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The physiological role of reversible methionine oxidation
Abstract
Sulfur-containing amino acids such as cysteine and methionine are particularly vulnerable to oxidation. Oxidation of cysteine and methionine in their free amino acid form renders them unavailable for metabolic processes while their oxidation in the protein-bound state is a common post-translational modification in all organisms and usually alters the function of the protein. In the majority of cases, oxidation causes inactivation of proteins. Yet, an increasing number of examples have been described where reversible cysteine oxidation is part of a sophisticated mechanism to control protein function based on the redox state of the protein. While for methionine the dogma is still that its oxidation inhibits protein function, reversible methionine oxidation is now being recognized as a powerful means of triggering protein activity. This mode of regulation involves oxidation of methionine to methionine sulfoxide leading to activated protein function, and inactivation is accomplished by reduction of methionine sulfoxide back to methionine catalyzed by methionine sulfoxide reductases. Given the similarity to thiol-based redox-regulation of protein function, methionine oxidation is now established as a novel mode of redox-regulation of protein function. This article is part of a Special Issue entitled: Thiol-Based Redox Processes.
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Cites
1 retracted
Oxidation of Helix-3 Methionines Precedes the Formation of PK Resistant PrPSc
Canello, T., Frid, K., Gabizon, R., Lisa, S., Friedler, A., Moskovitz, J., Gasset, M., & Gabizon, R. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000977 · Cited by 54
RetractedBuxton, G. V., Greenstock, C. L., Helman, W. P., & Ross, A. B. (1988) · Journal of Physical and Chemical Reference Data · doi:10.1063/1.555805 · Cited by 12,332
Ong, S.-E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., & Mann, M. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200025-mcp200 · Cited by 5,574
THE OXIDATIVE BURST IN PLANT DISEASE RESISTANCE
Lamb, C. J., & Dixon, R. A. (1997) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.48.1.251 · Cited by 3,219
H2O2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response
Levine, A., Tenhaken, R., Dixon, R. A., & Lamb, C. J. (1994) · Cell · doi:10.1016/0092-8674(94)90544-4 · Cited by 2,773
Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
Imlay, J. A., Chin, S. M., & Linn, S. (1988) · Science · doi:10.1126/science.2834821 · Cited by 1,555 · cited 1×
“Free intracellular iron is a major source of cytotoxic HO that is formed by Fenton chemistry [107].”
BackgroundThe oxidative environment and protein damage
Davies, M. J. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.08.007 · Cited by 1,392
A Dynamic Pathway for Calcium-Independent Activation of CaMKII by Methionine Oxidation
Erickson, J. R., Joiner, M.-L. A., Guan, X., Kutschke, W., Yang, J., Oddis, C. V., Bartlett, R. K., Lowe, J. S., O'Donnell, S. E., Aykin-Burns, N., et al. (2008) · Cell · doi:10.1016/j.cell.2008.02.048 · Cited by 1,122
Rapid proteolysis of IκB-α is necessary for activation of transcription factor NF-κB
Henkel, T., Machleidt, T., Alkalay, I., Krönke, M., Ben‐Neriah, Y., & Baeuerle, P. A. (1993) · Nature · doi:10.1038/365182a0 · Cited by 1,085
The Arabidopsis CDPK-SnRK Superfamily of Protein Kinases
Hrabak, E. M., Chan, C. W. M., Gribskov, M., Harper, J. F., Choi, J. H., Halford, N. G., Kudla, J., Luan, S., Nimmo, H. G., Sussman, M. R., et al. (2003) · PLANT PHYSIOLOGY · doi:10.1104/pp.102.011999 · Cited by 1,080
Cited by
Sorted by citations
Sies, H., Berndt, C., & Jones, D. P. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045037 · Cited by 3,520
Superoxide dismutases: Dual roles in controlling ROS damage and regulating ROS signaling
Wang, Y., Branicky, R. S., Noë, A., & Hekimi, S. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201708007 · Cited by 2,284
“Like cysteines, methionines also contain reactive sulfur atoms that are susceptible to reversible redox modifications and thus may also mediate redox signaling (Drazic and Winter, 2014).”
Cellular mechanisms and physiological consequences of redox-dependent signalling
Holmström, K. M., & Finkel, T. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3801 · Cited by 2,093
The world of protein acetylation
Drazic, A., Myklebust, L. M., Ree, R., & Arnesen, T. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.06.007 · Cited by 847
“Methionine sulfoxide reductase A (MSRA) plays a crucial role in protecting proteins from oxidation and repairs damages caused by reactive oxygen species (ROS), which also crucially affects tunorigenesis [2].”
