The DOI matches its Crossref record; 258 of the 259 references it cites were found in a registry or an index.
Nitric oxide and redox mechanisms in the immune response
Open accessAbstract
The role of redox molecules, such as NO and ROS, as key mediators of immunity has recently garnered renewed interest and appreciation. To regulate immune responses, these species trigger the eradication of pathogens on the one hand and modulate immunosuppression during tissue-restoration and wound-healing processes on the other. In the acidic environment of the phagosome, a variety of RNS and ROS is produced, thereby providing a cauldron of redox chemistry, which is the first line in fighting infection. Interestingly, fluctuations in the levels of these same reactive intermediates orchestrate other phases of the immune response. NO activates specific signal transduction pathways in tumor cells, endothelial cells, and monocytes in a concentration-dependent manner. As ROS can react directly with NO-forming RNS, NO bioavailability and therefore, NO response(s) are changed. The NO/ROS balance is also important during Th1 to Th2 transition. In this review, we discuss the chemistry of NO and ROS in the context of antipathogen activity and immune regulation and also discuss similarities and differences between murine and human production of these intermediates.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“nNOS and eNOS, which are expressed constitutively, produce a low level of NO for short periods (seconds to minutes).447”
From Role of neuroinflammation in neurodegeneration development (2023) · cites this paper as [447]
In the citing paper
“At present, three types of NOS have been identified, including neuronal NOS (nNOS, also named as NOS1), endothelial NOS (eNOS, also named as NOS3), and inducible NOS (iNOS, also named as NOS2).447”
From Role of neuroinflammation in neurodegeneration development (2023) · cites this paper as [447]
In the citing paper
“Intracellular communication and immune response are mediated by at least five classes of endogenously generated reactive small molecules (Figure 1): nitric oxide (NO) and reactive nitrogen oxide species (RNS), reactive oxygen species (ROS), eicosanoids and reactive lipid species (formed by oxidation of fatty acids), a variety of sulfur-based species such as hydrogen sulfide (H2S), thiols and disul”
From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [3]
In the citing paper
“An additional mechanism for IL-10 production is through NO-dependent increases of COX2 [3, 57]].”
From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [3]
In the citing paper
“In chronic disease, involving extended exposure to pathogens or particulates such as plaques in the brain or following a critical mutation, wound healing processes persist and can lead to fibrosis or tumor growth [3].”
From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [3]
In the citing paper
“These molecules can act as sensors to steer signaling cascades during inflammation, for example from a T helper (Th) 1 to a Th2 cytokine response [3, 87].”
From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [3]
In the citing paper
“In the phagosome, iron deposition facilitates the sterilization process in conjunction with ROS and nitrite [3].”
From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [3]
In the citing paper
“Lysis of Staphylococcus bacteria involves the sequential exposure to respiratory burst followed by •NO exposure [126].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [126]
In the citing paper
“•NO and RNS eradicate bacteria by nitrosylation and oxidation of bacterial macromolecules [126].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [126]
In the citing paper
“The •NO/ROS balance is also important during the transition from Th1 to Th2 [125,126].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [126]
In the citing paper
“Recognition of bacteria by macrophages leads to ROS production in different cellular compartments, where they fulfill different antibacterial functions.”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [234]
Citations
Cites
Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178
Nitric oxide: physiology, pathophysiology, and pharmacology.
Moncada, S., Palmer, R. M., & Higgs, E. A. (1991) · Pharmacological Reviews · doi:10.1016/s0031-6997(25)06663-3 · Cited by 15,525
Free Radicals in Biology and Medicine
Land, E. J. (1990) · International Journal of Radiation Biology · doi:10.1080/09553009014552071 · Cited by 4,871
Function and Activation of NF-kappaB in the Immune System
Baeuerle, P. A., & Henkel, T. (1994) · Annual Review of Immunology · doi:10.1146/annurev.iy.12.040194.001041 · Cited by 4,745
Macrophage activation and polarization
Martinez, F. O. (2008) · Frontiers in Bioscience · doi:10.2741/2692 · Cited by 3,160
Nitric oxide: an endogenous modulator of leukocyte adhesion.
Kubes, P., Suzuki, M., & Granger, D. N. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.11.4651 · Cited by 3,036
Ren, G., Zhang, L., Zhao, X., Xu, G., Zhang, Y., Roberts, A. I., Zhao, R. C., & Shi, Y. (2008) · Cell Stem Cell · doi:10.1016/j.stem.2007.11.014 · Cited by 2,101
Nitric oxide: A cytotoxic activated macrophage effector molecule
Hibbs, J. B., Taintor, R. R., Vavrin, Z., & Rachlin, E. M. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(88)80015-9 · Cited by 2,034
