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Given the high structural conservation between CUL5s binding modes with RBX1 and RBX2 (83) found that neddylation-induced structural rearrangement of CUL5 facilitates its interaction with another key RBR-type E3 ligase, ARIH2, thereby activating the ubiquitin ligase activity of CUL5

Our results revealed that SFN treatment considerably inhibited the phosphorylation of STAT3 and the expression of K16 and K17 (Fig

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