The DOI matches its Crossref record; 147 of the 147 references it cites were found in a registry or an index.
Peroxynitrite reactivity with amino acids and proteins
Abstract
Peroxynitrite, the product of the fast reaction between nitric oxide ((*)NO) and superoxide O(2)(*-) radicals, is an oxidizing and nitrating agent which is able to traverse biological membranes. The reaction of peroxynitrite with proteins occurs through three possible pathways. First, peroxynitrite reacts directly with cysteine, methionine and tryptophan residues. Second, peroxynitrite reacts fast with transition metal centers and selenium-containing amino acids. Third, secondary free radicals arising from peroxynitrite homolysis such as hydroxyl and nitrogen dioxide, and the carbonate radical formed in the presence of carbon dioxide, react with protein moieties too. Nitration of tyrosine residues is being recognized as a marker of the contribution of nitric oxide to oxidative damage. Peroxynitrite-dependent tyrosine nitration is likely to occur through the initial reaction of peroxynitrite with carbon dioxide or metal centers leading to secondary nitrating species. The preferential protein targets of peroxynitrite and the role of proteins in peroxynitrite detoxifying pathways are discussed.
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
“Interestingly, the nitroproteome appears to be quite specific, and pathological responses may be due to modification of particularly sensitive proteins, including those that regulate signaling and cell metabolism (49–52).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [49]
In the citing paper
“Interestingly, the nitroproteome appears to be quite specific, and pathological responses may be due to modification of particularly sensitive proteins, including those that regulate signaling and cell metabolism (49–52).”
From What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology (2010) · cites this paper as [49]
In the citing paper
“The protonated form of ONOO— (ONOOH, pKa = 6.5 to 6.8) decomposes rapidly to RNS, yielding approximately 28% of free •NO2 and •OH radical [123], Figure 5 down.”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [123]
In the citing paper
“Peroxynitrite and reactive species derived from it (e.g., nitrogen dioxide) are important in inflammatory responses [85] and can modulate cell signaling [87-90], in part by promoting the oxidation or nitration of a broad range of biomolecules [62].”
From Regulation of obesity and insulin resistance by nitric oxide (2014) · cites this paper as [87]
Citations
Cites
Beckman, J. S., Beckman, T. W., Chen, J., Marshall, P. A., & Freeman, B. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1620 · Cited by 7,029
Peroxynitrite oxidation of sulfhydryls.
Radí, R., Beckman, J. S., Bush, K., & Freeman, B. Α. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64313-7 · Cited by 2,492
The reaction of NO with superoxide
Huie, R. E., & Padmaja, S. (1993) · Free Radical Research Communications · doi:10.3109/10715769309145868 · Cited by 2,121
Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase
Ischiropoulos, H., Zhu, L., Chen, J., Tsai, M., Martin, J. C., Smith, C. D. L., & Beckman, J. S. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90431-u · Cited by 1,499
Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
Eiserich, J. P., Hristova, M., Cross, C. E., Jones, A. D., Freeman, B. A., Halliwell, B., & van der Vliet, A. (1998) · Nature · doi:10.1038/34923 · Cited by 1,496
Peroxynitrite, a cloaked oxidant formed by nitric oxide and superoxide
Koppenol, W. H., Moreno, J. J., Pryor, W. A., Ischiropoulos, H., & Beckman, J. S. (1992) · Chemical Research in Toxicology · doi:10.1021/tx00030a017 · Cited by 1,338
Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite
van der Vliet, A., Eiserich, J. P., Halliwell, B., & Cross, C. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.7617 · Cited by 780
MacMillan-Crow, L.-A., Crow, J. P., Kerby, J. D., Beckman, J. S., & Thompson, J. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11853 · Cited by 769
Unraveling peroxynitrite formation in biological systems
Radi, R., Peluffo, G., Alvarez, M. N., Naviliat, M., & Cayota, A. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00373-7 · Cited by 735
Inhibition of Mitochondrial Electron Transport by Peroxynitrite
Radi, R., Rodriguez, M., Castro, L., & Telleri, R. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1013 · Cited by 693
Cited by
Sorted by citations
Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390
Oxidative stress and neurodegeneration: where are we now?