The JAK/STAT signaling pathway
Rawlings, J. S., Rosler, K. M., & Harrison, D. A. (2004) · Journal of Cell Science · doi:10.1242/jcs.00963 · Cited by 1,858
Stuehr, D. J., & Nathan, C. F. (1989) · The Journal of Experimental Medicine · doi:10.1084/jem.169.5.1543 · Cited by 1,744
Protein tyrosine phosphatases: from genes, to function, to disease
Tonks, N. K. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2039 · Cited by 1,712
Meisel, R., Zibert, A., Laryea, M. D., Göbel, U., Däubener, W., & Dilloo, D. (2004) · Blood · doi:10.1182/blood-2003-11-3909 · Cited by 1,638
Wink, D. A., & Mitchell, J. B. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00092-6 · Cited by 1,606
Self-citationInwardly Rectifying Potassium Channels: Their Structure, Function, and Physiological Roles
Hibino, H., Inanobe, A., Furutani, K., Murakami, S., Findlay, I., & Kurachi, Y. (2010) · Physiological Reviews · doi:10.1152/physrev.00021.2009 · Cited by 1,579
Macrophage cytotoxicity: role for L-arginine deiminase and imino nitrogen oxidation to nitrite
Hibbs, J. B., Taintor, R. R., & Vavrin, Z. (1987) · Science · doi:10.1126/science.2432665 · Cited by 1,527
Superoxide generation by endothelial nitric oxide synthase: The influence of cofactors
Vásquez-Vivar, J., Kalyanaraman, B., Martásek, P., Hogg, N., Masters, B. S. S., Karoui, H., Tordo, P., & Pritchard, K. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9220 · Cited by 1,484
MacMicking, J. D., Nathan, C., Hom, G. J., Chartrain, N. A., Fletcher, D. S., Trumbauer, M. E., Stevens, K. A., Xie, Q. W., Sokol, K. A., Hutchinson, N. I., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90085-3 · Cited by 1,445
Schreck, R., Albermann, K., & Baeuerle, P. A. (1992) · Free Radical Research Communications · doi:10.3109/10715769209079515 · Cited by 1,388
Nitric Oxide Synthases: Properties and Catalytic Mechanism
Griffith, O. W., & Stuehr, D. J. (1995) · Annual Review of Physiology · doi:10.1146/annurev.ph.57.030195.003423 · Cited by 1,311
Heme oxygenase-1: unleashing the protective properties of heme
Otterbein, L. E., Soares, M. P., Yamashita, K., & Bach, F. H. (2003) · Trends in Immunology · doi:10.1016/s1471-4906(03)00181-9 · Cited by 1,166
Stuehr, D. J., & Marletta, M. A. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.22.7738 · Cited by 1,126
Active DNA demethylation: many roads lead to Rome
Wu, S. C., & Zhang, Y. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2950 · Cited by 1,091
Krötz, F., Sohn, H., & Pohl, U. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000145574.90840.7d · Cited by 1,030
Heme oxygenase-1 mediates the anti-inflammatory effect of interleukin-10 in mice
Lee, T.-S., & Chau, L.-Y. (2002) · Nature Medicine · doi:10.1038/nm0302-240 · Cited by 1,019
The chemical biology of nitric oxide: Implications in cellular signaling
Thomas, D. D., Ridnour, L. A., Isenberg, J. S., Flores-Santana, W., Switzer, C. H., Donzelli, S., Hussain, P., Vecoli, C., Paolocci, N., Ambs, S., et al. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.020 · Cited by 975
Self-citationStaal, F. J. T., Roederer, M., Herzenberg, L. A., & Herzenberg, L. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.24.9943 · Cited by 956
Heterogeneity of Microglial Activation in the Innate Immune Response in the Brain
Colton, C. A. (2009) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-009-9164-4 · Cited by 916
Self-citationRedox Regulation of NF-kappa B Activation
Flohé, L., Brigelius‐Flohé, R., Saliou, C., Traber, M. G., & Packer, L. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00501-1 · Cited by 859
Arginase-1–Expressing Macrophages Suppress Th2 Cytokine–Driven Inflammation and Fibrosis
Pesce, J. T., Ramalingam, T. R., Mentink-Kane, M. M., Wilson, M. S., El Kasmi, K. C., Smith, A. M., Thompson, R. W., Cheever, A. W., Murray, P. J., & Wynn, T. A. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000371 · Cited by 816
Serafini, P., Meckel, K. F., Kelso, M., Noonan, K. A., Califano, J. A., Koch, W. M., Dolcetti, L., Bronte, V., & Borrello, I. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20061104 · Cited by 780
Nitric oxide protects against cellular damage and cytotoxicity from reactive oxygen species.
Wink, D. A., Hanbauer, I., Krishna, M. C., DeGraff, W., Gamson, J., & Mitchell, J. B. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.21.9813 · Cited by 766
Self-citationSuperoxide and peroxynitrite generation from inducible nitric oxide synthase in macrophages
Xia, Y., & Zweier, J. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.13.6954 · Cited by 691
Simulation of the diffusion and reaction of endogenously produced nitric oxide.
Lancaster, J. R. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.17.8137 · Cited by 689
Nox enzymes, ROS, and chronic disease: An example of antagonistic pleiotropy
Lambeth, J. D. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.027 · Cited by 687
Peroxynitrite reductase activity of bacterial peroxiredoxins
Bryk, R., Griffin, P. R., & Nathan, C. (2000) · Nature · doi:10.1038/35025109 · Cited by 679
Green, L. C., Ruiz de Luzuriaga, K., Wagner, D. A., Rand, W., Istfan, N., Young, V. R., & Tannenbaum, S. R. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.12.7764 · Cited by 665
Modulation of transcription factor NF-kappa B binding activity by oxidation-reduction in vitro.
