Pham, P.V., Chapter 19 - Medical Biotechnology: Techniques and Applications. Barh, D., Azevedo, V., (eds.) Omics Technologies and Bio-Engineering, 2018, Academic Press, 449–469, 10.1016/B978-0-12-804659-3.00019-1.
Pitt, J.J., Principles and Applications of Liquid Chromatography-Mass Spectrometry in Clinical Biochemistry. Clin Biochem Rev 30 (2009), 19–34.
Cui, W., Rohrs, H.W., Gross, M.L., Top-Down Mass Spectrometry: Recent Developments, Applications and Perspectives. Analyst 136 (2011), 3854–3864, 10.1039/c1an15286f.
Pandeswari, P.B., Sabareesh, V., Middle-down approach: a choice to sequence and characterize proteins/proteomes by mass spectrometry. RSC Adv. 9 (2018), 313–344, 10.1039/C8RA07200K.
Amunugama, R., Jones, R., Ford, M., Allen, D., Bottom-Up Mass Spectrometry–Based Proteomics as an Investigative Analytical Tool for Discovery and Quantification of Proteins in Biological Samples. Adv Wound Care (New Rochelle) 2 (2013), 549–557, 10.1089/wound.2012.0384.
Lermyte, F., Tsybin, Y.O., O'Connor, P.B., Loo, J.A., Top or Middle? Up or Down? Toward a Standard Lexicon for Protein Top-Down and Allied Mass Spectrometry Approaches. J. Am. Soc. Mass Spectrom 30 (2019), 1149–1157, 10.1007/s13361-019-02201-x.
Morsa, D., Baiwir, D., Rocca, R.La, Zimmerman, T.A., Hanozin, E., Grifnée, E., Longuespée, R., Meuwis, M.-A., Smargiasso, N., Pauw, E.D., Mazzucchelli, G., Multi-Enzymatic Limited Digestion: The Next-Generation Sequencing for Proteomics?. J. Proteome Res. 18 (2019), 2501–2513, 10.1021/acs.jproteome.9b00044.
Morand, K., Talbo, G., Mann, M., Oxidation of peptides during electrospray ionization. Rapid Commun. Mass Spectrom. 7 (1993), 738–743, 10.1002/rcm.1290070811.
Chen, M., Cook, K.D., Oxidation Artifacts in the Electrospray Mass Spectrometry of Aβ Peptide. Anal. Chem. 79 (2007), 2031–2036, 10.1021/ac061743r.
Sen, K.I., Hepler, R., Nanda, H., Detection and Measurement of Methionine Oxidation in Proteins. Current Protocols in Protein Science 87 (2017), 14.16.1–14.16.11, 10.1002/cpps.25.
Kang, P., Mezhebovsky, T., Chen, W., McCardle, J.A., Zhang, S., Sullivan, E.P., Sass, P.M., Routhier, E., Use of a stable-isotope-labeled reporter peptide and antioxidants for reliable quantification of methionine oxidation in a monoclonal antibody by liquid chromatography/mass spectrometry. Rapid Commun. Mass Spectrom. 30 (2016), 1734–1742, 10.1002/rcm.7646.
Liu, H., Ponniah, G., Neill, A., Patel, R., Andrien, B., Accurate Determination of Protein Methionine Oxidation by Stable Isotope Labeling and LC-MS Analysis. Anal. Chem. 85 (2013), 11705–11709, 10.1021/ac403072w.
Shipman, J.T., Go, E.P., Desaire, H., Method for Quantifying Oxidized Methionines and Application to HIV-1 Env. J. Am. Soc. Mass Spectrom. 29 (2018), 2041–2047, 10.1007/s13361-018-2010-2.
Rougemont, B., Quantification de protéines dans des matrices complexes par spectrométrie de masse: nouveaux outils et apllications, phdthesis. 2016, Université de Lyon https://tel.archives-ouvertes.fr/tel-01555659 (accessed June 12, 2020).
Zang, L., Carlage, T., Murphy, D., Frenkel, R., Bryngelson, P., Madsen, M., Lyubarskaya, Y., Residual metals cause variability in methionine oxidation measurements in protein pharmaceuticals using LC-UV/MS peptide mapping. J. Chromatogr. B 895–896 (2012), 71–76, 10.1016/j.jchromb.2012.03.016.
Timm, V., Gruber, P., Wasiliu, M., Lindhofer, H., Chelius, D., Identification and characterization of oxidation and deamidation sites in monoclonal rat/mouse hybrid antibodies. J. Chromatogr. B 878 (2010), 777–784, 10.1016/j.jchromb.2010.01.036.
Ghesquière, B., Jonckheere, V., Colaert, N., Durme, J.V., Timmerman, E., Goethals, M., Schymkowitz, J., Rousseau, F., Vandekerckhove, J., Gevaert, K., Redox Proteomics of Protein-bound Methionine Oxidation. Mol. Cell. Proteomics, 10, 2011, 10.1074/mcp.M110.006866 M110.006866.
