The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
Proteomic method identifies proteins nitrated in vivo during inflammatory challenge
Open accessAbstract
Inflammation in asthma, sepsis, transplant rejection, and many neurodegenerative diseases associates an up-regulation of NO synthesis with increased protein nitration at tyrosine. Nitration can cause protein dysfunction and is implicated in pathogenesis, but few proteins that appear nitrated in vivo have been identified. To understand how this modification impacts physiology and disease, we used a proteomic approach toward targets of protein nitration in both in vivo and cell culture inflammatory disease models. This approach identified more than 40 nitrotyrosine-immunopositive proteins, including 30 not previously identified, that became modified as a consequence of the inflammatory response. These targets include proteins involved in oxidative stress, apoptosis, ATP production, and other metabolic functions. Our approach provides a means toward obtaining a comprehensive view of the nitroproteome and promises to broaden understanding of how NO regulates cellular processes.
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
“Although a growing number of proteins have now been shown to be nitrated, multiple studies have shown that nitration is a selective process (47, 484).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [47]
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 [52]
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 [52]
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 [90]
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
Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly
Beckman, J. S., & Koppenol, W. H. (1996) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1996.271.5.c1424 · Cited by 5,513
Mitochondrial diseases in man and mouse
Wallace, D. C. (1999) · Science · doi:10.1126/science.283.5407.1482 · Cited by 3,060
Protein S-nitrosylation: a physiological signal for neuronal nitric oxide
Jaffrey, S. R., Erdjument‐Bromage, H., Ferris, C. D., Tempst, P., & Snyder, S. H. (2001) · Nature Cell Biology · doi:10.1038/35055104 · Cited by 1,402
Mitochondrial abnormalities in Alzheimer's disease
Hirai, K., Aliev, G., Nunomura, A., Fujioka, H., Russell, R. L., Atwood, C. S., Johnson, A. B., Kress, Y., Vinters, H. V., Tabaton, M., et al. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-09-03017.2001 · Cited by 1,367
Oxidative Phosphorylation at the fin de siècle
Saraste, M. (1999) · Science · doi:10.1126/science.283.5407.1488 · Cited by 1,345
Ischiropoulos, H. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0755 · Cited by 1,025
Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
Oda, Y., Nagasu, T., & Chait, B. T. (2001) · Nature Biotechnology · doi:10.1038/86783 · Cited by 777
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
Flagged first, then by citations
Research works printed but not linked: 4
- H H W Schmidt Biochemica 2, 22 (1995).
- West K. A. Yan L. Miyagi M. Crabb J. S. Murmorstein A. D. Murmorstein L. & Crabb J. W. (2001) Exp. Eye Res. in press.
- M Zou, C Martin, V Ullrich Biol Chem Hoppe-Seyler 378, 707–713 (1997).
- D P Buchczyk, K Briviba, F U Hartl, H Sies Biol Chem Hoppe-Seyler 381, 121–126 (2000).