Toledano, M. B., & Leonard, W. J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.10.4328 · Cited by 657
Hydrogen Peroxide: A Key Messenger That Modulates Protein Phosphorylation Through Cysteine Oxidation
Rhee, S. G., Bae, Y. S., Lee, S.-R., & Kwon, J. (2000) · Science s STKE · doi:10.1126/stke.2000.53.pe1 · Cited by 646
Species Variation in the Mechanisms of Mesenchymal Stem Cell-Mediated Immunosuppression
Ren, G., Su, J., Zhang, L., Zhao, X., Ling, W., L'huillie, A., Zhang, J., Lu, Y., Roberts, A. I., Ji, W., et al. (2009) · Stem Cells · doi:10.1002/stem.118 · Cited by 597
Kabe, Y., Ando, K., Hirao, S., Yoshida, M., & Handa, H. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.395 · Cited by 585
STRUCTURE-FUNCTION ASPECTS IN THE NITRIC OXIDE SYNTHASES
Stuehr, D. J. (1997) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.37.1.339 · Cited by 547
Forman, H. J., Fukuto, J. M., & Torrès, M. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00516.2003 · Cited by 533
Rapid reaction between peroxonitrite ion and carbon dioxide: Implications for biological activity
Lymar, S. V., & Hurst, J. K. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00139a027 · Cited by 515
EPR demonstration of iron-nitrosyl complex formation by cytotoxic activated macrophages
Lancaster, J. R., & Hibbs, J. B. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.3.1223 · Cited by 507
Fulton, D. J., Gratton, J., & Sessa, W. C. (2001) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)29198-9 · Cited by 499
Recent advances in arginine metabolism: roles and regulation of the arginases
Morris Jr, S. M. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00278.x · Cited by 485
Hibbs, J. B., Westenfelder, C., Taintor, R., Vavrin, Z., Kablitz, C., Baranowski, R. L., Ward, J. H., Menlove, R. L., McMurry, M. P., & Kushner, J. P. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115666 · Cited by 485
Anstey, N. M., Weinberg, J. B., Hassanali, M. Y., Mwaikambo, E. D., Manyenga, D., Misukonis, M. A., Arnelle, D. R., Hollis, D. R., McDonald, M., & Granger, D. L. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.184.2.557 · Cited by 431
Assessing Activation States in Microglia
Colton, C. A., & Wilcock, D. M. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710791012053 · Cited by 430
Self-citationLuckhart, S., Yoram Vodovotz, B., Cui, L., & Rosenberg, R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.10.5700 · Cited by 401
p53 expression in nitric oxide‐induced apoptosis
Meßmer, U. K., Ankarcrona, M., Nicotera, P., & Brüne, B. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01161-3 · Cited by 400
Nitric Oxide Is a Physiological Substrate for Mammalian Peroxidases
Abu‐Soud, H. M., & Hazen, S. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.48.37524 · Cited by 399
Localizing NADPH Oxidase–Derived ROS
Ushio‐Fukai, M. (2006) · Science s STKE · doi:10.1126/stke.3492006re8 · Cited by 397
Carbon monoxide in biology and medicine
Ryter, S. W., & Otterbein, L. E. (2004) · BioEssays · doi:10.1002/bies.20005 · Cited by 394
Nitric oxide and wound repair: role of cytokines?
Schwentker, A., Vodovotz, Y., Weller, R., & Billiar, T. R. (2002) · Nitric Oxide · doi:10.1016/s1089-8603(02)00002-2 · Cited by 386
Triad3A, an E3 ubiquitin-protein ligase regulating Toll-like receptors
Chuang, T.-H., & Ulevitch, R. J. (2004) · Nature Immunology · doi:10.1038/ni1066 · Cited by 374
Maynard, A. T., Huang, M., Rice, W. G., & Covell, D. G. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.11578 · Cited by 368
Nitric oxide and virus infection
Akaike, T., & Maeda, H. (2000) · Immunology · doi:10.1046/j.1365-2567.2000.00142.x · Cited by 362
The Contributions of Cyclooxygenase-2 to Tumor Angiogenesis
Gately, S. T. (2000) · Cancer and Metastasis Reviews · doi:10.1023/a:1026575610124 · Cited by 359
Targeting and Regulation of Reactive Oxygen Species Generation by Nox Family NADPH Oxidases
Leto, T. L., Morand, S. C., Hurt, D. E., & Ueyama, T. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2637 · Cited by 347
Swierkosz, T. A., Mitchell, J. A., Warner, T. D., Botting, R. M., & Vane, J. R. (1995) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.1995.tb13353.x · Cited by 340
The role of cysteine residues as redox-sensitive regulatory switches
Barford, D. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.09.012 · Cited by 339
Li, L., Hsu, A., & Moore, P. K. (2009) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.05.005 · Cited by 331
Nitric oxide regulates angiogenesis through a functional switch involving thrombospondin-1
Ridnour, L. A., Isenberg, J. S., Espey, M. G., Thomas, D. D., Roberts, D. D., & Wink, D. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502979102 · Cited by 323
Self-citationComplex regulation of human inducible nitric oxide synthase gene transcription by Stat 1 and NF-κB
Ganster, R. W., Taylor, B. S., Shao, L., & Geller, D. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151239498 · Cited by 321
Connelly, L., Palacios‐Callender, M., Ameixa, C., Moncada, S., & Hobbs, A. J. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.6.3873 · Cited by 319
Doyle, A., Herbein, G., Montaner, L. J., Minty, A. J., Caput, D., Ferrara, P., & Gordon, S. (1994) · European Journal of Immunology · doi:10.1002/eji.1830240630 · Cited by 306
Killing of Plasmodium falciparum in vitro by nitric oxide derivatives
Rockett, K. A., Awburn, M. M., Cowden, W. B., & Clark, I. A. (1991) · Infection and Immunity · doi:10.1128/iai.59.9.3280-3283.1991 · Cited by 306
Singh, S., Vrishni, S., Singh, B. K., Rahman, I., & Kakkar, P. (2010) · Free Radical Research · doi:10.3109/10715762.2010.507670 · Cited by 305
TNF receptor superfamily‐induced cell death: redox‐dependent execution
Shen, H., & Pervaiz, S. (2006) · The FASEB Journal · doi:10.1096/fj.05-5603rev · Cited by 294
Thomas, D. D., Espey, M. G., Ridnour, L. A., Hofseth, L. J., Mancardi, D., Harris, C. C., & Wink, D. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400453101 · Cited by 289
Self-citationTalmadge, J. E. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-0182 · Cited by 286
Baetz, A., Frey, M., Heeg, K. M., & Dalpke, A. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410992200 · Cited by 273
CURRAN, R. D., Billiar, T. R., Stuehr, D. J., Ochoa, J. B., Harbrecht, B. G., FLINT, S. G., & Simmons, R. L. (1990) · Annals of Surgery · doi:10.1097/00000658-199010000-00009 · Cited by 269
Regulation and termination of NADPH oxidase activity
DeCoursey, T. E., & Ligeti, E. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5177-1 · Cited by 268
Maulik, N., & Das, D. K. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01005-5 · Cited by 267
Review: Hypoxia-Inducible Factor-1 (HIF-1): A Novel Transcription Factor in Immune Reactions
Hellwig‐Bürgel, T., Stiehl, D. P., Wagner, A. E., Metzen, E., & JELKMANN, W. E. B. (2005) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2005.25.297 · Cited by 264
Accumulation of HIF-1α under the influence of nitric oxide
Sandau, K. B., Fandrey, J., & Brüne, B. (2001) · Blood · doi:10.1182/blood.v97.4.1009 · Cited by 263
Nitric oxide potentiates hydrogen peroxide-induced killing of Escherichia coli.
