About: Tyrosines 868, 966, and 972 in the kinase domain of JAK2 are autophosphorylated and required for maximal JAK2 kinase activity

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About: Tyrosines 868, 966, and 972 in the kinase domain of JAK2 are autophosphorylated and required for maximal JAK2 kinase activity Goto Sponge NotDistinct Permalink

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description	artículu científicu espublizáu en 2010 (ast) vědecký článek publikovaný v roce 2010 (cs) 2010 թվականի մայիսին հրատարակված գիտական հոդված (hy) 2010 թուականի Մայիսին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в травні 2010 (uk) wetenschappelijk artikel (gepubliceerd op 2010/05/01) (nl) vedecký článok (publikovaný 2010/05/01) (sk) مقالة علمية (نشرت في مايو 2010) (ar) scientific journal article (en) im Mai 2010 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q28115584-5F83E00B-0B8B-4FCF-BA84-CE91235BE6C8
publication date	2010-05-01 00:00:00Z (xsd:dateTime)
cites work	wds:Q28115584-03F0D53C-EE09-46BD-B458-DA8BC8557005 wds:Q28115584-04C7CB15-9DB7-4B6C-B379-A85519311F55 wds:Q28115584-083C0641-7C35-4A96-8B75-B42800982048 wds:Q28115584-150251F0-C116-48BF-BDDF-0311EAEBBB5F wds:Q28115584-2CB3A1C8-0AD4-42FB-BD6C-9D8AC774D930 wds:Q28115584-3B31FFC5-FBB4-4F84-92C5-DBAA47D95FB7 wds:Q28115584-3FE6BFE1-1DE3-46E1-9A43-A5CF32AE5BA4 wds:Q28115584-40781B21-4FE9-4027-A342-45DA543367D3 wds:Q28115584-40944C84-915F-43D2-B1F7-944C77084D64 wds:Q28115584-42F895E7-D42D-4151-B04A-126A4257D928 wds:Q28115584-4A2BEB4B-793D-4D50-B613-9ADACC35F367 wds:Q28115584-4B62F397-5EAD-4ADB-ACD4-E96BD599956A wds:Q28115584-4BFD142C-4E41-4AF0-87FE-E39E88438BA4 wds:Q28115584-4C8C997C-9A85-430C-A4CB-6032C291662A wds:Q28115584-55F5E1CB-28EB-494D-BC3D-1283F7AE83B1 wds:Q28115584-585CD5A6-64BE-42AC-AAFC-9B711187B90D wds:Q28115584-5DF70D82-857D-4957-9BBF-6A642A9ED0F8 wds:Q28115584-6382BF57-5521-4EEF-9067-75F6B72E57B9 wds:Q28115584-63B7DF6B-4F10-48EF-8342-09F8B8BE632F wds:Q28115584-67FE8600-33CD-4CEE-9ED3-6474F4253F76 wds:Q28115584-725D8B8D-06EB-428D-A1ED-DD0FEB867537 wds:Q28115584-736FD2A2-9748-499E-8ECF-9DD2C7C84518 wds:Q28115584-77CA5820-9D42-4826-A352-E47E19DBCE54 wds:Q28115584-80B0F429-B1B4-42A1-B0DA-23037606F7D8 wds:Q28115584-95A4D848-CFC8-4869-8574-99A314664C2B wds:Q28115584-9BE2E694-19E4-4241-AE54-948C992246E3 wds:Q28115584-9D584FB0-3595-41C6-AB57-B3858D2ABBF4 wds:Q28115584-9F9D41E9-883C-4270-BE57-89F6BED3EB62 wds:Q28115584-A4127C09-CCDE-45E3-AD40-7E119FF9BAE1 wds:Q28115584-A4F0D83D-D5D1-4DE6-8A33-5A27B09EEDD3 wds:Q28115584-A5965CF5-F172-455E-AD99-14A949E473A5 wds:Q28115584-AA15271F-AD35-4AC4-A1C2-C52AFEAE2906 wds:Q28115584-AE6DBCF6-86D4-4A27-B054-770D1BF39050 wds:Q28115584-B3714F55-E3DD-40D7-BB12-F29424814353 wds:Q28115584-B5201A81-3FE7-4F88-9CB8-E2B0777293F5 wds:Q28115584-B921E3C9-20E4-4EF1-8CF9-386D866C1281 wds:Q28115584-B9DA0275-ECE0-49B1-A315-8D6770DC1963 wds:Q28115584-BC2A88DD-695B-4839-902F-93380E80F56A wds:Q28115584-C75500AD-34DD-4DA9-8EFF-AC756CC9E77E wds:Q28115584-CD7A8244-984B-44BA-A355-080764991E1C wds:Q28115584-CDB9DA48-88A0-4816-86AE-75E06B634794 wds:Q28115584-D398AF91-810A-4A0D-9699-3E7B104DB515 wds:Q28115584-D43A1E92-AFDA-469F-918E-77AAAF570065 wds:Q28115584-D4CDA5C5-F0EF-493F-BEE5-C60FD19DB68C wds:Q28115584-D9A9806C-2CB8-4EBA-9FD4-75FFE0F3C474 wds:Q28115584-DCCE54FF-5DA3-4AB4-B26F-EB16A7FC8DBE wds:Q28115584-E23DA7D9-47B5-4C56-B25E-781FE367B625 wds:Q28115584-E96846D3-B00C-461B-BB4C-2B0AA51E04E4 wds:Q28115584-F0DAEA5B-702F-4D22-8A17-BB573214CDE8 wds:Q28115584-F2209691-B787-4E64-9A9A-22F06B6883B7 wds:Q28115584-F7E02EB6-8242-4DF2-96CD-5F4043E29E60 wds:Q28115584-F8D93103-8154-4D60-9E20-DC921ADA9953 wds:Q28115584-F91C9F99-BA53-42CF-A4CB-F02F91A2C2DD wds:Q28115584-FC7AB9DE-2787-4F69-A45D-8A5E51A4FF9D
