The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
The effect of the inhibitor diphenylene iodonium on the superoxide-generating system of neutrophils. Specific labelling of a component polypeptide of the oxidase
Open accessAbstract
NADPH-dependent superoxide production by the solubilized oxidase of neutrophils was inhibited 36% by diphenylene iodonium at a 1:1 stoichiometry with the enzyme flavoprotein content. Addition of diphenylene iodonium strongly inhibited the NADPH-dependent reduction of both FAD and cytochrome b-245 in steady-state kinetic experiments. Incubation of solubilized enzyme with diphenylene [125I]iodonium resulted in the specific labelling of a polypeptide of Mr 45,000. In the presence of NADPH the amount of label incorporated into the polypeptide was reduced. There was no difference in labelling between enzyme prepared from stimulated or unstimulated cells.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
In the citing paper
“Diphenylene iodonium (DPI) (FIGURE 10) is a nonspecific inhibitor of all NOX isoforms (18, 197, 246).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [197]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,311
Oxygen-Dependent Microbial Killing by Phagocytes
BABIOR, B. M. (1978) · New England Journal of Medicine · doi:10.1056/nejm197803232981205 · Cited by 2,483
Oxidants from phagocytes: agents of defense and destruction
Babior, B. (1984) · Blood · doi:10.1182/blood.v64.5.959.959 · Cited by 804
Segal, A. W., Heyworth, P. G., Cockcroft, S., & Barrowman, M. M. (1985) · Nature · doi:10.1038/316547a0 · Cited by 281
Light, D. R., Walsh, C. T., O'Callaghan, A. M., Goetzl, E. J., & Tauber, A. I. (1981) · Biochemistry · doi:10.1021/bi00509a010 · Cited by 249
The enzymic reduction and kinetics of oxidation of cytochrome b.245 of neutrophils
Cross, A. R., Higson, F. K., Jones, O. T. G., Harper, A., & Segal, A. W. (1982) · Biochemical Journal · doi:10.1042/bj2040479 · Cited by 246
Self-citationCross, A. R., Jones, O. T., Harper, A., & Segal, A. W. (1981) · Biochemical Journal · doi:10.1042/bj1940599 · Cited by 229
Self-citationHafeman, D. G., & Lucas, Z. J. (1979) · The Journal of Immunology · doi:10.4049/jimmunol.123.1.55 · Cited by 142
Cross, A. R., Parkinson, J. F., & Jones, O. T. G. (1984) · Biochemical Journal · doi:10.1042/bj2230337 · Cited by 136
Self-citation
Flagged first, then by citations
Research works printed but not linked: 1
- Bloxham, D. P. (1979) Biochem. Soc. Trans. 7, 103-106
Cited by
Sorted by citations
Items 401–500 of 547
Halothane inhibits the pressor effect of diphenyleneiodonium
Wang, Y., & Pang, C. C. Y. (1993) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.1993.tb13747.x · Cited by 17
Luo, Y., Kokkonen, G. C., Hattori, A., Chrest, F. J., & Roth, G. S. (1999) · Brain Research · doi:10.1016/s0006-8993(99)02021-1 · Cited by 17
NADPH oxidase subunit gp91phox: A proton pathway
HENDERSON, L. M. (2001) · PROTOPLASMA · doi:10.1007/bf01289411 · Cited by 17
Spolarics, Z., Bautista, A. P., Jr., & Spitzer, J. J. (1993) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(93)90134-b · Cited by 17
Oxygen radical production by transformed B lymphocytes
Jones, O. T. G., Hancock, J. T., & HENDERSON, L. M. (1991) · Molecular Aspects of Medicine · doi:10.1016/0098-2997(91)90004-6 · Cited by 17
Self-citationGallop, P. M., Paz, M. A., Flückiger, R., & Henson, E. B. (1993) · Connective Tissue Research · doi:10.3109/03008209309014242 · Cited by 17