Pacelli, R., Wink, D. A., Cook, J. A., Krishna, M. C., DeGraff, W., Friedman, N., Tsokos, M., Samuni, A., & Mitchell, J. B. (1995) · The Journal of Experimental Medicine · doi:10.1084/jem.182.5.1469 · Cited by 260
Self-citationHydrogen sulfide: Neurochemistry and neurobiology
Qu, K., Lee, S. W., Bian, J., Low, C. M., & Wong, P. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.05.016 · Cited by 260
Buga, G. M., Singh, R., Pervin, S., Rogers, N. E., Schmitz, D. A., Jenkinson, C. P., Cederbaum, S. D., & Ignarro, L. J. (1996) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1996.271.5.h1988 · Cited by 257
Amin, A. R., Cesare, P. E. D., Vyas, P., Attur, M. G., Tzeng, E., Billiar, T. R., Stuchin, S. A., & Abramson, S. B. (1995) · The Journal of Experimental Medicine · doi:10.1084/jem.182.6.2097 · Cited by 253
The biphasic nature of nitric oxide responses in tumor biology
Ridnour, L. A., Thomas, D. D., Donzelli, S., Espey, M. G., Roberts, D. D., Wink, D. A., & Isenberg, J. S. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.1329 · Cited by 247
Self-citationDas, P., Lahiri, A., Lahiri, A., & Chakravortty, D. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000899 · Cited by 247
Mammalian synthesis of nitrite, nitrate, nitric oxide, and N-nitrosating agents
Marletta, M. A. (1988) · Chemical Research in Toxicology · doi:10.1021/tx00005a001 · Cited by 241
Homocysteine Metabolism in Children with Down Syndrome: In Vitro Modulation
Pogribna, M., Melnyk, S., Pogribny, I. P., Chango, A., Yi, P., & James, S. J. (2001) · The American Journal of Human Genetics · doi:10.1086/321262 · Cited by 241
MacNaul, K. L., & Hutchinson, N. I. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.2398 · Cited by 239
Endres, S., Fülle, H., Sinha, B. N. M., Stoll, D., Dinarello, C. A., Gerzer, R., & Weber, P. C. (1991) · PubMed Central · Cited by 238
Fang, F. C. (2002) · Springer eBooks · doi:10.1007/b111485 · Cited by 228
Wang, X. M., Kim, H. P., Nakahira, K., Ryter, S. W., & Choi, A. M. K. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0712437 · Cited by 227
Regulation of Nitric Oxide Synthesis and Apoptosis by Arginase and Arginine Recycling
Mori, M. (2007) · Journal of Nutrition · doi:10.1093/jn/137.6.1616s · Cited by 221
Li, Q., & Engelhardt, J. F. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511153200 · Cited by 219
Ridnour, L. A., Windhausen, A. N., Isenberg, J. S., Yeung, N., Thomas, D. D., Vitek, M. P., Roberts, D. D., & Wink, D. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702761104 · Cited by 219
Self-citationRiboflavin kinase couples TNF receptor 1 to NADPH oxidase
Yazdanpanah, B., Wiegmann, K., Tchikov, V., Krut, O., Pongratz, C., Schramm, M., Kleinridders, A., Wunderlich, T., Kashkar, H., Utermöhlen, O., et al. (2009) · Nature · doi:10.1038/nature08206 · Cited by 218
Fulton, D. J., Fontana, J. T., Sowa, G., Gratton, J., Lin, M. I., Li, K.-X., Michell, B. J., Kemp, B. E., Rodman, D. M., & Sessa, W. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106302200 · Cited by 217
Nitromation of amines by stimulated macrophages
Miwa, M., Stuehr, D. J., Marletta, M. A., Wishnok, J. S., & Tannenbaum, S. R. (1987) · Carcinogenesis · doi:10.1093/carcin/8.7.955 · Cited by 208
John, G. S., Brot, N., Ruan, J., Erdjument‐Bromage, H., Tempst, P., Weissbach, H., & Nathan, C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.161295398 · Cited by 206
Forman, H. J., Torrès, M., & Fukuto, J. M. (2002) · Molecular and Cellular Biochemistry · doi:10.1023/a:1015913229650 · Cited by 205
Essential Requirement of Cytosolic Phospholipase A2for Activation of the Phagocyte NADPH Oxidase
Dana, R., Leto, T. L., Malech, H. L., & Lévy, R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.1.441 · Cited by 199
Weinberg, J. B. (1998) · Molecular Medicine · doi:10.1007/bf03401758 · Cited by 196
Molecular mechanisms for discrete nitric oxide levels in cancer
Ridnour, L. A., Thomas, D. D., Switzer, C., Flores‐Santana, W., Isenberg, J. S., Ambs, S., Roberts, D. D., & Wink, D. A. (2008) · Nitric Oxide · doi:10.1016/j.niox.2008.04.006 · Cited by 196
Self-citationNADPH oxidase activity is required for endothelial cell proliferation and migration
Abid, M. R., Kachra, Z., Spokes, K., & Aird, W. C. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02305-x · Cited by 191
Toll-Like Receptor 2 Is Required for Optimal Control of Listeria monocytogenes Infection
Torres, D., Barrier, M., Bihl, F., Quesniaux, V. J. F., Maillet, I., Akira, S., Ryffel, B., & Erard, F. (2004) · Infection and Immunity · doi:10.1128/iai.72.4.2131-2139.2004 · Cited by 191
Carbon monoxide and hydrogen sulfide: gaseous messengers in cerebrovascular circulation
Leffler, C. W., Parfenova, H., Jaggar, J. H., & Wang, R. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00793.2005 · Cited by 186