Lao, Y.W., Gungormusler-Yilmaz, M., Shuvo, S., Verbeke, T., Spicer, V., Krokhin, O.V., Chromatographic behavior of peptides containing oxidized methionine residues in proteomic LC–MS experiments: Complex tale of a simple modification. J. Proteomics 125 (2015), 131–139, 10.1016/j.jprot.2015.05.018.
Wang, Y., Li, X., Liu, Y.-H., Richardson, D., Li, H., Shameem, M., Yang, X., Simultaneous monitoring of oxidation, deamidation, isomerization, and glycosylation of monoclonal antibodies by liquid chromatography-mass spectrometry method with ultrafast tryptic digestion. MAbs 8 (2016), 1477–1486, 10.1080/19420862.2016.1226715.
Verrastro, I., Pasha, S., Jensen, K.T., Pitt, A.R., Spickett, C.M., Mass Spectrometry-Based Methods for Identifying Oxidized Proteins in Disease: Advances and Challenges. Biomolecules 5 (2015), 378–411, 10.3390/biom5020378.
Potgieter, H.C., Ubbink, J.B., Bissbort, S., Bester, M.J., Spies, J.H., Vermaak, W.J.H., Spontaneous Oxidation of Methionine: Effect on the Quantification of Plasma Methionine Levels. Anal. Biochem. 248 (1997), 86–93, 10.1006/abio.1997.2075.
Pino, L.K., Searle, B.C., Bollinger, J.G., Nunn, B., MacLean, B., MacCoss, M.J., The Skyline ecosystem: Informatics for quantitative mass spectrometry proteomics. Mass Spectrom. Rev. 39 (2020), 229–244, 10.1002/mas.21540.
Le, D.T., Liang, X., Fomenko, D.E., Raza, A.S., Chong, C.-K., Carlson, B.A., Hatfield, D.L., Gladyshev, V.N., Analysis of Methionine/Selenomethionine Oxidation and Methionine Sulfoxide Reductase Function Using Methionine-Rich Proteins and Antibodies against Their Oxidized Forms. Biochemistry 47 (2008), 6685–6694, 10.1021/bi800422s.
Lee, B.C., Gladyshev, V.N., The biological significance of methionine sulfoxide stereochemistry. Free Radic. Biol. Med. 50 (2011), 221–227, 10.1016/j.freeradbiomed.2010.11.008.
Asensi, M., Sastre, J., Pallardo, F.V., Delaasuncion, J.G., Estrela, J.M., Vina, J., A High-Performance Liquid Chromatography Method for Measurement of Oxidized Glutathione in Biological Samples. Anal. Biochem. 217 (1994), 323–328, 10.1006/abio.1994.1126.
Mozziconacci, O., Ji, J.A., Wang, Y.J., Schöneich, C., Metal-Catalyzed Oxidation of Protein Methionine Residues in Human Parathyroid Hormone (1-34): Formation of Homocysteine and a Novel Methionine-Dependent Hydrolysis Reaction. Mol. Pharm. 10 (2013), 739–755, 10.1021/mp300563m.
Lam, X.M., Yang, J.Y., Cleland, J.L., Antioxidants for Prevention of Methionine Oxidation in Recombinant Monoclonal Antibody HER2. J. Pharm. Sci. 86 (1997), 1250–1255, 10.1021/js970143s.
Hawkins, C.L., Davies, M.J., Detection, identification, and quantification of oxidative protein modifications. J. Biol. Chem. 294 (2019), 19683–19708, 10.1074/jbc.REV119.006217.
Vogt, W., Oxidation of methionyl residues in proteins: Tools, targets, and reversal. Free Radic. Biol. Med. 18 (1995), 93–105, 10.1016/0891-5849(94)00158-G.
Bettinger, J.Q., Welle, K.A., Hryhorenko, J.R., Ghaemmaghami, S., Quantitative Analysis of in Vivo Methionine Oxidation of the Human Proteome. J. Proteome Res. 19 (2020), 624–633, 10.1021/acs.jproteome.9b00505.
Borges, E.M., Silica, hybrid silica, hydride silica and non-silica stationary phases for liquid chromatography. J. Chromatogr. Sci. 53 (2015), 580–597, 10.1093/chromsci/bmu090.
Kenny, H.C., Tascher, G., Ziemianin, A., Rudwill, F., Zahariev, A., Chery, I., Gauquelin-Koch, G., Barielle, M.-P., Heer, M., Blanc, S., O'Gorman, D.J., Bertile, F., Effectiveness of Resistive Vibration Exercise and Whey Protein Supplementation Plus Alkaline Salt on the Skeletal Muscle Proteome Following 21 Days of Bed Rest in Healthy Males. J. Proteome Res. 19 (2020), 3438–3451, 10.1021/acs.jproteome.0c00256.
