| Year |
Citation |
Score |
| 2022 |
Cook I, Leyh TS. The N-Terminus of Human Sulfotransferase 2B1b─a Sterol-Sensing Allosteric Site. Biochemistry. 61: 843-855. PMID 35523209 DOI: 10.1021/acs.biochem.1c00740 |
0.328 |
|
| 2019 |
Cook I, Asenjo AB, Sosa H, Leyh TS. The Human UGT2B7 Nanodisc. Drug Metabolism and Disposition: the Biological Fate of Chemicals. PMID 31892527 DOI: 10.1124/Dmd.119.089946 |
0.404 |
|
| 2018 |
Darrah K, Wang T, Cook I, Cacace M, Deiters A, Leyh TS. Allosteres to Regulate Neurotransmitter Sulfonation. The Journal of Biological Chemistry. PMID 30545938 DOI: 10.1074/Jbc.Ra118.006511 |
0.427 |
|
| 2018 |
Cook I, Wang T, Leyh TS. Isoform-Specific Therapeutic Control of Sulfonation in Humans. Biochemical Pharmacology. PMID 30423313 DOI: 10.1016/J.Bcp.2018.11.010 |
0.444 |
|
| 2017 |
Wang T, Cook I, Leyh TS. The NSAID allosteric site of human cytosolic sulfotransferases. The Journal of Biological Chemistry. PMID 29038294 DOI: 10.1074/Jbc.M117.817387 |
0.428 |
|
| 2017 |
Cook I, Wang T, Leyh TS. Tetrahydrobiopterin regulates monoamine neurotransmitter sulfonation. Proceedings of the National Academy of Sciences of the United States of America. PMID 28630292 DOI: 10.1073/Pnas.1704500114 |
0.407 |
|
| 2016 |
Cook I, Wang T, Girvin M, Leyh TS. The structure of the catechin-binding site of human sulfotransferase 1A1. Proceedings of the National Academy of Sciences of the United States of America. PMID 27911811 DOI: 10.1073/Pnas.1613913113 |
0.42 |
|
| 2016 |
Wang T, Cook I, Leyh TS. Isozyme Specific Allosteric Regulation of Human Sulfotransferase 1A1. Biochemistry. PMID 27356022 DOI: 10.1021/Acs.Biochem.6B00401 |
0.445 |
|
| 2016 |
Cook I, Wang T, Wang W, Kopp F, Wu P, Leyh TS. Controlling Sulfuryl-Transfer Biology. Cell Chemical Biology. 23: 579-586. PMID 27203377 DOI: 10.1016/J.Chembiol.2016.04.009 |
0.327 |
|
| 2015 |
Wang T, Cook I, Leyh T. The Design and Interpretation of Human SULT1A1 Assays. Drug Metabolism and Disposition: the Biological Fate of Chemicals. PMID 26658224 DOI: 10.1124/Dmd.115.068205 |
0.464 |
|
| 2015 |
Cook I, Wang T, Leyh TS. Sulfotransferase 1A1 Substrate Selectivity: A Molecular Clamp Mechanism. Biochemistry. 54: 6114-22. PMID 26340710 DOI: 10.1021/Acs.Biochem.5B00406 |
0.384 |
|
| 2015 |
Englander MT, Avins JL, Fleisher RC, Liu B, Effraim PR, Wang J, Schulten K, Leyh TS, Gonzalez RL, Cornish VW. The ribosome can discriminate the chirality of amino acids within its peptidyl-transferase center. Proceedings of the National Academy of Sciences of the United States of America. 112: 6038-43. PMID 25918365 DOI: 10.1073/Pnas.1424712112 |
0.314 |
|
| 2015 |
Cook I, Wang T, Falany CN, Leyh TS. The allosteric binding sites of sulfotransferase 1A1. Drug Metabolism and Disposition: the Biological Fate of Chemicals. 43: 418-23. PMID 25534770 DOI: 10.1124/Dmd.114.061887 |
