Mass spectrometric analysis of protein tyrosine nitration in aging and neurodegenerative diseases

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 · see citing works

The protein kinase complement of the human genome

Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145 · see citing works

Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062 · see citing works

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 · see citing works

Oxidants, antioxidants, and the degenerative diseases of aging.

Ames, B. N., Shigenaga, M. K., & Hagen, T. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.7915 · Cited by 5,958 · see citing works

Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide.

Ignarro, L. J., Buga, G. M., Wood, K. S., Byrns, R. E., & Chaudhuri, G. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.24.9265 · Cited by 5,074 · see citing works

Protein folding and misfolding

Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791 · see citing works

Alzheimer’s disease

Querfurth, H. W., & LaFerla, F. M. (2010) · New England Journal of Medicine · doi:10.1056/nejmra0909142 · Cited by 4,569 · see citing works

Nitric oxide as a secretory product of mammalian cells

Nathan, C. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.12.1381691 · Cited by 4,350 · see citing works

Nitric oxide synthases: structure, function and inhibition

ALDERTON, W. K., Cooper, C. E., & Knowles, R. G. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3570593 · Cited by 4,106 · see citing works

Mechanisms underlying inflammation in neurodegeneration

Glass, C. K., Saijo, K., Winner, B., Marchetto, M. C., & Gage, F. H. (2010) · Cell · doi:10.1016/j.cell.2010.02.016 · Cited by 3,580 · see citing works

Protein aggregation and neurodegenerative disease

Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454 · see citing works

Protein kinases and phosphatases: The Yin and Yang of protein phosphorylation and signaling

Hunter, T. R. (1995) · Cell · doi:10.1016/0092-8674(95)90405-0 · Cited by 2,959 · see citing works

Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process

Zubarev, R. A., Kelleher, N. L., & McLafferty, F. W. (1998) · Journal of the American Chemical Society · doi:10.1021/ja973478k · Cited by 1,881 · see citing works

Molecular Pathways of Neurodegeneration in Parkinson's Disease

Dawson, T. M., & Dawson, V. L. (2003) · Science · doi:10.1126/science.1087753 · Cited by 1,659 · see citing works

Oxidative Damage Linked to Neurodegeneration by Selective α-Synuclein Nitration in Synucleinopathy Lesions

Giasson, B. I., Duda, J. E., Murray, I. V. J., Chen, Q., Souza, J. M., Hurtig, H. I., Ischiropoulos, H., Trojanowski, J. Q., & Lee, V. M. ‐. (2000) · Science · doi:10.1126/science.290.5493.985 · Cited by 1,551 · see citing works

Nitric oxide, oxidants, and protein tyrosine nitration

Radí, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307446101 · Cited by 1,456 · see citing works

Aging, energy, and oxidative stress in neurodegenerative diseases

Beal, M. F. (1995) · Annals of Neurology · doi:10.1002/ana.410380304 · Cited by 1,434 · see citing works

Biosynthesis And Metabolism Of Endothelium-Derived Nitric Oxide

Ignarro, L. J. (1990) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.30.040190.002535 · Cited by 1,300 · see citing works

Immunoaffinity profiling of tyrosine phosphorylation in cancer cells

Rush, A. J., Moritz, A., Lee, K. A., Guo, A., Goss, V. L., Spek, E. J., Zhang, H., Zha, X., Polakiewicz, R. D., & Comb, M. J. (2004) · Nature Biotechnology · doi:10.1038/nbt1046 · Cited by 1,126 · see citing works

Paired Helical Filaments in Electron Microscopy of Alzheimer's Disease

KIDD, M. (1963) · Nature · doi:10.1038/197192b0 · Cited by 1,012 · see citing works

Description of Parkinson's Disease as a Clinical Syndrome

Fahn, S. (2003) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2003.tb07458.x · Cited by 979 · see citing works

Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome

Mann, M., Ong, S. E., Grønborg, M., Steen, H., Jensen, O. N., & Pandey, A. (2002) · Trends in biotechnology · doi:10.1016/s0167-7799(02)01944-3 · Cited by 901 · see citing works

Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease

Gamblin, T. C., Chen, F., Zambrano, A., Abraha, A., Lagalwar, S., Guillozet, A. L., Lu, M., Fu, Y., Garcia-Sierra, F., LaPointe, N., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1630428100 · Cited by 831 · see citing works

Therapeutic approaches to protein-misfolding diseases

Cohen, F. E., & Kelly, J. W. (2003) · Nature · doi:10.1038/nature02265 · Cited by 792 · see citing works

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 · see citing works

Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts.

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 768 · see citing works

Kinetics of superoxide dismutase- and iron-catalyzed nitration of phenolics by peroxynitrite

Beckman, J. S., Ischiropoulos, H., Zhu, L., van der Woerd, M., Smith, C. D. L., Chen, J., Harrison, J. G., Martin, J. C., & Tsai, M. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90432-v · Cited by 765 · see citing works

Oxidatively modified proteins in aging and disease1, 2 1Guest Editor: Earl Stadtman 2This article is part of a series of reviews on “Oxidatively Modified Proteins in Aging and Disease” The full list of papers may be found on the homepage of the journal

Beal, M. F. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00780-3 · Cited by 763 · see citing works

Quantitative Phosphoproteomics Applied to the Yeast Pheromone Signaling Pathway

Gruhler, A., Olsen, J. V., Mohammed, S., Mortensen, P., Færgeman, N. J., Mann, M., & Jensen, O. N. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400219-mcp200 · Cited by 758 · see citing works

Oxidative stress and nitration in neurodegeneration: Cause, effect, or association?

Ischiropoulos, H., & Beckman, J. S. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200317638 · Cited by 748 · see citing works

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 · see citing works

Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins

Kaji, H., Saito, H., Yamauchi, Y., Shinkawa, T., Taoka, M., Hirabayashi, J., Kasai, K., Takahashi, N., & Isobe, T. (2003) · Nature Biotechnology · doi:10.1038/nbt829 · Cited by 612 · see citing works

Quantitation of nitrotyrosine levels in lung sections of patients and animals with acute lung injury.

Haddad, I. Y., Pataki, G., Yu, Y., GALLIANI, C. A., Beckman, J. S., & Matalon, S. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117607 · Cited by 594 · see citing works

Dityrosine Cross-linking Promotes Formation of Stable α-Synuclein Polymers

Souza, J. M., Giasson, B. I., Chen, Q., Lee, V. M. ‐., & Ischiropoulos, H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000206200 · Cited by 561 · see citing works

Proteomic identification of nitrated proteins in Alzheimer's disease brain

Castegna, A., Thongboonkerd, V., Klein, J. B., Lynn, B. C., Markesbery, W. R., & Butterfield, D. A. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01786.x · Cited by 535 · see citing works

Peroxynitrite-Mediated Inactivation of Manganese Superoxide Dismutase Involves Nitration and Oxidation of Critical Tyrosine Residues

MacMillan-Crow, L. A., Crow, J. P., & Thompson, J. A. (1998) · Biochemistry · doi:10.1021/bi971894b · Cited by 508 · see citing works

Electrochemical Analysis of Protein Nitrotyrosine and Dityrosine in the Alzheimer Brain Indicates Region-Specific Accumulation

Hensley, K., Maidt, M. L., Yu, Z., Sang, H., Markesbery, W. R., & Floyd, R. A. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-20-08126.1998 · Cited by 508 · see citing works

Tyrosine nitration: Localisation, quantification, consequences for protein function and signal transduction

Greenacre, S., & Ischiropoulos, H. (2001) · Free Radical Research · doi:10.1080/10715760100300471 · Cited by 500 · see citing works

