TAK1-dependent signaling requires functional interaction with TAB2/TAB3
TAK1-dependent signaling requires functional interaction with TAB2/TAB3Inhibition of autophagy by TAB2 and TAB3Two-sided ubiquitin binding explains specificity of the TAB2 NZF domainThe RING domain and first zinc finger of TRAF6 coordinate signaling by interleukin-1, lipopolysaccharide, and RANKLInnate Immunity and Immune Evasion by Enterovirus 71Pathobiology of Paget's Disease of BoneA Nod to disease vectors: mitigation of pathogen sensing by arthropod salivaModulation of osteoclast differentiation and bone resorption by Rho GTPasesMolecular Basis for the Unique Deubiquitinating Activity of the NF-κB Inhibitor A20Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by NZF domains of TAB2 and TAB3The role of extracellular vesicles in mediating progression, metastasis and potential treatment of hepatocellular carcinomaAutoactivation of transforming growth factor beta-activated kinase 1 is a sequential bimolecular processMutations in MAP3K7 that Alter the Activity of the TAK1 Signaling Complex Cause Frontometaphyseal DysplasiaTAB4 stimulates TAK1-TAB1 phosphorylation and binds polyubiquitin to direct signaling to NF-kappaBDomain specificity of MAP3K family members, MLK and Tak1, for JNK signaling in DrosophilaAssociation between imatinib-resistant BCR-ABL mutation-negative leukemia and persistent activation of LYN kinase.Enterovirus 71 3C inhibits cytokine expression through cleavage of the TAK1/TAB1/TAB2/TAB3 complex.Tumor necrosis factor-alpha augments matrix metalloproteinase-9 production in skeletal muscle cells through the activation of transforming growth factor-beta-activated kinase 1 (TAK1)-dependent signaling pathwayDeletion of TAK1 in the myeloid lineage results in the spontaneous development of myelomonocytic leukemia in miceProtein ubiquitination in lymphoid malignancies.Transforming growth factor β-activated kinase 1 signaling pathway critically regulates myocardial survival and remodelingPolyubiquitination events mediate polymethylmethacrylate (PMMA) particle activation of NF-kappaB pathwayLoss of Trabid, a new negative regulator of the drosophila immune-deficiency pathway at the level of TAK1, reduces life span.Glycogen synthase kinase 3β ubiquitination by TRAF6 regulates TLR3-mediated pro-inflammatory cytokine productionRNF4 negatively regulates NF-κB signaling by down-regulating TAB2.Adenosine A1 receptor regulates osteoclast formation by altering TRAF6/TAK1 signaling.Notch signaling promotes osteoclast maturation and resorptive activity.TAK1 Regulates Myocardial Response to Pathological Stress via NFAT, NFκB, and Bnip3 Pathways.Sequence-specific activation of TAK1-D by short double-stranded RNAs induces apoptosis in NCI-H460 cellsTumor necrosis factor receptor-associated factor 6 (TRAF6) and TGFβ-activated kinase 1 (TAK1) play essential roles in the C-type lectin receptor signaling in response to Candida albicans infection.Lyn regulates BCR-ABL and Gab2 tyrosine phosphorylation and c-Cbl protein stability in imatinib-resistant chronic myelogenous leukemia cells.TAK1 is essential for osteoclast differentiation and is an important modulator of cell death by apoptosis and necroptosis.Altered TAB1:I kappaB kinase interaction promotes transforming growth factor beta-mediated nuclear factor-kappaB activation during breast cancer progression.Interaction between TAK1-TAB1-TAB2 and RCAN1-calcineurin defines a signalling nodal control point.TAB3 O-GlcNAcylation promotes metastasis of triple negative breast cancer.Breast cancer-derived factors stimulate osteoclastogenesis through the Ca2+/protein kinase C and transforming growth factor-beta/MAPK signaling pathways.Complex changes in alternative pre-mRNA splicing play a central role in the epithelial-to-mesenchymal transition (EMT).TAK1, more than just innate immunity.Molecular switches under TGFβ signalling during progression from cardiac hypertrophy to heart failure.Docosahexaenoic acid inhibits inflammation via free fatty acid receptor FFA4, disruption of TAB2 interaction with TAK1/TAB1 and downregulation of ERK-dependent Egr-1 expression in EA.hy926 cells.
