| Year |
Citation |
Score |
| 2021 |
Forshaw TE, Reisz JA, Nelson KJ, Gumpena R, Lawson JR, Jönsson TJ, Wu H, Clodfelter JE, Johnson LC, Furdui CM, Lowther WT. Specificity of Human Sulfiredoxin for Reductant and Peroxiredoxin Oligomeric State. Antioxidants (Basel, Switzerland). 10. PMID 34208049 DOI: 10.3390/antiox10060946 |
0.316 |
|
| 2019 |
Buchalski B, Wood KD, Challa A, Fargue S, Holmes RP, Lowther WT, Knight J. The effects of the inactivation of Hydroxyproline dehydrogenase on urinary oxalate and glycolate excretion in mouse models of primary hyperoxaluria. Biochimica Et Biophysica Acta. Molecular Basis of Disease. 165633. PMID 31821850 DOI: 10.1016/J.Bbadis.2019.165633 |
0.402 |
|
| 2019 |
Randall LM, Rizza JD, Parsonage D, Santos J, Mehl RA, Lowther WT, Poole LB, Denicola A. Unraveling the effects of peroxiredoxin 2 nitration; role of C-terminal tyrosine 193. Free Radical Biology & Medicine. PMID 31323313 DOI: 10.1016/J.Freeradbiomed.2019.07.016 |
0.435 |
|
| 2019 |
Loberg MA, Hurtig JE, Graff AH, Allan KM, Buchan JA, Spencer MK, Kelly JE, Clodfelter JE, Morano KA, Lowther WT, West JD. Aromatic Residues at the Dimer-Dimer Interface in the Peroxiredoxin Tsa1 Facilitate Decamer Formation and Biological Function. Chemical Research in Toxicology. PMID 30701970 DOI: 10.1021/Acs.Chemrestox.8B00346 |
0.391 |
|
| 2018 |
Akter S, Fu L, Jung Y, Conte ML, Lawson JR, Lowther WT, Sun R, Liu K, Yang J, Carroll KS. Chemical proteomics reveals new targets of cysteine sulfinic acid reductase. Nature Chemical Biology. PMID 30177848 DOI: 10.1038/S41589-018-0116-2 |
0.359 |
|
| 2018 |
Bolduc JA, Nelson KJ, Haynes AC, Lee J, Reisz JA, Graff AH, Clodfelter JE, Parsonage D, Poole LB, Furdui CM, Lowther WT. Novel hyperoxidation resistance motifs in 2-Cys peroxiredoxins. The Journal of Biological Chemistry. PMID 29884768 DOI: 10.1074/Jbc.Ra117.001690 |
0.311 |
|
| 2018 |
Fargue S, Milliner DS, Knight J, Olson JB, Lowther WT, Holmes RP. Hydroxyproline Metabolism and Oxalate Synthesis in Primary Hyperoxaluria. Journal of the American Society of Nephrology : Jasn. PMID 29588429 DOI: 10.1681/Asn.2017040390 |
0.321 |
|
| 2017 |
Chen X, Wu H, Park CM, Poole TH, Keceli G, Devarie Baez NO, Tsang AW, Lowther WT, Poole LB, King SB, Xian M, Furdui CM. Discovery of Heteroaromatic Sulfones As A New Class of Biologically Compatible Thiol-Selective Reagents. Acs Chemical Biology. PMID 28687042 DOI: 10.1021/Acschembio.7B00444 |
0.31 |
|
| 2016 |
Hill TK, Davis AL, Wheeler FB, Kelkar SS, Freund EC, Lowther WT, Kridel SJ, Mohs AM. Development of a Self-Assembled Nanoparticle Formulation of Orlistat, Nano-ORL, with Increased Cytotoxicity against Human Tumor Cell Lines. Molecular Pharmaceutics. PMID 26824142 DOI: 10.1021/Acs.Molpharmaceut.5B00447 |
0.339 |
|
| 2015 |
Ritchie MK, Johnson LC, Clodfelter JE, Pemble CW, Fulp BE, Furdui CM, Kridel SJ, Lowther WT. Crystal Structure and Substrate Specificity of Human Thioesterase 2: Insights into the Molecular Basis for the Modulation of Fatty Acid Synthase. The Journal of Biological Chemistry. PMID 26663084 DOI: 10.1074/Jbc.M115.702597 |
0.741 |
|
| 2015 |
Poynton RA, Peskin AV, Haynes AC, Lowther WT, Hampton MB, Winterbourn C. Kinetic Analysis of Structural Influences on the Susceptibility of Peroxiredoxins 2 and 3 to Hyperoxidation. The Biochemical Journal. PMID 26614766 DOI: 10.1042/Bj20150572 |
0.428 |
|
| 2015 |
Cunniff B, Newick K, Nelson KJ, Wozniak AN, Beuschel S, Leavitt B, Bhave A, Butnor K, Koenig A, Chouchani ET, James AM, Haynes AC, Lowther WT, Murphy MP, Shukla A, et al. Disabling Mitochondrial Peroxide Metabolism via Combinatorial Targeting of Peroxiredoxin 3 as an Effective Therapeutic Approach for Malignant Mesothelioma. Plos One. 10: e0127310. PMID 26011724 DOI: 10.1371/Journal.Pone.0127310 |
