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USP8 binds CD274. 28 / 28
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"Furthermore, a negative association between USP8 and PD-L1 was confirmed in lung squamous cancer tissues."
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"There is a positive interaction between PD-L1 and USP8 in pancreatic cancer."
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"The PD-1/PD-L1 inhibitory signal plays an important role in tumor immune escape and is an important target of anti-tumor immunotherapy; therefore, we further assessed whether USP8 interacts with PD-L1."
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"Moreover, we observed that endogenous USP8 and endogenous PD-L1 interacted in pancreatic cancer cell lines (KPC, BxPC-3, SW1990) (Fig.  xref )."
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"Furthermore, direct binding of USP8 to PD-L1 was demonstrated in vitro using a GST pull-down assay (Fig.  xref )."
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"These results revealed that USP8 and PD-L1 interact positively in pancreatic cancer."
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"The endogenous interaction between USP8 and PD-L1 was also confirmed by Co-IP and immunoblotting assays in DU145 and PC-3 cells (Fig. xref )."
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"There is a positive interaction between PD-L1 and USP8 in pancreatic cancer."
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"Furthermore, direct binding of USP8 to PD-L1 was demonstrated in vitro using a GST pull-down assay (Fig. 3h)."
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"These results revealed that USP8 specifically interacts with PD-L1 protein and affects the expression level of PD-L1 protein but not mRNA in PCa."
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"To illustrate the process of deubiquitination of PD-L1 in PDAC, Yang et al. reported that USP8 bound with PD-L1 and upregulated its expression by impairing the proteasome-mediated degradation pathway."
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"First, Co-IP assay was performed, the findings of which confirmed an interaction between USP8 and PD-L1 (Fig.  xref A)."
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"USP8, a new PD-L1 deubiquitinase, interacts with PD-L1, thereby inhibiting its ubiquitination-dependent proteasomal degradation in pancreatic cancer."
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"Mechanistically, USP8 directly interacts with PD-L1 and upregulates PD-L1 protein levels by blocking the ubiquitin-proteasome degradation pathway."
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"USP7, USP22, USP8, USP18, USP9X and USP5 have been demonstrated directly bind with PD-L1 to induce its deubiquitination and stabilization [60, 100–102, 143, 164, 186]."
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"ChIP assay confirmed the interaction between USP8 and PD-L1 proteins."
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"Moreover, USP8 interacted positively with PD-L1 and upregulated its expression by inhibiting the ubiquitination-regulated proteasome degradation pathway in pancreatic cancer."
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"Additionally, research by Bai et al. demonstrated that USP8 interacts with PD-L1 in pancreatic cancer, stabilizing PD-L1 expression by inhibiting its ubiquitin-mediated proteasomal degradation."
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"First, Co-IP assay was performed, the findings of which confirmed an interaction between USP8 and PD-L1 (Fig. 6A)."
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"A direct interaction between USP8 and PD-L1 leads to the upregulation of PD-L1 expression by inhibiting ubiquitination-regulated proteasomal degradation of PD-L1 proteins in pancreatic ductal adenocar[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Another study showed that USP8 can directly bind to PD-L1 and remove its ubiquitination modification, thereby stabilizing the protein expression level of PD-L1 and ultimately promoting the process of immune evasion in pancreatic cancer ( xref )."
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"Direct binding of SNHG12 to HuR, as well as binding of PD-L1 and USP8 to HuR, was predicted using RNA–protein interaction prediction (RPISeq) (http://pridb.gdcb.iastate.edu/RPISeq/, accessed on 19 June 2023) and validated by RIP assay [151]."
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"USP8 binds to PD-L1, enhancing K48-linked ubiquitination and reducing K63-linked ubiquitination levels, thereby balancing the action of TRAF6 and maintaining PD-L1 stability [ xref ]."
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No evidence text available
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No evidence text available
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"A direct interaction between USP8 and PD-L1 leads to the upregulation of PD-L1 expression by inhibiting ubiquitination-regulated proteasomal degradation of PD-L1 proteins in pancreatic ductal adenocar[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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