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Data indicate an association between TAK1-binding protein 2 (TAB2) mutations and a connective tissue disorder with severe polyvalvular heart disease and subtle facial dysmorphism.
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The combination of WES, genomic triangulation, and systems biology has uncovered perturbations in TGF-beta activated kinase 1 signaling as a novel pathogenic substrate for polyvalvular syndrome.
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Data suggest that mRNA/protein levels of NLRP6 are down-regulated in synovial tissues and synoviocytes of rheumatoid arthritis (RA) patients compared to osteoarthritis patients; NLRP6 provides docking site to facilitate interaction between TAB2/3 and TRIM38 in RA synoviocytes in response to TNFalpha. (NLRP6 = ; TAB2/3 = transforming growth factor-b-activated kinase 1-binding protein 2/3; TRIM38 = tripartite motif 38)
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A Novel Functional Domain of Tab2 Involved in the Interaction with Estrogen Receptor Alpha in Breast Cancer Cells
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The expression of miR-155 target gene, TAB2, and the downstream gene, iNOS, were found to be inhibited in psoriatic dermal mesenchymal stem cells.
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DK1 inhibits the formation of the TAK1-TAB2-TRAF6 complex and leads to the inhibition of TRAF6 ubiquitination.
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Authors demonstrate that enterovirus 71 3C interacts with TAB2 and TAK1 and suppresses cytokine expression via cleavage of the TAK1 complex proteins.
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SUMOylation may serve as a novel mechanism for the regulation of TAB2.
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conclude that TRIM38 negatively regulates TNFalpha- and IL-1beta-induced signaling by mediating lysosome-dependent degradation of TAB2/3, two critical components in TNFalpha- and IL-1beta-induced signaling pathways
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These data indicate that overexpression of TRIM22 may negatively regulate the TRAF6-stimulated NF-kappaB pathway by interacting with and degrading TAB2.
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our data implicate Tab2 as a mediator of resistance to endocrine therapy and as a potential new target to reverse pharmacological resistance and potentiate antiestrogen action.
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We found that endothelial TAK1 and TAB2, but not TAB1, were critically involved in vascular formation
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MiR-23b suppresses IL-17-, tumor necrosis factor alpha (TNF-alpha)- or IL-1beta-induced NF-kappaB activation and inflammatory cytokine expression by targeting TAB2, TAB3 and IKK-alpha.
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TAK1 and its adapter protein, TAB2, reciprocally regulate both TAK1- and ASK1-mediated signaling pathways to direct the activations of NF-kappaB and AP-1.
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human TAB2 and TAB3, ubiquitin-chain sensory proteins involved in NF-kappaB signalling, are directly inactivated by enteropathogenic Escherichia coli NleE, a conserved bacterial type-III-secreted effector responsible for blocking host NF-kappaB signalling
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These results point to the existence of an autophagy-stimulatory 'switch' whereby TAB2 and TAB3 abandon inhibitory interactions with Beclin 1 to engage in a stimulatory liaison with TAK1.
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these studies show that the TAK1-TAB2-TAB3 signaling axis is critical for carcinoma-induced bone lesions, mediating expression of proinvasive and osteolytic factors.
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microRNA-155 negatively regulates the expression of TAB2 and downstream IFN-gamma-inducible protein of 10 kDa as a negative feedback system.
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The ability of human Trim5alpha to regulate TAB2 levels, to activate NF-kappaB, and to recognize retroviral capsids are genetically separable.
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Co-expression of RelA and/or TAB2 markedly increased Tax-mediated NF-kappaB activation.