Swelling-induced O−2 generation in guinea-pig neutrophils
Miyahara, M., Watanabe, Y., Edashige, K., & Yagyu, K.-I. (1993) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(93)90158-l · Cited by 17
Studies on the NADPH oxidase of phagocytes
Berton, G., Dusi, S., Serra, M. C., Bellavite, P., & Rossi, F. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83583-9 · Cited by 17
Chen, X., Jin, S., Du, H., Liu, Z., Hou, C., Tang, L. Y., Wang, Y., Wang, Y., Yang, Z., Zhao, T., et al. (2025) · Nature Plants · doi:10.1038/s41477-025-02057-y · Cited by 16
Miller‐Pinsler, L., Sharma, A. M., & Wells, P. G. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1482-0 · Cited by 16
Gonzalez‐Dosal, R., Horan, K., & Paludan, S. R. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.01.108 · Cited by 16
Córdoba, M., Pintos, L. N., & Beconi, M. T. (2008) · Andrologia · doi:10.1111/j.1439-0272.2008.00871.x · Cited by 16
Lee, D. J., Choi, H. J., Moon, M., Chi, Y., Ji, K.-Y., & Choi, D. (2016) · Physiologia Plantarum · doi:10.1111/ppl.12487 · Cited by 16
Peng, X., Yang, Y., Luo, B., Wen, S., & Huang, P. (2020) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.202001080 · Cited by 16
Detection of urinary tract infections by reduction of nitroblue tetrazolium
Smith, S. D., Wheeler, M. A., & Weiss, R. M. (1998) · Kidney International · doi:10.1046/j.1523-1755.1998.00102.x · Cited by 15
Ma, Y., She, X., & Yang, S. (2012) · Canadian Journal of Plant Science · doi:10.4141/cjps2012-040 · Cited by 15
Kuan, Y., Lin, R., Tsao, L., Lin, C., & Wang, J.-P. (2005) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706205 · Cited by 15
Ma, Y., She, X., & Yang, S. (2012) · Science China Life Sciences · doi:10.1007/s11427-012-4386-8 · Cited by 15
Sharma, M., Sharma, K. B., Chauhan, S., Bhattacharyya, S., Vrati, S., & Kalia, M. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.05.149 · Cited by 15
Pintard, C., Khemis, M. B., Liu, D., Dang, P. M., Hurtado-Nédelec, M., & Benna, J. E. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.113950 · Cited by 14
Magnani, P., Doussière, J., & Lissolo, T. (2000) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00145-6 · Cited by 14
Aspects of the Release of Superoxide by Leukocytes, and a Means by Which This Is Switched off
Karnovsky, M. L., Bishop, A., Camerero, V. C. P. C., Paz, M. A., Colepicolo, P., Ribeiro, J. M. C., & Gallop, P. M. (1994) · Environmental Health Perspectives · doi:10.1289/ehp.94102s1043 · Cited by 14
Viačková, D., Pekarová, M., Crhák, T., Búcsaiová, M., Matiašovic, J., Lojek, A., & Kubala, L. (2010) · Immunobiology · doi:10.1016/j.imbio.2010.09.005 · Cited by 13
NADPH oxidase activity of cytochrome P-450 BM3 and its constituent reductase domain
Munro, A. W., LINDSAY, J. G., Coggins, J. R., Kelly, S. M., & Price, N. C. (1995) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(95)00083-u · Cited by 13
B Lymphoblasts show Oxidase Activity in Response to Cross‐Linking of Surface IgM and HLA‐DR
Furukawa, K., TENGLER, R., Nakamura, M., Urwyler, A., Weck, A., Kanegasaki, S., & Maly, F. E. (1992) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.1992.tb03255.x · Cited by 13
Björquist, P., Palmer, M., & Ek, B. A. (1994) · Biochemical Pharmacology · doi:10.1016/0006-2952(94)90595-9 · Cited by 13
Nakamura, Y., Tsuji, K., Shuto, M., Ogita, K., Yoneda, Y., Shimamoto, K., Shibata, T., & Kataoka, K. (1997) · Neuroscience · doi:10.1016/s0306-4522(96)00375-2 · Cited by 13
