Matches in UGent Biblio for { <https://biblio.ugent.be/publication/1202553#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B444344.
- aggregation creator B444345.
- aggregation creator B444346.
- aggregation creator B444347.
- aggregation creator B444348.
- aggregation creator B444349.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2007".
- aggregation format "application/pdf".
- aggregation hasFormat 1202553.bibtex.
- aggregation hasFormat 1202553.csv.
- aggregation hasFormat 1202553.dc.
- aggregation hasFormat 1202553.didl.
- aggregation hasFormat 1202553.doc.
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- aggregation hasFormat 1202553.txt.
- aggregation hasFormat 1202553.xls.
- aggregation hasFormat 1202553.yaml.
- aggregation isPartOf urn:issn:0261-4189.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappa B pathway".
- aggregation abstract "Upon DNA damage, a complex called the PIDDosome is formed and either signals NF-kappa B activation and thus cell survival or alternatively triggers caspase-2 activation and apoptosis. PIDD (p53-induced protein with a death domain) is constitutively processed giving rise to a 48-kDa N-terminal fragment containing the leucine-rich repeats (LRRs, PIDD-N) and a 51-kDa C-terminal fragment containing the death domain (DD, PIDD-C). The latter undergoes further cleavage resulting in a 37-kDa fragment (PIDD-CC). Here we show that processing occurs at S446 (generating PIDD-C) and S588 (generating PIDD-CC) by an auto-processing mechanism similar to that found in the nuclear pore protein Nup98/ 96 and inteins. Auto-cleavage of PIDD determines the outcome of the downstream signaling events. Whereas initially formed PIDD-C mediates the activation of NF-kappa B via the recruitment of RIP-1 and NEMO, subsequent formation of PIDD-CC causes caspase-2 activation and thus cell death. A non-cleavable PIDD mutant is unable to translocate from the cytoplasm to the nucleus and loses both activities. In this way, autoproteolysis of PIDD might participate in the orchestration of the DNA damage-induced life and death signaling pathways.".
- aggregation authorList BK775621.
- aggregation endPage "208".
- aggregation issue "1".
- aggregation startPage "197".
- aggregation volume "26".
- aggregation aggregates 1202721.
- aggregation isDescribedBy 1202553.
- aggregation similarTo sj.emboj.7601473.
- aggregation similarTo LU-1202553.