BackgroundSelf-citationHorsman, G. P., & Zechel, D. L. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00536 · Cited by 604
ROS: Basic Concepts, Sources, Cellular Signaling, and its Implications in Aging Pathways
de Almeida, A. J. P. O., de Oliveira, J. C. P. L., Pontes, L. V. D. S., Júnior, J. F. D. S., Gonçalves, T. A. F., Dantas, S. H., Feitosa, M. S. D. A., Silva, A. O., & de Medeiros, I. A. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/1225578 · Cited by 557
“In addition, methionine also has sulfur atoms that may be oxidized similarly to cysteine; however, the reactivity of methionine oxidation is slower than cysteine oxidation, probably due to sulfur atom methionine space impediment [186].”
BackgroundKehrer, J. P., & Klotz, L. (2015) · Critical Reviews in Toxicology · doi:10.3109/10408444.2015.1074159 · Cited by 359
“This disorder is caused by a defect in the NADPH oxidase activity in phagocytes, which impairs the killing of invading organisms (Kuhns et al. 2010).”
BackgroundInfluentialGo, Y., Chandler, J. D., & Jones, D. P. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.03.022 · Cited by 363
“[30,31], Cys became increasingly utilized with organizational complexity [28].”
Molecular mechanisms of oxidative stress in asthma
Michaeloudes, C., Abubakar-Waziri, H., Lakhdar, R., Raby, K., Dixey, P., Adcock, I. M., Mumby, S. E., Bhavsar, P. K., & Chung, K. F. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2021.101026 · Cited by 348
Protein Quality Control under Oxidative Stress Conditions
Dahl, J., Gray, M. J., & Jakob, U. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.02.014 · Cited by 206
“[52] Drazic A, Winter J.”
BackgroundMethionine production—a critical review
Willke, T. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-6156-y · Cited by 183
Protein Oxidation in Aging: Does It Play a Role in Aging Progression?
Reeg, S., & Grune, T. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6062 · Cited by 191
“In contrast, MSRBs are able to reduce R-stereoisomers and almost exclusively in proteins (38).”
BackgroundReactive Oxygen Species and Mitochondrial Homeostasis as Regulators of Stem Cell Fate and Function
Tan, D. Q., & Suda, T. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7273 · Cited by 183
“SO back to Met is catalyzed by methionine sulfoxide reductases [reviewed by Drazic and Winter (32)], whereas the reduction of Cys - SOH to Cys is dependent on several classes of proteins, including glutaredoxins, thioredoxins, and thioredoxin reductases.”
InfluentialFeatures and regulation of non-enzymatic post-translational modifications
Harmel, R. K., & Fiedler, D. (2018) · Nature Chemical Biology · doi:10.1038/nchembio.2575 · Cited by 171
Actin Post-translational Modifications: The Cinderella of Cytoskeletal Control
Varland, S., Vandekerckhove, J. S., & Drazic, A. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.11.010 · Cited by 150
Self-citationInfluence of vitamin C and vitamin E on redox signaling: implications for exercise adaptations
Cobley, J. N., McHardy, H., Morton, J. P., Nikolaidis, M. G., & Close, G. L. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.03.018 · Cited by 118
The Reactive Sulfur Species Concept: 15 Years On
Giles, G. I., Nasim, M. J., Ali, W., & Jacob, C. (2017) · Antioxidants · doi:10.3390/antiox6020038 · Cited by 121
“There are others, of course, such as the more traditional S-thio(ny)lation or S-glutathio(ny)lation, which play a pivotal role in cell signalling, the equally unusual and intriguing fact that “Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate” [20] reported in the year of dest…”
BackgroundCoughlan, M. T., & Sharma, K. (2016) · Kidney International · doi:10.1016/j.kint.2016.02.043 · Cited by 109
“It is now thought that redox-dependent signaling mechanisms are primarily based on the oxidation of cysteine residues, thereby altering redox-sensitive protein targets, such as inactivation of protein tyrosine phosphatases (PTPs) leading to unopposed tyrosine kinase activity,(66) although the reversible oxidation and…”
BackgroundProtein Methionine Sulfoxide Dynamics in Arabidopsis thaliana under Oxidative Stress
Jacques, S., Ghesquière, B., Bock, P. D., Demol, H., Wahni, K., Willems, P. J., Messens, J., Breusegem, F. V., & Gevaert, K. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.043729 · Cited by 105
“Methionine oxidation, on the other hand, received less attention, and in plants, only a few examples of functional consequences of this modification have been described (16-19).”
