Cited by 114Redox biology and oxidative stressAdvanced Proteomics Techniques and ApplicationsMass Spectrometry Techniques and Applications

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

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Verrastro, Ivan, Pasha, Sabah, Jensen, Karina, Pitt, Andrew, Spickett, Corinne·2015·Biomolecules

DOI 10.3390/biom5020378PMC PMC4496678

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Abstract

Many inflammatory diseases have an oxidative aetiology, which leads to oxidative damage to biomolecules, including proteins. It is now increasingly recognized that oxidative post-translational modifications (oxPTMs) of proteins affect cell signalling and behaviour, and can contribute to pathology. Moreover, oxidized proteins have potential as biomarkers for inflammatory diseases. Although many assays for generic protein oxidation and breakdown products of protein oxidation are available, only advanced tandem mass spectrometry approaches have the power to localize specific oxPTMs in identified proteins. While much work has been carried out using untargeted or discovery mass spectrometry approaches, identification of oxPTMs in disease has benefitted from the development of sophisticated targeted or semi-targeted scanning routines, combined with chemical labeling and enrichment approaches. Nevertheless, many potential pitfalls exist which can result in incorrect identifications. This review explains the limitations, advantages and challenges of all of these approaches to detecting oxidatively modified proteins, and provides an update on recent literature in which they have been used to detect and quantify protein oxidation in disease.

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Figure 1 Structures of oxidized residues most commonly detected and studied by mass spectrometry. In mixed disulfides, R can be cysteine or glutathione (glutathionylation).CC BY · PubMed Central

Figure 2 Summary of advanced methods for identification of proteins and oxPTMs. Labeling and enrichment can also be carried out at the protein level, but this approach is less common.CC BY · PubMed Central

Figure 3 Incorrectly assigned oxidation to proline using a probability-based search engine. (a) Search engine identified 2 modifications on one peptide: methionine-7 mono-oxidation and proline-9 oxidation; (b) de novo sequencing showed that methionine is dioxidised.CC BY · PubMed Central

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Chemical and cytokine features of innate immunity characterize serum and tissue profiles in inflammatory bowel disease
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Protein carbonylation: avoiding pitfalls in the 2,4-dinitrophenylhydrazine assay
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Proteomic profiling of human liver biopsies: hepatitis C virus-induced fibrosis and mitochondrial dysfunction
Diamond, D. L., Jacobs, J. M., Paeper, B., Proll, S. C., Gritsenko, M. A., Carithers, R. L., Larson, A. M., Yeh, M. M., Camp, D. G., Smith, R. D., et al. (2007) · Hepatology · doi:10.1002/hep.21751 · Cited by 114
High-Throughput Proteomic-Based Identification of Oxidatively Induced Protein Carbonylation in Mouse Brain
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Measurement and meaning of markers of reactive species of oxygen, nitrogen and sulfur in healthy human subjects and patients with inflammatory joint disease
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Functional impact of oxidative posttranslational modifications on fibrinogen and fibrin clots
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Nox isoforms in vascular pathophysiology: insights from transgenic and knockout mouse models
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Profiling Carbonylated Proteins in Human Plasma
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In Vivo Quantitative Proteomics: The SILAC Mouse
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Mass Spectrometry-Based Quantitative Proteomics for Dissecting Multiplexed Redox Cysteine Modifications in Nitric Oxide-Protected Cardiomyocyte Under Hypoxia
Pan, K., Chen, Y.-Y., Pu, T.-H., Chao, Y.-S., Yang, C., Bomgarden, R. D., Rogers, J. C., Meng, T., & Khoo, K. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5326 · Cited by 101
Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia
Ho, Y.-S., Xiong, Y., Ho, D. S., Gao, J., Chua, B. H. L., Pai, H. V., & Mieyal, J. J. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.07.025 · Cited by 101
Mass spectrometric identification of oxidative modifications of tryptophan residues in proteins: Chemical artifact or post-translational modification?
Perdivara, I., Deterding, L. J., Przybylski, M., & Tomer, K. B. (2010) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2010.02.016 · Cited by 100
Multiple reaction monitoring as a method for identifying protein posttranslational modifications.
Cox, D. M., Zhong, F., Du, ‬., Duchoslav, E., Sakuma, T., & McDermott, J. C. (2005) · PubMed Central · Cited by 99
Proteomic identification and quantification of S-glutathionylation in mouse macrophages using resin-assisted enrichment and isobaric labeling
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Integrated Redox Proteomics and Metabolomics of Mitochondria to Identify Mechanisms of Cd Toxicity
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Analysis of Biological Samples Using Paper Spray Mass Spectrometry: An Investigation of Impacts by the Substrates, Solvents and Elution Methods
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Oxidative stress occurs early in Down syndrome pregnancy: A redox proteomics analysis of amniotic fluid
Perluigi, M., di Domenico, F., Fiorini, A., Cocciolo, A., Giorgi, A., Foppoli, C., Butterfield, D. A., Giorlandino, M., Giorlandino, C., Eugenia Schininà, M., et al. (2011) · PROTEOMICS – Clinical Applications · doi:10.1002/prca.201000121 · Cited by 97
A rapid sample preparation method for mass spectrometric characterization of N‐linked glycans
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Optimizing capillary electrophoresis for top‐down proteomics of 30–80 kDa proteins
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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
In Vitro and in Vivo Protein-bound Tyrosine Nitration Characterized by Diagonal Chromatography
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Multiplexed Proteomic Analysis of Oxidation and Concentrations of Cerebrospinal Fluid Proteins in Alzheimer Disease
Korolainen, M. A., Nyman, T. A., Nyyssönen, P., Hartikainen, S., & Pirttilä, T. (2007) · Clinical Chemistry · doi:10.1373/clinchem.2006.078014 · Cited by 85
Proteomic identification of carbonylated proteins in the monkey hippocampus after ischemia–reperfusion
Oikawa, S., Yamada, T., Minohata, T., Kobayashi, H., Furukawa, A., Tada‐Oikawa, S., Hiraku, Y., Murata, M., Kikuchi, M., & Yamashima, T. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.02.029 · Cited by 84
Open MS/MS spectral library search to identify unanticipated post-translational modifications and increase spectral identification rate
Ding, Y., Fu, Y., Sun, R.-X., Wang, H., Yuan, Z., Chi, H., & He, S. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq185 · Cited by 84
DeNovoGUI: An Open Source Graphical User Interface for de Novo Sequencing of Tandem Mass Spectra
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Carbonylated Plasma Proteins As Potential Biomarkers of Obesity Induced Type 2 Diabetes Mellitus
Bollineni, R. C., Fedorova, M., Blüher, M., & Hoffmann, R. (2014) · Journal of Proteome Research · doi:10.1021/pr500324y · Cited by 82
A Platform for Accurate Mass and Time Analyses of Mass Spectrometry Data
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Signaling by S-nitrosylation in the heart
Murphy, E., Kohr, M., Menazza, S., Nguyen, T., Evangelista, A., Sun, J., & Steenbergen, C. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.01.003 · Cited by 82
Quantitative Proteomic Profiling of Muscle Type-Dependent and Age-Dependent Protein Carbonylation in Rat Skeletal Muscle Mitochondria
Feng, J., Xie, H., Meany, D. L., Thompson, L. V., Arriaga, E. A., & Griffin, T. J. (2008) · The Journals of Gerontology Series A · doi:10.1093/gerona/63.11.1137 · Cited by 82
UniNovo: a universal tool for de novo peptide sequencing
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A replaceable microreactor for on-line protein digestion in a two-dimensional capillary electrophoresis system with tandem mass spectrometry detection
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A rapid LC-FTMS method for the analysis of cysteine, cystine and cysteine/cystine steady-state redox potential in human plasma
Johnson, J. M., Strobel, F. H., Reed, M. S., Pohl, J., & Jones, D. P. (2008) · Clinica Chimica Acta · doi:10.1016/j.cca.2008.06.020 · Cited by 78
HNE Michael Adducts to Histidine and Histidine-Containing Peptides as Biomarkers of Lipid-Derived Carbonyl Stress in Urines: LC−MS/MS Profiling in Zucker Obese Rats
Orioli, M., Aldini, G., Benfatto, M. C., Facino, R. M., & Carini, M. (2007) · Analytical Chemistry · doi:10.1021/ac7016184 · Cited by 78
Gastric Cancer-Specific Protein Profile Identified Using Endoscopic Biopsy Samples via MALDI Mass Spectrometry
Kim, H. K., Reyzer, M. L., Choi, I. J., Kim, C. G., Kim, H. S., Oshima, A., Chertov, O., Colantonio, S., Fisher, R. J., Allen, J. L., et al. (2010) · Journal of Proteome Research · doi:10.1021/pr100302b · Cited by 78
The Influence of Oxidative Damage on Viscosity of Seminal Fluid in Infertile Men
Aydemir, B., Onaran, İ., Kızıler, A. R., Alıcı, B., & Akyolcu, M. C. (2007) · Journal of Andrology · doi:10.2164/jandrol.107.003046 · Cited by 78
Analytical methods for 3-nitrotyrosine quantification in biological samples: the unique role of tandem mass spectrometry
Tsikas, D. (2010) · Amino Acids · doi:10.1007/s00726-010-0604-5 · Cited by 75
In-Line Separation by Capillary Electrophoresis Prior to Analysis by Top-Down Mass Spectrometry Enables Sensitive Characterization of Protein Complexes
Han, X., Wang, Y., Aslanian, A., Fonslow, B., Graczyk, B., Davis, T. N., & Yates, J. R. (2014) · Journal of Proteome Research · doi:10.1021/pr500971h · Cited by 72
De Novo Protein Sequencing by Combining Top-Down and Bottom-Up Tandem Mass Spectra
Liu, X., Dekker, L. J. M., Wu, S., VanDuijn, M. M., Luider, T. M., Tolić, N., Kou, Q., Dvorkin, M. V., Alexandrova, S., Vyatkina, K., et al. (2014) · Journal of Proteome Research · doi:10.1021/pr401300m · Cited by 71
Evolutionary Acquisition of Cysteines Determines FOXO Paralog-Specific Redox Signaling
Putker, M., Vos, H. R., van Dorenmalen, K. M. A., de Ruiter, H., Duran, A. G., Snel, ‎., Burgering, B. M. T., Vermeulen, M., & Dansen, T. B. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6056 · Cited by 71
Immunoaffinity liquid chromatography–tandem mass spectrometry detection of nitrotyrosine in biological fluids: Development of a clinically translatable biomarker
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Protein redox chemistry: post-translational cysteine modifications that regulate signal transduction and drug pharmacology
Wani, R., Nagata, A., & Murray, B. W. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00224 · Cited by 70
Measurement of S -Nitrosylation Occupancy in the Myocardium With Cysteine-Reactive Tandem Mass Tags
Kohr, M. J., Aponte, A. M., Sun, J., Guček, M., Steenbergen, C., & Murphy, E. (2012) · Circulation Research · doi:10.1161/circresaha.112.271320 · Cited by 70
In Vivo Markers of Oxidative Stress and Therapeutic Interventions
Tsimikas, S. (2008) · The American Journal of Cardiology · doi:10.1016/j.amjcard.2008.02.006 · Cited by 67
Protein oxidation: role in signalling and detection by mass spectrometry
Spickett, C. M., & Pitt, A. R. (2012) · Amino Acids · doi:10.1007/s00726-010-0585-4 · Cited by 65
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Accurate Determination of Protein Methionine Oxidation by Stable Isotope Labeling and LC-MS Analysis
Liu, H., Ponniah, G., Neill, A., Patel, R., & Andrien, B. A. (2013) · Analytical Chemistry · doi:10.1021/ac403072w · Cited by 64
Proteomic analysis of protein S ‐nitrosylation
Torta, F. T., Usuelli, V., Malgaroli, A., & Bachi, A. (2008) · PROTEOMICS · doi:10.1002/pmic.200800089 · Cited by 63
Differential Carbonylation of Proteins as a Function of in vivo Oxidative Stress
Madian, A. G., Myracle, A. D., Diaz-Maldonado, N., Rochelle, N. S., Janle, E. M., & Regnier, F. E. (2011) · Journal of Proteome Research · doi:10.1021/pr200140x · Cited by 63
Mass Spectrometry Compatible Surfactant for Optimized In-Gel Protein Digestion
Saveliev, S. V., Woodroofe, C. C., Sabat, G., Adams, C. M., Klaubert, D., Wood, K., & Urh, M. (2013) · Analytical Chemistry · doi:10.1021/ac302423t · Cited by 62
Ubiquitination and cysteine nitrosylation during aging and Alzheimer's disease
Riederer, I. M., Schiffrin, M., Kövari, E., Bouras, C., & Riederer, B. M. (2009) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2009.04.018 · Cited by 61
Mass spectrometric analysis of protein tyrosine nitration in aging and neurodegenerative diseases
Yeo, W., Kim, Y. J., Kabir, M. H., Kang, J. W., & Kim, K. P. (2015) · Mass Spectrometry Reviews · doi:10.1002/mas.21429 · Cited by 61
Nitrosothiol signaling and protein nitrosation in cell death
Iyer, A. K. V., Rojanasakul, Y., & Azad, N. (2014) · Nitric Oxide · doi:10.1016/j.niox.2014.07.002 · Cited by 61
Circulating free nitrotyrosine in obstructive sleep apnea
Svatikova, A., Wolk, R. A., Wang, H. H., Otto, M. E. B., Bybee, K. A., Singh, R. J., & Somers, V. K. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00241.2004 · Cited by 60
Site-specific proteomic analysis of lipoxidation adducts in cardiac mitochondria reveals chemical diversity of 2-alkenal adduction
Chavez, J. D., Wu, J., Bisson, W. H., & Maier, C. S. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.03.031 · Cited by 60
Quantification of Modified Tyrosines in Healthy and Diabetic Human Urine using Liquid Chromatography/Tandem Mass Spectrometry
Kato, Y., Dozaki, N., Nakamura, T., Kitamoto, N., Yoshida, A., Naito, M., Kitamura, M., & Osawa, T. (2009) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.08-185 · Cited by 60
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
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 57
Proteome-wide profiling of carbonylated proteins and carbonylation sites in HeLa cells under mild oxidative stress conditions
Bollineni, R. C., Hoffmann, R., & Fedorova, M. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.11.030 · Cited by 57
Improved sequencing of oxidized cysteine and methionine containing peptides using electron transfer dissociation
Srikanth, R., Wilson, J. G., Bridgewater, J. D., Numbers, J. R., Lim, J., Olbris, M. R., Kettani, A., & Vachet, R. W. (2007) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2007.05.011 · Cited by 56
Redox proteomics of thiol proteins in mouse heart during ischemia/reperfusion using ICAT reagents and mass spectrometry
Kumar, V., Kleffmann, T., Hampton, M. B., Cannell, M. B., & Winterbourn, C. C. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.01.021 · Cited by 56
Quantitative proteomics and biomarker discovery in human cancer
Zhao, Y., Lee, W. P., & Xiao, G. G. (2009) · Expert Review of Proteomics · doi:10.1586/epr.09.8 · Cited by 56
Increased thrombin-induced polymerization of fibrinogen associated with high protein carbonyl levels in plasma from patients post myocardial infarction
Paton, L. N., Mocatta, T. J., Richards, M., & Winterbourn, C. C. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.10.044 · Cited by 52
Bidimensional Tandem Mass Spectrometry for Selective Identification of Nitration Sites in Proteins
Amoresano, A., Chiappetta, G., Pucci, P., d’Ischia, M., & Marino, G. (2007) · Analytical Chemistry · doi:10.1021/ac0620361 · Cited by 51
Identification of protein carbonylation sites by two-dimensional liquid chromatography in combination with MALDI- and ESI-MS
Bollineni, R. C., Hoffmann, R., & Fedorova, M. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.07.002 · Cited by 51
The SNO/SOH TMT strategy for combinatorial analysis of reversible cysteine oxidations
Wojdyła, K., Williamson, J. C., Roepstorff, P., & Rogowska-Wrzesińska, A. (2014) · Journal of Proteomics · doi:10.1016/j.jprot.2014.10.015 · Cited by 50
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
Multiplexed Proteomics Mapping of Yeast RNA Polymerase II and III Allows Near-Complete Sequence Coverage and Reveals Several Novel Phosphorylation Sites
Mohammed, S., Lorenzen, K., Kerkhoven, R., van Breukelen, B., Vannini, A., Cramer, P., & Heck, A. J. R. (2008) · Analytical Chemistry · doi:10.1021/ac7024283 · Cited by 49
Increased methionine sulfoxide content of apoA-I in type 1 diabetes
Brock, J. W. C., Jenkins, A. J., Lyons, T. J., Klein, R. L., Yim, E., Lopes-Virella, M. F., Carter, R. E., Thorpe, S. R., & Baynes, J. (2008) · Journal of Lipid Research · doi:10.1194/jlr.m800015-jlr200 · Cited by 49
Enhanced Sample Multiplexing for Nitrotyrosine-Modified Proteins Using Combined Precursor Isotopic Labeling and Isobaric Tagging
Robinson, R. A. S., & Evans, A. R. (2012) · Analytical Chemistry · doi:10.1021/ac202000v · Cited by 44
Plasma 3-nitrotyrosine is a biomarker in animal models of arthritis: Pharmacological dissection of iNOS’ role in disease
Nemirovskiy, O. V., Radabaugh, M. R., Aggarwal, P., Funckes-Shippy, C. L., Mnich, S. J., Meyer, D. M., Sunyer, T., Mathews, W. R., & Misko, T. P. (2008) · Nitric Oxide · doi:10.1016/j.niox.2008.12.005 · Cited by 44
A Rapid Approach for the Detection, Quantification, and Discovery of Novel Sulfenic Acid or S-Nitrosothiol Modified Proteins Using a Biotin-Switch Method
Burgoyne, J. R., & Eaton, P. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)73015-9 · Cited by 43
Oxidative stress induced carbonylation in human plasma
Madian, A. G., Diaz-Maldonado, N., Gao, Q., & Regnier, F. E. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.07.014 · Cited by 43
Selective quantification of free 3-nitrotyrosine in exhaled breath condensate in asthma using gas chromatography/tandem mass spectrometry
Lärstad, M., Söderling, A., Caidahl, K., & Olin, A. (2005) · Nitric Oxide · doi:10.1016/j.niox.2005.05.009 · Cited by 43
A quantitative proteomic workflow for characterization of frozen clinical biopsies: Laser capture microdissection coupled with label-free mass spectrometry
Shapiro, J. P., Biswas, S., Merchant, A. S., Satoskar, A. A., Taslim, C., Lin, S., Rovin, B. H., Sen, C. K., Roy, S., & Freitas, M. A. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.09.019 · Cited by 37
Development of novel mass spectrometric methods for identifying HOCl‐induced modifications to proteins
Mouls, L., Silajdžić, E., Haroune, N., Spickett, C. M., & Pitt, A. R. (2009) · PROTEOMICS · doi:10.1002/pmic.200800391 · Cited by 35
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Molecular Analysis of Serum and Bronchoalveolar Lavage in a Mouse Model of Influenza Reveals Markers of Disease Severity That Can Be Clinically Useful in Humans
Kumar, Y., Liang, C., Limmon, G. V., Li, L., Engelward, B. P., Ooi, E. E., Chen, J., & Tannenbaum, S. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086912 · Cited by 33
Top-down MS for rapid methionine oxidation site assignment in filgrastim
Holzmann, J., Hausberger, A., Rupprechter, A., & Toll, H. (2013) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-013-7138-0 · Cited by 32
Redox regulation of tumour suppressor protein p53: identification of the sites of hydrogen peroxide oxidation and glutathionylation
Scotcher, J., Clarke, D. J., Mackay, C. L., Hupp, T. R., Sadler, P. J., & Langridge‐Smith, P. R. R. (2013) · Chemical Science · doi:10.1039/c2sc21702c · Cited by 32
Assessment of Oxidative Damage to Proteins and DNA in Urine of Newborn Infants by a Validated UPLC-MS/MS Approach
Kuligowski, J., Torres-Cuevas, I., Quintás‐Cardama, A., Rook, D., van Goudoever, J. B., Cubells, E., Asensi, M. A., Lliso, I., Nuñez, A., Vento, M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093703 · Cited by 32
Differential Proteomic Analysis of Mammalian Tissues Using SILAM
McClatchy, D. B., Liao, L., Park, S. K., Xu, T., Lu, B., & Yates, J. R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016039 · Cited by 31
Novel method to investigate protein carbonylation by iTRAQ strategy
Palmese, A., Rosa, C. D., Chiappetta, G., Marino, G., & Amoresano, A. (2012) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-012-6324-9 · Cited by 30
Absolute proteomic quantification of the activity state of proteases and proteolytic cleavages using proteolytic signature peptides and isobaric tags
Fahlman, R. P., Chen, W., & Overall, C. M. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.09.006 · Cited by 30
Computer aided manual validation of mass spectrometry-based proteomic data
Curran, T. G., Bryson, B. D., Reigelhaupt, M., Johnson, H., & White, F. M. (2013) · Methods · doi:10.1016/j.ymeth.2013.03.004 · Cited by 28
On-Membrane Tryptic Digestion of Proteins for Mass Spectrometry Analysis
Luque-Garcia, J. L., & Neubert, T. A. (2009) · Methods in molecular biology · doi:10.1007/978-1-59745-542-8_35 · Cited by 27
Isotope‐coded dimethyl tagging for differential quantification of posttranslational protein carbonylation by 4‐hydroxy‐2‐nonenal, an end‐product of lipid peroxidation
Rauniyar, N., & Prókai, L. (2011) · Journal of Mass Spectrometry · doi:10.1002/jms.1978 · Cited by 25
Mass spectrometry-based identification of S-nitrosocysteine in vivo using organic mercury assisted enrichment
Doulias, P., Raju, K., Greene, J. L., Τενοπούλου, Μ., & Ischiropoulos, H. (2012) · Methods · doi:10.1016/j.ymeth.2012.10.009 · Cited by 25
Artifacts to avoid while taking advantage of top‐down mass spectrometry based detection of protein S‐thiolation
Auclair, J. R., Salisbury, J. P., Johnson, J. L., Petsko, G. A., Ringe, D., Bosco, D. A., Agar, N. Y. R., Santagata, S., Durham, H. D., & Agar, J. N. (2014) · PROTEOMICS · doi:10.1002/pmic.201300450 · Cited by 25
Mass Spectrometric Strategies and Their Applications for Molecular Mass Determination of Recombinant Therapeutic Proteins
Carini, M., Regazzoni, L., & Aldini, G. (2011) · Current Pharmaceutical Biotechnology · doi:10.2174/138920111798357348 · Cited by 22
Confident identification of 3-nitrotyrosine modifications in mass spectral data across multiple mass spectrometry platforms
Li, B., Held, J. M., Schilling, B., Danielson, S. R., & Gibson, B. W. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.04.007 · Cited by 22
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Authors: Verrastro, I., Pasha, S., Jensen, K., Pitt, A., & Spickett, C.
Affiliations: Aston University (GB)
Corresponding author: Spickett, Corinne
ORCID: Pitt, Andrew
Spickett, Corinne
Venue: Biomolecules
Publisher: MDPI AG
Published: 2015-04-14
Volume: 5
Issue: 2
Pages: 378-411
ISSN: 2218-273X (ISSN-L)
DOI: 10.3390/biom5020378
PMC: PMC4496678
OpenAlex: W2132553988
Cited by: 114
References: 189
Citations by year: 2026: 8 · 2025: 14 · 2024: 6 · 2023: 11 · 2022: 7 · 2021: 18 · 2020: 10 · 2019: 7 · 2018: 13 · 2017: 13 · 2016: 6
FWCI: 1.03
Type: journal article
Language: en
Open access: gold
dx.doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Biomolecules (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Aston Publications Explorer (Aston University) (acceptedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Research Explorer (The University of Manchester) (submittedVersion)
Funders: EPSRC (EP/I017887/1)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
Keywords: oxidized proteins, oxidative post-translational modifications, protein oxidation, inflammatory diseases, biomarkers, tandem mass spectrometry, targeted mass spectrometry, chemical labeling, oxidative damage
MeSH terms: Animals, Cardiovascular Diseases, Humans, Oxidation-Reduction, Protein Processing, Post-Translational, Mass Spectrometry, Advanced Oxidation Protein Products

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

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