Halliwell, B. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03907.x · Cited by 2,614
Reactive Species and Antioxidants. Redox Biology Is a Fundamental Theme of Aerobic Life
Halliwell, B. B. (2006) · PLANT PHYSIOLOGY · doi:10.1104/pp.106.077073 · Cited by 2,402
Human serum albumin: From bench to bedside
Fanali, G., di Masi, A., Trezza, V., Marino, M., Fasano, M., & Ascenzi, P. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.12.002 · Cited by 2,008
Altered recognition of antigen is a mechanism of CD8+ T cell tolerance in cancer
Nagaraj, S., Gupta, K., Писарев, В. М., Kinarsky, L., Sherman, S., Kang, L., Herber, D. L., Schneck, J. P., & Gabrilovich, D. I. (2007) · Nature Medicine · doi:10.1038/nm1609 · Cited by 1,176
Hydrocarbon Hydroxylation by Cytochrome P450 Enzymes
de Montellano, P. R. O. (2009) · Chemical Reviews · doi:10.1021/cr9002193 · Cited by 1,172
Clinical Relevance of Biomarkers of Oxidative Stress
Frijhoff, J., Winyard, P. G., Žarković, N., Davies, S. S., Stocker, R., Cheng, D., Knight, A. R., Taylor, E., Oettrich, J., Ruskovska, T., et al. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6317 · Cited by 918
Oxidative Stress and Neurotoxicity
Sayre, L. M., Perry, G. L., & Smith, M. A. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700210j · Cited by 884
Lenk, K., Schuler, G. C., & Adams, V. (2010) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-010-0007-1 · Cited by 498
Fundamentals on the biochemistry of peroxynitrite and protein tyrosine nitration
Bartesaghi, S., & Radi, R. (2018) · Redox Biology · doi:10.1016/j.redox.2017.09.009 · Cited by 485
Detection, identification, and quantification of oxidative protein modifications
Hawkins, C. L., & Davies, M. J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.006217 · Cited by 449
Photodynamic Therapy: Current Status and Future Directions
Benov, L. (2014) · Medical Principles and Practice · doi:10.1159/000362416 · Cited by 438
Chemistry of Peroxynitrites as Compared to Peroxynitrates
Goldstein, S., Lind, J., & Merényi, G. (2005) · Chemical Reviews · doi:10.1021/cr0307087 · Cited by 412
Maia, L. B., & Moura, J. J. G. (2014) · Chemical Reviews · doi:10.1021/cr400518y · Cited by 401
Protein tyrosine nitration—Functional alteration or just a biomarker?
Souza, J. M., Peluffo, G., & Radí, R. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.04.010 · Cited by 401
Tumor-infiltrating myeloid cells induce tumor cell resistance to cytotoxic T cells in mice
Lu, T., Ramakrishnan, R., Altiok, S., Youn, J. I., Cheng, P., Celis, E., Писарев, В. М., Sherman, S., Sporn, M. B., & Gabrilovich, D. I. (2011) · Journal of Clinical Investigation · doi:10.1172/jci45862 · Cited by 377
Melatonin and its metabolites vs oxidative stress: From individual actions to collective protection
Galano, A., & Reiter, R. J. (2018) · Journal of Pineal Research · doi:10.1111/jpi.12514 · Cited by 365
Abello, N., Kerstjens, H. A. M., Postma, D. S., & Bischoff, R. (2009) · Journal of Proteome Research · doi:10.1021/pr900039c · Cited by 359
Recent progress in the development of fluorescent probes for imaging pathological oxidative stress
Geng, Y., Wang, Z., Zhou, J., Zhu, M., Liu, J., & James, T. D. (2023) · Chemical Society Reviews · doi:10.1039/d2cs00172a · Cited by 364
Redox Signaling by Reactive Electrophiles and Oxidants
Parvez, S., Long, M. J. C., Poganik, J. R., & Aye, Y. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00698 · Cited by 372
Valderrama, R., Corpas, F. J., Carreras, A., Fernández-Ocaña, A. M., Chaki, M., Luque, F., Gómez-Rodríguez, M. V., Colmenero-Varea, P., del Río, L. A., & Barroso, J. B. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.01.006 · Cited by 350
Zeng, S., Liu, X., Kafuti, Y. S., Kim, H., Wang, J., Peng, X., Li, H., & Yoon, J. (2023) · Chemical Society Reviews · doi:10.1039/d2cs00799a · Cited by 353
van Gils, K., Hofmann, S., Boekema, B. K. H. L., Brandenburg, R., & Bruggeman, P. (2013) · Journal of Physics D Applied Physics · doi:10.1088/0022-3727/46/17/175203 · Cited by 345
