2020
DOI: 10.1007/s10637-020-00956-9
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Chemosensitivity to HM90822, a novel synthetic IAP antagonist, is determined by p-AKT-inducible XIAP phosphorylation in human pancreatic cancer cells

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Cited by 4 publications
(1 citation statement)
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“…On the other hand, XIAP regulation appears to be executed through post-translational modifications, particularly proteasome-mediated degradation. Notably, XIAP can be phosphorylated by Akt and protein kinase C (PKC), which prevents its ubiquitination and subsequent proteasomal degradation ( 54 , 55 ). XIAP is also well-known for its E3 ubiquitin ligase activity, allowing it to induce autoubiquitination.…”
Section: Discussionmentioning
confidence: 99%
“…On the other hand, XIAP regulation appears to be executed through post-translational modifications, particularly proteasome-mediated degradation. Notably, XIAP can be phosphorylated by Akt and protein kinase C (PKC), which prevents its ubiquitination and subsequent proteasomal degradation ( 54 , 55 ). XIAP is also well-known for its E3 ubiquitin ligase activity, allowing it to induce autoubiquitination.…”
Section: Discussionmentioning
confidence: 99%