P2860
about
Q24297091-C22618FF-8A82-4CD4-A42C-34B5F06E9999Q24320937-E433B2F9-48EC-4A49-8F87-5705508D7B9CQ24324222-2C06E588-1F1A-4B85-884E-C5CB5CA17249Q24654977-7EA66A3A-A8C3-49DA-982E-F654B1F4F813Q26773329-F00542F8-BB54-4DAF-8C33-724F17564D81Q26824476-56487F11-9DCF-48B7-9A04-E56C152736DAQ26830623-87020AD5-9804-4A53-B2B2-8D99CA43DC4CQ26851553-49074D5B-B539-407A-A5FA-DB930A0D6940Q27649460-6BAE6C6F-1973-41A9-A9DD-C19E1249BAC1Q27658279-E57200F8-5710-49B1-8D77-497491A3F892Q28066407-47A632CA-6983-4C35-BC70-499E655DD766Q28117206-44AE5F55-12B7-4FED-881E-7A2E21B2633BQ28117317-F54140C1-B3E7-4ADF-9AEF-D41AB0D05A2AQ30439229-3F3547D5-CDE2-421D-94F4-F8EB50BB1763Q33779539-184843B4-F8DE-425F-A22D-B3EF9016B57EQ33988398-E03D3D2D-00D9-4376-B8E1-42598B441675Q34059431-8A9729EB-4245-4A5F-886B-89EC5B4A0802Q34132341-830B81B0-EDF5-4633-962D-A50E85D4DF2FQ34516262-E25766EF-300D-46FB-82BD-9012B68DF526Q34722684-19A77151-6BEB-4492-9AE8-B631429377C9Q34995991-8A7D7BBD-D3DB-4A11-846E-BC1C7D5AECCEQ35084995-8977B0FF-FF8E-45D9-86D6-E0C9E0A2C3F3Q35105686-0CD49D27-1745-4FC6-9B2E-3D96A044699AQ35407394-0304442F-4AEB-48AA-B3B8-1560FEFBB1BAQ35753160-524C4FF1-600F-4225-8875-59318B0D3D10Q35953968-BD2D8578-9CB6-4DF4-BAAE-5C408A3A89D6Q36047882-0744D758-B630-4AA8-B4B9-092B36992C2DQ36275375-D18C9002-FC73-4B11-9580-74593099DA8AQ36470294-26E94B6B-D167-4167-A196-2B3F3DC6F6C7Q36492765-2A324445-C930-4154-A19A-77A30FD6B50AQ36508969-14BA8739-6272-4C58-8650-DF34F352C560Q36560045-E0C534A9-6246-40D6-BAAC-478179613734Q37041538-0F04B2C4-539D-4AC8-BBB4-9EF043146782Q37129709-73C7361D-7427-4D47-B204-DB606F002C17Q37225680-6F6AB960-1770-4BC3-A345-7C5DF2D81A13Q37446271-D60C461E-2131-4563-A1BD-581CC046235EQ38006770-171C5603-94F9-4A7C-B4F0-29D61AE656A7Q38040025-71E49F13-AA13-4D79-88D8-BE8862D500D9Q38597820-BFE90B09-3B96-4AB5-BB04-BBD796AD0611Q38818885-18A5E971-031B-4079-9EB9-92DABA6A2423
P2860
TAK1-dependent signaling requires functional interaction with TAB2/TAB3
description
2007 nî lūn-bûn
@nan
2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
TAK1-dependent signaling requires functional interaction with TAB2/TAB3
@ast
TAK1-dependent signaling requires functional interaction with TAB2/TAB3
@en
TAK1-dependent signaling requires functional interaction with TAB2/TAB3
@en-gb
TAK1-dependent signaling requires functional interaction with TAB2/TAB3
@nl
type
label
TAK1-dependent signaling requires functional interaction with TAB2/TAB3
@ast
TAK1-dependent signaling requires functional interaction with TAB2/TAB3
@en
TAK1-dependent signaling requires functional interaction with TAB2/TAB3
@en-gb
TAK1-dependent signaling requires functional interaction with TAB2/TAB3
@nl
prefLabel
TAK1-dependent signaling requires functional interaction with TAB2/TAB3
@ast
TAK1-dependent signaling requires functional interaction with TAB2/TAB3
@en
TAK1-dependent signaling requires functional interaction with TAB2/TAB3
@en-gb
TAK1-dependent signaling requires functional interaction with TAB2/TAB3
@nl
P2093
P2860
P921
P356
P1476
TAK1-dependent signaling requires functional interaction with TAB2/TAB3
@en
P2093
Alejandro D Campos
Arnaud Besse
Betty Lamothe
Bryant G Darnay
Su-Chang Lin
Upendra Maddineni
William K Webster
P2860
P304
P356
10.1074/JBC.M608867200
P407
P577
2007-02-09T00:00:00Z