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USP18 binds BCL2L1. 13 / 14
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"Interestingly, in transfected cells, we found that the deletion of the BH3 domain abrogated the interaction between USP18 with BCL2L1 ( Fig. 6 E)."
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"Mechanistically, USP18 can directly bind to anti-apoptotic protein BCL2L1 and up-regulate its expression, thus exerting its anti-apoptotic role ."
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"These results indicate that the BH3 domain of BCL2L1 is critical for the interaction between USP18 with BCL2L1."
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"Mechanistically, USP18 can directly bind to anti-apoptotic protein BCL2L1 and up-regulate its expression, thus exerting its anti-apoptotic role xref ."
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"The reciprocal immunoprecipitation experiment using anti-USP18 antibody also confirmed the binding of BCL2L1 and USP18 ( Fig. 6 A)."
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"The reciprocal immunoprecipitation experiment using anti-USP18 antibody also confirmed the binding of BCL2L1 and USP18."
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"Since the regulation of USP18 on BCL2L1, we further evaluated whether USP18 could directly bind BCL2L1 to affect cell-cycle progression."
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"These findings indicated that BCL2L1 was positively regulated by USP18, and the effect of USP18 on the proliferation and apoptosis of HCC cells was achieved by BCL2L1.Since the regulation of USP18 on [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In addition, a mitochondrial Co-IP also showed a direct interaction between BCL2L1 and USP18 in Hep3B cells."
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"In addition, a mitochondrial Co-IP also showed a direct interaction between BCL2L1 and USP18 in Hep3B cells ( Fig. 6 D)."
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