Cited by 275Biochemical and Molecular ResearchGout, Hyperuricemia, Uric AcidEnzyme Structure and Function

The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.

Proteolytic conversion of xanthine dehydrogenase from the NAD-dependent type to the O2-dependent type. Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin.

Open access

Amaya, Y., Yamazaki, K., Sato, M., Noda, K., Nishino, T., Nishino, T.·1990·Journal of Biological Chemistry

Open this paper in CoChat — free account

Abstract

The primary structure of rat liver xanthine dehydrogenase (EC 1.1.1.204) was determined by sequence analysis of cDNA and purified enzyme. The enzyme consists of 1,319 amino acid residues with a calculated molecular mass of 145,034 Da, including initiation methionine, and is homologous to the previously reported Drosophila melanogaster enzyme (Lee, C. S., Curtis, D., McCarron, M., Love, C., Gray, M., Bender, W., and Chovnick, A. (1987) Genetics 116, 55-66; Keith, T. P., Riley, M. A., Kreitman, M., Lewontin, R. C., Curtis, D., and Chambers, G. (1987) Genetics 116, 67-73) with an identity of 52%. The enzyme exists originally as the NAD-dependent type in a freshly prepared sample. When the purified NAD-dependent type enzyme was digested with trypsin, it cleaved into three fragments with molecular masses of 20, 40, and 85 kDa and was irreversibly converted to the O2-dependent type. Comparison of the amino-terminal sequences of the three peptide fragments with the cDNA-deduced sequence reveals that the 20-, 40-, and 85-kDa peptide fragments correspond residues to 1-184, 185-539, and 540-1319 of the enzyme, respectively. Comparison of the 5'-p-fluorosulfonylbenzoyladenosine-labeled peptide sequence of the chicken enzyme (Nishino, T., and Nishino, T. (1989) J. Biol. Chem. 264, 5468-5473) reveals that the NAD binding site is associated with the 40-kDa fragment portion of the enzyme. Hydropathy analysis around the cysteine residues suggests that the 2Fe/2S sites are associated with the 20-kDa fragment portion of the enzyme.

Integrity signals

Registry

Crossref · 10.1016/s0021-9258(18)77283-9

Cites

41 of 41 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589
DNA sequencing with chain-terminating inhibitors
Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572
Molecular Cloning. A Laboratory Manual
Wood, E. (1983) · Biochemical Education · doi:10.1016/0307-4412(83)90068-7 · Cited by 29,534
A simple method for displaying the hydropathic character of a protein
Kyte, J., & Doolittle, R. F. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90515-0 · Cited by 22,927
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
Efficient isolation of genes by using antibody probes.
Young, R. A., & Davis, R. W. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.5.1194 · Cited by 2,036
Dideoxy sequencing method using denatured plasmid templates
Hattori, M., & Sakaki, Y. (1986) · Analytical Biochemistry · doi:10.1016/0003-2697(86)90403-3 · Cited by 1,469
Transcription termination and 3′ processing: the end is in site!
Birnstiel, M. L., Busslinger, M., & Strub, K. (1985) · Cell · doi:10.1016/s0092-8674(85)80007-6 · Cited by 1,388
Flavins and Flavoproteins
Geary, P. J. (1977) · Biochemical Society Transactions · doi:10.1042/bst0050567 · Cited by 804
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