Melatonin: An Established Antioxidant Worthy of Use in Clinical Trials
Korkmaz, A., Reiter, R. J., Topal, T., Manchester, L. C., Öter, Ş., & Tan, D. (2009) · Molecular Medicine · doi:10.2119/molmed.2008.00117 · Cited by 319
What Part of NO Don't You Understand? Some Answers to the Cardinal Questions in Nitric Oxide Biology
Hill, B. G., Dranka, B. P., Bailey, S. M., Lancaster, J. R., & Darley-Usmar, V. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.101618 · Cited by 310
Peyrot, F., & Ducrocq, C. (2008) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2008.00580.x · Cited by 292
Role of oxidative stress and nitric oxide in atherothrombosis
Lubos, E. (2008) · Frontiers in bioscience · doi:10.2741/3084 · Cited by 296
Sadiq, I. Z. (2021) · Current Molecular Medicine · doi:10.2174/1566524022666211222161637 · Cited by 293
Galano, A., & Alvarez-Idaboy, J. R. (2018) · International Journal of Quantum Chemistry · doi:10.1002/qua.25665 · Cited by 287
Regulation of obesity and insulin resistance by nitric oxide
Sansbury, B. E., & Hill, B. G. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.05.016 · Cited by 274
“nitrogen dioxide) are important in inflammatory responses [85] and can modulate cell signaling [87–90], in part by promoting the”
BackgroundActivatable Photoacoustic Nanoprobes for In Vivo Ratiometric Imaging of Peroxynitrite
Zhang, J., Xu, Z. J., Upputuri, P. K., Pramanik, M., Chen, P., & Pu, K. (2016) · Advanced Materials · doi:10.1002/adma.201604764 · Cited by 273
Redox Proteomics: Chemical Principles, Methodological Approaches and Biological/Biomedical Promises
Bachi, A., Dalle‐Donne, I., & Scaloni, A. (2012) · Chemical Reviews · doi:10.1021/cr300073p · Cited by 265
Ahsan, H. (2013) · Human Immunology · doi:10.1016/j.humimm.2013.06.009 · Cited by 269
de Azevedo, M. I., Pereira, A. F., Nogueira, R. B., Rolim, F. E., Brito, G. A., Wong, D. V. T., Lima‐Júnior, R. C. P., Ribeiro, R. D. A., & Vale, M. L. (2013) · Molecular Pain · doi:10.1186/1744-8069-9-53 · Cited by 254
Chemical Design of Activatable Photoacoustic Probes for Precise Biomedical Applications
Liu, Y., Teng, L., Yin, B., Meng, H., Yin, X., Huan, S., Song, G., & Zhang, X. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00875 · Cited by 250
Barroso, J. B. (2006) · Journal of Experimental Botany · doi:10.1093/jxb/erj175 · Cited by 254
Kaushal, V., Koeberle, P. D., Wang, Y., & Schlichter, L. C. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3593-06.2007 · Cited by 235
Age-related muscle dysfunction
Thompson, L. V. (2009) · Experimental Gerontology · doi:10.1016/j.exger.2008.05.003 · Cited by 226
Resveratrol and Brain Mitochondria: a Review
Jardim, F. R., de Rossi, F. T., Nascimento, M. X., Barros, R. G. D. S., Borges, P. A., Prescilio, I. C., & de Oliveira, M. R. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0448-z · Cited by 225
Environmental pollutants and lifestyle factors induce oxidative stress and poor prenatal development
Al-Gubory, K. H. (2014) · Reproductive BioMedicine Online · doi:10.1016/j.rbmo.2014.03.002 · Cited by 222
Oxidative stress and antioxidant therapy in cystic fibrosis
Galli, F., Battistoni, A., Gambari, R., Alfonso Pompella, C., Bragonzi, A., Pilolli, F., Iuliano, L., Piroddi, M., Dechecchi, M. C., & Cabrini, G. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.012 · Cited by 223
Nitric Oxide in Cell Survival: A Janus Molecule
Calabrese, V., Cornelius, C., Rizzarelli, E., Owen, J. B., Dinkova‐Kostova, A. T., & Butterfield, D. A. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2721 · Cited by 198
Zhang, J., Xu, Z. J., Zeng, J., & Pu, K. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b01879 · Cited by 195
Reactive Oxygen Species and Their Involvement in Red Blood Cell Damage in Chronic Kidney Disease
Gwoździński, K., Pieniążek, A., & Gwoździński, Ł. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6639199 · Cited by 204
Phagocyte-derived reactive species: salvation or suicide?
