000008345 001__ 8345
000008345 005__ 20240415093542.0
000008345 0247_ $$2DOI$$a10.6083/qj72p7762
000008345 037__ $$aIR
000008345 041__ $$aeng
000008345 245__ $$aPIN1 provides dynamic control of MYC in response to extrinsic signals
000008345 260__ $$bOregon Health and Science University
000008345 269__ $$a2020
000008345 336__ $$aAbstract
000008345 520__ $$aPIN1 is a phosphorylation-directed member of the peptidyl-prolyl cis/trans isomerase family that facilitates conformational changes in phosphorylated targets such as c-MYC (MYC). Following signaling events that mediate phosphorylation of MYC at Serine 62, PIN1 establishes structurally distinct pools of MYC through its trans-cis and cis-trans isomerization activity at Proline 63. In my presentation, I will describe the molecular aspects of PIN1 target recognition and PIN1's function in the context of its temporal and spatial regulation of MYC.
000008345 540__ $$fCC BY
000008345 542__ $$fIn copyright - joint owners
000008345 650__ $$aNIMA-Interacting Peptidylprolyl Isomerase$$011992
000008345 650__ $$aIsomerism$$021071
000008345 6531_ $$acancer
000008345 6531_ $$aMYC
000008345 6531_ $$aneoplasms
000008345 691__ $$aSchool of Medicine$$041369
000008345 692__ $$aDepartment of Cell, Developmental and Cancer Biology$$041399
000008345 7001_ $$aCohn, Gabriel$$uOregon Health and Science University$$041354
000008345 7001_ $$aSears, Rosie$$uOregon Health and Science University$$041354
000008345 7001_ $$aLanger, Ellen$$uOregon Health and Science University$$041354
000008345 7001_ $$aLiefwalker, Daniel$$uOregon Health and Science University$$041354
000008345 711__ $$aResearch Week$$uOregon Health and Science University$$d2020
000008345 8564_ $$914e2f199-aab8-434a-91d5-ac8949cf666a$$s42103$$uhttps://digitalcollections.ohsu.edu/record/8345/files/ResearchWeek.2020.Cohn.Gabriel.pdf
000008345 905__ $$a/rest/prod/qj/72/p7/76/qj72p7762
000008345 980__ $$aResearch Week