IndraLab

Statements


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"However, at least in lymphoma cells both CYLD fragments are unstable and degraded by the proteasome in the presence of ibrutinib suggesting that MALT1 cleavage may inactivate CYLD functions (56)."

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"Moreover, TRIM47 promotes K48-linked ubiquitination, leading to the degradation of CYLD by the proteasome, thereby activating the NF-κB pathway and regulating the biological behavior of gastric cancer cells."

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"CYLD may be functionally inactivated through its phosphorylation, degraded by the ubiquitination and proteasome pathway, or repressed at the level of transcription."

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"The HPV encoded oncogenic protein E6 promotes hypoxia induced NF-kappaB activation by triggering the ubiquitination and proteasome mediated degradation of CYLD [XREF_BIBR]."

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"HeLa and SiHa cells were exposed to MG132 (10 microM) for one hour prior to harvesting protein in order to prevent E6 mediated, proteasome dependent degradation of CYLD."