0.463 |
|
| 2015 |
Kang S, Watanabe M, Jacobs JC, Yamaguchi M, Dahesh S, Nizet V, Leyh TS, Silverman RB. Synthesis of mevalonate- and fluorinated mevalonate prodrugs and their in vitro human plasma stability. European Journal of Medicinal Chemistry. 90: 448-61. PMID 25461893 DOI: 10.1016/J.Ejmech.2014.11.040 |
0.356 |
|
| 2014 |
Wang T, Cook I, Leyh TS. 3'-Phosphoadenosine 5'-phosphosulfate allosterically regulates sulfotransferase turnover. Biochemistry. 53: 6893-900. PMID 25314023 DOI: 10.1021/Bi501120P |
0.496 |
|
| 2014 |
Rodriguez SB, Leyh TS. An enzymatic platform for the synthesis of isoprenoid precursors. Plos One. 9: e105594. PMID 25153179 DOI: 10.1371/Journal.Pone.0105594 |
0.336 |
|
| 2014 |
Wang T, Cook I, Falany CN, Leyh TS. Paradigms of sulfotransferase catalysis: the mechanism of SULT2A1. The Journal of Biological Chemistry. 289: 26474-80. PMID 25056952 DOI: 10.1074/Jbc.M114.573501 |
0.385 |
|
| 2014 |
Tipton KF, Armstrong RN, Bakker BM, Bairoch A, Cornish-Bowden A, Halling PJ, Hofmeyr J, Leyh TS, Kettner C, Raushel FM, Rohwer J, Schomburg D, Steinbeck C. Standards for Reporting Enzyme Data: The STRENDA Consortium: What it aims to do and why it should be helpful Perspectives in Science. 1: 131-137. DOI: 10.1016/J.Pisc.2014.02.012 |
0.342 |
|
| 2013 |
Cook I, Wang T, Falany CN, Leyh TS. High accuracy in silico sulfotransferase models. The Journal of Biological Chemistry. 288: 34494-501. PMID 24129576 DOI: 10.1074/Jbc.M113.510974 |
0.38 |
|
| 2013 |
Leyh TS, Cook I, Wang T. Structure, dynamics and selectivity in the sulfotransferase family. Drug Metabolism Reviews. 45: 423-30. PMID 24025091 DOI: 10.3109/03602532.2013.835625 |
0.45 |
|
| 2013 |
Cook I, Wang T, Almo SC, Kim J, Falany CN, Leyh TS. Testing the sulfotransferase molecular pore hypothesis. The Journal of Biological Chemistry. 288: 8619-26. PMID 23362278 DOI: 10.1074/Jbc.M112.445015 |
0.426 |
|
| 2013 |
Cook I, Wang T, Almo SC, Kim J, Falany CN, Leyh TS. The gate that governs sulfotransferase selectivity. Biochemistry. 52: 415-24. PMID 23256751 DOI: 10.1021/Bi301492J |
0.459 |
|
| 2012 |
Cook I, Wang T, Falany CN, Leyh TS. A nucleotide-gated molecular pore selects sulfotransferase substrates. Biochemistry. 51: 5674-83. PMID 22703301 DOI: 10.1021/Bi300631G |
0.455 |
|
| 2012 |
Rohn KJ, Cook IT, Leyh TS, Kadlubar SA, Falany CN. Potent inhibition of human sulfotransferase 1A1 by 17α-ethinylestradiol: role of 3'-phosphoadenosine 5'-phosphosulfate binding and structural rearrangements in regulating inhibition and activity. Drug Metabolism and Disposition: the Biological Fate of Chemicals. 40: 1588-95. PMID 22593037 DOI: 10.1124/Dmd.112.045583 |
0.418 |
|
| 2012 |
Lefurgy ST, Leyh TS. Analytical expressions for the homotropic binding of ligand to protein dimers and trimers Analytical Biochemistry. 421: 433-438. PMID 22230282 DOI: 10.1016/J.Ab.2011.12.016 |