Yoo, J., Rejinold, N. S., Lee, D., Jon, S., & Kim, Y. (2017) · Journal of Controlled Release · doi:10.1016/j.jconrel.2017.08.026 · Cited by 99
“Among the various natural amino acids, a methionine residue is characterized as a ROSresponsive group containing a thioether moiety [12-15] and provides outstanding biocompatibility due to naturally occurring compounds [16].”
BackgroundSheppard, A. J., Barfield, A. M., Barton, R. S., & Dong, Y. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.836764 · Cited by 105
Kaya, A., Lee, B. C., & Gladyshev, V. N. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6385 · Cited by 96
“In contrast to most other previous cases, oxidation of HypT through its three Met residues could lead to its activation, thus avoiding HOCl-mediated bacterial killing, suggesting that Met sulfoxidation is required for functional regulation of HypT and might support survival on the attack by the host immune system (11).”
ResultLiao, X., Liu, D., & Ding, T. (2019) · Applied and Environmental Microbiology · doi:10.1128/aem.02216-19 · Cited by 96
Redox regulation by reversible protein S-thiolation in Gram-positive bacteria
Imber, M., Pietrzyk‐Brzezinska, A. J., & Antelmann, H. (2018) · Redox Biology · doi:10.1016/j.redox.2018.08.017 · Cited by 92
“MsrA and MsrB are further important redox enzymes which catalyze the reduction of two stereotypes of methionine sulfoxides (MetSO) to Lmethionine [51].”
BackgroundReducing systems protecting the bacterial cell envelope from oxidative damage
Arts, I. S., Gennaris, A., & Collet, J. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.04.057 · Cited by 90
“However, they possess a similar catalytic mechanism involving a catalytic cysteine residue [85,105].”
BackgroundThe Plasma Membrane: A Platform for Intra- and Intercellular Redox Signaling
Nordzieke, D. E., & Medraño-Fernandez, I. (2018) · Antioxidants · doi:10.3390/antiox7110168 · Cited by 90
“methionine, the second sulfur-containing amino acid, might provide an analogous redox-dependent system [48].”
BackgroundMetabolic Fingerprint of Dimethyl Sulfone (DMSO2) in Microbial–Mammalian Co-metabolism
He, X., & Slupsky, C. M. (2014) · Journal of Proteome Research · doi:10.1021/pr500629t · Cited by 86
Regulated methionine oxidation by monooxygenases
Manta, B., & Gladyshev, V. N. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.02.010 · Cited by 84
Strategies Employing Transition Metal Complexes To Modulate Amyloid-β Aggregation
Suh, J., Kim, G., Kang, J., & Lim, M. H. (2018) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.8b02813 · Cited by 71
Redox signaling in innate immunity and inflammation: focus on macrophages and neutrophils
Braunstein, I., Motohashi, H., Dallenga, T. K., Schaible, U. E., & Benhar, M. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.06.006 · Cited by 75
Strempel, N., Nusser, M., Neidig, A., Brenner‐Weiß, G., & Overhage, J. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02311 · Cited by 65
“In general, all tested oxidants are able to induce Met-SO formation; however, the reaction occurs considerably faster in case of HClO compared to the less reactive H2O2 (Pattison and Davies, 2001; Peskin and Winterbourn, 2001; Drazic and Winter, 2014).”
BackgroundOxidative Modification of Proteins: From Damage to Catalysis, Signaling, and Beyond
Demasi, M., Augusto, O., Bechara, E. J. H., Bicev, R. N., Cerqueira, F. M., da Cunha, F. M., Denicola, A., Gomes, F., Miyamoto, S., Netto, L. E. S., et al. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8176 · Cited by 71
Singh, P., Barman, B., & Thakur, M. K. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.944697 · Cited by 73
“Oxidation of a methionine residue of calmodulin causes the loss of its calcium-binding ability, responsible for the activation of several calcium-sensitive enzymes and ion channels (Smith et al., 1991; Kregel and Zhang, 2007; Drazic and Winter, 2014; Reeg and Grune, 2015).”