Halliwell, B. B. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.07.005 · Cited by 192
Principles in Redox Signaling: From Chemistry to Functional Significance
Bindoli, A., & Rigobello, M. P. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4655 · Cited by 194
Protein tyrosine nitration in pea roots during development and senescence
Begara-Morales, J. C., Chaki, M., Sánchez-Calvo, B., Mata-Pérez, C., Leterrier, M., Palma, J. M., Barroso, J. B., & Corpas, F. J. (2013) · Journal of Experimental Botany · doi:10.1093/jxb/ert006 · Cited by 179
Protein targets of tyrosine nitration in sunflower (Helianthus annuus L.) hypocotyls
Chaki, M., Valderrama, R., Fernández-Ocaña, A. M., Carreras, A., López-Jaramillo, J., Luque, F., Palma, J. M., Pedrajas, J. R., Begara-Morales, J. C., Sánchez-Calvo, B., et al. (2009) · Journal of Experimental Botany · doi:10.1093/jxb/erp263 · Cited by 183
Karimi, M., Ignasiak, M. T., Chan, B., Croft, A. K., Radom, L., Schiesser, C. H., Pattison, D. I., & Davies, M. J. (2016) · Scientific Reports · doi:10.1038/srep38572 · Cited by 175
The role of S-nitrosoglutathione reductase (GSNOR) in human disease and therapy
Barnett, S. D., & Buxton, I. L. O. (2017) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2017.1304353 · Cited by 175
Begara-Morales, J. C., Sánchez-Calvo, B., Chaki, M., Mata-Pérez, C., Valderrama, R., Padilla, M. N., López-Jaramillo, J., Luque, F., Corpas, F. J., & Barroso, J. B. (2015) · Journal of Experimental Botany · doi:10.1093/jxb/erv306 · Cited by 172
A Three-Channel Fluorescent Probe That Distinguishes Peroxynitrite from Hypochlorite
Zhang, Q., Zhu, Z., Zheng, Y., Cheng, J., Zhang, N., Long, Y., Zheng, J. L., Qian, X. H., & Yang, Y. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305046u · Cited by 171
de Souza, C. G., Moreira, J. D., Siqueira, I. R., Pereira, A. G., Rieger, D. K., Souza, D. O., Souza, T. M. E., Portela, L. V., & Perry, M. L. S. (2007) · Life Sciences · doi:10.1016/j.lfs.2007.05.001 · Cited by 168
Redox Proteomics in Selected Neurodegenerative Disorders: From Its Infancy to Future Applications
Butterfield, D. A., Marzia Perluigi, A., Reed, T. T., Muharib, T., Hughes, C. P., Robinson, R. A. S., & Rukhsana Sultana, A. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4109 · Cited by 171
Use of Fluorescence Probes for Detection of Reactive Nitrogen Species: A Review
Gomes, A. S., Fernandes, E. G. R., & Lima, J. L. F. C. (2006) · Journal of Fluorescence · doi:10.1007/s10895-005-0030-3 · Cited by 165
The proteasome and its role in the degradation of oxidized proteins
Jung, T., & Grune, T. (2008) · IUBMB Life · doi:10.1002/iub.114 · Cited by 162
van Golen, R. F., Reiniers, M. J., Olthof, P. B., van Gulik, T. M., & Heger, M. (2012) · Journal of Gastroenterology and Hepatology · doi:10.1111/jgh.12072 · Cited by 165
Peroxynitrite formation and function in plants
Vandelle, E., & Delledonne, M. (2011) · Plant Science · doi:10.1016/j.plantsci.2011.05.002 · Cited by 170
Bishayee, A., Barnes, K. F., Bhatia, D., Darvesh, A. S., & Carroll, R. T. (2010) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-09-0171 · Cited by 161
Kinetic and mechanistic considerations to assess the biological fate of peroxynitrite
Carballal, S., Bartesaghi, S., & Radí, R. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.07.005 · Cited by 162
Tompkins, A. J., Burwell, L. S., Digerness, S. B., Zaragoza, C., Holman, W. L., & Brookes, P. S. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2005.10.001 · Cited by 162
Ehrenshaft, M., Deterding, L. J., & Mason, R. P. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.08.003 · Cited by 158
Targeted contrast agents and activatable probes for photoacoustic imaging of cancer
Zhao, Z., Swartchick, C. B., & Chan, J. (2022) · Chemical Society Reviews · doi:10.1039/d0cs00771d · Cited by 155