0.318 |
|
| 2012 |
Wang T, Leyh TS. Three-stage assembly of the cysteine synthase complex from Escherichia coli. The Journal of Biological Chemistry. 287: 4360-7. PMID 22179612 DOI: 10.1074/Jbc.M111.288423 |
0.406 |
|
| 2011 |
Reuther G, Harris R, Girvin M, Leyh TS. Backbone 1H, 13C, 15N NMR assignments of the unliganded and substrate ternary complex forms of mevalonate diphosphate decarboxylase from Streptococcus pneumoniae. Biomolecular Nmr Assignments. 5: 11-4. PMID 20737255 DOI: 10.1007/S12104-010-9255-4 |
0.443 |
|
| 2010 |
Cook IT, Leyh TS, Kadlubar SA, Falany CN. Lack of substrate inhibition in a monomeric form of human cytosolic SULT2A1. Hormone Molecular Biology and Clinical Investigation. 3: 367-74. PMID 25961208 DOI: 10.1515/HMBCI.2010.041 |
0.352 |
|
| 2010 |
Cook IT, Leyh TS, Kadlubar SA, Falany CN. Lack of substrate inhibition in a monomeric form of human cytosolic SULT2A1. Hormone Molecular Biology and Clinical Investigation. 3: 357-366. PMID 21822453 |
0.38 |
|
| 2010 |
Cook IT, Leyh TS, Kadlubar SA, Falany CN. Structural rearrangement of SULT2A1: effects on dehydroepiandrosterone and raloxifene sulfation. Hormone Molecular Biology and Clinical Investigation. 1: 81-87. PMID 21822452 DOI: 10.1515/Hmbci.2010.012 |
0.45 |
|
| 2010 |
Bauler P, Huber G, Leyh T, McCammon JA. Channeling by Proximity: The Catalytic Advantages of Active Site Colocalization Using Brownian Dynamics. The Journal of Physical Chemistry Letters. 1: 1332-1335. PMID 20454551 DOI: 10.1021/Jz1002007 |
0.328 |
|
| 2010 |
Sun M, Leyh TS. The human estrogen sulfotransferase: a half-site reactive enzyme. Biochemistry. 49: 4779-85. PMID 20429582 DOI: 10.1021/Bi902190R |
0.404 |
|
| 2010 |
Lefurgy ST, Rodriguez SB, Park CS, Cahill S, Silverman RB, Leyh TS. Probing ligand-binding pockets of the mevalonate pathway enzymes from Streptococcus pneumoniae. The Journal of Biological Chemistry. 285: 20654-63. PMID 20404339 DOI: 10.1074/Jbc.M109.098350 |
0.445 |
|
| 2010 |
Kudoh T, Park CS, Lefurgy ST, Sun M, Michels T, Leyh TS, Silverman RB. Mevalonate analogues as substrates of enzymes in the isoprenoid biosynthetic pathway of Streptococcus pneumoniae Bioorganic and Medicinal Chemistry. 18: 1124-1134. PMID 20056424 DOI: 10.1016/J.Bmc.2009.12.050 |
0.451 |
|
| 2009 |
Andreassi JL, Vetting MW, Bilder PW, Roderick SL, Leyh TS. Structure of the ternary complex of phosphomevalonate kinase: the enzyme and its family. Biochemistry. 48: 6461-8. PMID 19485344 DOI: 10.1021/Bi900537U |
0.415 |
|
| 2009 |
Drumm JE, Mi K, Bilder P, Sun M, Lim J, Bielefeldt-Ohmann H, Basaraba R, So M, Zhu G, Tufariello JM, Izzo AA, Orme IM, Almo SC, Leyh TS, Chan J. Mycobacterium tuberculosis universal stress protein Rv2623 regulates bacillary growth by ATP-Binding: requirement for establishing chronic persistent infection. Plos Pathogens. 5: e1000460. PMID 19478878 DOI: 10.1371/Journal.Ppat.1000460 |