cites work	Activation of Jak2 catalytic activity requires phosphorylation of Y1007 in the kinase activation loop Autophosphorylation of JAK2 on tyrosines 221 and 570 regulates its activity Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates Raf activation is regulated by tyrosine 510 phosphorylation in Drosophila Receptor specific downregulation of cytokine signaling by autophosphorylation in the FERM domain of Jak2 Structure of the murine Jak2 protein-tyrosine kinase and its role in interleukin 3 signal transduction Identification of JAK2 as a growth hormone receptor-associated tyrosine kinase Introduction of exogenous growth hormone receptors augments growth hormone-responsive insulin biosynthesis in rat insulinoma cells JAK2T875N is a novel activating mutation that results in myeloproliferative disease with features of megakaryoblastic leukemia in a murine bone marrow transplantation model Improved immobilized metal affinity chromatography for large-scale phosphoproteomics applications Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity Cloning and expression of a protein-tyrosine-phosphatase Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog Identification and functional analysis of phosphorylated tyrosine residues within EphA2 receptor tyrosine kinase. Direct stimulation of Jak/STAT pathway by the angiotensin II AT1 receptor Structural modes of stabilization of permissive phosphorylation sites in protein kinases: distinct strategies in Ser/Thr and Tyr kinases Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction The conformational plasticity of protein kinases Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels Signaling networks assembled by oncogenic EGFR and c-Met A change in conformational dynamics underlies the activation of Eph receptor tyrosine kinases Transcriptional inhibition by Stat5. Differential activities at growth-related versus differentiation-specific promoters Multiple in vivo tyrosine phosphorylation sites in EphB receptors In vivo tyrosine phosphorylation sites of activated ephrin-B1 and ephB2 from neural tissue FGFR3 activates RSK2 to mediate hematopoietic transformation through tyrosine phosphorylation of RSK2 and activation of the MEK/ERK pathway Phosphorylation of human Jak3 at tyrosines 904 and 939 positively regulates its activity High-efficiency transformation of mammalian cells by plasmid DNA The RSK family of kinases: emerging roles in cellular signalling JAK mutations in high-risk childhood acute lymphoblastic leukemia Dominant negative stat3 mutant inhibits interleukin-6-induced Jak-STAT signal transduction Epidermal growth factor stimulates RSK2 activation through activation of the MEK/ERK pathway and src-dependent tyrosine phosphorylation of RSK2 at Tyr-529. Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism

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