Interaction of respiratory burst and uptake of dehydroascorbic acid in differentiated HL-60 cells
Laggner, H., & Goldenberg, H. (2000) · Biochemical Journal · doi:10.1042/bj3450195 · Cited by 13
Biologically Active Thiophene Derivatives Revisited: 1983–1988
Press, J. B. (1991) · The chemistry of heterocyclic compounds/The Chemistry of heterocyclic compounds · doi:10.1002/9780470187265.ch3 · Cited by 13
Lambertucci, R. H., Silveira, L. R., Hirabara, S. M., Curi, R., Sweeney, G., & Pithon‐Curi, T. C. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22989 · Cited by 12
Wang, J.-P., Chang, L., Lin, Y., Hsu, M., Chang, C., Huang, L., & Kuo, S. (2003) · Biochemical Pharmacology · doi:10.1016/s0006-2952(03)00006-6 · Cited by 12
El-On, J., ZVILLICH, M., & SAROV, I. (1990) · Parasite Immunology · doi:10.1111/j.1365-3024.1990.tb00955.x · Cited by 12
Wen, Z., Fan, Y., Xia, Y., & Jin, K. (2022) · Journal of Fungi · doi:10.3390/jof8060587 · Cited by 11
Espada, L., Meo-Evoli, N., Sancho, P., Real, S., Fabregat, I., Ambrosio, S., & Tauler, A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051544 · Cited by 11
Wang, J.-P., Chang, L., Hsu, M., Chen, S., & Kuo, S. (2002) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-002-0631-1 · Cited by 11
He, Y., Chen, H., Qian, L.-H., He, L., & Buzby, J. S. (2012) · Brain Research · doi:10.1016/j.brainres.2012.11.017 · Cited by 12
Neutrophil intracellular pH and phagocytosis after thermal trauma
Sachse, C., Wolterink, G., & Pallua, N. (2000) · Clinica Chimica Acta · doi:10.1016/s0009-8981(00)00189-3 · Cited by 11
Ma, Y., & Niu, J. (2016) · South African Journal of Botany · doi:10.1016/j.sajb.2016.11.002 · Cited by 11
Xiao-ping, S., Huang, A., Li, J., & Han, X.-Z. (2010) · Physiologia Plantarum · doi:10.1111/j.1399-3054.2010.01400.x · Cited by 11
Functional Expression of NAD(P)H Oxidase p47 in Lung Microvascular Endothelial Cells
Murphy, H. S., Yu, C., & Quddus, J. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3848 · Cited by 11
Scavenging of nitric oxide by hemoglobin in the tunica media of porcine coronary arteries
Kollau, A., Russwurm, M., Neubauer, A., Rechberger, G. N., Schmidt, K., Koesling, D., Fassett, J., Schrammel, A., & Mayer, B. (2016) · Nitric Oxide · doi:10.1016/j.niox.2016.01.005 · Cited by 10
NADPH oxidase 5 activation; a novel approach to human sperm cryoinjury
Keshtgar, S., Ebrahimi, B., Moosavi, S. M. S., & Erfani, N. (2020) · Cell and Tissue Banking · doi:10.1007/s10561-020-09845-0 · Cited by 10
NADPH‐oxidase‐derived ROS alters cell migration by modulating adhesions dynamics
Tamborindeguy, M. T., Matte, B. F., Ramos, G. D. O., Alves, A. M., Bernardi, L., & Lamers, M. L. (2018) · Biology of the Cell · doi:10.1111/boc.201800011 · Cited by 10
Inhibition of redox cycling of methoxatin (PQQ), and of superoxide release by phagocytic white cells
Bishop, A., Paz, M. A., Gallop, P. M., & Karnovsky, M. L. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)00178-m · Cited by 10
Blue Light Exposure Targets NADPH Oxidase to Plasma Membrane and Nucleus in Wheat Coleoptiles
Chandra-Kuntal, K., Shah, A. K., Thomas, N. M., Karthika, V., Laloraya, M., Kumar, P. G., & Laloraya, M. M. (2009) · Journal of Plant Growth Regulation · doi:10.1007/s00344-009-9127-2 · Cited by 10
Diversity of voltage gated proton channels
Morgan, D. (2003) · Frontiers in bioscience · doi:10.2741/1191 · Cited by 10
Simultaneous Detection of Whole Blood Chemiluminescence in Microtitre Plates
