IndraLab

Statements

CYLD inhibits NFASC. 10 / 10
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"Other E3 ligases regulating NF‐κB signalling include Makorin ring finger 2 (MKRN2) E3 ligase which suppresses NF‐κB signalling via proteasome degradation of p65 and the E3 ligase ITCH which cooperates with deubiquitinating enzyme cylindromatosis tumour suppressor protein (CYLD) to mediate deubiquitination and degradation of TAK1."
36881608
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"For example, the associated molecule with the SH3 domain of STAM (AMSH) and ubiquitin-specific protease Y (UBPY) DUB proteins were shown to rescue ubiquitylated cargo (such as receptor tyrosine kinase[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
19631546
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"In addition, CYLD negatively regulated NF‐κB activation by deconjugating its k63‐linked ubiquitin chains [87]."
39626954
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"CYLD, a crucial gene in clear K63 polyubiquitin and M1 linear ubiquitin chains, inhibits NFκB signaling activation at multiple distinct steps (20)."
38983924
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"Similarly, CYLD is also known to inhibit NFκB signaling and therefore, inhibitory phosphorylation of CYLD will also serve to enhance expression of prosurvival genes."
32024820
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"CYLD siRNA in a HCC cell line suppressed apoptosis via the NFκB-mediated tumor necrosis factor α signaling pathway by lowering caspase-3 activity [68]."
35884607
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"Using a shRNA library targeting 50 DUBs to identify candidates involved in the regulation of cancer related pathways, they demonstrated that knockdown of CYLD enhanced NF‐κB signalling following Tumour Necrosis Factor (TNF) stimulation (108)."
20073038
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"Prominent among them are A20 and CYLD which were reported to suppress NFκB activation through the inactivation of E3 ubiquitin ligase, TRAF6 [1] ."
28063927
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"After LPS treatment, activated NFκB signal in CYLD LΔ/Δ livers occurred earlier than in wild-type livers, suggesting that loss of CYLD sensitizes hepatocytes to LPS-mediated NFκB activation ( Figure 4[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
22698400
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"CYLD inhibits NFκB-mediated activation by different TNF receptor family members due to deubiquitination and inactivation of TNFR-associated factor 2 (TRAF2) and TRAF6."
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