A new protein containing an SH2 domain that inhibits JAK kinases
about
Bruton's tyrosine kinase activity is negatively regulated by Sab, the Btk-SH3 domain-binding proteinp56(dok-2) as a cytokine-inducible inhibitor of cell proliferation and signal transductionThe zinc finger protein Gfi-1 can enhance STAT3 signaling by interacting with the STAT3 inhibitor PIAS3Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing factor RNPS1: a possible regulation of splicing by a complex formationDirect inhibition of Bruton's tyrosine kinase by IBtk, a Btk-binding proteinIdentification of both positive and negative domains within the epidermal growth factor receptor COOH-terminal region for signal transducer and activator of transcription (STAT) activationInhibition of Stat1-mediated gene activation by PIAS1Requirement for microtubule integrity in the SOCS1-mediated intracellular dynamics of HIV-1 GagInteraction of human suppressor of cytokine signaling (SOCS)-2 with the insulin-like growth factor-I receptorTwenty proteins containing a C-terminal SOCS box form five structural classesECHS1 interacts with STAT3 and negatively regulates STAT3 signalingVHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligasesCOMMD1 promotes the ubiquitination of NF-kappaB subunits through a cullin-containing ubiquitin ligaseAnkyrin repeat and SOCS box 3 (ASB3) mediates ubiquitination and degradation of tumor necrosis factor receptor IIPrinciples of interleukin (IL)-6-type cytokine signalling and its regulationInterleukin-6-type cytokine signalling through the gp130/Jak/STAT pathwayInterleukin 9 induces expression of three cytokine signal inhibitors: cytokine-inducible SH2-containing protein, suppressor of cytokine signalling (SOCS)-2 and SOCS-3, but only SOCS-3 overexpression suppresses interleukin 9 signallingSocs1 binds to multiple signalling proteins and suppresses steel factor-dependent proliferationThe JAK-binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loopRegulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1.Selective regulatory function of Socs3 in the formation of IL-17-secreting T cellsAntiviral actions of interferonsGRIM-19, a death-regulatory gene product, suppresses Stat3 activity via functional interactionDifferential binding to and regulation of JAK2 by the SH2 domain and N-terminal region of SH2-bbetaA Drosophila PIAS homologue negatively regulates stat92ECentral role of suppressors of cytokine signaling proteins in hepatic steatosis, insulin resistance, and the metabolic syndrome in the mouseMast cell homeostasis and the JAK-STAT pathwayA DNA damage and stress inducible G protein-coupled receptor blocks cells in G2/MThe conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradationIdentification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complexActivation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complexEnhancing leptin response by preventing SH2-containing phosphatase 2 interaction with Ob receptorSignal transducer and activator of transcription (STAT)-induced STAT inhibitor 1 (SSI-1)/suppressor of cytokine signaling 1 (SOCS1) inhibits insulin signal transduction pathway through modulating insulin receptor substrate 1 (IRS-1) phosphorylationOverexpression of PIAS3 suppresses cell growth and restores the drug sensitivity of human lung cancer cells in association with PI3-K/Akt inactivationOntological visualization of protein-protein interactionsDistinct signal transduction processes by IL-4 and IL-13 and influences from the Q551R variant of the human IL-4 receptor alpha chainSignaling by STATsJanus kinases and signal transducers and activators of transcription: their roles in cytokine signaling, development and immunoregulation.Suppressors of Cytokine Signaling in Sickness and in Health of Pancreatic β-CellsPossible Pharmacological Approach Targeting Endoplasmic Reticulum Stress to Ameliorate Leptin Resistance in Obesity
