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Vidyadhar Daithankar, Markus Bröcker, Fei Li, Gulcin Unal Tosun, Dieter Soll and Sharon Rozovsky.  "An EF-Tu-Dependent Selenocysteine Insertion Approach to Studying Redox properties of Selenoproteins with a Minimal Thioredoxin Fold". Submitted (2014)

SelM

Jun Liu, Zhengqi Zhang and Sharon Rozovsky. Selenoprotein K can reduce phospholipid hydroperoxides. FEBS Lett. 2014  doi: 10.1016/j.febslet.2014.07.037.

SelK
Fei Li, Jun Liu and Sharon Rozovsky. Glutathione peroxidase's reaction intermediate selenenic acid is stabilized by the protein microenvironment. Free Radic Biol Med. 2014  doi: 10.1016/j.freeradbiomed.2014.07.041.

TCO

Fei Li, Patricia B. Lutz, Yuliya Pepelyayeva, Elias S.J. Arner, Craig A. Bayse and Sharon Rozovsky. Redox active motifs in selenoproteins.
Proceedings of the National Academy of Sciences 111 (19), 6976-6981 (2014). http://dx.doi.org/10.1073/pnas.1319022111

Stephanie Schaefer-Ramadan, Colin Thorpe and Sharon Rozovsky. Site-specific insertion of selenium into the redox-active disulfide of the flavoprotein Augmenter of Liver Regeneration.  Archives of Biochemistry and Biophysics 548, 60-65 (2014). http://dx.doi.org/10.1016/j.abb.2014.02.001

Jun Liu and Sharon Rozovsky. The contribution of selenocysteine to the peroxidase activity of selenoprotein S.  Biochemistry 52 (33), 5514–5516 (2013). http://dx.doi.org/10.1021/bi400741c

Sharon Rozovsky "77Se NMR Spectroscopy of Selenoproteins" Invited review "Biochalcogen Chemistry: The Biological Chemistry of Sulfur, Selenium, and Tellurium" edited by C.A. Bayse and J.L. Brumaghim, ACS press, chapter 6, 127-142 (2013). http://pubs.acs.org/isbn/9780841229037 also see  http://dx.doi.org/10.1021/bk-2013-1152

Jun Liu, Fei Li and Sharon Rozovsky. The intrinsically disordered membrane protein selenoprotein S is a reductase in vitro. Biochemistry 52 (18), 3051–3061 (2013). http://dx.doi.org/10.1021/bi4001358

This article was highlighted as a "Key Scientific Articles" in the Global Medical Discovery - a prominent research news website that highlights landmark papers in science and medicine. It was also highlighted on Biochemistry’s home page.
http://globalmedicaldiscovery.com/key-scientific-articles/the-intrinsically-disordered-membrane-protein-selenoprotein-s-is-a-reductase-in-vitro/

Stephanie A. Schaefer, Ming Dong, Renee P. Rubenstein, Wayne A. Wilkie, Brian J. Bahnson, Colin Thorpe and Sharon Rozovsky. 77Se Enrichment of Proteins Expands the Biological NMR Toolbox. Journal of Molecular Biology 425, 222-231 (2013). http://dx.doi.org/10.1016/j.jmb.2012.11.011

See a concise summary at http://thorpelab.chem.udel.edu/index.php/blog/114-expanding-the-biological-nmr-toolbox

Jun Liu, Prabha Srinivasan, Diane N. Pham and Sharon Rozovsky. Expression and purification of the membrane enzyme selenoprotein K. Protein Expression and Purification 86 (1), 27–34 (2012). http://dx.doi.org/10.1016/j.pep.2012.08.014

Rozovsky, S., Forstner, M.B., Sondermann, H. and Groves, J. T. Binding kinetics of Epsin N-terminal Homology (ENTH) to lipid bilayers measured by single molecule total internal reflection microscopy. Journal of Physical Chemistry 116 (17), 5122-5131 (2012). http://dx.doi.org/10.1021/jp210045r

Rozovsky, S. & McDermott, A. E. Substrate product equilibrium on a reversible enzyme: NMR detection for triosephosphate isomerase. Proceedings of the National Academy of Sciences 104 (7), 2080-2085 (2007). http://dx.doi.org/10.1073/pnas.0608876104

Rozovsky, S., Kaizuka, Y. & Groves, J. T. Formation and spatio-temporal evolution of periodic structures in lipid bilayers. Journal of the American Chemical Society 127 (1), 36-37 (2005). http://dx.doi.org/10.1021/ja046300o

Desamero, R, Rozovsky, S., Zhadin, N., McDermott, A. E. & Callender, R. Active site loop motion in triosephosphate isomerase: T-jump relaxation spectroscopy of thermal activation. Biochemistry 42 (10), 2941-2951 (2003). http://dx.doi.org/10.1021/bi026994i

Jogl, G., Rozovsky, S., McDermott, A. E. & Tong, L. Optimal alignment for enzymatic proton transfer: Structure of the Michaelis complex of triosephosphate isomerase at 1.2-Å resolution. Proceedings of the National Academy of Sciences 100, 50-55 (2003). http://dx.doi.org/10.1073/pnas.0233793100

Rozovsky, S., Jogl, G., Tong, L. & McDermott, A. E. Solution-state NMR investigations of triosephosphate isomerase active site motion: ligand release in relation to active site loop dynamics. Journal of Molecular Biology 310, 271-280 (2001). http://dx.doi.org/10.1006/jmbi.2001.4673

Rozovsky, S. & McDermott, A. E. The timescale of a catalytic loop motion in triosephosphate isomerase. Journal of Molecular Biology 310, 259-270 (2001). http://dx.doi.org/10.1006/jmbi.2001.4672