Sharon Rozovsky, Ph.D. - Publications

Affiliations: 
2000 Columbia University, New York, NY 
Area:
NMR Structural Studies of Membrane Proteins, Enzymes, Hydrogen Bonding Geometry, and Dynamics

32 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2019 Liu J, Cai L, Sun W, Cheng R, Wang N, Jin L, Rozovsky S, Seiple I, Wang L. Photocaged Quinone Methide Cross-linkers for Light-controlled Chemical Cross-linking of Protein-protein and Protein-DNA Complexes. Angewandte Chemie (International Ed. in English). PMID 31644827 DOI: 10.1002/anie.201910135  1
2019 Liu J, Ekanayake O, Santoleri D, Walker K, Rozovsky S. Efficient generation of hydrazides in proteins by RadA split intein. Chembiochem : a European Journal of Chemical Biology. PMID 31265209 DOI: 10.1002/cbic.201900160  1
2019 Scinto SL, Ekanayake O, Seneviratne UI, Pigga JE, Brannick SJ, Taylor MT, Liu J, Am Ende CW, Rozovsky S, Fox JM. Dual-Reactivity trans-Cyclooctenol Probes for Sulfenylation in Live Cells Enable Temporal Control via Bioorthogonal Quenching. Journal of the American Chemical Society. PMID 31246462 DOI: 10.1021/jacs.9b01164  1
2019 Liu J, Li S, Aslam NA, Zheng F, Yang B, Cheng R, Wang N, Rozovsky S, Wang PG, Wang Q, Wang L. Genetically Encoding Photocaged Quinone Methide to Multitarget Protein Residues Covalently in Vivo. Journal of the American Chemical Society. PMID 31184146 DOI: 10.1021/jacs.9b01738  1
2018 Liu J, Cheng R, Wu H, Li S, Wang PG, DeGrado WF, Rozovsky S, Wang L. Building and Breaking Bonds via a Compact S-propargyl-cysteine to Chemically Control Enzymes and Modify Proteins. Angewandte Chemie (International Ed. in English). PMID 30118570 DOI: 10.1002/anie.201806197  1
2018 Liu J, Zheng F, Cheng R, Li S, Rozovsky S, Wang Q, Wang L. Site-Specific Incorporation of Selenocysteine Using an Expanded Genetic Code and Palladium-Mediated Chemical Deprotection. Journal of the American Chemical Society. PMID 29984990 DOI: 10.1021/jacs.8b04603  1
2018 Liu J, Cheng R, Rozovsky S. Synthesis and semisynthesis of selenopeptides and selenoproteins. Current Opinion in Chemical Biology. 46: 41-47. PMID 29723718 DOI: 10.1016/j.cbpa.2018.04.008  1
2018 Liu J, Chen Q, Rozovsky S. Selenocysteine-Mediated Expressed Protein Ligation of SELENOM. Methods in Molecular Biology (Clifton, N.J.). 1661: 265-283. PMID 28917051 DOI: 10.1007/978-1-4939-7258-6_19  1
2018 Zhang Z, Liu J, Rozovsky S. Preparation of Selenocysteine-Containing Forms of Human SELENOK and SELENOS. Methods in Molecular Biology (Clifton, N.J.). 1661: 241-263. PMID 28917050 DOI: 10.1007/978-1-4939-7258-6_18  1
2017 Wolfe AJ, Si W, Zhang Z, Blanden AR, Hsueh YC, Gugel JF, Pham B, Chen M, Loh SN, Rozovsky S, Aksimentiev A, Movileanu L. Quantification of Membrane Protein-Detergent Complex Interactions. The Journal of Physical Chemistry. B. PMID 29035562 DOI: 10.1021/acs.jpcb.7b08045  0.68
2017 Chen Q, Rozovsky S, Chen W. Engineering multi-functional bacterial outer membrane vesicles as modular nanodevices for biosensing and bioimaging. Chemical Communications (Cambridge, England). PMID 28636010 DOI: 10.1039/c7cc04246a  0.76
2017 Liu J, Chen Q, Rozovsky S. Utilizing Selenocysteine for Expressed Protein Ligation and Bioconjugations. Journal of the American Chemical Society. PMID 28186733 DOI: 10.1021/jacs.6b10991  1
2016 Gladyshev VN, Arnér ES, Berry MJ, Brigelius-Flohé R, Bruford EA, Burk RF, Carlson BA, Castellano S, Chavatte L, Conrad M, Copeland PR, Diamond AM, Driscoll DM, Ferreiro A, Flohé L, ... ... Rozovsky S, et al. Selenoprotein Gene Nomenclature. The Journal of Biological Chemistry. PMID 27645994 DOI: 10.1074/jbc.M116.756155  0.52
2016 Block E, Booker S, Flores-Penalba S, George G, Gundala S, Landgraf B, Liu J, Lodge S, Pushie J, Rozovsky S, Vattekkatte A, Yaghi R, Zeng H. Trifluoroselenomethionine - a New Non-Natural Amino Acid. Chembiochem : a European Journal of Chemical Biology. PMID 27383291 DOI: 10.1002/cbic.201600266  1