Kaever, V., Robitzsch, J. T., Stangel, W., Schleinkofer, L., & Resch, K. (1992) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.1992.30.4.209 · Cited by 10
Hepatic Responses to Bacterial Endotoxin (LPS)
Bautista, A. P., Jr., Deaciuc, I. V., Jaeschke, H., Spolarics, Z., & Spitzer, J. J. (1993) · Springer eBooks · doi:10.1007/978-3-642-76736-4_62 · Cited by 10
Belavgeni, A., & Dailianis, S. (2017) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2017.07.015 · Cited by 9
Modulation of phagocytosis-induced cell death of human neutrophils by Neisseria gonorrhoeae
Cho, C., Teghanemt, A., Apicella, M. A., & Nauseef, W. M. (2020) · Journal of Leukocyte Biology · doi:10.1002/jlb.4ma0820-649r · Cited by 9
Song, X., She, X., & Wang, J. (2012) · Australian Journal of Botany · doi:10.1071/bt11144 · Cited by 9
Hypoxia inhibits semicarbazide-sensitive amine oxidase activity in adipocytes
Repessé, X., Moldes, M., Muscat, A., Vatier, C., Chetrite, G. S., Gille, T., Planès, C., Filip, A., Mercier, N., Duranteau, J., et al. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.04.011 · Cited by 9
Mechanisms for Hypoxia Detection in O2-Sensitive Cells
Fujishiro, N., Endo, Y., Warashina, A., & Inoue, M. (2004) · The Japanese Journal of Physiology · doi:10.2170/jjphysiol.54.109 · Cited by 9
Novikov, V. V., Yablokova, E. V., Shaev, I. A., & Fesenko, E. E. (2020) · BIOPHYSICS · doi:10.1134/s0006350920040120 · Cited by 10
Wang, J.-P., Chang, L., Hsu, M., & Lin, C. (2003) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-003-0782-8 · Cited by 9
The superoxide-generating oxidase of phagocytic cells
Morel, F., Doussière, J., & Vignais, P. V. (1991) · Springer eBooks · doi:10.1007/978-3-642-77200-9_17 · Cited by 9
Nitric Oxide: A Mediator in Anaphylactic Shock in Guinea-Pigs
Abend, Y., Ashkenazy, Y., Witzling, V., Feigl, D., David Geltner, Moshonov, S., & Zor, U. (1996) · Journal of Basic and Clinical Physiology and Pharmacology · doi:10.1515/jbcpp.1996.7.1.57 · Cited by 9
Ma, Y., Zhang, W., & Niu, J. (2019) · South African Journal of Botany · doi:10.1016/j.sajb.2019.04.031 · Cited by 8
Baker, C. J., Orlandi, E. W., & Deahl, K. L. (2001) · Physiological and Molecular Plant Pathology · doi:10.1006/pmpp.2001.0340 · Cited by 8
Lundqvist, H., Dånmark, S., Johansson, U., Gustafsson, H., & Öllinger, K. M. (2007) · Journal of Biochemical and Biophysical Methods · doi:10.1016/j.jbbm.2007.05.014 · Cited by 8
Relationship between calcium release and NADPH oxidase inhibition in human neutrophils
Salmon, M. D., & Ahluwalia, J. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.04.079 · Cited by 8
Characterisation of electron currents generated by the human neutrophil NADPH oxidase
Ahluwalia, J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.01.161 · Cited by 8
The mechanism of the production of superoxide by phagocytes
Jones, O. T. G. (1993) · Molecular and Chemical Neuropathology · doi:10.1007/bf03160177 · Cited by 8
Self-citationKuta, D., & Gaivaronskaya, L. M. (2004) · AFRICAN JOURNAL OF BIOTECHNOLOGY · doi:10.5897/ajb2004.000-2014 · Cited by 8
Shuto, M., Ogita, K., & Yoneda, Y. (1997) · Neurochemistry International · doi:10.1016/s0197-0186(96)00140-4 · Cited by 8
Triggering and Regulation of the Free Radical Production by Phagocytes
Bellavite, P., Serra, M. C., Bazzoni, F., Miron, S., & Dusi, S. (1990) · Springer eBooks · doi:10.1007/978-1-4684-7427-5_3 · Cited by 8
