000002569 001__ 2569
000002569 005__ 20250521091514.0
000002569 0247_ $$2DOI$$a10.6083/M46Q1VHC
000002569 037__ $$aETD
000002569 245__ $$aRegulation of protein traffic in the TGN endosomal system by acidic cluster sorting motifs
000002569 269__ $$a2000
000002569 336__ $$aDissertation
000002569 502__ $$bPh.D.
000002569 502__ $$gCell & Developmental Biology (sunsetting)
000002569 520__ $$aMammalian proprotein convertases (PCs) are a group of endoproteases that process a variety of molecules, including growth factors, hormones, serum proteins, bacterial toxins, and viral envelope glycoproteins. Biochemical and cellular studies have provided valuable insights into the functions of these proteases. Although both PC6B and furin are expressed throughout the body and share nearly identical enzymatic characteristics, my research presented in this thesis demonstrates that these two proteases are concentrated in distinct subcellular compartments.
000002569 542__ $$fIn copyright - single owner
000002569 650__ $$aSerine Endopeptidases$$025887
000002569 650__ $$aGolgi Apparatus$$019689
000002569 650__ $$aMembrane Proteins$$022009
000002569 650__ $$aViral Envelope Proteins$$027831
000002569 650__ $$aEndosomes$$025226
000002569 691__ $$aSchool of Medicine$$041369
000002569 692__ $$aDepartment of Cell, Developmental and Cancer Biology$$041399
000002569 7001_ $$aXiang, Yang$$uOregon Health Sciences University$$041355
000002569 7201_ $$aChristian, Jan$$uOregon Health Sciences University$$041355$$7Personal$$eAdvisor
000002569 8564_ $$994480e84-2cce-432f-8f1c-2ddb427a6f59$$s21280737$$uhttps://digitalcollections.ohsu.edu/record/2569/files/3312_etd.pdf$$ePublic$$2499e2063cff02cd9066dd615c4767eeb$$31
000002569 905__ $$a/rest/prod/8p/58/pd/06/8p58pd06v
000002569 909CO $$ooai:digitalcollections.ohsu.edu:2569$$pstudent-work
000002569 980__ $$aTheses and Dissertations