BackgroundThe polar oxy-metabolome reveals the 4-hydroxymandelate CoQ10 synthesis pathway
Banh, R. S., Kim, E. S., Spillier, Q., Biancur, D. E., Yamamoto, K., Sohn, A. S. W., Shi, G., Jones, D. R., Kimmelman, A. C., & Pacold, M. E. (2021) · Nature · doi:10.1038/s41586-021-03865-w · Cited by 59
Humin: No longer inactive natural organic matter
Pham, D. M., Kasai, T., Yamaura, M., & Katayama, A. (2020) · Chemosphere · doi:10.1016/j.chemosphere.2020.128697 · Cited by 60
In Vivo Imaging of Hydrogen Peroxide with HyPer Probes
Bilan, D. S., & Belousov, V. V. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7540 · Cited by 56
“In addition to cysteine residues, some others can also be modified by H 2 O 2 , such as methionine residues (31, 71, 111).”
NADPH Oxidases: Redox Regulators of Stem Cell Fate and Function
Maraldi, T., Angeloni, C., Prata, C., & Hrelia, S. (2021) · Antioxidants · doi:10.3390/antiox10060973 · Cited by 60
Mandal, P. K., Roy, R. G., & Samkaria, A. (2022) · ACS Omega · doi:10.1021/acsomega.2c02760 · Cited by 56
Pinho, B. R., Reis, S., Hartley, R. C., Murphy, M. P., & Oliveira, J. M. A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.446 · Cited by 52
“There is now compelling evidence that ROS also participate in physiological signaling, regulating redox-dependent switches in proteins that govern proliferation, metabolism, gene transcription, inflammation and ageing [11,20,46].”
BackgroundReactive species driven oxidative modifications of peptides—Tracing physical plasma liquid chemistry
Wenske, S., Lackmann, J., Busch, L. M., Bekeschus, S., von Woedtke, T., & Wende, K. (2021) · Journal of Applied Physics · doi:10.1063/5.0046685 · Cited by 50
Makukhin, N., Tretyachenko, V., Moskovitz, J., & Míšek, J. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201605833 · Cited by 46
Protein Tyrosine Nitration in Plant Nitric Oxide Signaling
León, J. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.859374 · Cited by 45
Oxidative post-translational modifications controlling plant-pathogen interaction
Camejo, D. M., Guzmán-Cedeño, Á. M., Vera-Macías, L. R., & Jiménez, A. (2019) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2019.09.020 · Cited by 42
Proteolysis and Oxidation of Therapeutic Proteins After Intradermal or Subcutaneous Administration
Varkhede, N. R., Bommana, R., Schöneich, C., & Forrest, M. L. (2019) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2019.08.005 · Cited by 40
Regulation of RhoA GTPase and novel target proteins for ROCK
Choi, E.-K., Kim, J.-G., Kim, H.-J., Cho, J.-Y., Jeong, H., Park, Y., Islam, R., Cap, C. K., & Park, J.-B. (2020) · Small GTPases · doi:10.1080/21541248.2017.1364831 · Cited by 39
Substrate specificity of thioredoxins and glutaredoxins – towards a functional classification
Gellert, M., Hossain, M. F., Berens, F. J. F., Bruhn, W., Urbainsky, C., Liebscher, V., & Lillig, C. H. (2019) · Heliyon · doi:10.1016/j.heliyon.2019.e02943 · Cited by 38
“Redox modifications of cysteinyl and also methionyl side chains are a vital part of numerous signal transduction pathways as well as the reaction cycle of essential metabolic enzymes [1, 2, 3, 4].”
BackgroundShin, S.-H., Yoon, H., Chun, Y.-S., Shin, H.-W., Lee, M.-N., Oh, G. T., & Park, J.-W. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.456 · Cited by 37
“against MetO have been evolutionally conserved in prokaryotic and eukaryotic cells.(13) One such system, methionine”
BackgroundEmerging Omics Approaches in Aging Research
Lorusso, J. S., Sviderskiy, O., & Labunskyy, V. M. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7163 · Cited by 39
“More recently, targeted oxidation/reduction of methionine residues in proteins has been also implicated in signaling and redox regulation of diverse cellular functions (35, 124).”