Cited by
Sorted by citations
Items 101–200 of 350
The oxidative damage theory of aging
Lin, M. T., & Flint Beal, M. (2003) · Clinical Neuroscience Research · doi:10.1016/s1566-2772(03)00007-0 · Cited by 89
Perrelli, A., Goitre, L., Salzano, A. M., Moglia, A., Scaloni, A., & Retta, S. F. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/6015351 · Cited by 93
Heijnen, H. F. G., van Donselaar, E. G., Slot, J. W., Fries, D. M., Blanchard-Fillion, B., Hodara, R., Lightfoot, R. T., Polydoro, M., Spielberg, D., Thomson, L., et al. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.09.006 · Cited by 89
Kehoe, J. W., Velappan, N., Walbolt, M., Rasmussen, J., King, D., Lou, J., Knopp, K. A., Pavlik, P., Marks, J. D., Bertozzi, C. R., et al. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600314-mcp200 · Cited by 87
Starr, M. E., Ueda, J., Yamamoto, S., Evers, B. M., & Saito, H. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.11.013 · Cited by 86
Görg, B., Wettstein, M., Metzger, S. U., Schliess, F., & Häussinger, D. (2005) · Hepatology · doi:10.1002/hep.20662 · Cited by 86
Role 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
Mass spectrometry of protein modifications by reactive oxygen and nitrogen species
Schöneich, C., & Sharov, V. S. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.08.013 · Cited by 88
Predonzani, A. (2015) · World Journal of Experimental Medicine · doi:10.5493/wjem.v5.i2.64 · Cited by 83
Strategies for shotgun identification of post-translational modifications by mass spectrometry
Cantin, G. T., & YATESIII, J. (2004) · Journal of Chromatography A · doi:10.1016/s0021-9673(04)00971-9 · Cited by 84
Proteomics and systems biology approaches to signal transduction in sepsis
Nguyen, A., & Yaffe, M. B. (2003) · Critical Care Medicine · doi:10.1097/00003246-200301001-00001 · Cited by 82
Proteomic analysis of phosphorylation, oxidation and nitrosylation in signal transduction
Spickett, C. M., Pitt, A. R., Morrice, N. A., & Kölch, W. (2006) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2006.09.013 · Cited by 82
Pathophysiological functions of nitric oxide-mediated protein modifications
Ischiropoulos, H., & Gow, A. J. (2004) · Toxicology · doi:10.1016/j.tox.2004.11.018 · Cited by 83
Brookes, P. S., & Darley-Usmar, V. M. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00742.2003 · Cited by 77
Vassilakopoulos, T., Deckman, G., Kebbewar, M., Rallis, G., Harfouche, R., & Hussain, S. N. A. (2003) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00270.2002 · Cited by 75
Selective Nitration of Histone Tyrosine Residues in Vivo in Mutatect Tumors
Haqqani, A. S., Kelly, J. F., & Birnboim, H. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m105730200 · Cited by 75
Shibuya, A., Wada, K., Nakajima, A., Saeki, M., Katayama, K., Mayumi, T., Kadowaki, T., Niwa, H., & Kamisaki, Y. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03059-4 · Cited by 74
Mitochondrial proteomics in free radical research
Bailey, S. M., Landar, A. L., & Darley-Usmar, V. M. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.10.011 · Cited by 73
Nitric oxide signalling via cytoskeleton in plants
Yemets, A. I., Krasylenko, Y. A., Lytvyn, D. I., Sheremet, Y. A., & Blume, Y. B. (2011) · Plant Science · doi:10.1016/j.plantsci.2011.04.017 · Cited by 74
Fries, D. M., Paxinou, E., Themistocleous, M. S., Swanberg, E., Griendling, K. K., Salvemini, D., Slot, J. W., Heijnen, H. F. G., Hazen, S. L., & Ischiropoulos, H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210806200 · Cited by 72
