Matches in UGent Biblio for { <https://biblio.ugent.be/publication/1202569#aggregation> ?p ?o. }
Showing items 1 to 39 of
39
with 100 items per page.
- aggregation classification "A1".
- aggregation creator B383892.
- aggregation creator B383893.
- aggregation creator B383894.
- aggregation creator B383895.
- aggregation creator B383896.
- aggregation creator B383897.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2011".
- aggregation format "application/pdf".
- aggregation hasFormat 1202569.bibtex.
- aggregation hasFormat 1202569.csv.
- aggregation hasFormat 1202569.dc.
- aggregation hasFormat 1202569.didl.
- aggregation hasFormat 1202569.doc.
- aggregation hasFormat 1202569.json.
- aggregation hasFormat 1202569.mets.
- aggregation hasFormat 1202569.mods.
- aggregation hasFormat 1202569.rdf.
- aggregation hasFormat 1202569.ris.
- aggregation hasFormat 1202569.txt.
- aggregation hasFormat 1202569.xls.
- aggregation hasFormat 1202569.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 "Regulation of PIDD auto-proteolysis and activity by the molecular chaperone Hsp90".
- aggregation abstract "In response to DNA damage, p53-induced protein with a death domain (PIDD) forms a complex called the PIDDosome, which either consists of PIDD, RIP-associated protein with a death domain and caspase-2, forming a platform for the activation of caspase-2, or contains PIDD, RIP1 and NEMO, important for NF-kappa B activation. PIDDosome activation is dependent on auto-processing of PIDD at two different sites, generating the fragments PIDD-C and PIDD-CC. Despite constitutive cleavage, endogenous PIDD remains inactive. In this study, we screened for novel PIDD regulators and identified heat shock protein 90 (Hsp90) as a major effector in both PIDD protein maturation and activation. Hsp90, together with p23, binds PIDD and inhibition of Hsp90 activity with geldanamycin efficiently disrupts this association and impairs PIDD auto-processing. Consequently, both PIDD-mediated NF-kappa B and caspase-2 activation are abrogated. Interestingly, PIDDosome formation itself is associated with Hsp90 release. Characterisation of cytoplasmic and nuclear pools of PIDD showed that active PIDD accumulates in the nucleus and that only cytoplasmic PIDD is bound to Hsp90. Finally, heat shock induces Hsp90 release from PIDD and PIDD nuclear translocation. Thus, Hsp90 has a major role in controlling PIDD functional activity.".
- aggregation authorList BK693968.
- aggregation endPage "515".
- aggregation issue "3".
- aggregation startPage "506".
- aggregation volume "18".
- aggregation aggregates 3146947.
- aggregation isDescribedBy 1202569.
- aggregation similarTo cdd.2010.124.
- aggregation similarTo LU-1202569.