Role of nitric oxide in the regulation of T cell functions
Niedbała, W., Cai, B., & Liew, F. Y. (2006) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2006.058446 · Cited by 186
Karupiah, G., Chen, J.-H., Mahalingam, S., Nathan, C., & MacMicking, J. D. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.8.1541 · Cited by 183
Grumbach, I. M., Chen, W., Mertens, S., & Harrison, D. G. (2005) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2005.06.012 · Cited by 182
HENDERSON, L. M., Chappell, J., & Jones, O. T. G. (1988) · Biochemical Journal · doi:10.1042/bj2510563 · Cited by 179
Connelly, L., Jacobs, A. T., Palacios‐Callender, M., Moncada, S., & Hobbs, A. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302238200 · Cited by 178
L-arginine metabolism and its impact on host immunity against Leishmania infection
Wanasen, N., & Soong, L. (2007) · Immunologic Research · doi:10.1007/s12026-007-8012-y · Cited by 178
Vasquez-Vivar, J. M., Hogg, N., Pavel Martasek, E., Karoui, H., Pritchard, K. A., & Kalyanaraman, B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.38.26736 · Cited by 176
Oxidative Stress Regulation of Stem and Progenitor Cells
Pervaiz, S., Taneja, R., & Ghaffari, S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2804 · Cited by 176
Murad, F. (1994) · Elsevier eBooks · doi:10.1016/b978-0-12-571149-4.50016-7 · Cited by 175
Basu, J. M., Mookerjee, A., Sen, P., Bhaumik, S., Sen, P., Banerjee, S. B., Naskar, K., Choudhuri, S. K., Saha, B., Raha, S., et al. (2006) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.50.5.1788-1797.2006 · Cited by 175
Tzeng, E., Billiar, T. R., Robbins, P. D., Loftus, M., & Stuehr, D. J. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.25.11771 · Cited by 174
de Miranda, K. R., Pace, D. A., Cintrón, R., Rodrigues, J. C. F., Fang, J., Smith, A. N., Rohloff, P. J., Coelho, E., de Haas, F., de Souza, W., et al. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07165.x · Cited by 174
Boucher, J., Custot, J., Goff, S. V., Delaforge, M., Lepoivre, M., Tenu, J., Yapo, A., & Mansuy, D. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.2371 · Cited by 172
Viral Subversion of Apoptotic Enzymes: Escape from Death Row
Best, S. M. (2008) · Annual Review of Microbiology · doi:10.1146/annurev.micro.62.081307.163009 · Cited by 171
Vandal, O. H., Roberts, J., Odaira, T., Schnappinger, D., Nathan, C., & Ehrt, S. (2008) · Journal of Bacteriology · doi:10.1128/jb.00932-08 · Cited by 163
Chen, Y.-Y., Chu, H., Pan, K., Teng, C.-H., Wang, D.-L., Wang, A. H. ‐., Khoo, K., & Meng, T. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805287200 · Cited by 160
S-nitrosylation: Physiological regulation of NF-κB
Marshall, H. E., Hess, D. T., & Stamler, J. S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403034101 · Cited by 160
Role of Nitric Oxide in Liver Injury
Chen, T., Zamora, R., Zuckerbraun, B. S., & Billiar, T. R. (2003) · Current Molecular Medicine · doi:10.2174/1566524033479582 · Cited by 158
Niedbala, W., Cai, B., Liu, H., Pitman, N., Chang, L., & Liew, F. Y. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703725104 · Cited by 156
von Bülow, V., Rink, L., & Haase, H. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.7.4697 · Cited by 154
Kun, J. F., Mordmüller, B., Perkins, D. J., May, J., Mercereau‐Puijalon, O., Alpers, M., Weinberg, J. B., & Kremsner, P. G. (2001) · The Journal of Infectious Diseases · doi:10.1086/322037 · Cited by 153
The O2–producing enzyme of human neutrophils. Further properties.
BABIOR, B. M., & Peters, W. A. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69781-4 · Cited by 150
NADPH Oxidase Activity Selectively Modulates Vascular Endothelial Growth Factor Signaling Pathways
Abid, M. R., Spokes, K. C., Shih, S.-C., & Aird, W. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702175200 · Cited by 150
Kanayama, A., Inoue, J.-I., Sugita-Konishi, Y., Shimizu, M., & Miyamoto, Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110832200 · Cited by 147
Moreland, J. G., Volk, A. P. D., Bailey, G., Nauseef, W. M., & Lamb, F. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511030200 · Cited by 142
Physiology and pathophysiology of nitric oxide.
IGNARRO, L. (1996) · PubMed · Cited by 141
Selective Inhibition of Inducible Nitric Oxide Synthase Exacerbates Erosive Joint Disease
McCartney-Francis, N. L., Song, X.-Y., Mizel, D. E., & Wahl, S. M. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.4.2734 · Cited by 139
Regulation of transforming growth factor beta1 by nitric oxide.
Yoram Vodovotz, B., Chesler, L., Chong, H., Kim, S. J., Simpson, J. T., DeGraff, W., Cox, G. W., Roberts, A. B., Wink, D. A., & Barcellos‐Hoff, M. H. (1999) · PubMed · Cited by 139
Self-citationNitric oxide regulates endotoxin-induced TNF-alpha production by human neutrophils.