Coumarins from Angelica decursiva inhibit α-glucosidase activity and protein tyrosine phosphatase 1B
Ali, M. Y., Jannat, S., Jung, H. A., Jeong, H. O., Chung, H. Y., & Choi, J. S. (2016) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2016.04.020 · Cited by 72
Impact of Reactive Species on Amino Acids—Biological Relevance in Proteins and Induced Pathologies
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214049 · Cited by 71
Sanctis, F. D., Sandri, S., Ferrarini, G., Pagliarello, I., Sartoris, S., Ugel, S., Marigo, I., Molon, B., & Bronte, V. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00069 · Cited by 74
Proteomics in Pulmonary Medicine
Bowler, R. P., Ellison, M. C., & Reisdorph, N. A. (2006) · CHEST Journal · doi:10.1378/chest.130.2.567 · Cited by 70
Han, F., Shirasaki, Y., & Fukunaga, K. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04048.x · Cited by 69
Distler, A. M., Kerner, J., & Hoppel, C. L. (2007) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.03.012 · Cited by 69
How post-translational modifications influence the biological activity of chemokines
Vanheule, V., Metzemaekers, M., Janssens, R., Struyf, S., & Proost, P. (2018) · Cytokine · doi:10.1016/j.cyto.2018.02.026 · Cited by 76
Modulation of human T‐cell functions by reactive nitrogen species
Kasic, T., Colombo, P., Soldani, C., Wang, C. M., Miranda, E., Roncalli, M. G., Bronte, V., & Viola, A. (2011) · European Journal of Immunology · doi:10.1002/eji.201040868 · Cited by 68
Ali, M. Y., Kim, D., Seong, S. H., Kim, H., Jung, H. A., & Choi, J. S. (2017) · Marine Drugs · doi:10.3390/md15120368 · Cited by 68
Kharitonov, S. A., & Barnes, P. J. (2004) · Proceedings of the American Thoracic Society · doi:10.1513/pats.200402-011ms · Cited by 68
Mechanistic studies of the immunochemical termination of self-tolerance with unnatural amino acids
Grünewald, J., Hunt, G. S., Dong, L., Niessen, F., Wen, B. G., Tsao, M., Perera, R., Kang, M., Laffitte, B. A., Azarian, S. M., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900507106 · Cited by 67
Dynamic Characterization of the Molecular Events During In Vitro Epidermal Wound Healing
Rezzonico, R., Yeow, K., Loubat, A., Ferruà, B., Le'Negrate, G., Turchi, L., Chassot, A., Ortonne, J. P., & Ponzio, G. (2002) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2002.01805.x · Cited by 67
Tyrosine Nitration Impairs Mammalian Aldolase A Activity
Koeck, T., Levison, B. S., Hazen, S. L., Crabb, J. W., Stuehr, D. J., & Aulak, K. S. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m300141-mcp200 · Cited by 68
Self-citationModifications of proteins by 4-hydroxy-2-nonenal in the ventilatory muscles of rats
Hussain, S. N. A., Matar, G., Barreiro, E., Florian, M., Divangahi, M., & Vassilakopoulos, T. P. (2006) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00337.2005 · Cited by 66
Deficiency of Lung Antioxidants in Idiopathic Pulmonary Arterial Hypertension
Masri, F. A., COMHAIR, S. A. A., Dostanic‐Larson, I., Kaneko, F. T., Dweik, R. A., Arroliga, A. C., & ERZURUM, S. C. (2008) · Clinical and Translational Science · doi:10.1111/j.1752-8062.2008.00035.x · Cited by 63
Reactive Nitrogen Species and Cell Signaling: Implications for Death or Survival of Lung Epithelium
Janssen-Heininger, Y. M. W., Persinger, R. L., Korn, S. H., Pantano, C., McElhinney, B., Reynaert, N. L., LANGEN, R. C. J., Ckless, K., Shrivastava, P., & Poynter, M. E. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.2206008 · Cited by 64
