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dc.contributor.advisorHartson, Steven D.
dc.contributor.authorJia, Letong
dc.date.accessioned2014-04-15T20:25:33Z
dc.date.available2014-04-15T20:25:33Z
dc.date.issued2006-05-01
dc.identifier.urihttps://hdl.handle.net/11244/8918
dc.description.abstractThe purpose of this study was to confirm identify of Armadillo Repeat Chaperone Binding Protein 2 (ARCBP2) and interaction with ARCBP2 and Hsp90; to characterize 15-lipoxygenase-1 (15-LOX-1) interaction with Hsp90. Pull-down assays, Western blotting and Mass spectrum fingerprinting assay determined the association between Hsp90 and proteins. The mechanism of inhibition of Hsp90 by drug geldanamycin and molybdate in vitro was studied using coupled transcription/translation in nuclease reticulocyte lysate, and was analyzed using pull-down assays, Western blotting and autoradiography. Hsp90-dependent signaling pathway were examined in K562 cell using transfection by treating with drug geldanamycin, followed by immunoadsorption and Western blotting.
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dc.languageen_US
dc.publisherOklahoma State University
dc.rightsCopyright is held by the author who has granted the Oklahoma State University Library the non-exclusive right to share this material in its institutional repository. Contact Digital Library Services at lib-dls@okstate.edu or 405-744-9161 for the permission policy on the use, reproduction or distribution of this material.
dc.titleHsp90 Interactome
dc.typetext
dc.contributor.committeeMemberMatts, Robert L.
dc.contributor.committeeMemberEssenberg, Richard C.
osu.filenameJia_okstate_0664M_1725.pdf
osu.collegeAgricultural Sciences and Natural Resources
osu.accesstypeOpen Access
dc.description.departmentDepartment of Biochemistry and Molecular Biology
dc.type.genreThesis


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