An Extremely Potent Inhibitor of Xanthine Oxidoreductase

[20] Processing of X-ray diffraction data collected in oscillation mode

Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475 · see citing works

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,720 · see citing works

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,157 · see citing works

Improved methods for building protein models in electron density maps and the location of errors in these models

Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,650 · see citing works

Oxygen-Derived Free Radicals in Postischemic Tissue Injury

Epstein, F. H., & McCord, J. M. (1985) · New England Journal of Medicine · doi:10.1056/nejm198501173120305 · Cited by 5,399 · see citing works

[26] Raster3D: Photorealistic molecular graphics

Merritt, E. A., & Bacon, D. (1997) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(97)77028-9 · Cited by 3,749 · see citing works

Aromatic-Aromatic Interaction: A Mechanism of Protein Structure Stabilization

Burley, S. K., & Petsko, G. A. (1985) · Science · doi:10.1126/science.3892686 · Cited by 2,547 · see citing works

The mononuclear molybdenum enzymes

Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738 · see citing works

Harrison's Principles of Internal Medicine

Freeman, D. (2001) · JAMA · doi:10.1001/jama.286.8.971-a · Cited by 1,638 · see citing works

The Mononuclear Molybdenum Enzymes

Hille, R. (1996) · Chemical Reviews · doi:10.1021/cr950061t · Cited by 1,501 · see citing works

The Regulation of Rat Liver Xanthine Oxidase

Stirpe, F., Corte, E. D., & Lorenzoni, E. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36428-1 · Cited by 733 · see citing works

Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion

Enroth, C., Eger, B. T., Okamoto, K., Nishino, T., Nishino, T., & Pai, E. F. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.20.10723 · Cited by 733 · see citing works

Rapid automated molecular replacement by evolutionary search

Kissinger, C. R., Gehlhaar, D. K., & Fogel, D. B. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998012517 · Cited by 580 · see citing works

Tight-binding inhibitors—I

Cha, S. (1975) · Biochemical Pharmacology · doi:10.1016/0006-2952(75)90050-7 · Cited by 504 · see citing works

Xanthine oxidoreductase catalyses the reduction of nitrates and nitrite to nitric oxide under hypoxic conditions

Millar, T. M., Stevens, C. R., Benjamin, N., Eisenthal, R., Harrison, R., & Blake, D. R. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00430-x · Cited by 491 · see citing works

Xanthine oxidase and xanthine dehydrogenase

Hille, R., & Nishino, T. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.11.7649415 · Cited by 445 · see citing works

The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme

Corte, E. D., & Stirpe, F. (1972) · Biochemical Journal · doi:10.1042/bj1260739 · Cited by 437 · see citing works

Allopurinol and oxypurinol are hydroxyl radical scavengers

Moorhouse, P. C., Grootveld, M. C., Halliwell, B. B., Quinlan, J. G., & Gutteridge, J. M. C. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)81458-8 · Cited by 393 · see citing works

On the Mechanism of Inactivation of Xanthine Oxidase by Allopurinol and Other Pyrazolo[3,4-d]pyrimidines

Massey, V., Komai, H., Palmer, G., & Elion, G. B. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63065-0 · Cited by 380 · see citing works

Studies on Milk Xanthine Oxidase

Massey, V., Brumby, P. E., Komai, H., & Palmer, G. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91738-2 · Cited by 379 · see citing works

On the Mechanism of Inactivation of Xanthine Oxidase by Cyanide

Massey, V., & Edmondson, D. E. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62575-x · Cited by 368 · see citing works

Potentiation by inhibition of drug degradation : 6-substituted purines and xanthine oxidase

Elion, G. B., Sw, C., Nathan, H. C., et al. (1963) · Biochemical Pharmacology · doi:10.1016/0006-2952(63)90012-1 · Cited by 306 · see citing works

xdlMAPMANandxdlDATAMAN– Programs for Reformatting, Analysis and Manipulation of Biomacromolecular Electron-Density Maps and Reflection Data Sets

Kleywegt, G. J., & Jones, T. A. (1996) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444995014983 · Cited by 271 · see citing works

Xanthine oxidase activity associated with arterial blood pressure in spontaneously hypertensive rats

Suzuki, H., DeLano, F. A., Parks, D. A., Jamshidi, N., Granger, D. N., Ishii, H., Suematsu, M., Zweifach, B. W., & Schmid‐Schönbein, G. W. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.8.4754 · Cited by 262 · see citing works

XANTHINE OXIDASE: PURIFICATION AND PROPERTIES

Ball, E. G. (1939) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)73729-0 · Cited by 254 · see citing works

The Conversion of Xanthine Dehydrogenase to Xanthine Oxidase and the Role of the Enzyme in Reperfusion Injury1

Nishino, T. (1994) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a124480 · Cited by 212 · see citing works

