000042299 001__ 42299
000042299 005__ 20240124114340.0
000042299 0247_ $$2doi$$a10.6083/bpxhc42299
000042299 037__ $$aETD
000042299 041__ $$aeng
000042299 245__ $$aLeveraging small molecule tools to study protein ADP-ribosylation
000042299 260__ $$bOregon Health and Science University
000042299 269__ $$a2023-10-31
000042299 336__ $$aDissertation
000042299 502__ $$bPh.D.
000042299 502__ $$gPhysiology & Pharmacology
000042299 520__ $$aPoly-(ADP)-ribose polymerases (PARPs) are a family 17 enzymes in humans that have diverse roles in cell biology including innate immune response, DNA repair, and regulation of signaling pathways. PARPs catalyze the transfer of ADP-ribose from nicotinamide adenine dinucleotide (NAD+) to target proteins or biomolecules. This enigmatic post- translational modification comes in two varieties: the transfer of a single unit of ADP-ribose, known as mono-ADP-ribosylation (MARylation) or the transfer of multiple units of ADP-ribose, known as poly-ADP-ribosylation (PARylation). The overarching goal of this work was to leverage chemical tools to further the field’s understanding of the biological roles and regulation of PARPs. The work can be divided into two distinct parts: 1) the development of tools for studying cellular mechanisms and 2) the application of small-molecule tools to uncover previously unknown relationships between writers and erasers of MARylation.
000042299 540__ $$fCC BY
000042299 542__ $$fIn copyright - single owner
000042299 650__ $$aPoly(ADP-ribose) Polymerases$$024351
000042299 650__ $$aADP Ribose Transferases$$034709
000042299 650__ $$aPhotoaffinity Labels$$031991
000042299 650__ $$aPoly(ADP-ribose) Polymerase Inhibitors$$011198
000042299 6531_ $$aparps
000042299 6531_ $$achemical tools
000042299 6531_ $$aadp-ribosylation
000042299 6531_ $$amarylation
000042299 6531_ $$aparg
000042299 691__ $$aSchool of Medicine$$041369
000042299 692__ $$aDepartment of Chemical Physiology and Biochemistry$$041400
000042299 7001_ $$aSanderson, Daniel J
000042299 7201_ $$aCohen, Michael$$uOregon Health and Science University$$041354$$ePI$$7Personal
000042299 8564_ $$9ef010554-9058-4de8-9af6-3f9656adc045$$s34982011$$uhttps://digitalcollections.ohsu.edu/record/42299/files/Sanderson.Daniel.2023.pdf
000042299 909CO $$ooai:digitalcollections.ohsu.edu:42299$$pstudent-work
000042299 980__ $$aTheses and Dissertations
000042299 981__ $$aPublished$$b2023-11-06