000007482 001__ 7482
000007482 005__ 20231129124941.0
000007482 0247_ $$2DOI$$a10.6083/xw42n845p
000007482 037__ $$aETD
000007482 245__ $$aTowards selective poly-ADP-ribose polymerase inhibitors
000007482 260__ $$bOregon Health and Science University
000007482 269__ $$a2019
000007482 336__ $$aDissertation
000007482 502__ $$bPh.D.
000007482 520__ $$aPoly-ADP-ribose-polymerases (PARPs) are a family of 17 post translationally modifying enzymes in humans that catalyze the transfer of ADP-ribose from nicotinamide adenine dinucleotide (NAD+) onto target amino acids and nucleotides. PARPs can append long dendritic chains of ADP-ribose (poly-ADP-ribosylation, or PARylation) or monomers of ADP-ribose targets (mono-ADP ribosylation, or MARylation) to their). While the majority of the PARPs catalyze MARylation, there has been surprisingly little attention given to these enzymes or modification the last ten years. Even now, as evidence of the MARylating PARPs importance in basic biology and human diseases masses, very little is known about the function, targets, or biological mechanisms of these PARPs. Conversely, the PARylating PARPs are well understood.
000007482 542__ $$fIn copyright - single owner
000007482 650__ $$aDrug Design$$028208
000007482 650__ $$aDihydrouracil Dehydrogenase (NAD+)$$036521
000007482 650__ $$aPoly(ADP-ribose) Polymerase Inhibitors$$011198
000007482 6531_ $$apost-translational modification
000007482 6531_ $$aposttranslational protein processing
000007482 691__ $$aSchool of Medicine$$041369
000007482 692__ $$aDepartment of Physiology and Pharmacology$$041442
000007482 7001_ $$aKirby, Ilsa
000007482 8564_ $$93e5f0853-1f37-4ad1-9f55-c6b203ab1f32$$s31715409$$uhttps://digitalcollections.ohsu.edu/record/7482/files/ilsa.kirby.2019.pdf
000007482 905__ $$a/rest/prod/xw/42/n8/45/xw42n845p
000007482 909CO $$ooai:digitalcollections.ohsu.edu:7482$$pstudent-work
000007482 980__ $$aTheses and Dissertations