Publications

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Author Title [ Type(Desc)] Year
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Journal Article
Kim D.Y, Scalf M., Smith L.M, Vierstra R.D.  2013.  Advanced Proteomic Analyses Yield a Deep Catalog of Ubiquitylation Targets in Arabidopsis. Plant Cell. 25:1523-1540.
Russell J.D, Scalf M., Book A.J, Ladror D.T, Vierstra R.D, Smith L.M, Coon J.J.  2013.  Characterization and Quantification of Intact 26S Proteasome Proteins by Real-Time Measurement of Intrinsic Fluorescence Prior to Top-down Mass Spectrometry. Plos One. 8
Aguilar-Hernandez V., Kim D.Y, Stankey R.J, Scalf M., Smith L.M, Vierstra R.D.  2017.  Mass Spectrometric Analyses Reveal a Central Role for Ubiquitylation in Remodeling the Arabidopsis Proteome during Photomorphogenesis. Molecular Plant. 10:846-865.
Gemperline D.C, Scalf M., Smith L.M, Vierstra R.D.  2016.  Morpheus Spectral Counter: A computational tool for label-free quantitative mass spectrometry using the Morpheus search engine. Proteomics. 16:920-924.
Gemperline D.C, Marshall R.S, Lee K.H, Zhao Q.Z, Hu W.M, McLoughlin F., Scalf M., Smith L.M, Vierstra R.D.  2019.  Proteomic analysis of affinity-purified 26S proteasomes identifies a suite of assembly chaperones in Arabidopsis. Journal of Biological Chemistry. 294:17570-17592.
Miller M.J, Scalf M., Rytz T.C, Hubler S.L, Smith L.M, Vierstra R.D.  2013.  Quantitative Proteomics Reveals Factors Regulating RNA Biology as Dynamic Targets of Stress-induced SUMOylation in Arabidopsis. Molecular & Cellular Proteomics. 12:449-463.
Rytz T.C, Miller M.J, McLoughlin F., Augustine R.C, Marshall R.S, Juan Y.T, Charng Y.Y, Scalf M., Smith L.M, Vierstra R.D.  2018.  SUMOylome Profiling Reveals a Diverse Array of Nuclear Targets Modified by the SUMO Ligase SIZ1 during Heat Stress. Plant Cell. 30:1077-1099.
Saracco S.A, Hansson M., Scalf M., Walker J.M, Smith L.M, Vierstra R.D.  2009.  Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis. Plant Journal. 59:344-358.
Book A.J, Yang P.Z, Scalf M., Smith L.M, Vierstra R.D.  2005.  Tripeptidyl peptidase II. An oligomeric protease complex from Arabidopsis. Plant Physiology. 138:1046-1057.