Year |
Citation |
Score |
2024 |
Odunsi A, Kapitonova MA, Woodward G, Rahmani E, Ghelichkhani F, Liu J, Rozovsky S. Selenoprotein K at the intersection of cellular pathways. Archives of Biochemistry and Biophysics. 110221. PMID 39571956 DOI: 10.1016/j.abb.2024.110221 |
0.324 |
|
2022 |
Ghelichkhani F, Gonzalez FA, Kapitonova MA, Schaefer-Ramadan SA, Liu J, Cheng R, Rozovsky S. Selenoprotein S: A versatile disordered protein. Archives of Biochemistry and Biophysics. 109427. PMID 36241082 DOI: 10.1016/j.abb.2022.109427 |
0.333 |
|
2022 |
Quinn CM, Xu S, Hou G, Chen Q, Sail D, Andrew Byrd R, Rozovsky S. Se-C based dipolar correlation experiments to map selenium sites in microcrystalline proteins. Journal of Biomolecular Nmr. 76: 29-37. PMID 35320434 DOI: 10.1007/s10858-022-00390-4 |
0.605 |
|
2021 |
Cheng R, Liu J, Daithankar V, Rozovsky S. Applying selenocysteine-mediated expressed protein ligation to prepare the membrane enzyme selenoprotein S. Methods in Enzymology. 662: 159-185. PMID 35101209 DOI: 10.1016/bs.mie.2021.10.023 |
0.369 |
|
2021 |
Liu J, Cao L, Klauser PC, Cheng R, Berdan VY, Sun W, Wang N, Ghelichkhani F, Yu B, Rozovsky S, Wang L. A Genetically Encoded Fluorosulfonyloxybenzoyl-l-lysine for Expansive Covalent Bonding of Proteins via SuFEx Chemistry. Journal of the American Chemical Society. PMID 34213894 DOI: 10.1021/jacs.1c04259 |
0.386 |
|
2021 |
Cao L, Liu J, Ghelichkhani F, Rozovsky S, Wang L. Genetic Incorporation of ε-N-benzoyllysine by Engineering Methanomethylophilus alvus Pyrrolysyl-tRNA Synthetase. Chembiochem : a European Journal of Chemical Biology. PMID 34118176 DOI: 10.1002/cbic.202100218 |
0.398 |
|
2020 |
Liu J, Cheng R, Van Eps N, Wang N, Morizumi T, Ou WL, Klauser P, Rozovsky S, Ernst OP, Wang L. Genetically Encoded Quinone Methides Enabling Rapid, Site-specific, and Photo-controlled Protein Modification with Amine Reagents. Journal of the American Chemical Society. PMID 32915556 DOI: 10.1021/Jacs.0C06820 |
0.516 |
|
2020 |
Liu J, Ekanayake O, Santoleri D, Walker K, Rozovsky S. Cover Feature: Efficient Generation of Hydrazides in Proteins by RadA Split Intein (ChemBioChem 3/2020) Chembiochem. 21: 281-281. DOI: 10.1002/Cbic.202000013 |
0.375 |
|
2019 |
Chen Q, Xu SP, Lu X, Boeri MV, Pepelyayeva Y, Diaz EL, Soni SD, Allaire M, Forstner MB, Bahnson BJ, Rozovsky S. Se-NMR Probes the Protein Environment of Selenomethionine. The Journal of Physical Chemistry. B. PMID 31846581 DOI: 10.1021/Acs.Jpcb.9B07466 |
0.663 |
|
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 |
0.421 |
|
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 |
0.46 |
|
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 |
0.433 |
|
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 |
0.486 |
|
2019 |
Chen Q, Xu S, Lu X, Boeri MV, Pepelyayeva Y, Diaz EL, Soni S, Allaire M, Forstner MB, Bahnson BJ, Rozovsky S. 77Se NMR Probes the Protein Environmentof Selenomethionine Journal of Physical Chemistry B. DOI: 10.1021/Acs.Jpcb.9B07466.S001 |
0.66 |
|
2019 |
Rozovsky S. Selenium NMR Spectroscopy: A Versatile Probe for Biological Macromolecules Biophysical Journal. 116: 48a. DOI: 10.1016/J.Bpj.2018.11.303 |
0.321 |
|
2019 |
Xu S, Chen M, Boeri M, Rozovsky S. 77Se-NMR Probes the Protein Environment of Selenomethionine Biophysical Journal. 116. DOI: 10.1016/J.Bpj.2018.11.2566 |
0.412 |
|
2019 |
Cheng R, Grossi M, Liu J, Hoffmann PR, Rozovsky S. A Membrane-Bound Selenoprotein Regulates its Activity by Autoproteolysis Biophysical Journal. 116: 201a. DOI: 10.1016/J.Bpj.2018.11.1111 |