0.337 |
|
| 2015 |
Summitt CB, Johnson LC, Jönsson TJ, Parsonage D, Holmes RP, Lowther WT. Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria. The Biochemical Journal. 466: 273-81. PMID 25697095 DOI: 10.1042/Bj20141159 |
0.414 |
|
| 2013 |
Haynes AC, Qian J, Reisz JA, Furdui CM, Lowther WT. Molecular basis for the resistance of human mitochondrial 2-Cys peroxiredoxin 3 to hyperoxidation. The Journal of Biological Chemistry. 288: 29714-23. PMID 24003226 DOI: 10.1074/Jbc.M113.473470 |
0.377 |
|
| 2013 |
Chen H, Gu Z, Zhang H, Wang M, Chen W, Lowther WT, Chen YQ. Expression and purification of integral membrane fatty acid desaturases. Plos One. 8: e58139. PMID 23520490 DOI: 10.1371/Journal.Pone.0058139 |
0.304 |
|
| 2012 |
Riedel TJ, Knight J, Murray MS, Milliner DS, Holmes RP, Lowther WT. 4-Hydroxy-2-oxoglutarate aldolase inactivity in primary hyperoxaluria type 3 and glyoxylate reductase inhibition. Biochimica Et Biophysica Acta. 1822: 1544-52. PMID 22771891 DOI: 10.1016/J.Bbadis.2012.06.014 |
0.7 |
|
| 2012 |
Lema Tomé CM, Palma E, Ferluga S, Lowther WT, Hantgan R, Wykosky J, Debinski W. Structural and functional characterization of monomeric EphrinA1 binding site to EphA2 receptor. The Journal of Biological Chemistry. 287: 14012-22. PMID 22362770 DOI: 10.1074/Jbc.M111.311670 |
0.325 |
|
| 2012 |
Jiang J, Johnson LC, Knight J, Callahan MF, Riedel TJ, Holmes RP, Lowther WT. Metabolism of [13C5]hydroxyproline in vitro and in vivo: implications for primary hyperoxaluria. American Journal of Physiology. Gastrointestinal and Liver Physiology. 302: G637-43. PMID 22207577 DOI: 10.1152/Ajpgi.00331.2011 |
0.682 |
|
| 2011 |
Riedel TJ, Johnson LC, Knight J, Hantgan RR, Holmes RP, Lowther WT. Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria. Plos One. 6: e26021. PMID 21998747 DOI: 10.1371/Journal.Pone.0026021 |
0.722 |
|
| 2011 |
Lowther WT, Haynes AC. Reduction of cysteine sulfinic acid in eukaryotic, typical 2-Cys peroxiredoxins by sulfiredoxin. Antioxidants & Redox Signaling. 15: 99-109. PMID 20712415 DOI: 10.1089/Ars.2010.3564 |
0.43 |
|
| 2010 |
Klomsiri C, Nelson KJ, Bechtold E, Soito L, Johnson LC, Lowther WT, Ryu SE, King SB, Furdui CM, Poole LB. Use of dimedone-based chemical probes for sulfenic acid detection evaluation of conditions affecting probe incorporation into redox-sensitive proteins. Methods in Enzymology. 473: 77-94. PMID 20513472 DOI: 10.1016/S0076-6879(10)73003-2 |
0.35 |
|
| 2010 |
Ritchie MK, Johnson LC, Watts LA, Kridel SJ, Lowther WT. Abstract 2675: Characterization of human thioesterase 2 and its potential for breast cancer drug discovery Cancer Research. 70: 2675-2675. DOI: 10.1158/1538-7445.Am10-2675 |
0.312 |
|
| 2010 |
SAWYER TK, STAPLES DJ, LIU L, TOMASSELLI AG, HUI JO, O'CONNELL K, SCHOSTAREZ H, HESTER JB, MOON J, HOWE WJ, SMITH CW, DECAMP DL, CRAIK C, DUNN BM, LOWTHER WT, et al. ChemInform Abstract: HIV Protease (HIV PR) Inhibitor Structure-Activity-Selectivity, and Active Site Molecular Modeling of High Affinity Leu(CH(OH)CH2)Val Modified Viral and Nonviral Substrate Analogs. Cheminform. 24: no-no. DOI: 10.1002/chin.199307301 |
0.462 |
|
| 2009 |
Jönsson TJ, Johnson LC, Lowther WT. Protein engineering of the quaternary sulfiredoxin.peroxiredoxin enzyme.substrate complex reveals the molecular basis for cysteine sulfinic acid phosphorylation. The Journal of Biological Chemistry. 284: 33305-10. PMID 19812042 DOI: 10.1074/Jbc.M109.036400 |
0.439 |
|
| 2009 |