Murphy, T. M., Vu, H., & Nguyen, T. (1998) · Cited by 7
Ratz, J. D., McGuire, J. J., & Bennett, B. M. (1999) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0702268 · Cited by 7
Hsu, M. F., Raung, S. L., Tsao, L. T., Kuo, S., & Wang, J. P. (1997) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0700974 · Cited by 7
Park (1992) · International Journal of Oncology · doi:10.3892/ijo_00000121 · Cited by 7
Gómez‐Piñeiro, R. J., Dali, M.-M., Mansuy, D., & Boucher, J. (2022) · Biochimie · doi:10.1016/j.biochi.2022.04.009 · Cited by 6
Nguyen, P. T., Wacker, T., Brown, A. J. P., Dantas, A. D. S., & Shekhova, E. (2022) · Journal of Fungi · doi:10.3390/jof8070736 · Cited by 6
Wang, J.-P., Tsao, L., Shen, A., Raung, S., & Chang, L. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00288-3 · Cited by 6
高橋, 計., & 森, 勝. (2001) · Institutional Repositories DataBase (IRDB) · doi:10.11233/aquaculturesci1953.49.389 · Cited by 6
Mechanisms of Oxidase Activation in Neutrophils
Al-Mohanna, F. A., & Hallett, M. B. (1991) · Blood cell biochemistry · doi:10.1007/978-1-4615-3796-0_11 · Cited by 6
Antisense Oligodeoxyribonucleotides: A Better Way to Inhibit Monocyte Superoxide Anion Production?
Bey, E. A., & Cathcart, M. K. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)53066-4 · Cited by 6
Isoform-Selective Nox Inhibitors: Advances and Future Perspectives
Dustin, C. M., Cifuentes-Pagano, E., & Pagano, P. J. (2023) · Springer eBooks · doi:10.1007/978-3-031-23752-2_21 · Cited by 5
Derochette, S., Serteyn, D., Mouithys-Mickalad, A. A., Ceusters, J. D., Deby-Dupont, G. P., Neven, P., & Franck, T. J. (2015) · Talanta · doi:10.1016/j.talanta.2015.08.007 · Cited by 5
NAD(P)H oxidase isoforms as therapeutic targets for diabetic complications
Gray, S. P., Jha, J. C., Marco, E. D., & Jandeleit-Dahm, K. A. M. (2014) · Expert Review of Endocrinology & Metabolism · doi:10.1586/17446651.2014.887984 · Cited by 5
Lack of inhibition of glyceryl trinitrate by diphenyleneiodonium in bovine coronary artery
de la Lande, I. S., Philp, T., Stafford, I., & Horowitz, J. D. (1996) · European Journal of Pharmacology · doi:10.1016/s0014-2999(96)00729-7 · Cited by 5
Bartík, P., Chalupský, K., Müller, B., Jc, S., & Entlicher, G. (2006) · Physiological Research · doi:10.33549/physiolres.930508 · Cited by 5
Tejima, K. (2007) · World Journal of Gastroenterology · doi:10.3748/wjg.v13.i38.5071 · Cited by 5
The Respiratory Burst and the NADPH Oxidase of Phagocytic Leukocytes
Roos, D., Lutter, R., & Bolscher, B. G. J. M. (1988) · Springer eBooks · doi:10.1007/978-1-4684-5496-3_3 · Cited by 5
Maly, F. E., Urwyler, A., TENGLER, R., Steinitz, M. O., Golding, B., & Weck, A. (1990) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.1990.tb03208.x · Cited by 5
Reactive Oxygen Intermediates as Signaling Molecules Regulating Leukocyte Activation
Fialkow, L., & Downey, G. P. (1997) · Springer eBooks · doi:10.1007/978-1-4615-5981-8_9 · Cited by 5
Impact of Cellular Mechanisms of Ischemia on CABG Failure
Amuzescu, B. P., Istrate, B. M., & Mubagwa, K. (2016) · Springer eBooks · doi:10.1007/978-3-319-26515-5_31 · Cited by 4
Real-time functional analysis of Hv1 channel in neutrophils: a new approach from zebrafish model
Ratanayotha, A., Kawai, T., & Okamura, Y. (2019) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00326.2018 · Cited by 4
An almitrine analog acts as hypoxia in isolated rat lungs
Robineau, P., Dhainaut, A., & Canet, E. (1996) · Respiration Physiology · doi:10.1016/0034-5687(96)00055-2 · Cited by 4