Dervort, A. L. V., Yan, L., Madara, P., Cobb, J. P., WESLEY, R. A., Corriveau, C. C., Tropea, M., & Danner, R. L. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.152.8.4102 · Cited by 136
HENDERSON, L. M., Chappell, J., & Jones, O. T. (1988) · PubMed · Cited by 134
Nitric Oxide, a Mediator of Inflammation, Suppresses Tumorigenesis
Hussain, S. P., Trivers, G. E., Hofseth, L. J., He, P., Shaikh, I. A., Mechanic, L. E., Doja, S., Jiang, W., Subleski, J. J., Shorts, L., et al. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-2201 · Cited by 131
The reemergence of nitric oxide and cancer
Wink, D. A., Ridnour, L. A., Hussain, S. P., & Harris, C. C. (2008) · Nitric Oxide · doi:10.1016/j.niox.2008.05.003 · Cited by 130
Self-citationExpression and Activity of Nitric Oxide Synthases in Human Airway Epithelium
Watkins, D. N., Peroni, D. J., Basclain, K., Garlepp, M. J., & Thompson, P. J. (1997) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.16.6.9191464 · Cited by 128
Reactive nitrogen intermediates suppress the primary immunologic response to Listeria
Gregory, S. H., Wing, E. J., Hoffman, R., & Simmons, R. L. (1993) · The Journal of Immunology · doi:10.4049/jimmunol.150.7.2901 · Cited by 126
Brusko, T. M., Wasserfall, C. H., Agarwal, A., Kapturczak, M., & Atkinson, M. A. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.9.5181 · Cited by 126
Du, Q., Zhang, X., Cardinal, J. S., Cao, Z., Guo, Z., Shao, L., & Geller, D. A. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-0014 · Cited by 124
Therapeutic Antioxidant Medical Gas
Nakao, A., Sugimoto, R., Billiar, T. R., & McCurry, K. R. (2009) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.08-193r · Cited by 123
The Intimate Relation Between Nitric Oxide and Superoxide in Apoptosis and Cell Survival
Brüne, B. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.497 · Cited by 122
Reactive Oxygen Species in Biological Systems
Gilbert, D. L., & Colton, C. A. (2002) · Springer eBooks · doi:10.1007/b113066 · Cited by 121
Self-citationDäubener, W., & MacKenzie, C. R. (1999) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-4709-9_64 · Cited by 121
Superoxide fluxes limit nitric oxide-induced signaling
Thomas, D. D., Ridnour, L. A., Espey, M. G., Donzelli, S., Ambs, S., Hussain, S. P., Harris, C. C., DeGraff, W., Roberts, D. D., Mitchell, J. B., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602242200 · Cited by 121
Self-citationCarbon Monoxide: To Boldly Go Where NO Has Gone Before
Ryter, S. W., Morse, D., & Choi, A. M. K. (2004) · Science s STKE · doi:10.1126/stke.2302004re6 · Cited by 120
Effect of nitric oxide on staphylococcal killing and interactive effect with superoxide
Kaplan, S. S., Lancaster, J. R., BASFORD, R. E., & Simmons, R. L. (1996) · Infection and Immunity · doi:10.1128/iai.64.1.69-76.1996 · Cited by 119
Expression of nitric oxide system in clinically evaluated cases of Alzheimer's disease
Fernández‐Vizarra, P., Fernández, A. P., Castro‐Blanco, S., Encinas, J. M., Serrano, J., Bentura, M. L., Muñoz, P., Martínez‐Murillo, R., & Rodrigo, J. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.10.010 · Cited by 115
[43] Antioxidant effects of nitric oxide
Wink, D. A., Yoram Vodovotz, B., Grisham, M. B., DeGraff, W., Cook, J. C., Pacelli, R., Krishna, M. C., & Mitchell, J. B. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)01105-2 · Cited by 109
Self-citationSchwentker, A. R., & Billiar, T. R. (2003) · Surgical Clinics of North America · doi:10.1016/s0039-6109(02)00207-4 · Cited by 109
Recent advances in arginine metabolism
Morris, S. M. (2003) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-200401000-00009 · Cited by 109
Neves-Souza, P. C., de Azeredo, E. L., Zagne, S. M., de Souza, R. V., Reis, S. R. N. I., Cerqueira, D. I., Nogueira, R. M., & Kubelka, C. F. (2005) · BMC Infectious Diseases · doi:10.1186/1471-2334-5-64 · Cited by 109
Yu, K., Mitchell, C. E., Xing, Y., Magliozzo, R. S., Bloom, B. R., & Chan, J. (1999) · Tubercle and Lung Disease · doi:10.1054/tuld.1998.0203 · Cited by 108
Reactive Oxygen Species in Biological Systems: An Interdisciplinary Approach
Daniel, L. G., & Colton, C. A. (2013) · Cited by 108
Self-citationNitric Oxide Is a Key Component in Inflammation-Accelerated Tumorigenesis
Hussain, S. P., He, P., Subleski, J. J., Hofseth, L. J., Trivers, G. E., Mechanic, L. E., Hofseth, A. B., Bernard, M., Schwank, J., Nguyen, G. H., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0410 · Cited by 108
Regulation of Human Nitric Oxide Synthase 2 Expression by Wnt β-Catenin Signaling
Du, Q., Park, K. S., Guo, Z., He, P., Nagashima, M., Shao, L., Sahai, R., Geller, D. A., & Hussain, S. P. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4110 · Cited by 107
Signal Transduction by Reactive Oxygen and Nitrogen Species: Pathways and Chemical Principles
Forman, H. J., Torrès, M., & Fukuto, J. (2003) · Springer eBooks · doi:10.1007/0-306-48412-9 · Cited by 104
Species differences in the generation of reactive oxygen species by microglia
Colton, C. A., Wilt, S. G., Gilbert, D. L., Chernyshev, O. N., Snell, J. C., & Dubois-Dalcq, M. E. (1996) · Molecular and Chemical Neuropathology · doi:10.1007/bf02815200 · Cited by 104
Self-citationRedox Regulation of Interleukin-4 Signaling