Site-Specific Quantitation of Protein Nitration Using Liquid Chromatography/Tandem Mass Spectrometry
Willard, B. B., Ruse, C. I., Keightley, J. A., Bond, M., & Kinter, M. T. (2003) · Analytical Chemistry · doi:10.1021/ac034033j · Cited by 61
Proteomic analysis of protein nitration in rat cerebellum: effect of biological aging
Gokulrangan, G., Zaidi, A., Michaelis, M. L., & Schöneich, C. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04334.x · Cited by 61
Peroxynitrite inactivates human‐tissue inhibitor of metalloproteinase‐4
Donnini, S., Monti, M., Roncone, R., Morbidelli, L., Rocchigiani, M., Oliviero, S., Casella, L., Giachetti, A., Schulz, R., & Ziche, M. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.02.080 · Cited by 60
Protein Tyrosine Nitration in the Ventilatory Muscles
Barreiro, E., Comtois, A. S., Gea, J., Laubach, V. E., & Hussain, S. N. A. (2002) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.26.4.4634 · Cited by 60
Zhang, Y., Huang, Y., Deng, X., Xu, Y., Gao, Z., & Li, H. (2012) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2012.01.010 · Cited by 59
Targeting the NO/superoxide ratio in adipose tissue: relevance to obesity and diabetes management
Janković, A., Korać, A., Buzadžić, B., Stančić, A., Otašević, V., Ferdinándy, P., Daiber, A., & Korać, B. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13498 · Cited by 60
Protein Database, Human Retinal Pigment Epithelium
West, K. A., Yan, L., Shadrach, K. G., Jian, S., Hasan, A., Miyagi, M., Crabb, J. S., Hollyfield, J. G., Marmorstein, A. D., & Crabb, J. W. (2003) · Molecular & Cellular Proteomics · doi:10.1074/mcp.d200001-mcp200 · Cited by 60
Self-citationProtective Effect of Metalloporphyrins against Cisplatin-Induced Kidney Injury in Mice
Pan, H., Shen, K., Wang, X., Meng, H., Wang, C., & Jin, B. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086057 · Cited by 58
Jung, H. A., Ali, M. Y., Bhakta, H. K., Min, B.-S., & Choi, J. S. (2016) · Archives of Pharmacal Research · doi:10.1007/s12272-016-0852-3 · Cited by 58
Choi, J. S., Ali, M. Y., Jung, H. A., Oh, S. H., Choi, R. J., & Kim, E. J. (2015) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2015.05.020 · Cited by 57
Mass spectrometry analysis of nitrotyrosine‐containing proteins
Zhan, X., Wang, X., & Desiderio, D. M. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21413 · Cited by 56
Lee, K. K., & Boelsterli, U. A. (2014) · Redox Biology · doi:10.1016/j.redox.2014.03.003 · Cited by 57
Proteomics of mitochondrial inner and outer membranes
Distler, A. M., Kerner, J., & Hoppel, C. L. (2008) · PROTEOMICS · doi:10.1002/pmic.200800102 · Cited by 57
Nín, N., Cassina, A., Boggia, J. G., Alfonso, E., Botti, H., Peluffo, G., Trostchansky, A., Batthyány, C., Radí, R., Rubbo, H., et al. (2004) · Intensive Care Medicine · doi:10.1007/s00134-004-2427-x · Cited by 56
Hardy, L., Wick, D. A., & Webb, J. R. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.9.5956 · Cited by 56
Hsieh, C.-C., & Papaconstantinou, J. (2002) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(02)00084-2 · Cited by 55
Tuning cancer fate: the unremitting role of host immunity
Calì, B., Molon, B., & Viola, A. (2017) · Open Biology · doi:10.1098/rsob.170006 · Cited by 58
Protein modification in aging: An update
Schöneich, C. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.07.002 · Cited by 54
Filipović, M. R., Stanić-Vučinić, D., Raicevic, S., Spasić, M. B., & Niketić, V. (2006) · Free Radical Research · doi:10.1080/10715760600944296 · Cited by 52
