Erythropoietin stimulates the tyrosine phosphorylation of Shc and its association with Grb2 and a 145-Kd tyrosine phosphorylated protein.
about
Recombinant human erythropoietin antagonizes trastuzumab treatment of breast cancer cells via Jak2-mediated Src activation and PTEN inactivationThe 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphataseA mammalian adaptor protein with conserved Src homology 2 and phosphotyrosine-binding domains is related to Shc and is specifically expressed in the brainShc, Grb2, Sos1, and a 150-kilodalton tyrosine-phosphorylated protein form complexes with Fms in hematopoietic cellsDirect association with and dephosphorylation of Jak2 kinase by the SH2-domain-containing protein tyrosine phosphatase SHP-1Targeted disruption of SHIP leads to hemopoietic perturbations, lung pathology, and a shortened life spanInteraction of Shc with Grb2 regulates association of Grb2 with mSOSEssential role for the C-terminal noncatalytic region of SHIP in FcgammaRIIB1-mediated inhibitory signalingErythropoietin and Friend virus gp55 activate different JAK/STAT pathways through the erythropoietin receptor in erythroid cellsAP1 regulation of proliferation and initiation of apoptosis in erythropoietin-dependent erythroid cellsErythroid cells rendered erythropoietin independent by infection with Friend spleen focus-forming virus show constitutive activation of phosphatidylinositol 3-kinase and Akt kinase: involvement of insulin receptor substrate-related adapter proteins.Growth factor-independent proliferation of erythroid cells infected with Friend spleen focus-forming virus is protein kinase C dependent but does not require Ras-GTP.Both the polycythemia- and anemia-inducing strains of Friend spleen focus-forming virus induce constitutive activation of the Raf-1/mitogen-activated protein kinase signal transduction pathwayErythropoietin protects against diabetes through direct effects on pancreatic beta cellsMolecular Mechanisms of Trastuzumab Resistance in HER2 Overexpressing Breast CancerActivated Ki-Ras complements erythropoietin signaling in CTLL-2 cells, inducing tyrosine phosphorylation of a 160-kDa protein.Target points in trastuzumab resistanceDeletions in one domain of the Friend virus-encoded membrane glycoprotein overcome host range restrictions for erythroleukemia.Shc adaptor proteins are key transducers of mitogenic signaling mediated by the G protein-coupled thrombin receptorIdentification of a novel pathway important for proliferation and differentiation of primary erythroid progenitors.Expression and activation of SH2/PTB-containing ShcA adaptor protein reflects the pattern of neurogenesis in the mammalian brain.Association between GRB2/Sos and insulin receptor substrate 1 is not sufficient for activation of extracellular signal-regulated kinases by interleukin-4: implications for Ras activation by insulin.Recruitment and phosphorylation of SH2-containing inositol phosphatase and Shc to the B-cell Fc gamma immunoreceptor tyrosine-based inhibition motif peptide motif.A dominant negative erythropoietin (EPO) receptor inhibits EPO-dependent growth and blocks F-gp55-dependent transformation.Murine pluripotent hematopoietic progenitors constitutively expressing a normal erythropoietin receptor proliferate in response to erythropoietin without preferential erythroid cell differentiation.Multiple cytokines stimulate the binding