000008417 001__ 8417
000008417 005__ 20240329105917.0
000008417 0247_ $$2DOI$$a10.6083/ng451j316
000008417 037__ $$aIR
000008417 041__ $$aeng
000008417 245__ $$aCorrelative super-resolution fluorescence and electron microscopies unravel the nanocluster formation of ras proteins on the cell membrane
000008417 260__ $$bOregon Health and Science University
000008417 269__ $$a2020
000008417 336__ $$aAbstract
000008417 520__ $$aPhysical and functional partitioning of the biological membrane have been implicated in regulating heterotypic and homotypic interactions of proteins on the membrane. Among others, human Ras small GTPases are prototypical examples of membrane proteins that have been shown to preferentially compartmentalize on the plasma membrane.
000008417 540__ $$fCC BY
000008417 542__ $$fIn copyright - joint owners
000008417 650__ $$aras Proteins$$030965
000008417 650__ $$aCell Membrane$$016286
000008417 6531_ $$aSRM
000008417 6531_ $$aSEM
000008417 6531_ $$amembrane proteins
000008417 6531_ $$ananocluster
000008417 692__ $$aOHSU Center for Spatial Systems Biomedicine$$041486
000008417 7001_ $$aTao, Kai$$uOregon Health and Science University$$041354
000008417 7001_ $$aZhang, Ying$$uOregon Health and Science University$$041354
000008417 7001_ $$aWu, Lei$$uOregon Health and Science University$$041354
000008417 7001_ $$aLee, Yerirn$$uOregon Health and Science University$$041354
000008417 7001_ $$aChang, Young Hwan$$uOregon Health and Science University$$041354
000008417 7001_ $$aNan, Xiaolin$$uOregon Health and Science University$$041354
000008417 711__ $$aResearch Week$$uOregon Health and Science University$$d2020
000008417 8564_ $$9d3bc837e-9476-4d14-b02f-c6ce07cc9ca4$$s40842$$uhttps://digitalcollections.ohsu.edu/record/8417/files/ResearchWeek.2020.Tao.Kai.pdf
000008417 905__ $$a/rest/prod/ng/45/1j/31/ng451j316
000008417 980__ $$aResearch Week