:Q56918626-A95EE542-61A0-479D-A333-221A000F60CD wds:Q56918626-B835D00E-1CD6-43FF-BF44-AB2C8BF340AB wds:Q56918626-BC37C649-8393-4E26-A869-7D34DF320236 wds:Q56918626-DBC7AE27-191D-4EFB-B2A6-E2AD4E99543B wds:Q56918626-DC29E6B0-09B2-4299-AC9A-AF5925032EF0 wds:Q56918626-FC268117-92C8-4252-8B78-DF04FA505511 wds:Q56918626-FF04FF71-ED96-4325-BCA1-87187748EB09
cites work	Role of IRS-2 in insulin and cytokine signalling Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product An alternative to SH2 domains for binding tyrosine-phosphorylated proteins A phosphotyrosine interaction domain SH2/SH3 signaling proteins Protein modules and signalling networks Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain The phosphotyrosine interaction domain of Shc binds an LXNPXY motif on the epidermal growth factor receptor A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine Epidermal growth factor-receptor mutant lacking the autophosphorylation sites induces phosphorylation of Shc protein and Shc-Grb2/ASH association and retains mitogenic activity A conserved amino-terminal Shc domain binds to phosphotyrosine motifs in activated receptors and phosphopeptides Shc Binding to Nerve Growth Factor Receptor Is Mediated by the Phosphotyrosine Interaction Domain High-efficiency transformation of mammalian cells by plasmid DNA The phosphotyrosine interaction domain of SHC recognizes tyrosine-phosphorylated NPXY motif Analysis of the role of the Shc and Grb2 proteins in signal transduction by the v-ErbB protein Use of tyrosine-phosphorylated proteins to screen bacterial expression libraries for SH2 domains
author name string	wds:Q56918626-8E207282-F70B-4820-8D9B-9212622D0F56 wds:Q56918626-8EBFBA0F-FDE0-41F3-9374-FC41F1296A47 wds:Q56918626-B0F7BBE3-54AD-45DC-A149-D79FB4D6EEBB
author name string	B Margolis V Yajnik P Blaikie
rdfs:label	Identification of Residues within the SHC Phosphotyrosine Binding/Phosphotyrosine Interaction Domain Crucial for Phosphopeptide Interaction (en) Identification of Residues within the SHC Phosphotyrosine Binding/Phosphotyrosine Interaction Domain Crucial for Phosphopeptide Interaction (nl)
skos:prefLabel	Identification of Residues within the SHC Phosphotyrosine Binding/Phosphotyrosine Interaction Domain Crucial for Phosphopeptide Interaction (en) Identification of Residues within the SHC Phosphotyrosine Binding/Phosphotyrosine Interaction Domain Crucial for Phosphopeptide Interaction (nl)
name	Identification of Residues within the SHC Phosphotyrosine Binding/Phosphotyrosine Interaction Domain Crucial for Phosphopeptide Interaction (en) Identification of Residues within the SHC Phosphotyrosine Binding/Phosphotyrosine Interaction Domain Crucial for Phosphopeptide Interaction (nl)
author	wds:Q56918626-BD965F8A-2EC3-401B-9A08-D9A7F126D12A
author	Peer Bork
title	wds:Q56918626-FFD415AE-9157-4030-9D77-7A57ED90C3B0
title	Identification of residues within the SHC phosphotyrosine binding/phosphotyrosine interaction domain crucial for phosphopeptide interaction (en)
page(s)	wds:Q56918626-6365E9C3-2F2C-471C-88E1-D39909D52F8A
page(s)	1813-1816
instance of	wds:Q56918626-F707E4DA-42FF-4E3A-85CB-6580036A709F
instance of	scholarly article
PubMed ID	wds:Q56918626-AB24E7C3-21AC-4D9D-A232-D913EB2A77F9
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8567619
PubMed ID	8567619
published in	wds:Q56918626-A445836E-7629-4F92-80D8-0956D2BC81F5
published in	Journal of Biological Chemistry
issue	wds:Q56918626-8DAE7AC4-8576-4869-BD4D-D1CB955AB7CB
volume	wds:Q56918626-B041EC1F-B778-4E69-A044-B97AC9FB9610
issue	4
volume	271
number of pages	wds:Q56918626-6F5B5B55-3999-4790-AFBB-BD20639D5079
number of pages	4 (xsd:decimal)
DOI	wds:Q56918626-3A691340-931E-42E6-8C7A-0EBD049AED81
DOI	http://dx.doi.org/10.1074/JBC.271.4.1813
DOI	10.1074/JBC.271.4.1813
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q56918626
is cites work of	The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein Epidermal growth factor directs sex-specific steroid signaling through Src activation The mammalian numb phosphotyrosine-binding domain. Characterization of binding specificity and identification of a novel PDZ domain-containing numb binding protein, LNX The role of the PH domain in the signal-dependent membrane targeting of Sos. Functional analysis of the Numb phosphotyrosine-binding domain using site-directed mutagenesis The adaptor molecule Disabled-2 links the transforming growth factor beta receptors to the Smad pathway Fe65 and the protein network centered around the cytosolic domain of the Alzheimer's beta-amyloid precursor protein Interaction of c-Jun amino-terminal kinase interacting protein-1 with p190 rhoGEF and its localization in differentiated neurons Evidence for a requirement for both phospholipid and phosphotyrosine binding via the Shc phosphotyrosine-binding domain in vivo Tyrosine phosphorylation of the beta 4 integrin cytoplasmic domain mediates Shc signaling to extracellular signal-regulated kinase and antagonizes formation of hemidesmosomes The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids Shc phosphotyrosine-binding domain dominantly interacts with epidermal growth factor receptors and mediates Ras activation in intact cells Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses Structural determinants of integrin recognition by talin Mammalian NUMB is an evolutionarily conserved signaling adapter protein that specifies cell fate The role of the Shc phosphotyrosine interaction/phosphotyrosine binding domain and tyrosine phosphorylation sites in polyoma middle T antigen-mediated cell transformation. Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer's beta-amyloid precursor proteins Differential roles of JIP scaffold proteins in the modulation of amyloid precursor protein metabolism GULP1 is a novel APP-interacting protein that alters APP processing. Engineering a single ubiquitin ligase for the selective degradation of all activated ErbB receptor tyrosine kinases

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