Crystal Structures of the Active and Alloxanthine-Inhibited Forms of Xanthine Dehydrogenase from Rhodobacter capsulatus

Truglio, J. J., Theis, K. W., Leimkühler, S., Rappa, R., Rajagopalan, K. V., & Kisker, C. (2002) · Structure · doi:10.1016/s0969-2126(01)00697-9 · Cited by 204 · see citing works

NADH Oxidase Activity of Human Xanthine Oxidoreductase

Sanders, S. A., Eisenthal, R., & Harrison, R. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00541.x · Cited by 170 · see citing works

The Reaction of Xanthine Oxidase with Molecular Oxygen

Olson, J. S., Ballou, D. P., Palmer, G., & Massey, V. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42427-7 · Cited by 170 · see citing works

Hypouricemic effect of the novel xanthine oxidase inhibitor, TEI-6720, in rodents

Osada, Y., Tsuchimoto, M., Fukushima, H., Takahashi, K., Kondo, S., Hasegawa, M., & Komoriya, K. (1993) · European Journal of Pharmacology · doi:10.1016/0014-2999(93)90201-r · Cited by 163 · see citing works

Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): Structural analysis of the protein and chromosomal location of the gene

Ichida, K., Amaya, Y., Nöda, K., Shinsei, M., Hosoya, T., Sakai, O., Shimizu, N., & Takeshi, N. (1993) · Gene · doi:10.1016/0378-1119(93)90652-j · Cited by 144 · see citing works

3 Molybdenum Hydroxylases: Biological Distribution and Substrate-Inhibitor Specificity

Beedham, C. (1987) · Progress in medicinal chemistry · doi:10.1016/s0079-6468(08)70420-x · Cited by 129 · see citing works

The Reductive Half-reaction of Xanthine Oxidase

Xia, M., Dempski, R. E., & Hille, R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.6.3323 · Cited by 99 · see citing works

The Conversion from the Dehydrogenase Type to the Oxidase Type of Rat Liver Xanthine Dehydrogenase by Modification of Cysteine Residues with Fluorodinitrobenzene

Nishino, T., & Nishino, T. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.47.29859 · Cited by 93 · see citing works

Purification of highly active milk xanthine oxidase by affinity chromatography on sepharose 4B/folate gel

Nishino, T., Nishino, T., & Tsushima, K. (1981) · FEBS Letters · doi:10.1016/0014-5793(81)80406-1 · Cited by 93 · see citing works

Hypouricemic effect of allopurinol and the novel xanthine oxidase inhibitor TEI-6720 in chimpanzees

Komoriya, K., Osada, Y., Hasegawa, M., et al. (1993) · European Journal of Pharmacology · doi:10.1016/0014-2999(93)90033-e · Cited by 73 · see citing works

Purification of the Bovine Xanthine Oxidoreductase from Milk Fat Globule Membranes and Cloning of Complementary Deoxyribonucleic Acid

Berglund, L., Rasmussen, J. T., Andersen, M. D., Rasmussen, M. S., & Petersen, T. E. (1996) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(96)76351-8 · Cited by 71 · see citing works

Mechanism of Inhibition of Xanthine Oxidase with a New Tight Binding Inhibitor

Okamoto, K., & Nishino, T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.14.7816 · Cited by 69 · see citing works

The regulation of xanthine oxidase. Inhibition by reduced nicotinamide–adenine dinucleotide of rat liver xanthine oxidase type D and of chick liver xanthine dehydrogenase

Corte, E. D., & Stirpe, F. (1970) · Biochemical Journal · doi:10.1042/bj1170097 · Cited by 43 · see citing works

Purification, crystallization and preliminary X-ray diffraction studies of xanthine dehydrogenase and xanthine oxidase isolated from bovine milk

Eger, B. T., Okamoto, K., Enroth, C., Sato, M., Nishino, T., PAI, E. F., & Nishino, T. (2000) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444900012890 · Cited by 37 · see citing works

Xanthine Oxidase Inhibition Attenuates Kupffer Cell Production of Neutrophil Chemoattractant Following Ischemia–Reperfusion in Rat Liver

Matsumura, F., Yamaguchi, Y., Goto, M., Ichiguchi, O., Akizuki, E., Matsuda, T., Okabe, K., Liang, J., Ohshiro, H., Iwamoto, T., et al. (1998) · Hepatology · doi:10.1002/hep.510280618 · Cited by 36 · see citing works

The Existence of Nonfunctional Active Sites in Milk Xanthine Oxidase; Reaction with Functional Active Site Inhibitors

Massey, V., Komai, H., Palmer, G., et al. (1971) · Vitamins and hormones · doi:10.1016/s0083-6729(08)60909-7 · Cited by 36 · see citing works

The Molybdenum Centers of Xanthine Oxidase and Xanthine Dehydrogenase

Ryan, M. G., Ratnam, K., & Hille, R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.33.19209 · Cited by 27 · see citing works

Oxidation of 4-hydroxypyrazolo(3,4-d)pyrimidine by xanthine oxidase: The route of electron transfer from substrate to acceptor dyes

Spector, T., & Johns, D. G. (1968) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(68)90134-4 · Cited by 25 · see citing works

Inhibition of milk xanthine oxidase by fluorodinitrobenzene.