Show all 41 references

Research works printed but not linked: 1

Saito, 1987, Yokohama Med. Bull., 38, 151

Sorted by citations

Items 201–275 of 275

Measurement of intracellular biomolecular oxidation in liver ischemia–reperfusion injury via immuno-spin trapping
Doğan, S., Elpek, G. Ö., Konuk, E., Demir, N., & Aslan, M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.05.028 · Cited by 15
Lung Injury and Oxidoreductases
Hoidal, J. R., Xu, P., Huecksteadt, T. P., Sanders, K. A., Pfeffer, K. D., & Sturrock, A. (1998) · Environmental Health Perspectives · doi:10.1289/ehp.98106s51235 · Cited by 17
XDH and XO Research and Drug Discovery—Personal History
Nishino, T. (2023) · Molecules · doi:10.3390/molecules28114440 · Cited by 15
Self-citation
Plasma Xanthine Oxidoreductase Activity Is Associated with a High Risk of Cardiovascular Disease in a General Japanese Population
Kotozaki, Y., Satoh, M., Tanno, K., Ohmomo, H., Otomo, R., Tanaka, F., Nasu, T., Taguchi, S., Kikuchi, H., Kobayashi, T., et al. (2021) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph18041894 · Cited by 14
Xanthine oxidase injurious response in acute joint injury
Stäbler, T., Zura, R., Hsueh, M.-F., & Kraus, V. B. (2015) · Clinica Chimica Acta · doi:10.1016/j.cca.2015.09.025 · Cited by 14
A Case of Hereditary Xanthinuria Type 1 Accompanied by Bilateral Renal Calculi
Fujiwara, Y., Kawakami, Y., Shinohara, Y., & Ichida, K. (2012) · Internal Medicine · doi:10.2169/internalmedicine.51.6891 · Cited by 14
Xanthine Oxidase in Biology and Medicine
Parks, D. A., Skinner, K. A., Tan, S., & Skinner, H. B. (2002) · Springer eBooks · doi:10.1007/0-306-46806-9_15 · Cited by 14
Novel aerobic 2‐aminobenzoate metabolism
Altenschmidt, U., Bokranz, M., & Fuchs, G. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17100.x · Cited by 14
Multiple organ dysfunction syndrome: Role of xanthine oxidase and nitric oxide
Parks, D. A., Skinner, K. A., Skinner, H. B., & Tan, S. (1998) · Pathophysiology · doi:10.1016/s0928-4680(98)00008-x · Cited by 13
Xanthine oxidoreductase-mediated injury is amplified by upregulated AMP deaminase in type 2 diabetic rat hearts under the condition of pressure overload
Igaki, Y., Tanno, M., Sato, T., Kouzu, H., Ogawa, T., Osanami, A., Yano, T., Kuno, A., Miki, T., Nakamura, T., et al. (2021) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2021.01.002 · Cited by 12
L ‐Arginine inhibits xanthine oxidase‐dependent endothelial dysfunction in hypercholesterolemia
White, C. R., Parks, D. A., Patel, R. P., Shelton, J. E., Tarpey, M. M., Freeman, B. Α., & Darley-Usmar, V. M. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00137-1 · Cited by 12
Xanthine oxidoreductase activity in marathon runners: potential implications for marathon-induced acute kidney injury
Kosaki, K., Kumamoto, S., Tokinoya, K., Yoshida, Y., Sugaya, T., Murase, T., Akari, S., Nakamura, T., Nabekura, Y., Takekoshi, K., et al. (2022) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00669.2021 · Cited by 11
The influence of albumin on the plasma xanthine oxidoreductase inhibitory activity of allopurinol, febuxostat and topiroxostat: Insight into extra-urate lowering effect
Nakamura, T., Murase, T., Satoh, E., Miyachi, A., Ogawa, N., Abe, K., Katoh, N., & Nakayama, Y. (2019) · Integrative Molecular Medicine · doi:10.15761/imm.1000368 · Cited by 11
Nitric Oxide in Influenza
Akaike, T., & Maeda, H. (2002) · Springer eBooks · doi:10.1007/0-306-46816-6_19 · Cited by 11
One- and Two-Electron-Mediated Reduction of Quinones: Enzymology and Toxicological Implications
Siegel, D. M., Reigan, P., & Ross, D. (2008) · Springer eBooks · doi:10.1007/978-0-387-77300-1_7 · Cited by 10
Adsorbed and spread films of bovine milk xanthine oxidase at the air–water interface
Kristensen, D., Nylander, T., Rasmussen, J. T., Paulsson, M. A., & Birdi, K. S. (1998) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/s0927-7757(98)00258-1 · Cited by 10
Isolation and Characterization of the Xanthine Dehydrogenase Gene of the Mediterranean Fruit Fly, Ceratitis capitata