Unveiling the human nitroproteome: Protein tyrosine nitration in cell signaling and cancer
Griswold‐Prenner, I., Kashyap, A. K., Mazhar, S., Hall, Z. W., Fazelinia, H., & Ischiropoulos, H. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105038 · Cited by 52
Shrivastava, P., Pantano, C., Watkin, R., McElhinney, B., Guala, A. S., Poynter, M. E., Persinger, R. L., Budd, R. C., & Janssen-Heininger, Y. M. W. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.15.6763-6772.2004 · Cited by 53
Stanyer, L., Jørgensen, W., Hori, O., Clark, J. B., & Heales, S. (2008) · Neurochemistry International · doi:10.1016/j.neuint.2008.06.004 · Cited by 51
Okunuki, Y., Usui, Y., Takeuchi, M., Kezuka, T., Hattori, T., Masuko, K., Nakamura, H., Yudoh, K., Usui, M., Nishioka, K., et al. (2007) · Experimental Eye Research · doi:10.1016/j.exer.2007.01.003 · Cited by 51
Poggioli, S., Bakala, H., & Friguet, B. (2002) · Experimental Gerontology · doi:10.1016/s0531-5565(02)00145-6 · Cited by 51
Cappelletti, G. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(03)00209-x · Cited by 50
The nitration of proteins in platelets: significance in platelet function
Sabetkar, M., Low, S. Y., Naseem, K. M., & Bruckdorfer, K. R. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00890-0 · Cited by 50
Tubulin tyrosine nitration regulates microtubule organization in plant cells
Blume, Y. B., Krasylenko, Y. A., Demchuk, O. M., & Yemets, A. I. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00530 · Cited by 53
Han, Z., Chen, Y., Jones, C. I., Meenakshisundaram, G., Zweier, J. L., & Alevriadou, B. R. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00389.2006 · Cited by 50
Kański, J., & Schöneich, C. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)96016-3 · Cited by 48
Söderling, A., Ryberg, H., Gabrielsson, A., Lärstad, M., Torén, K., Niari, S., & Caidahl, K. (2003) · Journal of Mass Spectrometry · doi:10.1002/jms.543 · Cited by 48
Vasilaki, A., Simpson, D. M., McArdle, F., McLean, L., Beynon, R. J., Remmen, H. V., Richardson, A. G., McArdle, A., Faulkner, J. A., & Jackson, M. J. (2007) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.200600702 · Cited by 48
Chemical labeling and enrichment of nitrotyrosine-containing peptides
Abello, N., Barroso, B., Kerstjens, H. A. M., Postma, D. S., & Bischoff, R. (2009) · Talanta · doi:10.1016/j.talanta.2009.02.002 · Cited by 47
Role of nitric oxide and its metabolites as potential markers in lung cancer
Masri, F. A. (2010) · Annals of Thoracic Medicine · doi:10.4103/1817-1737.65036 · Cited by 47
Post-translational Tyrosine Nitration of Eosinophil Granule Toxins Mediated by Eosinophil Peroxidase
Ulrich, M., Petre, A., Youhnovski, N., Prömm, F., Schirle, M., Schumm, M., Pero, R. S., Doyle, A. D., Checkel, J. L., Kita, H., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801196200 · Cited by 48
Chen, H. C., & Chen, Y.-C. (2012) · Analytical Chemistry · doi:10.1021/ac301597r · Cited by 47
Fibulin-4 Is a Target of Autoimmunity Predominantly in Patients with Osteoarthritis
Xiang, Y., Sekine, T., Nakamura, H., Imajoh‐Ohmi, S., Fukuda, H., Yudoh, K., Masuko, K., Nishioka, K., & Kato, T. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.5.3196 · Cited by 46
Bruemmer, K. J., Merrikhihaghi, S., Lollar, C., Morris, S. N. S., Bauer, J. H., & Lippert, A. R. (2014) · Chemical Communications · doi:10.1039/c4cc04292a · Cited by 44
Yadav, S., David, A., Baluška, F., & Bhatla, S. C. (2013) · Plant Signaling & Behavior · doi:10.4161/psb.23196 · Cited by 44