2015 Carpenter MR, Rozovsky S, Boyd EF. Pathogenicity island cross-talk mediated by recombination directionality factors (RDFs) facilitates excision from the chromosome. Journal of Bacteriology. PMID 26668266 DOI: 10.1128/JB.00704-15  1
2015 Liu J, Rozovsky S. Membrane-Bound Selenoproteins. Antioxidants & Redox Signaling. 23: 795-813. PMID 26168272 DOI: 10.1089/ars.2015.6388  1
2015 Struppe J, Zhang Y, Rozovsky S. (77)Se chemical shift tensor of L-selenocystine: experimental NMR measurements and quantum chemical investigations of structural effects. The Journal of Physical Chemistry. B. 119: 3643-50. PMID 25654666 DOI: 10.1021/jp510857s  0.52
2014 Li F, Liu J, Rozovsky S. Glutathione peroxidase's reaction intermediate selenenic acid is stabilized by the protein microenvironment. Free Radical Biology & Medicine. 76: 127-35. PMID 25124921 DOI: 10.1016/j.freeradbiomed.2014.07.041  1
2014 Liu J, Zhang Z, Rozovsky S. Selenoprotein K form an intermolecular diselenide bond with unusually high redox potential. Febs Letters. 588: 3311-21. PMID 25117454 DOI: 10.1016/j.febslet.2014.07.037  1
2014 Li F, Lutz PB, Pepelyayeva Y, Arnér ES, Bayse CA, Rozovsky S. Redox active motifs in selenoproteins. Proceedings of the National Academy of Sciences of the United States of America. 111: 6976-81. PMID 24769567 DOI: 10.1073/pnas.1319022111  1
2014 Schaefer-Ramadan S, Thorpe C, Rozovsky S. Site-specific insertion of selenium into the redox-active disulfide of the flavoprotein augmenter of liver regeneration. Archives of Biochemistry and Biophysics. 548: 60-5. PMID 24582598 DOI: 10.1016/j.abb.2014.02.001  1
2013 Liu J, Rozovsky S. Contribution of selenocysteine to the peroxidase activity of selenoprotein S. Biochemistry. 52: 5514-6. PMID 23914919 DOI: 10.1021/bi400741c  1
2013 Liu J, Li F, Rozovsky S. The intrinsically disordered membrane protein selenoprotein S is a reductase in vitro. Biochemistry. 52: 3051-61. PMID 23566202 DOI: 10.1021/bi4001358  1
2013 Schaefer SA, Dong M, Rubenstein RP, Wilkie WA, Bahnson BJ, Thorpe C, Rozovsky S. (77)Se enrichment of proteins expands the biological NMR toolbox. Journal of Molecular Biology. 425: 222-31. PMID 23159557 DOI: 10.1016/j.jmb.2012.11.011  1
2012 Liu J, Srinivasan P, Pham DN, Rozovsky S. Expression and purification of the membrane enzyme selenoprotein K. Protein Expression and Purification. 86: 27-34. PMID 22963794 DOI: 10.1016/j.pep.2012.08.014  1
2012 Rozovsky S, Forstner MB, Sondermann H, Groves JT. Single molecule kinetics of ENTH binding to lipid membranes. The Journal of Physical Chemistry. B. 116: 5122-31. PMID 22471245 DOI: 10.1021/jp210045r  1
2007 Rozovsky S, McDermott AE. Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase Proceedings of the National Academy of Sciences of the United States of America. 104: 2080-2085. PMID 17287353 DOI: 10.1073/pnas.0608876104  1
2005 Rozovsky S, Kaizuka Y, Groves JT. Formation and spatio-temporal evolution of periodic structures in lipid bilayers. Journal of the American Chemical Society. 127: 36-7. PMID 15631436 DOI: 10.1021/ja046300o  1
2003 Desamero R, Rozovsky S, Zhadin N, McDermott A, Callender R. Active site loop motion in triosephosphate isomerase: T-jump relaxation spectroscopy of thermal activation. Biochemistry. 42: 2941-51. PMID 12627960 DOI: 10.1021/bi026994i  1
2003 Jogl G, Rozovsky S, McDermott AE, 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 of the United States of America. 100: 50-55. PMID 12509510 DOI: 10.1073/pnas.0233793100  1
2001 Rozovsky S, Jogl G, Tong L, McDermott AE. Solution-state NMR investigations of triosephosphate isomerase active site loop motion: Ligand release in relation to active site loop dynamics Journal of Molecular Biology. 310: 271-280. PMID 11419952 DOI: 10.1006/jmbi.2001.4673  1
2001 Rozovsky S, McDermott AE. The time scale of the catalytic loop motion in triosephosphate isomerase Journal of Molecular Biology. 310: 259-270. PMID 11419951 DOI: 10.1006/jmbi.2001.4672  1
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