Pitts, R. J., & Zwiebel, L. J. (2001) · Genetics · doi:10.1093/genetics/158.4.1645 · Cited by 10
Mass Spectrometric Analysis of Purine Intermediary Metabolism Indicates Cyanide Induces Purine Catabolism in Rabbits
Morningstar, J. E., Lee, J., Mahon, S. B., Brenner, M., & Nath, A. K. (2024) · Metabolites · doi:10.3390/metabo14050279 · Cited by 9
Mechanism of Transition from Xanthine Dehydrogenase to Xanthine Oxidase: Effect of Guanidine-HCL or Urea on the Activity
Tsujii, A., & Nishino, T. (2008) · Nucleosides Nucleotides & Nucleic Acids · doi:10.1080/15257770802146569 · Cited by 9
Self-citation
NADH oxidation and superoxide production by caprine milk xanthine oxidoreductase
Atmani, D., Baghiani, A., Harrison, R., & Benboubetra, M. (2005) · International Dairy Journal · doi:10.1016/j.idairyj.2004.11.004 · Cited by 9
N-Hydroxyguanidine Compound 1-(3,4-Dimethoxy- 2-chlorobenzylideneamino)-3-hydroxyguanidine Inhibits the Xanthine Oxidase Mediated Generation of Superoxide Radical
Dambrova, M., Baumane, L., Kiuru, A., Kalvinsh, I., & Wikberg, J. E. S. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1745 · Cited by 9
Assembly and Secretion of the Lipid Globules of Milk
Keenan, T. W. (2001) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-1371-1_16 · Cited by 8
Computational analysis of xanthine dehydrogenase enzyme from different source organisms
Dwivedi, V. D., Arora, S., Kumar, A., & Mishra, S. K. (2013) · Network Modeling Analysis in Health Informatics and Bioinformatics · doi:10.1007/s13721-013-0029-7 · Cited by 8
Localization of xanthine dehydrogenase mRNA in horse skeletal muscle by in situ hybridization with digoxigenin-labelled probe
Räsänen, L. A., Karvonen, U., & Pösö, A. R. (1993) · Biochemical Journal · doi:10.1042/bj2920639 · Cited by 8
Cardioprotective effects of N‐hydroxyguanidine PR5 in myocardial ischaemia and reperfusion in rats
Vēveris, M., Dambrova, M., Cirule, H., Meirena, D., Kalvinsh, I., & Wikberg, J. E. S. (1999) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0702887 · Cited by 8
Activation of xanthine oxidase by 1,4-naphthoquinones: A novel potential research topic for diet management and risk assessment
Liang, S., Liu, L., He, B., Zhao, W., Zhang, W., Xiao, L., Deng, M., Zhong, X., Zeng, S., Qi, X., et al. (2023) · Food Chemistry · doi:10.1016/j.foodchem.2023.136264 · Cited by 7
Studies on the induction and phosphorylation of xanthine dehydrogenase in cultured chick embryo hepatocytes
Schieber, A., & Edmondson, D. E. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18036.x · Cited by 7
Molecular Cloning of a cDNA Coding for Feline Liver Xanthine Dehydrogenase.
Tsuchida, S., Yamada, R., Ikemoto, S., & TAGAWA, M. (2001) · Journal of Veterinary Medical Science · doi:10.1292/jvms.63.353 · Cited by 7
Potential Opportunities for Pharmacogenetic-Based Therapeutic Exploitation of Xanthine Dehydrogenase in Cardiovascular Disease
Massimo, G., Dyson, N., Olotu, F. A., Khambata, R. S., & Ahluwalia, A. (2024) · Antioxidants · doi:10.3390/antiox13121439 · Cited by 7
Enhanced catalytic properties of novel (αbγ)2 heterohexameric Rhodobacter capsulatus xanthine dehydrogenase by separate expression of the redox domains in Escherichia coli
Wang, C., Li, G., Zhang, C., & Xing, X. (2016) · Biochemical Engineering Journal · doi:10.1016/j.bej.2016.12.009 · Cited by 6
Molecular cloning and characterisation of a novel xanthine oxidase from Cellulosimicrobium cellulans ATCC21606
Chen, Y., Li, Y., Chao, H., Wu, J., Zhu, W., Fang, T., Gao, X., & Yan, D. (2019) · Process Biochemistry · doi:10.1016/j.procbio.2019.11.033 · Cited by 6
Biochemistry of Molybdopterin Nitrate/Nitrite Reductases
Kelley, E. E. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-804273-1.00013-2 · Cited by 7
A Risky Job: In Search of Noncanonical Pathways
Skulachev, V. P. (2003) · Comprehensive biochemistry · doi:10.1016/s0069-8032(03)42011-1 · Cited by 5
Chemiluminescence imaging systems for the analysis of macrosamples: Microtiter format, blot membrane, and whole organs
Roda, A., Pasini, P., Musiani, M., & Baraldini, M. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)05482-3 · Cited by 6