Nishino, T., Tsushima, K., Hille, R., & Massey, V. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34383-7 · Cited by 20 · see citing works

The mononuclear molybdenum enzymes

Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738 · see citing works

Febuxostat Compared with Allopurinol in Patients with Hyperuricemia and Gout

Becker, M. A., Schumacher, H. R., Wortmann, R. L., MacDonald, P. A., Eustace, D., Palo, W. A., Streit, J., & Joseph-Ridge, N. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa050373 · Cited by 1,357 · see citing works

Therapeutic Effects of Xanthine Oxidase Inhibitors: Renaissance Half a Century after the Discovery of Allopurinol

Pacher, P., Nivorozhkin, A., & Szabó, C. (2006) · Pharmacological Reviews · doi:10.1124/pr.58.1.6 · Cited by 1,218 · see citing works

Effects of febuxostat versus allopurinol and placebo in reducing serum urate in subjects with hyperuricemia and gout: A 28‐week, phase III, randomized, double‐blind, parallel‐group trial

Schumacher, H. R., Becker, M. A., Wortmann, R. L., MacDonald, P. A., Hunt, B., Streit, J., Lademacher, C., & Joseph‐Ridge, N. (2008) · Arthritis Care & Research · doi:10.1002/art.24209 · Cited by 638 · see citing works

Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation

Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works

How biology handles nitrite

Maia, L. B., & Moura, J. J. G. (2014) · Chemical Reviews · doi:10.1021/cr400518y · Cited by 401 · see citing works

The crystal structure of xanthine oxidoreductase during catalysis: Implications for reaction mechanism and enzyme inhibition

Okamoto, K., Matsumoto, K., Hille, R., Eger, B. T., Pai, E. F., & Nishino, T. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400973101 · Cited by 286 · see citing works

Febuxostat inhibition of endothelial-bound XO: Implications for targeting vascular ROS production

Malik, U. Z., Hundley, N. J., Romero, G., Radi, R., Freeman, B. A., Tarpey, M. M., & Kelley, E. E. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.004 · Cited by 126 · see citing works

Uric Acid Is a Biomarker of Oxidative Stress in the Failing Heart: Lessons Learned from Trials With Allopurinol and SGLT2 Inhibitors

Packer, M. (2020) · Journal of Cardiac Failure · doi:10.1016/j.cardfail.2020.08.015 · Cited by 95 · see citing works

Pharmacology and Clinical Drug Candidates in Redox Medicine

Dao, V. T.-V., Casas, A. I., Maghzal, G. J., Seredenina, T., Kaludercic, N., Robledinos-Anton, N., Di Lisa, F., Stocker, R., Ghezzi, P., Jaquet, V., et al. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2015.6430 · Cited by 88 · see citing works

Febuxostat, a novel xanthine oxidoreductase inhibitor, improves hypertension and endothelial dysfunction in spontaneously hypertensive rats

Shirakura, T., Nomura, J., Matsui, C., Kobayashi, T., Tamura, M., & Masuzaki, H. (2016) · Naunyn-Schmiedeberg's Archives of Pharmacology · doi:10.1007/s00210-016-1239-1 · Cited by 36 · see citing works

Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains

Wootton, J. C., Nicolson, R. E., Cock, J. M., Walters, D. E., Burke, J. F., Doyle, W. A., & Bray, R. C. (1991) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(05)80100-8 · Cited by 164 · see citing works

BIOCHEMICAL GENETICS OF PURINE CATABOLISM IN DROSOPHILA MELANOGASTER

Morita, T. (1964) · The Japanese Journal of Genetics · doi:10.1266/jjg.39.222 · Cited by 6 · see citing works

Correlations of tissue oxypurine levels with xanthine dehydrogenase changes in the chick

DeLapp, N. W., & Fisher, J. R. (1972) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(72)90138-4 · Cited by 10 · see citing works

Induction of chick liver xanthine dehydrogenase by purines

Woodward, W. D., Lee, P. C., DeLapp, N. W., et al. (1972) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(72)90372-4 · Cited by 16 · see citing works

Lower Xanthine Oxidoreductase Activity in Isolated Perfused Hearts if Xanthine Replaces Hypoxanthine as Substrate

Janssen, M., de Jong, J. W., Nieukoop, A. S., et al. (1991) · Advances in experimental medicine and biology · doi:10.1007/978-1-4899-2638-8_81 · Cited by 1 · see citing works