P2860
Q22009897-8A423C70-D535-4D22-A062-17594CCFC308Q24290345-BCF8C89C-195B-4BF3-B5F1-6B4658B7EC65Q24290464-F494B30C-6022-4AC8-999A-98CA4672C3A3Q24291494-462ABA71-181A-4471-B493-F5D1B6D6B98DQ24291740-7099D71F-1DC7-4001-9C4D-601C5E8D153DQ24299920-66E9B560-548C-4AA9-8420-1057A4075515Q24310082-C87C9C8D-D3DB-4136-BB45-0CB0A7F7CEE7Q24310319-07171839-CFF4-4233-9517-A82B1A607DEFQ24310472-5A1EC114-6EAF-4A40-8646-9A0840D10A08Q24317684-9AE5968E-5BB7-400D-A786-B7F8E0C01784Q24317798-6EE0B146-6DD5-4553-BE11-80176DB125F9Q24322407-6B3502FE-9382-4F92-A123-B4090E99356EQ24337774-3FBBC863-5395-49EE-9D7E-BB974732641EQ24529081-0AD5A9D7-9658-4869-A113-9158EBF332BBQ24530173-52DA8576-67C6-447D-8165-2BC50DC890BCQ24531184-E6491309-24C0-4A21-A35D-759B64DC24DBQ24532238-BBF93864-135C-4573-80A5-2819672D19C1Q24533574-F69469AF-CD69-4FFD-B7B2-5EFA8ACF647FQ24533774-5669B2F5-E44B-441C-9E25-9F77D5772867Q24537294-2FEC5D34-8768-4ACC-ADAE-D9AA5C3B4C87Q24547568-4B91DEDE-F85D-4318-8CC0-CFFC2B57EF39Q24550676-1BEB25D9-9DA1-4F33-8A96-D1D5862F2126Q24553130-B40BED47-A02C-4B87-818A-7AEDE77E5BE2Q24554240-89A7CAA9-07AB-4233-B539-7B6B5398FA41Q24555776-1B1204E1-4E17-4BDD-BFB3-C2BF677E55B2Q24564225-5D63E895-8952-4AED-BE05-B3D9BB93C4A7Q24632515-D6E025B7-8C77-42E2-8547-AB8380CA5AD2Q24645905-AAB6F83B-42BC-48A8-86F1-AE8E4CE6B56CQ24654107-FFB5F99C-DFE4-4997-A7D8-78EFB0B0B31FQ24654714-44F1C007-B5F2-4AD4-9AC0-9CB2F1A58C65Q24655274-5CED28BD-5F8F-4743-A0A8-71891A184CCFQ24656029-05D59E68-4D1F-4324-91DE-0216F7821737Q24675835-415BF8B9-15E3-4495-8FBC-CAB3A347AD54Q24678516-106B4308-E610-4AE1-8011-7F6429B59160Q24795348-B387DC68-4BBE-4FD9-ADD1-F08BFECCB0FBQ24802418-0BCA970A-8494-40E9-88BA-4E5BF034DE36Q24805570-F03AE945-A6FD-4B8A-B462-2F25840CA40EQ24806655-7C39610D-7679-4272-A35F-E8B963359317Q26744658-85CF201E-14C6-4FA2-A439-2674C2A2DC69Q26745134-179B91BF-B528-4AE6-8B4B-A98F88AA29D6
P2860
A new protein containing an SH2 domain that inhibits JAK kinases
description
1997 nî lūn-bûn
@nan
1997 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
A new protein containing an SH2 domain that inhibits JAK kinases
@ast
A new protein containing an SH2 domain that inhibits JAK kinases
@en
A new protein containing an SH2 domain that inhibits JAK kinases
@en-gb
A new protein containing an SH2 domain that inhibits JAK kinases
@nl
type
label
A new protein containing an SH2 domain that inhibits JAK kinases
@ast
A new protein containing an SH2 domain that inhibits JAK kinases
@en
A new protein containing an SH2 domain that inhibits JAK kinases
@en-gb
A new protein containing an SH2 domain that inhibits JAK kinases
@nl
prefLabel
A new protein containing an SH2 domain that inhibits JAK kinases
@ast
A new protein containing an SH2 domain that inhibits JAK kinases
@en
A new protein containing an SH2 domain that inhibits JAK kinases
@en-gb
A new protein containing an SH2 domain that inhibits JAK kinases
@nl
P2093
P3181
P356
P1433
P1476
A new protein containing an SH2 domain that inhibits JAK kinases
@en
P2093
A Matsumoto
A Yoshimura
H Sakamoto
M Masuhara
M Yokouchi
S Tanimura
P2888
P304
P3181
P356
10.1038/43213
P407
P577
1997-06-01T00:00:00Z
P6179
1015325599