Nitrotyrosine‐modified proteins and oxidative stress induced by diesel exhaust particles
Xiao, G. G., Nel, A. E., & Loo, J. A. (2004) · Electrophoresis · doi:10.1002/elps.200406145 · Cited by 44
RACK1/Asc1p, a Ribosomal Node in Cellular Signaling
Rachfall, N., Schmitt, K., Bandau, S., Smolinski, N., Ehrenreich, A., Valerius, O., & Braus, G. H. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.017277 · Cited by 43
Role of Peroxynitrite in the Cardiovascular Dysfunction of Septic Shock
Liaudet, L., Rosenblatt‐Velin, N., & Pacher, P. (2013) · Current Vascular Pharmacology · doi:10.2174/1570161111311020009 · Cited by 43
Measurement and Significance of 3‐Nitrotyrosine in Systemic Lupus Erythematosus
Khan, F. H., Siddiqui, A. A., & Ali, R. (2006) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.2006.01794.x · Cited by 43
Tazawa, H., Tatemichi, M., Sawa, T., Gilibert, I., Ma, N., Hiraku, Y., Donehower, L. A., Ohgaki, H., Kawanishi, S., & Ohshima, H. (2006) · Carcinogenesis · doi:10.1093/carcin/bgl128 · Cited by 43
Proteomic identification of tyrosine nitration targets in kidney of spontaneously hypertensive rats
Tyther, R., Ahmeda, A. F., Johns, E. J., & Sheehan, D. (2007) · PROTEOMICS · doi:10.1002/pmic.200700503 · Cited by 42
Scandroglio, F., Tórtora, V., Radí, R., & Castro, L. (2014) · Free Radical Research · doi:10.3109/10715762.2014.900175 · Cited by 42
Glucose-modulated tyrosine nitration in beta cells: Targets and consequences
Koeck, T., Corbett, J. A., Crabb, J. W., Stuehr, D. J., & Aulak, K. S. (2009) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2009.01.021 · Cited by 41
Self-citationProteomic Analysis of Nitrated and 4-Hydroxy-2-Nonenal-Modified Serum Proteins During Aging
Kim, C. H., Zou, Y., Kim, D. H., Kim, N. D., Yu, B., & Chung, H. Y. (2006) · The Journals of Gerontology Series A · doi:10.1093/gerona/61.4.332 · Cited by 40
Lu, L., Gu, X., Hong, L., Laird, J. M., Jaffe, K., Choi, J. W., Crabb, J. W., & Salomon, R. G. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.09.009 · Cited by 40
Self-citationYang, M., Camara, A. K. S., Wakim, B. T., Zhou, Y., Gadicherla, A. K., Kwok, W., & Stowe, D. F. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.06.004 · Cited by 40
Specific O-GlcNAc modification at Ser-615 modulates eNOS function
Aulak, K. S., Barnes, J. W., Tian, L., Mellor, N. E., Haque, M. M., Willard, B. B., Li, L., Comhair, S., Stuehr, D. J., & Dweik, R. A. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101625 · Cited by 39
Self-citationDavid, A., Yadav, S., Baluška, F., & Bhatla, S. C. (2015) · Nitric Oxide · doi:10.1016/j.niox.2015.08.003 · Cited by 39
López, A., Ortiz, F., Doerrier, C., Venegas, C., Fernández‐Ortiz, M., Aranda‐Martínez, P., Díaz-Casado, M. E., Fernández-Gil, B. I., Barriocanal‐Casado, E., Escames, G., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0183090 · Cited by 38
Janssens, R., Mortier, A., Boff, D., Vanheule, V., Gouwy, M., Franck, C., Larsen, O., ROSENKILDE, M. M., Damme, J. V., Amaral, F. A., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.11516 · Cited by 36
Role of peroxynitrite-modified biomolecules in the etiopathogenesis of systemic lupus erythematosus
Ahmad, R., & Ahsan, H. (2012) · Clinical and Experimental Medicine · doi:10.1007/s10238-012-0222-5 · Cited by 36
Banta, S. A., Vemula, M., Yokoyama, T., Jayaraman, A., Francois Berthiaume, B., & Yarmush, M. L. (2006) · Biotechnology and Bioengineering · doi:10.1002/bit.21200 · Cited by 36