0.374 |
|
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 |
0.514 |
|
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 |
0.496 |
|
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 |
0.453 |
|
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 |
0.468 |
|
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 |
0.462 |
|
2017 |
Fredericks GJ, Hoffmann FW, Hondal RJ, Rozovsky S, Urschitz J, Hoffmann PR. Selenoprotein K Increases Efficiency of DHHC6 Catalyzed Protein Palmitoylation by Stabilizing the Acyl-DHHC6 Intermediate. Antioxidants (Basel, Switzerland). 7. PMID 29286308 DOI: 10.3390/Antiox7010004 |
0.429 |
|
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 |
0.462 |
|
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 |
0.354 |
|
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 |
0.46 |
|
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 |
0.396 |
|
2015 |
Li F, Liu J, Rozovsky S. Retraction notice to “Glutathione peroxidase’s reaction intermediate selenenic acid is stabilized by the protein microenvironment” [Free Radic. Biol. Med. 76 (2014) 127–135] Free Radical Biology and Medicine. 87: 385. PMID 26740980 DOI: 10.1016/J.Freeradbiomed.2015.07.014 |
0.385 |
|
2015 |
Liu J, Rozovsky S. Membrane-Bound Selenoproteins. Antioxidants & Redox Signaling. 23: 795-813. PMID 26168272 DOI: 10.1089/Ars.2015.6388 |
0.394 |
|
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 |
0.396 |
|
2015 |
Jun L, Zhang z, Rozovsky S. The Intrinsically Disordered Membrane Enzymes Selenoprotein S and Selenoprotein K Biophysical Journal. 108: 496. DOI: 10.1016/J.Bpj.2014.11.2715 |
0.451 |
|
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 |
0.436 |
|
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 |
0.447 |
|
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 |
0.357 |
|
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 |
0.337 |
|
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 |
0.372 |
|
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 |
0.454 |
|
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 |
0.422 |
|
2013 |
Aron Schaefer S, Dong M, Bahnson B, Thorpe C, Rozovsky S. Conversion of the Sulfhydryl Oxidase Augmenter of Liver Regeneration into a Selenoprotein Biophysical Journal. 104: 396a. DOI: 10.1016/J.Bpj.2012.11.2208 |
0.438 |
|
2013 |
Li F, Rozovsky S. 77Se NMR of Selenoproteins Biophysical Journal. 104: 180a. DOI: 10.1016/J.Bpj.2012.11.1014 |
0.409 |
|
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 |
0.495 |
|
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: 10.1017/S1431927613002754 |
0.689 |
|
2011 |
Li F, Rozovsky S. Selenium NMR Spectroscopy as Versatile Probe of Selenoproteins Biophysical Journal. 100: 193a. DOI: 10.1016/J.Bpj.2010.12.1273 |
0.382 |
|
2010 |
Huang HH, Pesavento JB, Rozovsky S, Downing KH, Groves JT. A Platform to Study Curvature Effects of Proteins on Membranes Biophysical Journal. 98: 669a. DOI: 10.1016/J.Bpj.2009.12.3674 |
0.565 |
|
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 |
0.563 |
|
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 |
0.683 |
|
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 |
0.591 |
|
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 |
0.554 |
|
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 |
0.586 |
|
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 |
0.571 |
|
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