of a common 145-kilodalton protein to Shc at the Grb2 recognition site of ShcTyrosine 343 in the erythropoietin receptor positively regulates erythropoietin-induced cell proliferation and Stat5 activation.Polyomavirus large T antigen induces alterations in cytoplasmic signalling pathways involving Shc activation.Sch proteins are localized on endoplasmic reticulum membranes and are redistributed after tyrosine kinase receptor activation.SHIP is a negative regulator of growth factor receptor-mediated PKB/Akt activation and myeloid cell survival.Interleukin 2 and erythropoietin activate STAT5/MGF via distinct pathwaysMultiple myeloma: increasing evidence for a multistep transformation process.Core erythropoietin receptor signals for late erythroblast development.Spatial signaling networks converge at the adaptor protein Shc.The inositol polyphosphate 5-phosphatase ship is a crucial negative regulator of B cell antigen receptor signalingJAK2 phosphorylates SHC1 in EPO:p-8Y-EPOR:p-12Y-JAK2:LYN:p-CRKL:RABGEF1:SHC1EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:phospho-CRKL:RAPGEF1:phospho-SHC1 binds GRB2:SOS1
P2860
Q24306910-F613993F-BC09-4E9C-9433-8E322A1F051DQ24567715-5C53CD34-7607-4FF0-8937-4F504CB8B8C0Q24568236-CAE3239E-3D68-404E-964C-A88608C74F96Q24610231-BDFDB539-2AE9-41D9-9BA1-62BD262429FFQ24647567-D6CEDEF9-AB83-47F6-929B-6664EA48F2C7Q28590421-05E9E555-E50A-4A93-B9A4-29AE1C8365D7Q28592794-63209FEE-A941-4DCD-B411-B85072016E32Q30305586-920B395D-E199-400E-A773-1A4B9F4C2BE7Q33771858-1A68EEFA-EA53-42CC-8D72-DF948DD77527Q33774503-43115DF5-ACD8-4CFD-AB15-24E5C8FC4372Q33800942-3584BC5C-3F7F-4003-9F1B-BA1A3BF357D3Q33874057-599B8137-7925-4015-BA1B-6624C0BF3D15Q34068968-9A13D4A5-F857-43A8-BFD8-825C4F7DB799Q34420833-B3FCBE7C-1069-48B1-932A-EBCA00A11540Q35684440-B6B6883F-ED5C-4747-8936-86101E9D72C3Q35751753-3DB40C81-6FE0-4CF1-A8A6-4374B7EA39F9Q35821286-FCFDAEC1-80FF-4545-BE40-5766CDFE1FB0Q35831703-2E580773-8BF7-48CE-AAA9-DE7B57F55FA9Q35845039-59C5D8F3-9683-45B1-871F-F2D86FEDA8E5Q36074883-C752ACF8-8D8B-407A-9103-263D09BB56C2Q36304091-38A12FFC-1189-4D9E-9BE1-1278931E3DB4Q36550151-98235480-BD27-4BBD-A712-D0C12B7A852FQ36569569-BD2F409B-BA31-47EB-837E-47D587D18563Q36649362-D0712030-ABBD-4425-AF99-005468428841Q36657459-750FA794-7593-4DA2-B4B2-1172BEE062BDQ36668147-90B1F202-EBE7-4818-9D1A-225992200F0FQ37624851-6E46A9FE-6A30-4E96-AE09-5988CD54E090Q39549444-464623DD-C134-4A37-8035-D1234E144C60Q40018683-173F2A42-48EA-4599-A068-31F132B9ACE7Q40443155-6AFB45A1-99AC-4072-93E2-9F1C2CC9F628Q40806909-9B970197-A662-4E33-BEEC-EF838BA83DF3Q41670812-E4BE240C-C3EB-4EB1-83ED-1716EA5783E1Q41996778-B19D5E3D-5603-4273-8BE5-D1C36976BF60Q42411756-6D771DC1-F6A9-489C-8B41-DCCC1A6E1377Q42462089-BDF591BA-ACD8-4F9E-BBF7-247073C8B2ACQ56860807-8A2C8266-867B-474F-BC0F-422D9BA2F2C0Q56860808-47017C5E-1538-4F76-90DE-037AF1648536
P2860
Erythropoietin stimulates the tyrosine phosphorylation of Shc and its association with Grb2 and a 145-Kd tyrosine phosphorylated protein.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Erythropoietin stimulates the ...... rosine phosphorylated protein.
@en
type
label
Erythropoietin stimulates the ...... rosine phosphorylated protein.
@en
prefLabel
Erythropoietin stimulates the ...... rosine phosphorylated protein.
@en
P2093
P921
P1433
P1476
Erythropoietin stimulates the ...... rosine phosphorylated protein.
@en
P2093
P304
P407
P577
1993-10-01T00:00:00Z