0.37 |
|
| 2007 |
Andreassi JL, Bilder PW, Vetting MW, Roderick SL, Leyh TS. Crystal structure of the Streptococcus pneumoniae mevalonate kinase in complex with diphosphomevalonate. Protein Science : a Publication of the Protein Society. 16: 983-9. PMID 17400916 DOI: 10.1110/Ps.072755707 |
0.313 |
|
| 2006 |
Sun M, Leyh TS. Channeling in sulfate activating complexes. Biochemistry. 45: 11304-11. PMID 16981690 DOI: 10.1021/Bi060421E |
0.462 |
|
| 2006 |
Falany JL, Pilloff DE, Leyh TS, Falany CN. Sulfation of raloxifene and 4-hydroxytamoxifen by human cytosolic sulfotransferases. Drug Metabolism and Disposition: the Biological Fate of Chemicals. 34: 361-8. PMID 16381672 DOI: 10.1124/Dmd.105.006551 |
0.688 |
|
| 2005 |
Sun M, Leyh TS. Anatomy of an energy-coupling mechanism--the interlocking catalytic cycles of the ATP sulfurylase-GTPase system. Biochemistry. 44: 13941-8. PMID 16229483 DOI: 10.1021/Bi051303E |
0.444 |
|
| 2005 |
Sun M, Andreassi JL, Liu S, Pinto R, Triccas JA, Leyh TS. The trifunctional sulfate-activating complex (SAC) of Mycobacterium tuberculosis. The Journal of Biological Chemistry. 280: 7861-6. PMID 15615729 DOI: 10.1074/Jbc.M409613200 |
0.449 |
|
| 2004 |
Andreassi JL, Leyh TS. Molecular functions of conserved aspects of the GHMP kinase family. Biochemistry. 43: 14594-601. PMID 15544330 DOI: 10.1021/Bi048963O |
0.411 |
|
| 2004 |
Pinto R, Tang QX, Britton WJ, Leyh TS, Triccas JA. The Mycobacterium tuberculosis cysD and cysNC genes form a stress-induced operon that encodes a tri-functional sulfate-activating complex. Microbiology (Reading, England). 150: 1681-6. PMID 15184554 DOI: 10.1099/Mic.0.26894-0 |
0.389 |
|
| 2003 |
Lalor DJ, Schnyder T, Saridakis V, Pilloff DE, Dong A, Tang H, Leyh TS, Pai EF. Structural and functional analysis of a truncated form of Saccharomyces cerevisiae ATP sulfurylase: C-terminal domain essential for oligomer formation but not for activity. Protein Engineering. 16: 1071-9. PMID 14983089 DOI: 10.1093/protein/gzg133 |
0.712 |
|
| 2003 |
Pilloff DE, Leyh TS. Allosteric and catalytic functions of the PPi-binding motif in the ATP sulfurylase-GTPase system. The Journal of Biological Chemistry. 278: 50435-41. PMID 14506286 DOI: 10.1074/Jbc.M306897200 |
0.722 |
|
| 2003 |
Pilloff D, Dabovic K, Romanowski MJ, Bonanno JB, Doherty M, Burley SK, Leyh TS. The kinetic mechanism of phosphomevalonate kinase. The Journal of Biological Chemistry. 278: 4510-5. PMID 12424232 DOI: 10.1074/Jbc.M210551200 |
0.693 |
|
| 2002 |
Wei J, Tang QX, Varlamova O, Roche C, Lee R, Leyh TS. Cysteine biosynthetic enzymes are the pieces of a metabolic energy pump. Biochemistry. 41: 8493-8. PMID 12081500 DOI: 10.1021/Bi025953J |
0.412 |
|
| 2002 |
