IndraLab

Statements


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"Otub1 deficiency not only promotes signal induced p100 processing and noncanonical NF-kappaB activation but also causes steady-state p100 degradation, leading to aberrant NF-kappaB activation in the canonical pathway."

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"Recently, it was also observed that OTUB-1 promotes NF-kappaB activation in dendritic cells during stimulated inflammatory conditions by lysine48 deubiquitination of UBC13 [XREF_BIBR]."

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"Recent reports showed that TAK1 kinase and OTUB1 controls NF-κB activation using similar Ube2v1-UBC13/TRAF6 signaling axis."

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"Furthermore, knockdown of OTUB1 reduces TWEAK induced activation of canonical NF-kappaB and MAPK signalling pathways and modulates TWEAK induced gene expression."

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"Mechanistically, OTUB1 promoted NF-kappaB activity in DCs by K48-linked deubiquitination and stabilization of the E2-conjugating enzyme UBC13, resulting in increased K63-linked ubiquitination of IRAK1 (IL-1 receptor-associated kinase 1) and TRAF6 (TNF receptor-associated factor 6)."

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"OTUB1 positively regulates proinflammatory NF-kappaB signaling in DCs."