BackgroundSimon, J. N., Žiberna, K., & Casadei, B. (2016) · Cardiovascular Research · doi:10.1093/cvr/cvw012 · Cited by 39
“proteins primarily on the sulphur-containing amino acids cysteine and methionine, with reactivity of the cysteine thiolate (S(2)) being approximately four-fold faster than that of methionine.(28) The types of reversible oxidative cysteine thiol modifications include S-nitrosylation,”
BackgroundLow-molecular-weight thiol transferases in redox regulation and antioxidant defence
Tossounian, M., Zhao, Y., Yu, B. Y. K., Markey, S. A., Malanchuk, O., Zhu, Y., Cain, A., & Gout, I. T. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103094 · Cited by 35
“Protein oxidation can alter the function, structure, and downstream interactions of proteins [95 – 98].”
BackgroundMetabolic Response of Escherichia coli upon Treatment with Hypochlorite at Sub-Lethal Concentrations
Drazic, A., Kutzner, E., Winter, J., & Eisenreich, W. (2015) · PLoS ONE · doi:10.1371/journal.pone.0125823 · Cited by 35
“Importantly, all these proteins use the normally destructive post-translational modifications such as oxidative unfolding and, cysteine and methionine oxidation to initiate their activation [13, 18, 22].”
BackgroundInfluentialSelf-citationIrreversible oxidative post-translational modifications in heart disease
Tomin, T., Schittmayer, M., Honeder, S. E., Heininger, C., & Birner‐Gruenberger, R. (2019) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1645602 · Cited by 35
Chemoselective Methionine Bioconjugation on a Polypeptide, Protein, and Proteome
Zang, J., Chen, Y., Zhu, W., & Lin, S. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00789 · Cited by 35
Multienzyme Redox System with Cofactor Regeneration for Cyclic Deracemization of Sulfoxides
Peng, T., Tian, J., Zhao, Y., Jiang, X., Cheng, X., Deng, G., Zhang, Q., Wang, Z., Yang, J., & Chen, Y. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202209272 · Cited by 35
Time dynamics of the Bacillus cereus exoproteome are shaped by cellular oxidation
Madeira, J.-P., Alpha‐Bazin, B., Armengaud, J., & Duport, C. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00342 · Cited by 38
“Oxidized Met can be repaired by antioxidant systems (Drazic and Winter, 2014).”
BackgroundMathew, S., Krug, S., Skurk, T., Halama, A., Stank, A., Artati, A., Prehn, C. P., Malek, J. A., Kastenmüller, G., Römisch‐Margl, W., et al. (2014) · Journal of Translational Medicine · doi:10.1186/1479-5876-12-161 · Cited by 33
“Methionine oxidation is part of a highly regulated machinery, controlling the function of signaling factors under physiological challenge conditions and conditions of oxidative stress [34].”
Sulfur Radical-Induced Redox Modifications in Proteins: Analysis and Mechanistic Aspects
Schöneich, C. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6779 · Cited by 34
“Protein-Lys-NH-CO-CH NH2 ð ÞCH2CH2S Ð Protein-Lys-NH-CO-C NH2 ð ÞCH2CH2SH (42)”
Redox regulation of cytoskeletal dynamics during differentiation and de-differentiation
Gellert, M., Hanschmann, E.-M., Lepka, K., Berndt, C., & Lillig, C. H. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.10.030 · Cited by 35
“Similar to the variety of thiol redox modifications, reversible methionine oxidation is now being recognised as a redox signalling mechanism [21].”