Uric Acid Metabolism, Uric Acid Transporters and Dysuricemia
Ichida, K. (2024) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.23-00217 · Cited by 5
Established and Proposed Roles of Xanthine Oxidoreductase in Oxidative and Reductive Pathways in Plants
Urarte, E., Esteban, R., Morán, J. F., & Bittner, F. (2014) · Signaling and communication in plants · doi:10.1007/978-3-319-10079-1_2 · Cited by 6
Molecular and biochemical analysis of XDH from Phaseolus vulgaris suggest that uric acid protects the enzyme against the inhibitory effects of nitric oxide in nodules
Coleto, I., Pineda, M., & Alamillo, J. M. (2019) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2019.09.008 · Cited by 5
Association of Plasma Xanthine Oxidoreductase with Arterial Stiffness in Type 2 Diabetes with Liver Dysfunction
Ohira, M., Tanaka, S., Watanabe, Y., Nakamura, S., Oka, R., Yamaguchi, T., Ban, N., Saiki, A., Ishihara, N., Murano, T., et al. (2021) · The American Journal of the Medical Sciences · doi:10.1016/j.amjms.2021.09.011 · Cited by 5
Human xanthine dehydrogenase cDNA sequence and protein in an atypical case of type I xanthinuria in comparison with normal subjects
Yamamoto, T., Moriwaki, Y., Shibutani, Y., Matsui, K., Ueo, T., Takahashi, S., Tsutsumi, Z., & Hada, T. (2001) · Clinica Chimica Acta · doi:10.1016/s0009-8981(00)00413-7 · Cited by 5
Relationship between the BmXDH1 gene and the oq translucent-skin silkworm mutant
Kômoto, N., Yukuhiro, K., & Tamura, T. (1999) · Nihon sanshigaku zasshi · doi:10.11416/kontyushigen1930.68.357 · Cited by 5
Effect of interferon-γ on purine catabolic and salvage enzyme activities in rats
Moriwaki, Y., Yamamoto, T., Yamakita, J.-I., Takahashi, S., Tsutsumi, Z., & Higashino, K. (1999) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(99)00038-0 · Cited by 4
Molybdenum Cofactor in Humans
Belaidi, A. A., & Schwarz, G. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802168-2.00033-6 · Cited by 4
Xanthinuria Type 1 with a Novel Mutation in Xanthine Dehydrogenase and a Normal Endothelial Function
Miyazaki, S., Hamada, T., Sugihara, S., Mizuta, E., Endo, Y., Ohtahara, A., Komatsu, K., Kuwabara, M., Fukuuchi, T., Kaneko, K., et al. (2022) · Internal Medicine · doi:10.2169/internalmedicine.7897-21 · Cited by 4
Mononuclear Molybdenum-Containing Enzymes
Maia, L. B., & Moura, J. J. G. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.13932-0 · Cited by 4
Molybdenum Enzymes
Hille, R. (2000) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/0-306-46828-x_13 · Cited by 4
Anti-xanthine oxidase antibodies in sera and synovial fluid of patients with rheumatoid arthritis and other joint inflammations
Arrar, L., Hanachi, N., Rouba, K., Charef, N., Khennouf, S., & Baghiani, A. (2008) · Saudi Medical Journal · doi:10.15537/1658-3175.4351 · Cited by 3
Exercise and xanthine oxidase in the vasculature: superoxide and nitric oxide interactions
White, C. R., Shelton, J. E., Moellering, D. R., Jo, H., Patel, R. P., & Darley-Usmar, V. M. (2000) · Elsevier eBooks · doi:10.1016/b978-044482650-3/50003-1 · Cited by 3
Associations of circulating xanthine oxidoreductase activity with cardiometabolic risk markers in overweight and obese Japanese men: a cross-sectional pilot study
Kosaki, K., Yokota, A., Tanahashi, K., Myoenzono, K., Park, J., Yoshikawa, T., Yoshida, Y., Murase, T., Akari, S., Nakamura, T., et al. (2022) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.21-118 · Cited by 2
Biomarkers of Oxidative Stress in Neonatal Hypoxic-Ischemic Encephalopathy
Martini, S., Parladori, R., & Corvaglia, L. (2023) · Biomarkers in disease · doi:10.1007/978-3-031-07395-3_12 · Cited by 2
Der bakterielle Abbau von Chinolin und seinen Derivaten – Abbauwege und Biokatalysatoren
Fetzner, S., Tshisuaka, B., Lingens, F., Kappl, R., & Hüttermann, J. (1998) · Angewandte Chemie · doi:10.1002/(sici)1521-3757(19980302)110:5 · Cited by 2
Molybdenum and Tungsten
Tejada‐Jiménez, M., & Schwarz, G. (2014) · Royal Society of Chemistry eBooks · doi:10.1039/9781849739979-00223 · Cited by 2
Application of EPR and related methods to molybdenum-containing enzymes