Cox AG, Pearson AG, Pullar JM, Jönsson TJ, Lowther WT, Winterbourn CC, Hampton MB. Mitochondrial peroxiredoxin 3 is more resilient to hyperoxidation than cytoplasmic peroxiredoxins. The Biochemical Journal. 421: 51-8. PMID 19356151 DOI: 10.1042/Bj20090242 |
0.305 |
|
| 2008 |
Jönsson TJ, Tsang AW, Lowther WT, Furdui CM. Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin. The Journal of Biological Chemistry. 283: 22890-4. PMID 18593714 DOI: 10.1074/Jbc.C800124200 |
0.36 |
|
| 2008 |
Murray MS, Holmes RP, Lowther WT. Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design. Biochemistry. 47: 2439-49. PMID 18215067 DOI: 10.1021/Bi701710R |
0.306 |
|
| 2008 |
Jönsson TJ, Johnson LC, Lowther WT. Structure of the sulphiredoxin-peroxiredoxin complex reveals an essential repair embrace. Nature. 451: 98-101. PMID 18172504 DOI: 10.1038/Nature06415 |
0.424 |
|
| 2007 |
Jönsson TJ, Lowther WT. The peroxiredoxin repair proteins. Sub-Cellular Biochemistry. 44: 115-41. PMID 18084892 DOI: 10.1007/978-1-4020-6051-9_6 |
0.412 |
|
| 2007 |
Kridel SJ, Lowther WT, Pemble CW. Fatty acid synthase inhibitors: new directions for oncology. Expert Opinion On Investigational Drugs. 16: 1817-29. PMID 17970640 DOI: 10.1517/13543784.16.11.1817 |
0.725 |
|
| 2007 |
Pemble CW, Johnson LC, Kridel SJ, Lowther WT. Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat. Nature Structural & Molecular Biology. 14: 704-9. PMID 17618296 DOI: 10.1038/Nsmb1265 |
0.742 |
|
| 2007 |
Lin Z, Johnson LC, Weissbach H, Brot N, Lively MO, Lowther WT. Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function Proceedings of the National Academy of Sciences of the United States of America. 104: 9597-9602. PMID 17535911 DOI: 10.1073/Pnas.0703774104 |
0.409 |
|
| 2005 |
Jönsson TJ, Murray MS, Johnson LC, Poole LB, Lowther WT. Structural basis for the retroreduction of inactivated peroxiredoxins by human sulfiredoxin. Biochemistry. 44: 8634-42. PMID 15952770 DOI: 10.1021/bi050131i |
0.309 |
|
| 2003 |
Copik AJ, Swierczek SI, Lowther WT, D'souza VM, Matthews BW, Holz RC. Kinetic and spectroscopic characterization of the H178A methionyl aminopeptidase from Escherichia coli. Biochemistry. 42: 6283-92. PMID 12755633 DOI: 10.1021/Bi027327S |
0.451 |
|
| 2002 |
Lowther WT, Matthews BW. Metalloaminopeptidases: common functional themes in disparate structural surroundings. Chemical Reviews. 102: 4581-608. PMID 12475202 DOI: 10.1021/Cr0101757 |
0.398 |
|
| 2002 |
Lowther WT, Weissbach H, Etienne F, Brot N, Matthews BW. The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB. Nature Structural Biology. 9: 348-52. PMID 11938352 DOI: 10.1038/Nsb783 |
0.549 |
|
| 2002 |
Weissbach H, Etienne F, Hoshi T, Heinemann SH, Lowther WT, Matthews B, St John G, Nathan C, Brot N. Peptide methionine sulfoxide reductase: structure, mechanism of action, and biological function. Archives of Biochemistry and Biophysics. 397: 172-8. PMID 11795868 DOI: 10.1006/Abbi.2001.2664 |
0.474 |
|
| 2000 |
Lowther WT, Brot N, Weissbach H, Matthews BW. Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme. Biochemistry. 39: 13307-12. PMID 11063566 DOI: 10.1021/Bi0020269 |
0.514 |
|
| 2000 |
Lowther WT, Brot N, Weissbach H, Honek JF, Matthews BW. Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase. Proceedings of the National Academy of Sciences of the United States of America. 97: 6463-8. PMID 10841552 DOI: 10.1073/Pnas.97.12.6463 |
0.539 |
|
| 2000 |
Lowther WT, Matthews BW. Structure and function of the methionine aminopeptidases. Biochimica Et Biophysica Acta. 1477: 157-67. PMID 10708856 DOI: 10.1016/S0167-4838(99)00271-X |
0.548 |
|
| 1999 |
