IndraLab

Statements


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"Additionally, inhibition of CDK4/6 by palbociclib upregulates and CSN5 by curcumin downregulates the stability of PD-L1, leading to increased therapeutic effect of anti-PD-1 and anti-CTLA-4 therapy, respectively."

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"CSN6 and Jab1/CSN5 inhibit the degradation of PD-L1 and subsequently sustain PD-L1 stability in cancer cells ."

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"COPS5 and COPS6 can prevent PD-L1 from degrading, thereby maintaining PD-L1 stability in cancer cells [69, 70]."

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"Disrupting the MPN domain of CSN5 affected CSN5 mediated PD-L1 stabilization and deubiquitination XREF_BIBR."

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"The regulation of PD-L1 degradation by CSN5 or OTUB1 is mainly found in breast cancer ."

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"Moreover, the circRNA CircIGF2BP3 and lncRNA KCNQ1OT1 facilitate the stabilization of PD-L1 through targeting OTUB1 and USP22 respectively.91 103 In addition, BBR, compound-15 and shikonin are all reported to target the CSN5 to accelerate the protein degradation of PD-L1 by previous researches.117 118 120Although the anticancer potential of targeting E3s or DUBs has been reported by multitudes of emerging studies, there are still some significant problems that worth being further investigated."

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"The overexpression of CSN5 effectively countered the PMT-O9-1A-induced PD-L1 downregulation, which further demonstrated that PMT-O9-1A enhances PD-L1 degradation by inhibiting CSN5 (Figure 5L)."

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"As shown in Fig. 7 A and B, DHA reduced the expression of CSN5 in LLC cells and xenograft tumor tissues, indicating that CSN5 is involved in DHA-induced Ub-dependent degradation of PD-L1."

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"COP9 signalosome 5 ( CSN5 ) was reported to deubiquitinate PD-L1 , thereby inhibiting PD-L1 degradation ."

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"Taken together, our observations suggest that immunization with B68‐induced senescent cancer cells can promote an antitumor immune response that contributes to tumor prevention.2.7 B68 Mediates PD-L1 Degradation by Targeting CSN5."

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"PD-L-1 stability and nuclear localization can be decreased by inhibitors of CSN5 and HDAC2, which are known to be the post-translational modification regulators of PD-L-1."

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"Emerging research shows that diverse agents targeting ubiquitin-protein enzymes might affect PD-L1 proteasomal degradation, such as STUB1 (Mezzadra et al. 2017), while compounds targeting deubiquitinating enzymes regulate PD-L1 deubiquitination, such as CSN5 (Lim et al. 2016)."