Hille, R., & Niks, D. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.02.006 · Cited by 2
Expression and regulation of human xanthine oxidoreductase
Linder, N. (2005) · Työväentutkimus Vuosikirja · Cited by 2
Enzymes Associated with Milk Phospholipid Membrane Structures: Milk Fat Globule Membranes and Extracellular Vesicles
Hansen, M. S., & Rasmussen, J. T. (2021) · Food engineering series · doi:10.1007/978-3-030-55482-8_6 · Cited by 1
Density Functional Theory, Molecular-Docking Studies and Inhibition Effects of Pharmaceutical Active Ingredients on Xanthine Oxidase
Kaya, M. O., Dandan, E., Demirci, T., Özdemir, O., Kaya, Y., & Arslan, M. (2025) · Pharmaceutical Chemistry Journal · doi:10.1007/s11094-025-03320-4 · Cited by 1
Molybdenum‐Containing Hydroxylases
Zientek, M. A., Kang, P., Hutzler, J. M., & Obach, R. S. (2012) · Encyclopedia of Drug Metabolism and Interactions · doi:10.1002/9780470921920.edm011 · Cited by 1
SOD Enzymes in a Human Fungal Pathogen: Oxidative Stress Protection Versus Cellular Signaling
Broxton, C. N. (2017) · Cited by 1
Xanthine Oxidoreductase
Nishino, T., & PAI, E. F. (2011) · Wiley eBooks · doi:10.1002/9781119951438.eibc0634 · Cited by 1
Self-citation
Metals, Metalloids and Oxidative Stress
Ariza, M. E., Bijur, G. N., & Williams, M. V. (1999) · Springer eBooks · doi:10.1007/978-1-4615-5153-9_3
Biosíntesis, señalización y modo de acción del óxido nítrico en Arabidopsis thaliana
Lozano‐Juste, J. (2011) · RiuNet (Universitat Politècnica de València) · doi:10.4995/thesis/10251/11276
The Mechanism of Conversion of Xanthine Dehydrogenase to Xanthine Oxidase
Nishino, T., Okamoto, K., Nakanishi, S., Hori, H., & Nishino, T. (1998) · Springer eBooks · doi:10.1007/978-4-431-68476-3_42
Self-citation
This student paper was written as an assignment in the graduate course Free Radicals in Biology and Medicine
Buettner, G. R., Oberley, L. W., Spitz, D. R., & Domann, F. E. (2003)
Resposta à insulina no músculo esquelético de ratos tratados com apocinina.
Fujiwara, H. (2013) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.42.2013.tde-12062013-094713
Memories of a Senior Scientist Functions of mitochondria: from intracellular power stations to mediators of a senescence program
Skulachev, V. P. (2009)
Oxidative Stress and Cell Death in Osmotically Swollen Glial Cells
Stuckey, C. E. (2008) · Journal of Bioresource Management
Evaluation of Drug-Induced Liver Injury in an In Vitro Oxidative Stress Inflammation System
Maruf, A. A. (2014) · TSpace (University of Toronto)
Activation of bioreductive antitumour agents by DT-diaphorase
Bailey, S. M. (1995) · Enlighten: Theses (The University of Glasgow)
Oxidative Stress and Pulmonary Vascular Disorders
Groß, C., Aggarwal, S., Rafikov, R., & Black, S. M. (2014) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-1-4939-0679-6_27
Enzymes Indigenous to Milk: Xanthine Oxidoreductase
Zou, Z., Duley, J. A., Cowley, D. M., & Bansal, N. (2021) · Encyclopedia of Dairy Sciences · doi:10.1016/b978-0-12-818766-1.00258-0
Xanthine Oxidoreductase
Nishino, T., & PAI, E. F. (2004) · Wiley eBooks · doi:10.1002/0470028637.met207
Self-citation
Biomarkers of Oxidative Stress in Neonatal Hypoxic-Ischemic Encephalopathy
Martini, S., Parladori, R., & Corvaglia, L. (2022) · Biomarkers in disease · doi:10.1007/978-3-030-87302-8_12-1
Biomarcadores de estrés oxidante en la enfermedad renal crónica
Gallardo, J. M., Flores-Maldonado, C., González‐Márquez, H., Guerra‐Araiza, C., & Paniagua, R. (2021) · Revista Mexicana de Patología Clínica y Medicina de Laboratorio · doi:10.35366/105523
Drépanocytose et polymorphismes génétiques : épidémiologie, prédiction de gravité et stress-oxydant
Gueye, F. (2019) · theses.fr (ABES) · doi:10.70675/ba1cd2c2z7fe6z4d0dzb10fz91439ce84eb9
BindingDB Entry 50020020: Past, present and future of xanthine oxidase inhibitors: design strategies, structural and pharmacological insights, patents and clinical trials.
BindingDB (2024) · UC San Diego · doi:10.7270/q2cz3ck0
REGULATION OF THE HUMAN XANTHINE OXIDOREDUCTASE GENE
Martelin, E. (2004) · Työväentutkimus Vuosikirja

