|136 Brown Lab||Newark, DE 19716||<div class="ExternalClass6C239B83017D40E0965AE4A2EE442557"><p style="text-align:justify;"><strong>B.S., 1994, Tel Aviv University; Ph.D., 2000, Columbia University</strong></p></div>||<div class="ExternalClassDEB8D3D8D4C244A5B7D08433E1C4E169"><p>My research focuses on enzymes that orchestrate a cell's response to oxidative stress that arises when cellular oxidants and antioxidants are not in balance. Such oxidative stress leads to impaired signaling as well as damage to cellular components. Within this broader context, my group studies the relationship between oxidative stress and the control of protein quality which for many proteins involves the ER-associated protein degradation (ERAD) pathway. This pathway governs the recognition and extraction of dysfunctional proteins from the ER’s membrane and lumen and is responsible for their transport to the cytoplasm for further degradation. Motivated by the ERAD pathway's crucial role in human health, we try to develop an understanding of its working principles on a molecular level. </p><p>Our lab currently focuses on the integral membrane proteins involved in recognition of degradation substrates as well as the proteins regulating this process. We have recently shown that, surprisingly, some of these undergo autoproteolysis, which seems to modulate both their association and enzymatic activity.</p><p>Closely related to our work on the ERAD is our work on trying to decipher the biological role of selenium in proteins that utilize the rare amino acid selenocysteine. My team studies individual members of this family of selenoproteins, with a focus on the structure and function of those that reside in membranes.</p><p>We also devise new approaches for preparation of selenoproteins by expressed chemical ligation and develop 77Se NMR spectroscopy methods to study the family of selenoproteins, thus significantly advancing our understanding of the unique biochemistry of selenium.</p><p>To learn more about our work, visit <a href="https://sites.udel.edu/rozovskyresearch/">https://sites.udel.edu/rozovskyresearch/</a></p><p>And Twitter: <a href="https://twitter.com/sharonrozovsky">@sharonrozovsky</a></p><p><br></p></div>||<div class="ExternalClass86EFB1A214674FC6AC504DA436C985D3"><p></p><ul><li>Samuel L. Scinto, Oshini
Ekanayake, Uthpala Seneviratne, Jessica Pigga, Samantha J. Boyd, Michael
T. Taylor, Jun Liu, Christopher W. am Ende, Sharon Rozovsky, Joe Fox.
Dual reactivity trans-Cyclooctenol probes for sulfenylation in live
cells enable temporal control via bioorthogonal quenching. JACS, 141,
28,10932-10937 (2019) <a href="https://doi.org/10.1021/jacs.9b01164">https://doi.org/10.1021/jacs.9b01164</a></li><li>Liu,
J., Chen, Q. & Rozovsky, S. (2017). Utilizing Selenocysteine for
Expressed Protein Ligation and Bioconjugation. Journal of the American
Chemical Society 139(9):3430-3437. <a href="http://dx.doi.org/10.1021/jacs.6b10991">http://dx.doi.org/10.1021/jacs.6b10991</a></li><li>Jun Liu and Sharon Rozovsky. Membrane-bound selenoproteins. Antioxidant and Redox Signaling 23 (10), 795-813 (2015) <a href="http://online.liebertpub.com/doi/abs/10.1089/ars.2015.6388">http://online.liebertpub.com/doi/abs/10.1089/ars.2015.6388</a></li><li>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) <a href="http://dx.doi.org/10.1073/pnas.1319022111">http://dx.doi.org/10.1073/pnas.1319022111</a></li></ul><p></p></div>||Current Research||Representative Publicationsfirstname.lastname@example.org||Rozovsky, Sharon ||(302) 831-7028||<img alt="" src="/Images%20Bios/Rozovsky2011headshot.png" width="640" style="BORDER:0px solid;" />||Associate Professor||https://sites.udel.edu/rozovskyresearch/|