Analytical strategies for phosphoproteomics

Thingholm, T. E., Jensen, O. N., & Larsen, M. R. (2009) · PROTEOMICS · doi:10.1002/pmic.200800454 · Cited by 478 · see citing works

Reactive Nitrogen Intermediates Promote Low Density Lipoprotein Oxidation in Human Atherosclerotic Intima

Leeuwenburgh, C., Hardy, M. M., Hazen, S. L., Wagner, P. D., Oh‐ishi, S., Steinbrecher, U. P., & Heinecke, J. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.3.1433 · Cited by 461 · see citing works

Direct binding and functional coupling of α-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis

Lee, F. J. S., Liu, F., Pristupa, Z. B., & Niznik, H. B. (2001) · The FASEB Journal · doi:10.1096/fj.00-0334com · Cited by 455 · see citing works

Effects of peroxynitrite‐induced protein modifications on tyrosine phosphorylation and degradation

Gow, A. J., Duran, D., Malcolm, S., & Ischiropoulos, H. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00347-x · Cited by 449 · see citing works

SPECIAL FEATURE: TUTORIAL Slow Heating Methods in Tandem Mass Spectrometry

McLuckey, S. A., & Goeringer, D. E. (1997) · Journal of Mass Spectrometry · doi:10.1002/(sici)1096-9888(199705)32:5 · Cited by 425 · see citing works

Inactivation of tyrosine hydroxylase by nitration following exposure to peroxynitrite and 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)

Ara, J. E., Przedborski, S., Naini, A., Jackson-Lewis, V. R., Trifiletti, R. R., Horwitz, J., & Ischiropoulos, H. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7659 · Cited by 414 · see citing works

The Structural Basis of Monoclonal Antibody Alz50's Selectivity for Alzheimer's Disease Pathology

Carmel, G., Mager, E. M., Binder, L. I., & Kuret, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.51.32789 · Cited by 402 · see citing works

β-Synuclein Inhibits α-Synuclein Aggregation

Hashimoto, M., Rockenstein, E., Mante, M., Mallory, M., & Masliah, E. (2001) · Neuron · doi:10.1016/s0896-6273(01)00462-7 · Cited by 398 · see citing works

A Mass Spectrometry-based Proteomic Approach for Identification of Serine/Threonine-phosphorylated Proteins by Enrichment with Phospho-specific Antibodies

Grønborg, M., Kristiansen, T. Z., Stensballe, A., Andersen, J., Ohara, O., Mann, M., Jensen, O. N., & Pandey, A. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200010-mcp200 · Cited by 387 · see citing works

Biological significance of nitric oxide-mediated protein modifications

Gow, A. J., Farkouh‐Karoleski, C., Munson, D. A., Posencheg, M. A., & Ischiropoulos, H. (2004) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00295.2003 · Cited by 384 · see citing works

Protein Nitration in Cardiovascular Diseases

Turko, I. V., & Murad, F. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.4.619 · Cited by 372 · see citing works

Copper Mediates Dityrosine Cross-Linking of Alzheimer's Amyloid-β

Atwood, C., Perry, G. L., Zeng, H., Kato, Y., Jones, W. D., Ling, K.-Q., Huang, X., Moir, R. D., Wang, D., Sayre, L. M., et al. (2003) · Biochemistry · doi:10.1021/bi0358824 · Cited by 371 · see citing works

Localization of Labile Posttranslational Modifications by Electron Capture Dissociation: The Case of γ-Carboxyglutamic Acid

Kelleher, N. L., Zubarev, R. A., Bush, K. A., Furie, B., Furie, B. C., McLafferty, F. W., & Walsh, C. T. (1999) · Analytical Chemistry · doi:10.1021/ac990684x · Cited by 369 · see citing works

NO-dependent protein nitration: a cell signaling event or an oxidative inflammatory response?

Schopfer, F. J. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.10.006 · Cited by 369 · see citing works

Identification of nitrated proteins in Alzheimer’s disease brain using a redox proteomics approach

Sultana, R., Poon, H. F., Cai, J., Pierce, W. M., Merchant, M., Klein, J. B., Markesbery, W. R., & Butterfield, D. A. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.10.004 · Cited by 364 · see citing works

Nitration of Tyrosine 10 Critically Enhances Amyloid β Aggregation and Plaque Formation

Kummer, M. P., Hermes, M., Delekarte, A., Hammerschmidt, T., Kumar, S., Terwel, D., Walter, J., Pape, H.-C., König, S., Roeber, S., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.07.001 · Cited by 336 · see citing works

Peroxynitrite disables the tyrosine phosphorylation regulatory mechanism: Lymphocyte-specific tyrosine kinase fails to phosphorylate nitrated cdc2(6-20)NH2 peptide.

Kong, S. K., Yim, M. B., Stadtman, E. R., & Chock, P. B. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.8.3377 · Cited by 335 · see citing works

Role of the arginine-nitric oxide pathway in the regulation of vascular smooth muscle cell proliferation

Ignarro, L. J., Buga, G. M., Liu, W., Bauer, P. M., Wu, G., & Soldato, P. D. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.071054698 · Cited by 331 · see citing works

Factors Determining the Selectivity of Protein Tyrosine Nitration

Souza, J. M., Daikhin, E., Yudkoff, M., Raman, C. S., & Ischiropoulos, H. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1480 · Cited by 315 · see citing works

Fluorous Mixture Synthesis: A Fluorous-Tagging Strategy for the Synthesis and Separation of Mixtures of Organic Compounds

Luo, Z., Zhang, Q., Oderaotoshi, Y., & Curran, D. P. (2001) · Science · doi:10.1126/science.1057567 · Cited by 299 · see citing works

Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant

Bruijn, L. I., Beal, M. F., Bêcher, M. W., Schulz, J. B., Wong, P. C., Price, D. L., & Cleveland, D. W. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.14.7606 · Cited by 290 · see citing works

Functional Consequences of α-Synuclein Tyrosine Nitration

Hodara, R., Norris, E. H., Giasson, B. I., Mishizen-Eberz, A. J., Lynch, D. R., Lee, V. M. ‐., & Ischiropoulos, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408906200 · Cited by 286 · see citing works

An activity in rat tissues that modifies nitrotyrosine-containing proteins

Kamisaki, Y., Wada, K., Bian, K., Balabanlı, B., Davis, K. L., Martin, E., Behbod, F., Lee, Y.-C., & Murad, F. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.11584 · Cited by 275 · see citing works

Mutant SOD1 causes motor neuron disease independent of copper chaperone–mediated copper loading

Subramaniam, J. R., Lyons, W. E., Liu, J., Bartnikas, T. B., Rothstein, J. D., Price, D. L., Cleveland, D. W., Gitlin, J. D., & Wong, P. C. (2002) · Nature Neuroscience · doi:10.1038/nn823 · Cited by 267 · see citing works

Superoxide Dismutase Catalyzes Nitration of Tyrosines by Peroxynitrite in the Rod and Head Domains of Neurofilament‐L

Crow, J. P., Ye, Y. Z., Strong, M. J., KIRK, M. C., Barnes, S., & Beckman, J. S. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69051945.x · Cited by 260 · see citing works

Aging and the Role of Reactive Nitrogen Species

Drew, B., & Leeuwenburgh, C. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb02084.x · Cited by 251 · see citing works

Molecular Pathogenesis of Parkinson Disease

Eriksen, J. L., Wszołek, Z. K., & Petrucelli, L. (2005) · Archives of Neurology · doi:10.1001/archneur.62.3.353 · Cited by 248 · see citing works

Y402H polymorphism of complement factor H affects binding affinity to C-reactive protein

Laine, M., Jarva, H., Seitsonen, S., Haapasalo, K., Lehtinen, M. J., Lindeman, N., Anderson, D. H., Johnson, P. T., Järvelä, I., Jokiranta, T. S., et al. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.6.3831 · Cited by 246 · see citing works

Expression of nitric oxide synthases and formation of nitrotyrosine and reactive oxygen species in inflammatory bowel disease

Dijkstra, G. D. H., Moshage, H. J., van Dullemen, H. M., de Jager-Krikken, A., Tiebosch, A. T. M. G., Kleibeuker, J. H., Jansen, P. L. M., & van Goor, H. (1998) · The Journal of Pathology · doi:10.1002/(sici)1096-9896(199812)186:4 · Cited by 223 · see citing works

Proteomic identification of 3-nitrotyrosine-containing rat cardiac proteins: effects of biological aging

Kanski, J., Behring, A., Pelling, J., & Schöneich, C. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01030.2003 · Cited by 217 · see citing works

Proteomic identification of brain proteins in the canine model of human aging following a long-term treatment with antioxidants and a program of behavioral enrichment: Relevance to Alzheimer's disease

Opii, W. O., Joshi, G., Head, E., Milgram, N. W., Muggenburg, B. A., Klein, J. B., Pierce, W. M., Cotman, C. W., & Butterfield, D. A. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.09.012 · Cited by 202 · see citing works

Enrichment and analysis of peptide subsets using fluorous affinity tags and mass spectrometry

Brittain, S. M., Ficarro, S. B., Brock, A., & Peters, E. C. (2005) · Nature Biotechnology · doi:10.1038/nbt1076 · Cited by 194 · see citing works

[17] Detection and quantitation of nitrotyrosine residues in proteins: In vivo marker of peroxynitrite

Crow, J. P., & Ischiropoulos, H. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)69020-x · Cited by 192 · see citing works

Protein Nitration in a Mouse Model of Familial Amyotrophic Lateral Sclerosis

Casoni, F., Basso, M., Massignan, T., Gianazza, E., Cheroni, C., Salmona, M., Bendotti, C., & Bonetto, V. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413111200 · Cited by 180 · see citing works

Conformational changes and truncation of tau protein during tangle evolution in Alzheimer's disease

García-Sierra, F., Ghoshal, N., Quinn, B., Berry, R., & Binder, L. (2003) · Journal of Alzheimer's Disease · doi:10.3233/jad-2003-5201 · Cited by 179 · see citing works

Protein oxidation and age-dependent alterations in calcium homeostasis

Thomas, C. (2000) · Frontiers in bioscience · doi:10.2741/squier · Cited by 179 · see citing works

Proteomic Analysis of Protein Nitration in Aging Skeletal Muscle and Identification of Nitrotyrosine-containing Sequences in Vivo by Nanoelectrospray Ionization Tandem Mass Spectrometry

Kański, J., Hong, S. J., & Schöneich, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501773200 · Cited by 177 · see citing works

Inflammation and NO x -induced nitration: Assay for 3-nitrotyrosine by HPLC with electrochemical detection

Shigenaga, M. K., Lee, H. H., Blount, B. C., Christen, S., Shigeno, E. T., Yip, H. T., & Ames, B. N. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.7.3211 · Cited by 171 · see citing works

Nitration inhibits fibrillation of human α‐synuclein in vitro by formation of soluble oligomers

Yamin, G., Uversky, V. N., & Fink, A. L. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00367-3 · Cited by 167 · see citing works

Pathogenetic mechanisms of parkin in Parkinson's disease

Hattori, N., & Mizuno, Y. (2004) · The Lancet · doi:10.1016/s0140-6736(04)16901-8 · Cited by 162 · see citing works

Effects of nitration on the structure and aggregation of α-synuclein

Uversky, V. N., Yamin, G., Munishkina, L. A., Karymov, M. A., Millett, I. S., Doniach, S., Lyubchenko, Y. L., & Fink, A. L. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.11.014 · Cited by 157 · see citing works

Endogenously Nitrated Proteins in Mouse Brain: Links to Neurodegenerative Disease

Sacksteder, C. A., Qian, W., Knyushko, T. V., Wang, H., Chin, M. H., Laćan, G., Melega, W. P., Camp, D., Smith, R. D., Smith, D., et al. (2006) · Biochemistry · doi:10.1021/bi060474w · Cited by 151 · see citing works

Site-Specific Nitration and Oxidative Dityrosine Bridging of the τ Protein by Peroxynitrite: Implications for Alzheimer's Disease

Reynolds, M. R., Berry, R. W., & Binder, L. I. (2005) · Biochemistry · doi:10.1021/bi047982v · Cited by 149 · see citing works

Analysis of peptides and proteins containing nitrotyrosine by matrix-assisted laser desorption/ionization mass spectrometry

Sarver, A. L., Scheffler, N. K., Shetlar, M. D., & Gibson, B. W. (2001) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(01)00213-6 · Cited by 149 · see citing works

Ischaemic injury mediator

Beckman, J. S. (1990) · Nature · doi:10.1038/345027b0 · Cited by 146 · see citing works

Investigation of tyrosine nitration in proteins by mass spectrometry

Petersson, A., Steen, H., Kalume, D. E., Caidahl, K., & Roepstorff, P. (2001) · Journal of Mass Spectrometry · doi:10.1002/jms.161 · Cited by 141 · see citing works

High-Throughput Comparative Proteome Analysis Using a Quantitative Cysteinyl-peptide Enrichment Technology

Liu, T., Qian, W., Strittmatter, E. F., Camp, D., Anderson, G., Thrall, B. D., & Smith, R. D. (2004) · Analytical Chemistry · doi:10.1021/ac049485q · Cited by 135 · see citing works

Proteomic identification of nitrated brain proteins in early Alzheimer’s disease inferior parietal lobule

Reed, T. T., Pierce Jr., W. M., Turner, D. M., Markesbery, W. R., & Allan Butterfield, D. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00478.x · Cited by 135 · see citing works

Protein tyrosine nitration in hydrophilic and hydrophobic environments

Bartesaghi, S., Ferrer‐Sueta, G., Peluffo, G., Valez, V., Zhang, H., Kalyanaraman, B., & Radí, R. (2006) · Amino Acids · doi:10.1007/s00726-006-0425-8 · Cited by 130 · see citing works

Nitric oxide and cancer

Muntané, J. (2010) · World Journal of Hepatology · doi:10.4254/wjh.v2.i9.337 · Cited by 128 · see citing works

Histone H1.2 is a substrate for denitrase, an activity that reduces nitrotyrosine immunoreactivity in proteins

Irie, Y., Saeki, M., Kamisaki, Y., Martin, E., & Murad, F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1131756100 · Cited by 128 · see citing works

Phosphoproteomics by mass spectrometry and classical protein chemistry approaches

Salih, E. (2004) · Mass Spectrometry Reviews · doi:10.1002/mas.20042 · Cited by 126 · see citing works

Peroxynitrite Targets the Epidermal Growth Factor Receptor, Raf-1, and MEK Independently to Activate MAPK

Zhang, P., Wang, Y.-Z., Kagan, E., & Bonner, J. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910425199 · Cited by 126 · see citing works

Relationship between Antioxidants, Prooxidants, and the Aging Processa

Sohal, R. S., & Orr, W. C. (1992) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1992.tb38651.x · Cited by 125 · see citing works

Preferentially Increased Nitration of α-Synuclein at Tyrosine-39 in a Cellular Oxidative Model of Parkinson’s Disease

Danielson, S. R., Held, J. M., Schilling, B., Oo, M. L., Gibson, B. W., & Andersen, J. K. (2009) · Analytical Chemistry · doi:10.1021/ac901176t · Cited by 123 · see citing works

Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry

Zhan, X., & Desiderio, D. M. (2006) · Analytical Biochemistry · doi:10.1016/j.ab.2006.05.024 · Cited by 122 · see citing works

Structural changes in α‐synuclein affect its chaperone‐like activity in vitro

Kim, T. D., Paik, S. R., Yang, C., & Kim, J. (2000) · Protein Science · doi:10.1110/ps.9.12.2489 · Cited by 122 · see citing works

Overexpression of Neutrophil Neuronal Nitric Oxide Synthase in Parkinson's Disease

Gatto, E. M., Galdo, N. A. R., Carreras, M. C., Cherñavsky, A. C., Rubio, A., Satz, M. L., & Poderoso, J. J. (2000) · Nitric Oxide · doi:10.1006/niox.2000.0288 · Cited by 117 · see citing works

Proteomic analysis of protein tyrosine nitration after ischemia reperfusion injury: Mitochondria as the major target

Liu, B., Tewari, A. K., Zhang, L., Green‐Church, K. B., Zweier, J. L., Chen, Y., & He, G. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.12.008 · Cited by 116 · see citing works

Chemistry meets proteomics: The use of chemical tagging reactions for MS‐based proteomics

Leitner, A., & Lindner, W. F. (2006) · PROTEOMICS · doi:10.1002/pmic.200600255 · Cited by 116 · see citing works

Tau Polymerization: Role of the Amino Terminus

Gamblin, T. C., Berry, R. W., & Binder, L. I. (2003) · Biochemistry · doi:10.1021/bi0272510 · Cited by 116 · see citing works

Nitration in Neurodegeneration: Deciphering the “Hows” “nYs”

Reynolds, M. R., Berry, R. W., & Binder, L. I. (2007) · Biochemistry · doi:10.1021/bi700430y · Cited by 114 · see citing works

Peroxynitrite modulates tyrosine phosphorylation and phosphoinositide signalling in human neuroblastoma SH-SY5Y cells: attenuated effects in human 1321N1 astrocytoma cells

Li, X., Sarno, P. D., Ling, S. O. N. G., Beckman, J. S., & Jope, R. S. (1998) · Biochemical Journal · doi:10.1042/bj3310599 · Cited by 113 · see citing works

Markers of protein oxidation by hydroxyl radical and reactive nitrogen species in tissues of aging rats

Leeuwenburgh, C., Hansen, P. A., Shaish, A., Holloszy, J. O., & Heinecke, J. W. (1998) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1998.274.2.r453 · Cited by 110 · see citing works

Eosinophil peroxidase produces hypobromous acid in the airways of stable asthmatics

Aldridge, R. E., Chan, T., van Dalen, C. J., Senthilmohan, R., WINN, M. C., Venge, P., Town, G. I., & Kettle, A. J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00976-0 · Cited by 109 · see citing works

Proteomic identification of age-dependent protein nitration in rat skeletal muscle

Kański, J., Alterman, M. A., & Schöneich, C. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00500-8 · Cited by 108 · see citing works

Protein tyrosine nitration

Corpas, F. J., Chaki, M., Leterrier, M., & Barroso, J. B. (2009) · Plant Signaling & Behavior · doi:10.4161/psb.4.10.9466 · Cited by 106 · see citing works

Peroxynitrite Induces Tyrosine Nitration and Modulates Tyrosine Phosphorylation of Synaptic Proteins

Stasi, A. M. M. D., Mallozzi, C., Macchia, G., Petrucci, T. C., & Minetti, M. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0730727.x · Cited by 102 · see citing works

Analysis of nitrated proteins by nitrotyrosine-specific affinity probes and mass spectrometry

Nikov, G. N., Bhat, V. B., Wishnok, J. S., & Tannenbaum, S. R. (2003) · Analytical Biochemistry · doi:10.1016/s0003-2697(03)00359-2 · Cited by 98 · see citing works

Aspects, mechanism, and biological relevance of mitochondrial protein nitration sustained by mitochondrial nitric oxide synthase

Elfering, S. L., Haynes, V. L., Traaseth, N. J., Ettl, A., & Giulivi, C. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00766.2003 · Cited by 98 · see citing works

Tyrosine 125 of α-synuclein plays a critical role for dimerization following nitrative stress

Takahashi, T., Yamashita, H., Nakamura, T., Nagano, Y., & Nakamura, S. (2002) · Brain Research · doi:10.1016/s0006-8993(02)02498-8 · Cited by 97 · see citing works

The human pituitary nitroproteome: detection of nitrotyrosyl-proteins with two-dimensional Western blotting, and amino acid sequence determination with mass spectrometry

Zhan, X., & Desiderio, D. M. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.10.169 · Cited by 96 · see citing works

A Method for Selective Enrichment and Analysis of Nitrotyrosine-Containing Peptides in Complex Proteome Samples

Zhang, Q., Qian, W., Knyushko, T. V., Clauss, T. R., Purvine, S. O., Moore, R. J., Sacksteder, C. A., Chin, M. H., Smith, D., Camp, D., et al. (2007) · Journal of Proteome Research · doi:10.1021/pr0606934 · Cited by 95 · see citing works

In Vitro and in Vivo Protein-bound Tyrosine Nitration Characterized by Diagonal Chromatography

Ghesquière, B., Colaert, N., Helsens, K., Dejager, L., Vanhaute, C., Verleysen, K., Kas, K., Timmerman, E., Goethals, M., Libert, C., et al. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900259-mcp200 · Cited by 92 · see citing works

Isotope Dilution Mass Spectrometric Quantification of 3-Nitrotyrosine in Proteins and Tissues Is Facilitated by Reduction to 3-Aminotyrosine

Crowley, J. R., Yarasheski, K. E., Leeuwenburgh, C., TURK, J. W., & Heinecke, J. W. (1998) · Analytical Biochemistry · doi:10.1006/abio.1998.2635 · Cited by 86 · see citing works

Electron capture dissociation of substance P using a commercially available Fourier transform ion cyclotron resonance mass spectrometer

Axelsson, J., Palmblad, M., Håkansson, K., & Håkansson, P. (1999) · Rapid Communications in Mass Spectrometry · doi:10.1002/(sici)1097-0231(19990330)13:6 · Cited by 85 · see citing works

Secondary fragmentation of linear peptides in electron capture dissociation

Cooper, H. J., Hudgins, R. R., Håkansson, K., & Marshall, A. G. (2003) · International Journal of Mass Spectrometry · doi:10.1016/s1387-3806(03)00202-1 · Cited by 82 · see citing works

Differences in eNOS Activity Because of Subcellular Localization Are Dictated by Phosphorylation State Rather than the Local Calcium Environment

Church, J. E., & Fulton, D. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505968200 · Cited by 78 · see citing works

Role of protein tyrosine nitration in neurodegenerative diseases and atherosclerosis

Lee, J. R., Kim, J. K., Lee, S. J., & Kim, K. P. (2009) · Archives of Pharmacal Research · doi:10.1007/s12272-009-1802-0 · Cited by 75 · see citing works

Diseases of protein conformation: what do in vitro experiments tell us about in vivo diseases?

Buxbaum, J. N. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.09.009 · Cited by 73 · see citing works

Nitrotyrosine mimics phosphotyrosine binding to the SH2 domain of the src family tyrosine kinase lyn

Mallozzi, C., Stasi, A. M. M. D., & Minetti, M. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02726-0 · Cited by 71 · see citing works

Peroxynitrite in the Pathogenesis of Parkinson's Disease and the Neuroprotective Role of Metallothioneins

Ebadi, M., SHARMA, S. K., Ghafourifar, P., Brown‐Borg, H. M., & Refaey, H. E. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)96024-2 · Cited by 64 · see citing works

The formation of peroxynitrite in the applied physiology of mitochondrial nitric oxide

Poderoso, J. J. (2009) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.12.020 · Cited by 63 · see citing works

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 · see citing works

Quantitative phosphoproteomics – an emerging key technology in signal‐transduction research

Schreiber, T. B., Mäusbacher, N., Breitkopf, S. B., Grundner‐Culemann, K., & Daub, H. (2008) · PROTEOMICS · doi:10.1002/pmic.200800132 · Cited by 60 · see citing works

Factors That Contribute to the Misidentification of Tyrosine Nitration by Shotgun Proteomics

Stevens, S. M., Prókai-Tátrai, K., & Prókai, L. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800065-mcp200 · Cited by 60 · see citing works

Analysis of nitrated proteins and tryptic peptides by HPLC-chip-MS/MS: site-specific quantification, nitration degree, and reactivity of tyrosine residues

Zhang, Y., Yang, H., & Pöschl, U. (2010) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-010-4280-9 · Cited by 59 · see citing works

Age-related accumulation of 3-nitrotyrosine and nitro-A2E in human Bruch's membrane

Murdaugh, L. S., Wang, Z., Priore, L. V. D., Dillon, J. P., & Gaillard, E. R. (2010) · Experimental Eye Research · doi:10.1016/j.exer.2010.01.014 · Cited by 59 · see citing works

Increased Protein Nitration Burden in the Atherosclerotic Lesions and Plasma of Apolipoprotein A-I–Deficient Mice

Parastatidis, I., Thomson, L., Fries, D. M., Moore, R. E., Tohyama, J., Fu, X., Hazen, S. L., Heijnen, H. F. G., Dennehy, M. K., Liebler, D. C., et al. (2007) · Circulation Research · doi:10.1161/circresaha.107.157537 · Cited by 58 · see citing works

Metastable atom‐activated dissociation mass spectrometry: leucine/isoleucine differentiation and ring cleavage of proline residues

Cook, S. L., Collin, O. L., & Jackson, G. P. (2009) · Journal of Mass Spectrometry · doi:10.1002/jms.1598 · Cited by 58 · see citing works

Protein Nitration With Aging in the Rat Semimembranosus and Soleus Muscles

Fugere, N. A., Ferrington, D. A., & Thompson, L. V. (2006) · The Journals of Gerontology Series A · doi:10.1093/gerona/61.8.806 · Cited by 57 · see citing works

Relevance of protein nitration in brain injury: a key pathophysiological mechanism in neurodegenerative, autoimmune, or inflammatory CNS diseases and stroke

Sarchielli, P., Galli, F., Floridi, A., Floridi, A., & Gallai, V. (2003) · Amino Acids · doi:10.1007/s00726-003-0028-6 · Cited by 54 · see citing works

Selective Enrichment and Mass Spectrometric Identification of Nitrated Peptides Using Fluorinated Carbon Tags

Kim, J. K., Lee, J. R., Kang, J. W., Lee, S. J., Shin, G., Yeo, W., Kim, K., Park, H. S., & Kim, K. P. (2010) · Analytical Chemistry · doi:10.1021/ac102080d · Cited by 50 · see citing works

Peroxynitrite-Mediated τ Modifications Stabilize Preformed Filaments and Destabilize Microtubules through Distinct Mechanisms

Reynolds, M. R., Lukas, T. J., Berry, R. W., & Binder, L. I. (2006) · Biochemistry · doi:10.1021/bi052142h · Cited by 50 · see citing works

Angiotensin II induces tyrosine nitration and activation of ERK1/2 in vascular smooth muscle cells

Pinzar, E., Wang, T., Garrido, M. R., Xu, W., Levy, P. A., & Bottari, S. P. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.08.019 · Cited by 49 · see citing works

Protein tyrosine nitration in rat brain is associated with raft proteins, flotillin‐1 and α‐tubulin: effect of biological aging

Dremina, E. S., Sharov, V. S., & Schöneich, C. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03115.x · Cited by 49 · see citing works

Protein Nitration in Biological Aging: Proteomic and Tandem Mass Spectrometric Characterization of Nitrated Sites

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 · see citing works

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 · see citing works

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 · see citing works

Proteomic analysis of age dependent nitration of rat cardiac proteins by solution isoelectric focusing coupled to nanoHPLC tandem mass spectrometry

Hong, S. J., Gokulrangan, G., & Schöneich, C. (2007) · Experimental Gerontology · doi:10.1016/j.exger.2007.03.005 · Cited by 47 · see citing works

Characterization of nitroproteome in neuron‐like PC12 cells differentiated with nerve growth factor: Identification of two nitration sites in α‐tubulin

Tedeschi, G., Cappelletti, G., Negri, A. L., Pagliato, L., Maggioni, M. G., Maci, R., & Ronchi, S. (2005) · PROTEOMICS · doi:10.1002/pmic.200401208 · Cited by 46 · see citing works

Electron capture dissociation mass spectrometry of tyrosine nitrated peptides

Jones, A. W., Mikhailov, V. A., Iniesta, J., & Cooper, H. J. (2009) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2009.10.011 · Cited by 44 · see citing works

Age-associated tyrosine nitration of rat skeletal muscle glycogen phosphorylase b: characterization by HPLC–nanoelectrospray–Tandem mass spectrometry

Sharov, V. S., Galeva, N. A., Kański, J., Williams, T. D., & Schöneich, C. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.02.012 · Cited by 42 · see citing works

Nitroproteomics of Peripheral Blood Mononuclear Cells from Patients and a Rat Model of ALS

Nardo, G., Pozzi, S., Mantovani, S., Garbelli, S., Marinou, K., Basso, M., Mora, G., Bendotti, C., & Bonetto, V. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2548 · Cited by 39 · see citing works

Chemical Approach for Specific Enrichment and Mass Analysis of Nitrated Peptides

Lee, J. R., Lee, S. J., Kim, T. W., Kim, J. K., Park, H. S., Kim, D., Kim, K. P., & Yeo, W. (2009) · Analytical Chemistry · doi:10.1021/ac9005099 · Cited by 39 · see citing works

[14] Immunoprecipitation of nitrotyrosine-containing proteins

MacMillan-Crow, L. A., & Thompson, J. A. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)01076-9 · Cited by 38 · see citing works

Electron capture dissociation mass spectrometry in characterization of post-translational modifications

Bakhtiar, R., & Guan, Z. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.05.138 · Cited by 34 · see citing works

Dynamic interplay between nitration and phosphorylation of tubulin cofactor B in the control of microtubule dynamics

Rayala, S. K., Martin, E., Sharina, I. G., Molli, P. R., Wang, X., Jacobson, R. H., Murad, F., & Kumar, R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705149104 · Cited by 34 · see citing works

Selective Chemoprecipitation and Subsequent Release of Tagged Species for the Analysis of Nitropeptides by Liquid Chromatography–Tandem Mass Spectrometry

Prókai-Tátrai, K., Guo, J., & Prókai, L. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.002923 · Cited by 33 · see citing works

Characterization of Tyrosine Nitration and Cysteine Nitrosylation Modifications by Metastable Atom-Activation Dissociation Mass Spectrometry

Cook, S. L., & Jackson, G. P. (2011) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-010-0041-4 · Cited by 33 · see citing works

A methodology for simultaneous fluorogenic derivatization and boronate affinity enrichment of 3-nitrotyrosine-containing peptides

Dremina, E. S., Li, X., Galeva, N. A., Sharov, V. S., Stobaugh, J. F., & Schöneich, C. (2011) · Analytical Biochemistry · doi:10.1016/j.ab.2011.07.024 · Cited by 31 · see citing works

Fluorogenic Tagging of Peptide and Protein 3-Nitrotyrosine with 4-(Aminomethyl)benzenesulfonic Acid for Quantitative Analysis of Protein Tyrosine Nitration

Sharov, V. S., Dremina, E. S., Galeva, N. A., Gerstenecker, G. S., Li, X., Dobrowsky, R. T., Stobaugh, J. F., & Schöneich, C. (2009) · Chromatographia · doi:10.1365/s10337-009-1409-0 · Cited by 30 · see citing works

Top-Down Mass Analysis of Protein Tyrosine Nitration: Comparison of Electron Capture Dissociation with “Slow-Heating” Tandem Mass Spectrometry Methods

Mikhailov, V. A., Iniesta, J., & Cooper, H. J. (2010) · Analytical Chemistry · doi:10.1021/ac101177r · Cited by 28 · see citing works

Antibody‐Free Detection of Protein Tyrosine Nitration in Tissue Sections

Wisastra, R., Poelstra, K., Bischoff, R., Maarsingh, H., Haisma, H. J., & Dekker, F. J. (2011) · ChemBioChem · doi:10.1002/cbic.201100148 · Cited by 24 · see citing works

MALDI-induced fragmentation of leucine enkephalin, nitro-Tyr-leucine enkaphalin, and d5-Phe-nitro-Tyr-leucine enkephalin

Zhan, X., & Desiderio, D. M. (2008) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2008.08.020 · Cited by 23 · see citing works

The nitration of platelet vasodilator stimulated phosphoprotein following exposure to low concentrations of hydrogen peroxide

Sabetkar, M., Low, S. Y., Bradley, N. J., Jacobs, M., Naseem, K. M., & Bruckdorfer, K. R. (2008) · Platelets · doi:10.1080/09537100801915142 · Cited by 23 · see citing works

Efficient Identification and Quantification of Peptides Containing Nitrotyrosine by Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry after Derivatization

Tsumoto, H., Taguchi, R., & Kohda, K. (2010) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.58.488 · Cited by 23 · see citing works

Selective Fluorogenic Derivatization of 3-Nitrotyrosine and 3,4-Dihydroxyphenylalanine in Peptides: A Method Designed for Quantitative Proteomic Analysis

Sharov, V. S., Dremina, E. S., Pennington, J. P., Killmer, J., Asmus, C., Thorson, M., Hong, S. J., Li, X., Stobaugh, J. F., & Schöneich, C. (2008) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)01202-0 · Cited by 20 · see citing works

The detection of nitrated tyrosine in neuropeptides: a MALDI matrix-dependent response

Sheeley, S. A., Rubakhin, S. S., & Sweedler, J. V. (2005) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-005-3145-0 · Cited by 16 · see citing works

Characterization of neuron-specific huntingtin aggregates in human huntingtin knock-in mice

Sawada, H., Ishiguro, H., Nishii, K., Yamada, K., Tsuchida, K., Takahashi, H., Goto, J., Kanazawa, I., & Nagatsu, T. (2007) · Neuroscience Research · doi:10.1016/j.neures.2007.01.002 · Cited by 16 · see citing works

Tyrosine phosphorylation/dephosphorylation regulates peroxynitrite-mediated peptide nitration

Shi, W., Cai, H., Xu, D., Su, X., Lei, P., Zhao, Y., & Li, Y. (2007) · Regulatory Peptides · doi:10.1016/j.regpep.2007.06.011 · Cited by 15 · see citing works

Nitroproteins Identified in Human Ex-smoker Bronchoalveolar Lavage Fluid.

Zhan, X., & Desiderio, D. M. (2011) · Europe PMC (PubMed Central) · Cited by 15 · see citing works

Tau is Endogenously Nitrated in Mouse Brain: Identification of a Tyrosine Residue Modified In vivo by NO

Nonnis, S., Cappelletti, G., Taverna, F., Ronchi, C. L., Ronchi, S., Negri, A. L., Grassi, E., & Tedeschi, G. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9467-x · Cited by 15 · see citing works

Understanding the causes of aging and cancer.

Bn, A. (1995) · PubMed · Cited by 14 · see citing works

Ishemia-Reperfusion enhances GAPDH nitration in aging skeletal muscle

Bailey, C. E., Hammers, D. W., DeFord, J. H., Dimayuga, V. L., Amaning, J. K., Farrar, R. P., & Papaconstantinou, J. (2011) · Aging · doi:10.18632/aging.100394 · Cited by 10 · see citing works

Untitled work

Mattson, M. (1999) · doi:10.1002/(sici)1097-4547(19991001)58:1

Measurement and Clinical Significance of Biomarkers of Oxidative Stress in Humans

Marrocco, I., Fabio Altieri, F., & Peluso, I. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/6501046 · Cited by 874 · see citing works

Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases

Kehm, R., Baldensperger, T., Raupbach, J., & Höhn, A. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101901 · Cited by 348 · see citing works

Oxidative and nitrative stress in neurodegeneration

Cobb, C. A., & Cole, M. P. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.04.020 · Cited by 300 · see citing works

Origin and pathophysiology of protein carbonylation, nitration and chlorination in age-related brain diseases and aging

Gonos, E. S., Καπετάνου, Μ., Sereikaitė, J., Bartosz, G., Naparło, K., Grzesik, M., & Sadowska‐Bartosz, I. (2018) · Aging · doi:10.18632/aging.101450 · Cited by 133 · see citing works

Protein tyrosine nitration in plants: Present knowledge, computational prediction and future perspectives

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 · see citing works

Mass Spectrometry-Based Methods for Identifying Oxidized Proteins in Disease: Advances and Challenges

Verrastro, I., Pasha, S., Jensen, K., Pitt, A., & Spickett, C. (2015) · Biomolecules · doi:10.3390/biom5020378 · Cited by 114 · see citing works

Enrichment of extracellular vesicles from tissues of the central nervous system by PROSPR

Gallart‐Palau, X., Serra, A., & Sze, S. K. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0108-1 · Cited by 111 · see citing works

Association of Oxidative Stress with Neurological Disorders

Hassan, W., Noreen, H., Rehman, S., Kamal, M. A., & da Rocha, J. B. T. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666211111141246 · Cited by 105 · see citing works

Insights into the Molecular Mechanisms of Alzheimer’s and Parkinson’s Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology

Coskuner‐Weber, O., & Uversky, V. N. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020336 · Cited by 66 · see citing works

Gas Plasma Technology Augments Ovalbumin Immunogenicity and OT‐II T Cell Activation Conferring Tumor Protection in Mice

Clemen, R., Freund, E., Mrochen, D. M., Miebach, L., Schmidt, A., Rauch, B. H., Lackmann, J., Martens, U., Wende, K., Lalk, M., et al. (2021) · Advanced Science · doi:10.1002/advs.202003395 · Cited by 62 · see citing works

Advancements in the Analytical Quantification of Nitroxidative Stress Biomarker 3-Nitrotyrosine in Biological Matrices

Bandookwala, M., Thakkar, D., & Sengupta, P. (2019) · Critical Reviews in Analytical Chemistry · doi:10.1080/10408347.2019.1623010 · Cited by 60 · see citing works

Modulation of the Interactions Between α-Synuclein and Lipid Membranes by Post-translational Modifications

Bell, R., & Vendruscolo, M. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.661117 · Cited by 52 · see citing works

High Fat Diet and Inflammation – Modulation of Haptoglobin Level in Rat Brain

Spagnuolo, M. S., Mollica, M. P., Maresca, B., Cavaliere, G., Cefaliello, C., Trinchese, G., Scudiero, R., Crispino, M., & Cigliano, L. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00479 · Cited by 47 · see citing works

Tyrosine Regulates β-Sheet Structure Formation in Amyloid-β42: A New Clustering Algorithm for Disordered Proteins

Coskuner‐Weber, O., & Uversky, V. N. (2017) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.6b00761 · Cited by 43 · see citing works

Proteomics of the heart

Karpov, O. A., Stotland, A. B., Raedschelders, K., Chazarin, B., Ai, L., Murray, C. I., & Eyk, J. E. V. (2024) · Physiological Reviews · doi:10.1152/physrev.00026.2023 · Cited by 42 · see citing works

The effects of nitric oxide in Alzheimer’s disease

Wang, L., Lu, D., Wang, X., Wang, Z., Li, W., & Chen, G. (2023) · Medical Gas Research · doi:10.4103/2045-9912.385939 · Cited by 37 · see citing works

Protein species as diagnostic markers

Steffen, P., Kwiatkowski, M., Robertson, W. D., Zarrine‐Afsar, A., Deterra, D., Richter, V., & Schlüter, H. (2015) · Journal of Proteomics · doi:10.1016/j.jprot.2015.12.015 · Cited by 35 · see citing works

Simultaneous Detection of 3-Nitrotyrosine and 3-Nitro-4-hydroxyphenylacetic Acid in Human Urine by Online SPE LC-MS/MS and Their Association with Oxidative and Methylated DNA Lesions

Chao, M., Hsu, Y., Liu, H., Lin, J.-H., & Hu, C. (2015) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.5b00031 · Cited by 34 · see citing works

Conjugation site analysis of antibody-drug-conjugates (ADCs) by signature ion fingerprinting and normalized area quantitation approach using nano-liquid chromatography coupled to high resolution mass spectrometry

Sang, H., Lu, G., Liu, Y., Hu, Q., Weifeng, X., Cui, D., Zhou, F., Zhang, J., Hao, H., Wang, G., et al. (2016) · Analytica Chimica Acta · doi:10.1016/j.aca.2016.11.073 · Cited by 34 · see citing works

Cadmium-Induced Oxidative and Nitrosative Stress in Plants

Gallego, S. M., & Benavides, M. P. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814864-8.00010-3 · Cited by 34 · see citing works

Uncovering Neurodegenerative Protein Modifications via Proteomic Profiling

Gallart‐Palau, X., Serra, A., & Sze, S. K. (2015) · International review of neurobiology · doi:10.1016/bs.irn.2015.06.002 · Cited by 31 · see citing works

Selective Affinity Enrichment of Nitrotyrosine-Containing Peptides for Quantitative Analysis in Complex Samples

Zhao, Y., Zhang, Y., Sun, H., Maroto, R., & Brasier, A. R. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00275 · Cited by 28 · see citing works

Neuronal Nitric Oxide Synthase Induction in the Antitumorigenic and Neurotoxic Effects of 2-Methoxyestradiol

Górska‐Ponikowska, M., Kuban‐Jankowska, A., Zmijewski, M. A., Gorzynik-Debicka, M., Szkatuła, M., & Woźniak, M. (2014) · Molecules · doi:10.3390/molecules190913267 · Cited by 28 · see citing works

Insights Into the Mechanism of Tyrosine Nitration in Preventing β-Amyloid Aggregation in Alzheimer’s Disease

Zhao, J. J., Shi, Q., Zheng, Y., Liu, Q., He, Z., Gao, Z., & Liu, Q. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.619836 · Cited by 22 · see citing works

Uncommon posttranslational modifications in proteomics: ADP‐ribosylation, tyrosine nitration, and tyrosine sulfation

Bashyal, A., & Brodbelt, J. S. (2022) · Mass Spectrometry Reviews · doi:10.1002/mas.21811 · Cited by 22 · see citing works

Mechanism of oxidative stress and neurotoxicity associated with heme and copper–Aβ relevant to Alzheimer's disease

Dey, C., Roy, M., Pal, P., Ghosh, R., & Dey, S. G. (2025) · Chemical Society Reviews · doi:10.1039/d5cs00544b · Cited by 21 · see citing works

ZnO nanoparticles as a sensitive platform for detection of nitration in tyrosine and tryptophan: A DFT study

Maddahi, P. S., Yeganeh, M., & Baghsiyahi, F. B. (2019) · Materials Chemistry and Physics · doi:10.1016/j.matchemphys.2019.121857 · Cited by 20 · see citing works

Nitrated food proteins induce a regulatory immune response associated with allergy prevention after oral exposure in a Balb/c mouse food allergy model

Samadi, N., Klems, M., Heiden, D., Bauer, R., Kitzmüller, C., Weidmann, E., Ret, D., Ondracek, A. S., Duschl, A., Horejs‐Hoeck, J., et al. (2019) · Allergy · doi:10.1111/all.14030 · Cited by 18 · see citing works

Regulation of glutamine synthetase activity by transcriptional and posttranslational modifications negatively influences ganoderic acid biosynthesis in Ganoderma lucidum

Zhu, J. K., Song, S., Sun, Z., Lian, L., Shi, L., Ren, A., & Zhao, M. (2021) · Environmental Microbiology · doi:10.1111/1462-2920.15400 · Cited by 17 · see citing works

Nitration of β-Lactoglobulin but Not of Ovomucoid Enhances Anaphylactic Responses in Food Allergic Mice

Diesner, S. C., Schultz, C., Ackaert, C., Oostingh, G. J., Ondracek, A. S., Stremnitzer, C., Singer, J., Heiden, D., Roth‐Walter, F., Fazekas, J., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126279 · Cited by 17 · see citing works

Nitric Oxide: Regulation and Function in Neutrophil Immune Responses

Kumar, S., & Dikshit, M. (2024) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0220 · Cited by 14 · see citing works

Metabolic profiling of 19 amino acids in triptolide-induced liver injured rats by gas chromatography-triple quadrupole mass spectrometry

Hu, C., Li, H., Wu, L., Ke, J.-Q., Yu, X.-C., Xiong, Y., & Tang, X. (2021) · Human & Experimental Toxicology · doi:10.1177/09603271211006167 · Cited by 14 · see citing works

Decreased proteasomal cleavage at nitrotyrosine sites in proteins and peptides

Ott, C., Tomasina, F., Campolo, N., Bartesaghi, S., Mastrogiovanni, M., Leyva, A., Batthyány, C., Meinl, W., Grune, T., & Radí, R. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102106 · Cited by 13 · see citing works

Exploration of Nitrotyrosine-Containing Proteins and Peptides by Antibody-Based Enrichment Strategies

Bhat, F. A., Mangalaparthi, K. K., Ding, H., Jain, A., Hsu, J.-S., Peterson, J. A., Zenka, R. M., Mun, D., Kandasamy, R. K., & Pandey, A. (2024) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2024.100733 · Cited by 11 · see citing works

Computational prediction of NO-dependent posttranslational modifications in plants: Current status and perspectives

Kolbert, Z., & Lindermayr, C. (2021) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2021.09.011 · Cited by 11 · see citing works

Cross‐talk of Reactive Oxygen Species and Nitric Oxide in Various Processes of Plant Development

Kolbert, Z., & Feigl, G. (2017) · doi:10.1002/9781119324928.ch14 · Cited by 11 · see citing works

Switchable Nitroproteome States of Phytophthora infestans Biology and Pathobiology

Izbiańska, K., Floryszak‐Wieczorek, J., Gajewska, J., Gzyl, J., Jelonek, T., & Arasimowicz‐Jelonek, M. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01516 · Cited by 10 · see citing works

Biomarkers of nitro-oxidation and oxidative stress

Gašparović, A. Č., Žarković, N., & Bottari, S. P. (2017) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2017.10.002 · Cited by 11 · see citing works