Authors: Amaya, Y., Yamazaki, K., Sato, M., Noda, K., Nishino, T., & Nishino, T.
Affiliations: Yokohama City University (JP)
ORCID: Amaya, Y.
Sato, M.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1990-08
Volume: 265
Issue: 24
Pages: 14170-14175
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(18)77283-9
OpenAlex: W1568002412
Cited by: 275
References: 41
Citations by year: 2025: 1 · 2024: 4 · 2023: 7 · 2022: 7 · 2021: 11 · 2020: 3 · 2019: 8 · 2018: 6 · 2017: 3 · 2016: 5 · 2015: 7 · 2014: 9 · 2013: 8 · 2012: 8
FWCI: 3.42
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 11102 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Health Sciences › Medicine › Nephrology › Gout, Hyperuricemia, Uric Acid
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: xanthine dehydrogenase, trypsin cleavage site, primary structure, rat liver enzyme, NAD+ binding site, [2Fe-2S] cluster, cysteine residues, hydropathy analysis
MeSH terms: Chlorophyta, Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, DNA, Drosophila, Ferredoxins, Ketone Oxidoreductases, Liver, Molecular Sequence Data, NAD, Oxygen, Protein Conformation, Sequence Homology, Nucleic Acid, Trypsin, Xanthine Dehydrogenase, Restriction Mapping, Gene Library, Rats

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Proteolytic conversion of xanthine dehydrogenase from the NAD-dependent type to the O2-dependent type. Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks