Matches in Nanopublications for { <http://www.tkuhn.ch/bel2nanopub/RAaYDMQyCesJjNCBdHuTC4DBtexTc0aBdobWVBgY69XLo#_6> ?p ?o ?g. }
Showing items 1 to 2 of
2
with 100 items per page.
- _6 value "Hydroxylation at two prolyl residues (Pro402 and Pro564 in human HIF-1?) mediates interactions with the von Hippel-Lindau (VHL) E3 ubiquitin ligase complex that targets HIF-? for proteasomal destruction28, 29, 30, 34. Each site can interact independently with VHL E3, potentially contributing to the extremely rapid proteolysis of HIF-? that is observed in oxygenated cells34. These sites contain a conserved LxxLAP motif and are targeted by a newly defined prolyl hydroxylase activity, that in mammalian cells is provided by three isoforms termed PHD (prolyl hydroxylase domain) 1-3 (refs. 31,32)." provenance.
- _6 wasQuotedFrom 12778166 provenance.