Swell activated chloride channel function in human neutrophils
Salmon, M. D., & Ahluwalia, J. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.02.147 · Cited by 4
Activation of Human Neutrophils by NAP-1 and Other Chemotactic Agonists
Baggiolini, M., Dewald, B., & Walz, A. (1991) · Advances in experimental medicine and biology · doi:10.1007/978-1-4684-6009-4_2 · Cited by 4
Ravel, P., & Lederer, F. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)92074-t · Cited by 4
Suppressive effects of a novel antioxidant compound on human T cell functionsin vitro
Kalsi, J., Clay, K., Rickard, D. J., & Hall, N. D. (1993) · Inflammation Research · doi:10.1007/bf01972738 · Cited by 4
The Elusive Oxidase The Respiratory Burst Oxidase of Human Phagocytes
Smith, R. M., Woodman, R. C., & BABIOR, B. M. (1991) · Blood cell biochemistry · doi:10.1007/978-1-4615-3796-0_9 · Cited by 4
Liu, N.-N., Uppuluri, P., Broggi, A., Besold, A., Ryman, K., Kambara, H., Solis, N., Lorenz, V., Qi, W., Acosta-Zaldivar, M., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/317933 · Cited by 4
Inoue, M., Iizuka, Y., Nakamura, K., Sato, G. E., & Mizowaki, T. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.10.015 · Cited by 3
Antioxidant drugs as modulators of lymphocyte activation in vitro
Kalsi, J., Clay, K., & Hall, N. D. (1991) · Molecular Aspects of Medicine · doi:10.1016/0098-2997(91)90011-a · Cited by 3
Chemiluminescence of mononuclear cells is enhanced during antigen recognition
TENGLER, R., Furukawa, K., de Weck, A. L., & Maly, F. E. (1993) · Journal of Bioluminescence and Chemiluminescence · doi:10.1002/bio.1170080306 · Cited by 3
Aging-associated dysbiosis increases susceptibility to enteric viral infection in DrosophilaPreprint
Sansone, C. L., Cohen, J. A., Gold, B., Zhu, W., Misic, A. M., Beiting, D. P., Winter, S., & Cherry, S. R. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/156455 · Cited by 3
Involvement of Ca2+ in globular adiponectin-induced reactive oxygen species
Akifusa, S., Kamio, N., Shimazaki, Y., Yamaguchi, N., & Yamashita, Y. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.02.115 · Cited by 2
Le, Q. A., Trinh, T. N., Luong, P. K., Anh, V. T. V., Tran, H. N., Kim, J., & Woo, S. (2024) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2024.28.4.335 · Cited by 3
Metadata
- Authors
- Cross, A. R., & Jones, O. T. G.
- Affiliations
- University of Bristol (GB)
- ORCID
- Jones, O T G
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1986-07-01
- Volume
- 237
- Issue
- 1
- Pages
- 111-116
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1146954
- OpenAlex
- W1801129364
- Cited by
- 551
- References
- 22
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 1 · 2023: 5 · 2022: 7 · 2021: 5 · 2020: 9 · 2019: 12 · 2018: 13 · 2017: 14 · 2016: 9 · 2015: 13 · 2014: 9 · 2013: 19 · 2012: 20
- FWCI
- 5.47
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Medical Research Council
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
- Keywords
- diphenyleneiodonium, neutrophil NADPH oxidase, superoxide production, flavoprotein, enzyme inhibition, FAD reduction, NADPH-dependent reduction, respiratory burst
- MeSH terms
- Animals, Electrophoresis, Polyacrylamide Gel, NADH, NADPH Oxidoreductases, NADP, Neutrophils, Onium Compounds, Protein Binding, Swine, NADPH Oxidases, In Vitro Techniques
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