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High TAB1 expression is associated with colorectal cancer.
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TAB1 was identified as a functional target of miR-134, and the expression of TAB1 was increased by the transcription factors of NF-kappaB1, c-Rel, and ELK1 via miR-134.
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we show that IL-1 induces robust p38a activation both in the nucleus and in the cytoplasm/membrane.Following stimulation, p38a activity returns to a basal level in absence of receptor degradation. While nuclear pulse is controlled by MKP1 through a negative feedback to pp38, its basal activity is controlled by both TAB1 and MKP1 through a positive feedback loop.
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TAK1/TAB1 expression in non-small cell lung carcinoma tissue is significantly increased and closely associated with patient clinical prognosis.
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miR-29a repressed TAB1-mediated TIMP-1 production in dermal fibroblasts, demonstrating that miR-29a may be a therapeutic target in SSc.
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Data indicate that mitogen-activated protein kinase (MAPK) p38 activation is triggered by AMP-activated protein kinases (AMPK) and mediated by TAB1 protein.
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The amino acid sequence between positions 373 and 502 of TAB1 is required for TP interaction.
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USP18 inhibits NF-kappaB and NFAT activation during Th17 differentiation by deubiquitinating the TAK1-TAB1 complex.
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We found that endothelial TAK1 and TAB2, but not TAB1, were critically involved in vascular formation
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TAK1 plays a critical role in accentuated epithelial to mesenchymal transition in obliterative bronchiolitis after lung transplantation.
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data suggest a complex role of aa 452-457 of TAB1 in controlling p38 MAPK activity and subcellular localization and implicate these residues in TAK1- or p38 MAPK-dependent post-transcriptional control of gene expression
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Phosphorylation and polyubiquitination of TAK1 are necessary for activation of NF-kappaB by the Kaposi's sarcoma-associated herpesvirus vGPCR.
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Co-expression of TAK1 and TAB1 resulted in a functional and active TAK1-TAB1 complex capable of directly activating full-length heterotrimeric mammalian AMP-activated protein kinase (AMPK) in vitro.
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interaction with p38alpha leads to autophosphorylation and activation of p38alpha
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The TAK1-TAB1 fusion protein is a novel constitutively active mitogen-activated protein kinase kinase kinase that stimulates AP-1 and NF-kappaB signaling pathways
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TauAlphaBeta1beta is involved in regulating p38alpha activity in physiological conditions
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These results suggest that the TAK1-NLK MAPK cascade is activated by the noncanonical Wnt-5a/Ca(2+) pathway and antagonizes canonical Wnt/beta-catenin signaling.
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characterized the molecular mechanisms of cellular stress-induced TAK1 activation, focusing mainly on the phosphorylation of TAK1 at Thr-187 and Ser-192 in the activation loop; TAB1 and TAB2 were differentially involved in the phosphorylation of TAK1
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Determinants that control the specific interactions between TAB1 and MAPK14 are identified.
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The protein phosphatase 2C alpha fold is conserved in TAB1(a TAK1 regulatory subunit) but some AAs needed for dual metal-binding & catalysis are missing. It is a pseudophosphatase, & may bind/regulate access to phosphorylated AAs on downstream substrates.