Significance of ERK nitration in portal hypertensive gastropathy and its therapeutic implications
Kinjo, N., Kawanaka, H., Akahoshi, T., Yamaguchi, S., Yoshida, D., Anegawa, G., Konishi, K., Tomikawa, M., Tanoue, K., Tarnawski, A. S., et al. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90329.2008 · Cited by 36
Tyrosine nitration as a key event of signal transduction that regulates functional state of the cell
Sabadashka, M., Nagalievska, M. R., & Sybirna, N. O. (2020) · Cell Biology International · doi:10.1002/cbin.11301 · Cited by 36
Proteomic Method for Identification of Tyrosine-Nitrated Proteins
Aulak, K. S., Koeck, T., Crabb, J. W., & Stuehr, D. J. (2004) · Humana Press eBooks · doi:10.1385/1-59259-807-2:151 · Cited by 35
Self-citationRuíz-Salinas, A. K., Vázquez‐Roque, R. A., Díaz, A., Pulido, G., Treviño, S., Florán, B., & Flores, G. (2020) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2020.108416 · Cited by 33
Hashiguchi, A., Kawano, T., Yano, S., Morioka, M., Hamada, J., Sato, T., Shirasaki, Y., Ushio, Y., & Fukunaga, K. (2003) · Neuroscience · doi:10.1016/s0306-4522(03)00490-1 · Cited by 34
A proteomic analysis of liver mitochondria during acute endotoxemia
Crouser, E. D., JULIAN, M. W., Huff, J. E., Mandich, D. V., & Green‐Church, K. B. (2006) · Intensive Care Medicine · doi:10.1007/s00134-006-0224-4 · Cited by 34
Morgan, E. T., Skubic, C., Lee, C., Cokan, K. B., & Rozman, D. (2020) · Drug Metabolism Reviews · doi:10.1080/03602532.2020.1817061 · Cited by 34
Annexin‐I as a potential target for green tea extract induced actin remodeling
Xiao, G., Jin, Y., Lu, Q., Zhang, Z., Belldegrun, A. S., Figlin, R. A., Pantuck, A. J., Yen, Y., Li, F., & Rao, J.-Y. (2006) · International Journal of Cancer · doi:10.1002/ijc.22164 · Cited by 33
Wang, X., Zhao, H., & Andersson, R. E. (2004) · Journal of Proteome Research · doi:10.1021/pr0499601 · Cited by 33
Metadata
- Authors
- Aulak, K. S., Miyagi, M., Yan, L., West, K. A., Massillon, D., Crabb, J. W., & Stuehr, D. J.
- Affiliations
- Cleveland Clinic (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2001-10-02
- Volume
- 98
- Issue
- 21
- Pages
- 12056-12061
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC59826
- OpenAlex
- W1980805550
- Cited by
- 350
- References
- 51
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 4 · 2023: 5 · 2022: 1 · 2021: 3 · 2020: 6 · 2019: 3 · 2018: 6 · 2017: 9 · 2016: 13 · 2015: 8 · 2014: 14 · 2013: 12 · 2012: 14
- FWCI
- 10.26
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Heart Association
- Cleveland Clinic
- Cleveland Clinic Foundation
- National Institutes of Health (5r21ns041644-02, CA53914, EY06603)
- National Eye Institute (EY06603, F32EY006603, R01EY006603)
- National Cancer Institute (CA-53914, R01CA053914)
- National Institute of General Medical Sciences (GM51491, R01GM051491)
- National Institute of Neurological Disorders and Stroke (NS41644)
- 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
- protein nitration, nitrotyrosine, nitric oxide, inflammation, oxidative stress, apoptosis, ATP production, metabolic proteins, asthma, sepsis, graft rejection, neurodegenerative diseases
- MeSH terms
- Animals, Humans, Interferon-gamma, Interleukin-1, Nitrates, Nitric Oxide, Tumor Cells, Cultured, Tumor Necrosis Factor-alpha, Electrophoresis, Gel, Two-Dimensional, Gene Expression, Rats, Sprague-Dawley, Nitric Oxide Synthase, Proteome, Rats, Nitric Oxide Synthase Type II
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