Sharma, P., Chakraborty, R., Wang, L., Min, B., Tremblay, M. L., Kawahara, T., Lambeth, J. D., & Haque, S. J. (2008) · Immunity · doi:10.1016/j.immuni.2008.07.019 · Cited by 103
Characterization and Inhibition of SARS-Coronavirus Main Protease
Liang, P. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802606776287090 · Cited by 98
Saavedra, J. E., Srinivasan, A., Bonifant, C. L., Chu, J., Shanklin, A. P., Flippen-Anderson, J. L., Rice, W. G., Turpin, J. A., Davies, K. M., & Keefer, L. K. (2001) · The Journal of Organic Chemistry · doi:10.1021/jo0016529 · Cited by 97
A Constitutive NADPH Oxidase-Like System Containing gp91phox Homologs in Human Keratinocytes
Chamulitrat, W., Stremmel, W., Kawahara, T., Rokutan, K., Fujii, H. G., Wingler, K., Schmidt, H. H. H. W., & Schmidt, R. (2004) · Journal of Investigative Dermatology · doi:10.1111/j.0022-202x.2004.22410.x · Cited by 96
Tsoyi, K., Kim, H. J., Shin, J.-S., Kim, D.-H., Cho, H. J., Lee, S. S., Ahn, S. K., Yun‐Choi, H. S., Lee, J. H., & Seo, H. G. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.06.012 · Cited by 96
Cytosolic phospholipase A2, lipoxygenase metabolites, and reactive oxygen species
Kim, C.-M., Kim, J., & Kim, J. (2008) · BMB Reports · doi:10.5483/bmbrep.2008.41.8.555 · Cited by 93
Complex Role of Heme Oxygenase-1 in Angiogenesis
Dulak, J., Łoboda, A., Zagórska, A., & Józkowicz, A. (2004) · Antioxidants and Redox Signaling · doi:10.1089/ars.2004.6.858 · Cited by 93
Hori, K., Burd, P. R., Furuke, K., Kutza, J., Weih, K. A., & Clouse, K. A. (1999) · Blood · doi:10.1182/blood.v93.6.1843.406k40_1843_1850 · Cited by 92
Perkins, D. J., & Kniss, D. A. (1999) · Journal of Leukocyte Biology · doi:10.1002/jlb.65.6.792 · Cited by 92
Antiviral action of nitric oxide on dengue virus type 2 replication
Takhampunya, R., Padmanabhan, R., & Ubol, S. (2006) · Journal of General Virology · doi:10.1099/vir.0.81880-0 · Cited by 91
Edwards, J. P., & Emens, L. A. (2010) · International Immunopharmacology · doi:10.1016/j.intimp.2010.07.002 · Cited by 91
Kupffer cell: Hepatocyte cocultures release nitric oxide in response to bacterial endotoxin
Billiar, T. R., CURRAN, R. D., Ferrari, F. K., Williams, D. L., & Simmons, R. L. (1990) · Journal of Surgical Research · doi:10.1016/0022-4804(90)90073-b · Cited by 90
Nitrosative Capacity of Macrophages Is Dependent on Nitric-oxide Synthase Induction Signals
Espey, M. G., Miranda, K. M., Pluta, R. M., & Wink, D. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.15.11341 · Cited by 89
Self-citationAnti-Adhesive Effect of Nitric Oxide on Plasmodium falciparum Cytoadherence under Flow
Serirom, S., Raharjo, W. H., Chotivanich, K., Loareesuwan, S., Kubes, P., & Ho, M. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64299-x · Cited by 88
Activation of Tumor Necrosis Factor-α-converting Enzyme-mediated Ectodomain Shedding by Nitric Oxide
Zhang, Z., Kolls, J. K., Oliver, P., Good, D. A., Schwarzenberger, P. O., Joshi, M. S., Ponthier, J. L., & Lancaster, J. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000604200 · Cited by 88
Kibbe, M. R., Tzeng, E., Gleixner, S. L., Watkins, S. C., Kovesdi, I., Lizonová, A., Makaroun, M. S., Billiar, T. R., & Rhee, R. Y. (2001) · Journal of Vascular Surgery · doi:10.1067/mva.2001.113983 · Cited by 88
Immunotherapy, Vascular Pathology, and Microhemorrhages in Transgenic Mice
Wilcock, D. M., & Colton, C. A. (2009) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152709787601858 · Cited by 86
Self-citationRole of epithelial nitric oxide in airway viral infection
Xu, W., Zheng, S., Dweik, R. A., & Erzurum, S. C. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.01.037 · Cited by 85
Maier, R., Bilbe, G., Rediske, J. J., & Lotz, M. (1994) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(94)90171-6 · Cited by 85
Hoebe, K. H. N., Witkamp, R. F., Fink‐Gremmels, J., van Miert, A. S. J. P. A. M., & Monshouwer, M. (2001) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2001.280.4.g720 · Cited by 83
Luckhart, S., Crampton, A. L., Zamora, R., Lieber, M. J., Santos, P. C. D., Peterson, T. M. L., Emmith, N., Lim, J.-H., Wink, D. A., & Yoram Vodovotz, B. (2003) · Infection and Immunity · doi:10.1128/iai.71.6.3000-3009.2003 · Cited by 82
Self-citationZhao, T., Planat‐Benard, V., Bohl, B. P., & Bokoch, G. (2003) · Journal of Clinical Investigation · doi:10.1172/jci19108 · Cited by 81
NO and TNF-α released from activated macrophages stabilize HIF-1α in resting tubular LLC-PK1 cells
Zhou, J., Fandrey, J., Schümann, J., Tiegs, G., & Brüne, B. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00294.2002 · Cited by 81
Inhibition of human arginase I by substrate and product analogues
Costanzo, L. D., Ilies, M., Thorn, K. J., & Christianson, D. W. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.02.004 · Cited by 81
Li, B., Bedard, K., Sorce, S., Hinz, B., Dubois‐Dauphin, M., & Krause, K. (2009) · Journal of Innate Immunity · doi:10.1159/000235563 · Cited by 79
Regulation of Macrophage Gene Expression by Pro- and Anti-Inflammatory Cytokines
Hamilton, T. A., Ohmori, Y., Tebo, J. M., & Kishore, R. (1999) · Pathobiology · doi:10.1159/000028101 · Cited by 79
Nitrosation by stimulated macrophages. Inhibitors, enhancers and substrates
Kosaka, H., Wishnok, J. S., Miwa, M., Leaf, C. D., & Tannenbaum, S. R. (1989) · Carcinogenesis · doi:10.1093/carcin/10.3.563 · Cited by 79