Sukal S, Leyh TS. Product release during the first turnover of the ATP sulfurylase-GTPase. Biochemistry. 40: 15009-16. PMID 11732922 DOI: 10.1021/Bi015735A |
0.386 |
|
| 2001 |
Cheng H, Sukal S, Deng H, Leyh TS, Callender R. Vibrational structure of GDP and GTP bound to RAS: an isotope-edited FTIR study. Biochemistry. 40: 4035-43. PMID 11300784 DOI: 10.1021/Bi0021131 |
0.303 |
|
| 2000 |
Wei J, Liu C, Leyh TS. The role of enzyme isomerization in the native catalytic cycle of the ATP sulfurylase-GTPase system. Biochemistry. 39: 4704-10. PMID 10769126 DOI: 10.1021/Bi992210Y |
0.451 |
|
| 1999 |
Wei J, Leyh TS. Isomerization couples chemistry in the ATP sulfurylase-GTPase system. Biochemistry. 38: 6311-6. PMID 10320361 DOI: 10.1021/Bi990216H |
0.506 |
|
| 1999 |
Wei J, Leyh TS. Conformational change rate-limits GTP hydrolysis: the mechanism of the ATP sulfurylase-GTPase. Biochemistry. 37: 17163-9. PMID 9860829 DOI: 10.1021/Bi9817461 |
0.439 |
|
| 1998 |
Zhang H, Varlamova O, Vargas FM, Falany CN, Leyh TS, Varmalova O. Sulfuryl transfer: the catalytic mechanism of human estrogen sulfotransferase. The Journal of Biological Chemistry. 273: 10888-92. PMID 9556564 DOI: 10.1074/Jbc.273.18.10888 |
0.426 |
|
| 1998 |
Edmonds BT, Bell A, Wyckoff J, Condeelis J, Leyh TS. The effect of F-actin on the binding and hydrolysis of guanine nucleotide by Dictyostelium elongation factor 1A Journal of Biological Chemistry. 273: 10288-10295. PMID 9553081 DOI: 10.1074/Jbc.273.17.10288 |
0.351 |
|
| 1998 |
Liu C, Wang R, Varlamova O, Leyh TS. Regulating energy transfer in the ATP sulfurylase-GTPase system. Biochemistry. 37: 3886-92. PMID 9521709 DOI: 10.1021/Bi971989D |
0.451 |
|
| 1997 |
Yang M, Leyh TS. Altering the reaction coordinate of the ATP sulfurylase-GTPase reaction. Biochemistry. 36: 3270-7. PMID 9116005 DOI: 10.1021/Bi962140K |
0.502 |
|
| 1995 |
Wang R, Liu C, Leyh TS. Allosteric regulation of the ATP sulfurylase associated GTPase. Biochemistry. 34: 490-5. PMID 7819241 DOI: 10.1021/Bi00002A013 |
0.481 |
|
| 1994 |
Leyh TS. The physical biochemistry and molecular genetics of sulfate activation. Critical Reviews in Biochemistry and Molecular Biology. 28: 515-42. PMID 8299360 DOI: 10.3109/10409239309085137 |
0.367 |
|
| 1994 |
Liu C, Martin E, Leyh TS. GTPase activation of ATP sulfurylase: the mechanism. Biochemistry. 33: 2042-7. PMID 8117661 DOI: 10.1021/Bi00174A009 |
0.462 |
|
| 1994 |
Liu C, Suo Y, Leyh TS. The energetic linkage of GTP hydrolysis and the synthesis of activated sulfate. Biochemistry. 33: 7309-14. PMID 8003495 DOI: 10.1021/Bi00189A036 |
0.481 |
|
| 1994 |
Schwedock JS, Liu C, Leyh TS, Long SR. Rhizobium meliloti NodP and NodQ form a multifunctional sulfate- activating complex requiring GTP for activity Journal of Bacteriology. 176: 7055-7064. PMID 7961471 DOI: 10.1128/Jb.176.22.7055-7064.1994 |
0.376 |
|
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