Matches in UGent Biblio for { <https://biblio.ugent.be/publication/3009479#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B284440.
- aggregation creator B284441.
- aggregation creator B284442.
- aggregation creator B284443.
- aggregation creator B284444.
- aggregation creator B284445.
- aggregation creator B284446.
- aggregation creator B284447.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2012".
- aggregation format "application/pdf".
- aggregation hasFormat 3009479.bibtex.
- aggregation hasFormat 3009479.csv.
- aggregation hasFormat 3009479.dc.
- aggregation hasFormat 3009479.didl.
- aggregation hasFormat 3009479.doc.
- aggregation hasFormat 3009479.json.
- aggregation hasFormat 3009479.mets.
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- aggregation hasFormat 3009479.rdf.
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- aggregation hasFormat 3009479.txt.
- aggregation hasFormat 3009479.xls.
- aggregation hasFormat 3009479.yaml.
- aggregation isPartOf urn:issn:1350-9047.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Proteolysis of Ambra1 during apoptosis has a role in the inhibition of the autophagic pro-survival response".
- aggregation abstract "Under stress conditions, pro-survival and pro-death processes are concomitantly activated and the final outcome depends on the complex crosstalk between these pathways. In most cases, autophagy functions as an early-induced cytoprotective response, favoring stress adaptation by removing damaged subcellular constituents. Moreover, several lines of evidence suggest that autophagy inactivation by the apoptotic machinery is a crucial event for cell death execution. Here we show that apoptotic stimuli induce a rapid decrease in the level of the autophagic factor Activating Molecule in Beclin1-Regulated Autophagy (Ambra1). Ambra1 degradation is prevented by concomitant inhibition of caspases and calpains. By both in vitro and in vivo approaches, we demonstrate that caspases are responsible for Ambra1 cleavage at the D482 site, whereas calpains are involved in complete Ambra1 degradation. Finally, we show that Ambra1 levels are critical for the rate of apoptosis induction. RNA interference-mediated Ambra1 downregulation further sensitizes cells to apoptotic stimuli, while Ambra1 overexpression and, more efficiently, a caspase non-cleavable mutant counteract cell death by prolonging autophagy induction. We conclude that Ambra1 is an important target of apoptotic proteases resulting in the dismantling of the autophagic machinery and the accomplishment of the cell death program.".
- aggregation authorList BK564647.
- aggregation endPage "1504".
- aggregation issue "9".
- aggregation startPage "1495".
- aggregation volume "19".
- aggregation aggregates 4381309.
- aggregation isDescribedBy 3009479.
- aggregation similarTo cdd.2012.27.
- aggregation similarTo LU-3009479.