Chirino, Y. I., Hernández‐Pando, R., & Pedraza‐Chaverrí, J. (2004) · BMC Pharmacology · doi:10.1186/1471-2210-4-20 · Cited by 149
Amyloid β-Induced Nerve Growth Factor Dysmetabolism in Alzheimer Disease
Bruno, M. A., León, W., Fragoso, G., Mushynski, W. E., Almazán, G., & Cuello, A. C. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181aed9e6 · Cited by 152
Peroxynitrite and drug-dependent toxicity
Denicola, A., & Radí, R. (2004) · Toxicology · doi:10.1016/j.tox.2004.11.023 · Cited by 145
The Role of Reactive Species on Innate Immunity
Andrés, C., Pérez de la Lastra, J., Juan, C., Plou, F., & Pérez-Lebeña, E. (2022) · Vaccines · doi:10.3390/vaccines10101735 · Cited by 142
Singh, I. N., Sullivan, P. G., & Hall, E. D. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21360 · Cited by 142
Chokshi, N. K., Guner, Y. S., Hunter, C. J., Upperman, J. S., Grishin, A., & Ford, H. R. (2008) · Seminars in Perinatology · doi:10.1053/j.semperi.2008.01.002 · Cited by 137
McCarty, M. F. (2007) · Medical Hypotheses · doi:10.1016/j.mehy.2006.12.069 · Cited by 137
Hyperglycemic Stress and Carbon Stress in Diabetic Glucotoxicity
Luo, X., Wu, J., Jing, S., & Yan, L. (2016) · Aging and Disease · doi:10.14336/ad.2015.0702 · Cited by 145
Buonocore, G., & Groenendaal, F. (2007) · Seminars in Fetal and Neonatal Medicine · doi:10.1016/j.siny.2007.01.020 · Cited by 137
Validation of protein carbonyl measurement: A multi-centre study
Augustyniak, E., Adam, A., Wojdyla, K., Rogowska-Wrzesinska, A., Willetts, R., Korkmaz, A., Atalay, M., Weber, D., Grune, T., Borsa, C., et al. (2015) · Redox Biology · doi:10.1016/j.redox.2014.12.014 · Cited by 135
Metal ions and oxidative protein modification in neurological disease.
Sayre, L. M., Moreira, P. I., Smith, M. A., & Perry, G. L. (2005) · PubMed · Cited by 135
Chinta, S. J., & Andersen, J. K. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.08.002 · Cited by 134
Galano, A. (2017) · Journal of the Mexican Chemical Society · doi:10.29356/jmcs.v59i4.81 · Cited by 136
Fundamental mechanisms of the cell death caused by Nitrosative stress
Wang, F., Yuan, Q., Chen, F., Pang, J., Pan, C., Xu, F., & Chen, Y. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.742483 · Cited by 133
Begara-Morales, J. C., Sánchez-Calvo, B., Luque, F., Leyva‐Pérez, M. D. L. O., Leterrier, M., Corpas, F. J., & Barroso, J. B. (2014) · Plant and Cell Physiology · doi:10.1093/pcp/pcu044 · Cited by 133
Reiniers, M. J., van Golen, R. F., van Gulik, T. M., & Heger, M. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5486 · Cited by 134
Role for Nucleotide Excision Repair in Virulence of Mycobacterium tuberculosis
Darwin, K. H., & Nathan, C. (2005) · Infection and Immunity · doi:10.1128/iai.73.8.4581-4587.2005 · Cited by 129
Tórtora, V., Quijano, C., Freeman, B. Α., Radí, R., & Castro, L. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.01.007 · Cited by 129
Houée-Lévin, C., Bobrowski, K., Horakova, L., Karademir, B., Schöneich, C., Davies, M. J., & Spickett, C. M. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1007968 · Cited by 126
A Key Role for Redox Signaling in Rapid P2X7 Receptor-Induced IL-1β Processing in Human Monocytes
Hewinson, J., Moore, S., Glover, C., Watts, A. G., & Mackenzie, A. B. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.12.8410 · Cited by 123
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
Sharov, V. S., Dremina, E. S., Galeva, N. A., Williams, T. D., & Schöneich, C. (2006) · Biochemical Journal · doi:10.1042/bj20051214 · Cited by 121
Kolbert, Z., Feigl, G., Bordé, Á., Molnár, Á., & Erdei, L. (2017) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2017.01.028 · Cited by 120
Mitochondrial protection after traumatic brain injury by scavenging lipid peroxyl radicals