Jung, Y., LaCourse, R., Ryan, L., & North, R. J. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20021186 · Cited by 79
Maghzal, G. J., Thomas, S. R., Hunt, N. H., & Stocker, R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710266200 · Cited by 79
The polyamines: past, present and future
WALLACE, H. M. (2009) · Essays in Biochemistry · doi:10.1042/bse0460001 · Cited by 78
Jourd’heuil, D., Miranda, K. M., Kim, S. M., Espey, M. G., Yoram Vodovotz, B., Laroux, S., Mai, C. T., Miles, A. M., Grisham, M. B., & Wink, D. A. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1143 · Cited by 76
Self-citationInhibition of Cysteine Protease Activity by NO-donors
Ascenzi, P., Salvati, L., Bolognesi, M., Colasanti, M., Polticelli, F., & Venturini, G. (2001) · Current Protein and Peptide Science · doi:10.2174/1389203013381170 · Cited by 76
von Knethen, A., & Brüne, B. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.5.2619 · Cited by 75
Nussler, A. K., Silvio, M. D., Liu, Z.-Z., Geller, D. A., Freeswick, P. D., Dorko, K., Bartoli, F., & Billiar, T. R. (1995) · Hepatology · doi:10.1002/hep.1840210613 · Cited by 75
Hydrogen Peroxide Activates the SoxRS Regulon In Vivo
Manchado, M., Michán, C., & Pueyo, C. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.23.6842-6844.2000 · Cited by 74
Delledonne, M., Polverari, A., & Murgia, I. (2003) · Antioxidants and Redox Signaling · doi:10.1089/152308603321223522 · Cited by 72
Perkins, D. J., Kremsner, P. G., Schmid, D., Misukonis, M. A., Kelly, M. A., & Weinberg, J. B. (1999) · Infection and Immunity · doi:10.1128/iai.67.9.4977-4981.1999 · Cited by 68
Nuclear Factor Kappa B: A Potential Target for Anti-HIV Chemotherapy
Pande, V., & Ramos, M. J. (2003) · Current Medicinal Chemistry · doi:10.2174/0929867033457250 · Cited by 68
Forman, H. J., Torrès, M., & Fukuto, J. M. (2002) · PubMed · Cited by 67
Gyan, B. A., Troye‐Blomberg, M., Perlmann, P., & Björkman, A. (1994) · Parasite Immunology · doi:10.1111/j.1365-3024.1994.tb00362.x · Cited by 66
Nitric Oxide in Experimental Joint Inflammation
Wahl, S. M., McCartney-Francis, N. L., Chan, J. M. K., Dionne, R. A., Ta, L., & Orenstein, J. M. (2003) · Cells Tissues Organs · doi:10.1159/000070572 · Cited by 65
Mechanisms of Endogenous Nitrosation
Tannenbaum, S. R. (1988) · Springer eBooks · doi:10.1007/978-1-4757-9640-7_67 · Cited by 64
Flagged first, then by citations
1 of the 259 references couldn’t be matched to a known paper.
Research works printed but not linked: 2
- Williams, 1988, Nitrosation
- Rhee, 2000, Sci. STKE
Cited by
Sorted by citations
Role of neuroinflammation in neurodegeneration development
Zhang, W., Xiao, D., Mao, Q., & Xia, H. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01486-5 · Cited by 1,668
“At present, three types of NOS have been identified, including neuronal NOS (nNOS, also named as NOS1), endothelial NOS (eNOS, also named as NOS3), and inducible NOS (iNOS, also named as NOS2).(447) nNOS and eNOS, which are expressed constitutively, produce a low level of NO for short periods (seconds to minutes).”
BackgroundBeyond oxidative stress: an immunologist's guide to reactive oxygen species
Nathan, C., & Cunningham-Bussel, A. (2013) · Nature Reviews Immunology · doi:10.1038/nri3423 · Cited by 1,619
TNF and ROS crosstalk in inflammation
Blaser, H., Dostert, C., Mak, T. W., & Brenner, D. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.12.002 · Cited by 1,008
Nitric oxide synthase in innate and adaptive immunity: an update
Bogdan, C. (2015) · Trends in Immunology · doi:10.1016/j.it.2015.01.003 · Cited by 862
The Potential Benefits of Red Beetroot Supplementation in Health and Disease
Clifford, T., Howatson, G., West, D., & Stevenson, E. (2015) · Nutrients · doi:10.3390/nu7042801 · Cited by 635
Metadata
- Authors
- Wink, D. A., Hines, H. B., Cheng, R. Y. S., Switzer, C. H., Flores-Santana, W., Vitek, M. P., Ridnour, L. A., & Colton, C. A.
- Affiliations
- National Institutes of Health (US)
- United States Army Medical Research Institute of Infectious Diseases (US)
- Radiation Biology Branch, National Cancer Institute, National Institutes of Health , Bethesda, Maryland, USA
- Duke Medical Center (US)
- Corresponding author
- Wink, David A
- Colton, Carol A
- ORCID
- Venue
- Journal of Leukocyte Biology
- Publisher
- Oxford University Press (OUP)
- Published
- 2011-01-13
- Volume
- 89
- Issue
- 6
- Pages
- 873-891
- ISSN
- 0741-5400 (ISSN-L)
- 1938-3673
- PMC
- PMC3100761
- OpenAlex
- W2171480404
- Cited by
- 765
- References
- 259
- Citations by year
- 2026: 25 · 2025: 58 · 2024: 46 · 2023: 57 · 2022: 69 · 2021: 74 · 2020: 56 · 2019: 44 · 2018: 40 · 2017: 60 · 2016: 53 · 2015: 57 · 2014: 48 · 2013: 35 · 2012: 27
- FWCI
- 3.58
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Leukocyte Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (R01AG031845, R01AG031124)
- 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
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- nitric oxide, reactive oxygen species, reactive nitrogen species, redox signaling, immune regulation, phagosome, immunosuppression, wound healing, Th1/Th2 balance, signal transduction, pathogen eradication
- MeSH terms
- Animals, Humans, Immunity, Cellular, Nitric Oxide, Oxidation-Reduction, Signal Transduction
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