Design of a Protein Motif Responsive to Tyrosine Nitration and an Encoded Turn-Off Sensor of Tyrosine Nitration

Urmey, A. R., & Zondlo, N. J. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00334 · Cited by 9 · see citing works

Nitric Oxide Mediated Degradation of CYP2A6 via the Ubiquitin-Proteasome Pathway in Human Hepatoma Cells

Cerrone, J., Lee, C., Tian, M., & Morgan, E. T. (2020) · Drug Metabolism and Disposition · doi:10.1124/dmd.119.089961 · Cited by 8 · see citing works

Reactive Species in Progeroid Syndromes and Aging-Related Processes

Crochemore, C., Cimmaruta, C., Molina, C. F., & Ricchetti, M. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8242 · Cited by 8 · see citing works

Glucose transporter 1 deficiency, AMP-activated protein kinase activation and immune dysregulation in autism spectrum disorder: Novel biomarker sources for clinical diagnosis

Al-Bishri, W. M. (2023) · Saudi Journal of Biological Sciences · doi:10.1016/j.sjbs.2023.103849 · Cited by 7 · see citing works

Recent Advances in the Synthesis of Antioxidant Derivatives: Pharmacological Insights for Neurological Disorders

Singh, K., Gupta, J. K., Sethi, P., Mathew, S., Bhatt, A., Sharma, M. C., Saha, S., Khan, S., & Kumar, S. (2024) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266305736240725052825 · Cited by 6 · see citing works

Immune Effects of the Nitrated Food Allergen Beta-Lactoglobulin in an Experimental Food Allergy Model

Ondracek, A. S., Heiden, D., Oostingh, G. J., Fuerst, E., Fazekas, J., Bergmayr, C., Rohrhofer, J., Jensen‐Jarolim, E., Duschl, A., & Untersmayr, E. (2019) · Nutrients · doi:10.3390/nu11102463 · Cited by 6 · see citing works

Evidence for the Prerequisite Formation of Phenoxyl Radicals in Radical‐Mediated Peptide Tyrosine Nitration In Vacuo

Lai, C., Tang, W. K., Siu, C., & Chu, I. K. (2019) · Chemistry - A European Journal · doi:10.1002/chem.201904484 · Cited by 6 · see citing works

In-vivo protein nitration facilitates Vibrio cholerae cell survival under anaerobic, nutrient deprived conditions

Patra, S. K., Sinha, N., Molla, F., Sengupta, A., Chakraborty, S., Roy, S., & Ghosh, S. (2022) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2022.109358 · Cited by 6 · see citing works

Biomarkers of Oxidative Damage

Khelfi, A. (2024) · Springer eBooks · doi:10.1007/978-3-031-60738-7_3 · Cited by 2 · see citing works

Protein Nitration in Patients with Mitochondrial Diseases

Livramento, J. B., Rodrigues, G. S., Faber, J., Filho, L. A. D. S., Moura, F. V., Barros, C. D. S., Pinto, W. B. V. D. R., Schmidt, B., Oliveira, A. S. B., Kiyomoto, B. H., et al. (2025) · Antioxidants · doi:10.3390/antiox14020211 · Cited by 2 · see citing works

Physiological, Biochemical, and Molecular Mechanism of Nitric Oxide-Mediated Abiotic Stress Tolerance

Singh, K., Shukla, I., Tiwari, A. K., & Azmi, L. (2021) · Springer eBooks · doi:10.1007/978-3-030-61153-8_11 · Cited by 2 · see citing works

Immuno-Affinity Study of Oxidative Tyrosine Containing Peptides

Darie‐Ion, L., Neamțu, A., Iliescu, R., & Petre, B. A. (2022) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-021-10329-2 · Cited by 2 · see citing works

Mixed-ligand Zr-MOF with dual-emissions for highly selective ratiometric detection of 3-nitrotyrosine

Tariq, M. A., Cheng, Y., Fatima, M., Wang, F., Ahmad, H. M., Gul, S., Ushna, & Xiao, Y. (2026) · Microchemical Journal · doi:10.1016/j.microc.2026.118114 · Cited by 1 · see citing works

Electrochemical, Mass Spectroscopic, Immunochemical, and Nuclear Magnetic Resonance Techniques

Villamena, F. A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-420017-3.00008-6 · Cited by 1 · see citing works

Exogenous ascorbic acid is a pro-nitrant in Arabidopsis thaliana

Feigl, G., Bordé, Á., Molnár, Á., & Kolbert, Z. (2019) · Acta Biologica Szegediensis · doi:10.14232/abs.2018.2.115-122 · Cited by 1 · see citing works

Tyrosine Nitration

Zhan, X., Long, Y., & Desiderio, D. M. (2016) · doi:10.1002/9781119250906.ch5 · Cited by 1 · see citing works

Multiplexing Techniques in Quantitative Proteomics to Study Disease

Evans, A. R. (2015) · D-Scholarship@Pitt (University of Pittsburgh)

Characterizing the Nitroproteome Using Bioinformatic Tools: A Mini-Review

Bhattacharjee, A. (2017) · Biostatistics and Biometrics Open Access Journal · doi:10.19080/bboaj.2017.01.555553

In-vivo Protein Nitration and De-Nitration Facilitate Vibrio cholerae Cell Survival Under Anaerobic Nutrient Deprived Condition: Consequences of Nitrite Induced Protein Nitration

Patra, S. K., Sinha, N., Sengupta, A., Chakraborty, S., Roy, S., & Ghosh, S. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.12.219

Proteomics

Moharana, A. K., Baskaran, S., Sikka, S. C., & Selvam, M. K. P. (2024) · Springer eBooks · doi:10.1007/978-3-031-60738-7_20

Proteomics of Nitrotyrosine: Integrating Mass Spectrometry and Immunodetection in Redox‐Driven Pathology

Petre, B. A. (2026) · Mass Spectrometry Reviews · doi:10.1002/mas.70020

Hydrophilicity of heme derivatives influences site-specific tyrosine nitration in MnSOD

Ye, H., Liu, Y., Zhou, T., Xiao, B., Gao, Z., & Li, H. (2026) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2026.113378

Oxidative Stress in Alzheimer’s Disease: Can Dietary Interventions Provide Neuroprotection?

Kupczyk, D., Bilski, R., Kozieł, I., Słota, A., Kurek, M., Stablewska, E., Baumgart, S., Słomka, A., & Studzińska, R. (2026) · Nutrients · doi:10.3390/nu18152436

Tyrosine nitration: An emerging mechanistic landscape in neurodegeneration and cardiopulmonary disease

Adrita, N., Claassen, I., Huerta, M., Black, S. M., Estévez, Á. G., Roberts, B. R., Beckman, J. S., & Franco, M. C. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104423

Protein Nitration in Biological Aging: Proteomic and Tandem Mass Spectrometric Characterization of Nitrated Sites

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 · see citing works

Mass Spectrometry-based Methods for the Detection and Characterization of Protein-Tyrosine Nitration

Seeley, K. W. (2013) · Digital Commons - University of South Florida (University of South Florida)

Proteomic Analysis of Protein Nitration in Aging Skeletal Muscle and Identification of Nitrotyrosine-containing Sequences in Vivo by Nanoelectrospray Ionization Tandem Mass Spectrometry

Kański, J., Hong, S. J., & Schöneich, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501773200 · Cited by 177 · see citing works

Nitrosative protein tyrosine modifications: biochemistry and functional significance

Yeo, W., Lee, S., Lee, J.-R., & Kim, K. P. (2008) · BMB Reports · doi:10.5483/bmbrep.2008.41.3.194 · Cited by 76 · see citing works

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 57 · see citing works