Mustafa, A., Singh, I. N., Wang, J. A., Carrico, K. M., & Hall, E. D. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06749.x · Cited by 119
Rossi, M. A., Celes, M. R. N., Prado, C. M., & Saggioro, F. P. (2006) · Shock · doi:10.1097/01.shk.0000235141.05528.47 · Cited by 119
Ahmad, R., Rasheed, Z., & Ahsan, H. (2009) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923970802709197 · Cited by 118
Sickle cell anemia and vascular dysfunction: The nitric oxide connection
Akinsheye, I., & Klings, E. S. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22195 · Cited by 120
Uremic Toxins and Their Relation with Oxidative Stress Induced in Patients with CKD
Pieniążek, A., Bernasinska-Slomczewska, J., & Gwoździński, Ł. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126196 · Cited by 116
A Bioluminescent Probe for Imaging Endogenous Peroxynitrite in Living Cells and Mice
Li, J., Chen, L., Wang, Q., Liu, H., Hu, X., Yuan, L., & Zhang, X. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b00198 · Cited by 115
Effects of macrophage inducible nitric oxide synthase in murine septic lung injury
Farley, K., Wang, L. F., Razavi, H. M., Law, C., Rohan, M., McCormack, D. G., & Mehta, S. (2006) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00248.2005 · Cited by 114
Nitric oxide-matrix metaloproteinase-9 interactions: Biological and pharmacological significance
O’Sullivan, S., Medina, C., Ledwidge, M. T., Radomski, M. W., & Gilmer, J. F. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.12.006 · Cited by 117
Butterfield, D. A., Domenico, F. D., Swomley, A. M., Head, E., & Marzia Perluigi, A. (2014) · Biochemical Journal · doi:10.1042/bj20140772 · Cited by 112
The key reactive species in the bactericidal process of plasma activated water
Ma, M., Zhang, Y., Lv, Y., & Sun, F. (2020) · Journal of Physics D Applied Physics · doi:10.1088/1361-6463/ab703a · Cited by 111
Oxidative stress in neurodegeneration and available means of protection
Fatokun, A. A. (2008) · Frontiers in bioscience · doi:10.2741/2926 · Cited by 105
Factors Affecting the Formation and Treatment of Thrombosis by Natural and Synthetic Compounds
Lichota, A., Szewczyk, E. M., & Gwoździński, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21217975 · Cited by 108
A Lanthanide‐Complex‐Based Ratiometric Luminescent Probe Specific for Peroxynitrite
Song, C., Ye, Z., Wang, G., Yuan, J., & Guan, Y. (2010) · Chemistry - A European Journal · doi:10.1002/chem.201000528 · Cited by 103
Inflammatory signaling in NEC: Role of NF-κB, cytokines and other inflammatory mediators
Hunter, C. J., & Plaen, I. G. D. (2014) · Pathophysiology · doi:10.1016/j.pathophys.2013.11.010 · Cited by 101
Metadata
- Authors
- Alvarez, B., & Radi, R.
- Venue
- Amino Acids
- Published
- 2003-09-26
- Volume
- 25
- Issue
- 3-4
- Pages
- 295-311
- ISSN
- 0939-4451 (ISSN-L)
- 1438-2199
- OpenAlex
- W2141352921
- Cited by
- 560
- References
- 147
- Citations by year
- 2026: 9 · 2025: 9 · 2024: 15 · 2023: 18 · 2022: 23 · 2021: 24 · 2020: 14 · 2019: 16 · 2018: 19 · 2017: 25 · 2016: 31 · 2015: 27 · 2014: 44 · 2013: 28 · 2012: 22
- FWCI
- 7.01
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Amino Acids (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- peroxynitrite, nitric oxide, superoxide, protein oxidation, protein nitration, tyrosine nitration, cysteine, methionine, tryptophan, transition metal centers, selenium-containing amino acids, hydroxyl radicals, nitrogen dioxide, carbonate radical, oxidative damage
- MeSH terms
- Amino Acids, Animals, Antioxidants, Cytosol, Free Radicals, Humans, Models, Chemical, Nitric Oxide, Oxidation-Reduction, Proteins, Superoxides, Molecular Structure, Peroxynitrous Acid
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