Lowther WT, Zhang Y, Sampson PB, Honek JF, Matthews BW. Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues. Biochemistry. 38: 14810-9. PMID 10555963 DOI: 10.1021/Bi991711G |
0.472 |
|
| 1999 |
Lowther WT, Orville AM, Madden DT, Lim S, Rich DH, Matthews BW. Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis. Biochemistry. 38: 7678-88. PMID 10387007 DOI: 10.1021/Bi990684R |
0.511 |
|
| 1998 |
Lowther WT, McMillen DA, Orville AM, Matthews BW. The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase. Proceedings of the National Academy of Sciences of the United States of America. 95: 12153-7. PMID 9770455 DOI: 10.1073/pnas.95.21.12153 |
0.537 |
|
| 1998 |
Dunn BM, Oda K, Kay J, Rao-Naik C, Lowther WT, Beyer BM, Scarborough PE, Bukhtiyarova M. Comparison of the specificity of the aspartic proteinases towards internally consistent sets of oligopeptide substrates. Advances in Experimental Medicine and Biology. 436: 133-8. PMID 9561210 DOI: 10.1007/978-1-4615-5373-1_18 |
0.518 |
|
| 1995 |
Lowther WT, Dunn BM. Site-directed mutagenesis of rhizopuspepsin: an analysis of unique specificity. Advances in Experimental Medicine and Biology. 362: 555-8. PMID 8540371 DOI: 10.1007/978-1-4615-1871-6_72 |
0.47 |
|
| 1995 |
Dunn BM, Scarborough PE, Lowther WT, Rao-Naik C. Comparison of the active site specificity of the aspartic proteinases based on a systematic series of peptide substrates. Advances in Experimental Medicine and Biology. 362: 1-9. PMID 8540305 DOI: 10.1007/978-1-4615-1871-6_1 |
0.487 |
|
| 1995 |
Lowther WT, Majer P, Dunn BM. Engineering the substrate specificity of rhizopuspepsin: the role of Asp 77 of fungal aspartic proteinases in facilitating the cleavage of oligopeptide substrates with lysine in P1. Protein Science : a Publication of the Protein Society. 4: 689-702. PMID 7613467 DOI: 10.1002/Pro.5560040409 |
0.584 |
|
| 1994 |
Lowther WT, Dunn BM. Kinetics of enzyme-catalyzed oligopeptide cleavage monitored by capillary zone electrophoresis: Comparison to spectrophotometric and HPLC methods Letters in Peptide Science. 1: 89-94. DOI: 10.1007/Bf00126278 |
0.506 |
|
| 1993 |
Lowther WT, DeWeerd W, Dunn BM. The role electrostatic interactions may play in the unique specificity of rhizopuspepsin Protein Engineering, Design and Selection. 6: 45. DOI: 10.1093/protein/6.Supplement.45-b |
0.41 |
|
| 1992 |
Cooper J, Quail W, Frazao C, Foundling SI, Blundell TL, Humblet C, Lunney EA, Lowther WT, Dunn BM. X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors. Biochemistry. 31: 8142-50. PMID 1525155 DOI: 10.1021/Bi00150A005 |
0.455 |
|
| 1992 |
Sawyer TK, Staples DJ, Liu L, Tomasselli AG, Hui JO, O'Connell K, Schostarez H, Hester JB, Moon J, Howe WJ, Smith CW, Decamp DL, Craik CS, Dunn BM, Lowther WT, et al. HIV protease (HIV PR) inhibitor structure-activity-selectivity, and active site molecular modeling of high affinity Leu [CH(OH)CH2]Val modified viral and nonviral substrate analogs International Journal of Peptide and Protein Research. 40: 274-281. PMID 1478785 DOI: 10.1111/J.1399-3011.1992.Tb00302.X |
0.47 |
|
| 1991 |
Lowther WT, Chen Z, Lin XL, Tang J, Dunn BM. Substrate specificity study of recombinant Rhizopus chinensis aspartic proteinase. Advances in Experimental Medicine and Biology. 306: 275-9. PMID 1812717 DOI: 10.1007/978-1-4684-6012-4_33 |
0.485 |
|
| 1991 |
Rao C, Scarborough PE, Lowther WT, Kay J, Batley B, Rapundalo S, Klutchko S, Taylor MD, Dunn BM. Structure-function database for active site binding to the aspartic proteinases. Advances in Experimental Medicine and Biology. 306: 143-7. PMID 1812702 DOI: 10.1007/978-1-4684-6012-4_19 |
0.536 |
|
| Show low-probability matches. |