BackgroundCadmium-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
Hentchel, K. L., & Escalante‐Semerena, J. C. (2014) · Journal of Bacteriology · doi:10.1128/jb.02311-14 · Cited by 32
Impact of methionine oxidation on calmodulin structural dynamics
McCarthy, M. R., Thompson, A. R., Nitu, F. R., Moen, R. J., Olenek, M., Klein, J. C., & Thomas, D. D. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.11.091 · Cited by 34
“Megan R. McCarthy a, Andrew R. Thompson a, Florentin Nitu a, Rebecca J. Moen c, Michael J. Olenek b, Jennifer C. Klein b,1, David D. Thomas a,1,⇑ a Biochemistry, Molecular Biology and Biophysics Department, University of Minnesota, Minneapolis, MN 55455, USA b Biology Department, University of Wisconsin, La Crosse, WI…”
BackgroundRhoA GTPase oxidation stimulates cell proliferation via nuclear factor-κB activation
Kim, J.-G., Kwon, H.-J., Wu, G., Park, Y., Lee, J.-Y., Kim, J., Kim, S.-C., Choe, M., Kang, S. G., Seo, G.-Y., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.12.013 · Cited by 31
Roerden, M., Castro, A., Cui, Y., Harake, N., Kim, B., Dye, J., Maiorino, L., White, F. M., Irvine, D. J., Litchfield, K., et al. (2024) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2024-010249 · Cited by 30
One-Pot Synthesis of Oxidation-Sensitive Supramolecular Gels and Vesicles
Duro‐Castaño, A., Rodríguez‐Arco, L., Ruiz‐Pérez, L., Pace, C. D., Marchello, G., Noble-Jesus, C., & Battaglia, G. (2021) · Biomacromolecules · doi:10.1021/acs.biomac.1c01039 · Cited by 29
Oxidant‐resistant LRRC8A/C anion channels support superoxide production by NADPH oxidase 1
Choi, H., Rohrbough, J. C., Nguyen, H. N., Dikalova, A., & Lamb, F. S. (2021) · The Journal of Physiology · doi:10.1113/jp281577 · Cited by 28
“…from each other and from 8A, with 8D EL1 containing 34 more residues than 8C. Methionine can also be oxidized by ChlorT, representing another potential target for regulation (Drazic&Winter, 2014) and methionine redox-dependent modulation can regulate protein function (Drazic & Winter, 2014).”
BackgroundTossounian, M., Pedre, B., Wahni, K., Erdoğan, H., Vertommen, D., Molle, I. V., & Messens, J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.632596 · Cited by 26
“Proteins sensitive to reactive oxygen species are particularly those with sulfurous amino acids like cysteine (2) and methionine (3).”
BackgroundEvidence of peptide oxidation from major myofibrillar proteins in dry-cured ham
Gallego, M., Mora, L., Aristoy, M., & Toldrá, F. (2015) · Food Chemistry · doi:10.1016/j.foodchem.2015.04.102 · Cited by 26
Perturbation in cellular redox homeostasis: Decisive regulator of T cell mediated immune responses
Gambhir, L., Sharma, V., Kandwal, P., & Saxena, S. (2018) · International Immunopharmacology · doi:10.1016/j.intimp.2018.12.049 · Cited by 26
Transcriptomic Response Analysis of Escherichia coli to Palladium Stress
Joudeh, N., Saragliadis, A., Schulz, C., Voigt, A., Almaas, E., & Linke, D. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.741836 · Cited by 26
“The oxidation of these amino acids makes them unavailable for metabolic processes (Drazic and Winter, 2014).”
BackgroundSadowska‐Bartosz, I., & Bartosz, G. (2023) · International Journal of Radiation Biology · doi:10.1080/09553002.2023.2241895 · Cited by 28
“Met-SO reduction by Msrs is coupled with oxidation of active site Cys residues, which can be then regenerated by Trx or Grx (Neiers et al. 2004; Drazic and Winter 2014).”
BackgroundMonnerat, G., Sanchez, C. A., dos Santos, C. G. M., Paulucio, D., Velasque, R., Evaristo, G. P. C., Evaristo, J. A. M., Nogueira, F. C. S., Domont, G. B., Serrato, M., et al. (2020) · International Journal of Sports Physiology and Performance · doi:10.1123/ijspp.2019-0267 · Cited by 26
Peng, T., Cheng, X., Chen, Y., & Yang, J. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.714899 · Cited by 25
Antioxidant role of methionine-containing intra- and extracellular proteins
Rosenfeld, M. A., Yurina, L. V., & Vasilyeva, A. D. (2023) · Biophysical Reviews · doi:10.1007/s12551-023-01056-7 · Cited by 26
“2014; Drazic and Winter 2014; Levine et al.”
BackgroundVanhove, A. S., Hang, S., Vijayakumar, V., Wong, A. C.-N., Asara, J. M., & Watnick, P. I. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006428 · Cited by 25
·OH Oxidation Toward S- and OH-Containing Amino Acids
Uranga, J., Mujika, J. I., & Matxain, J. M. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b09825 · Cited by 23
Tossounian, M., Molle, I. V., Wahni, K., Jacques, S., Gevaert, K., Breusegem, F. V., Vertommen, D., Young, D., Rosado, L. A., & Messens, J. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.10.007 · Cited by 23
Tavella, D., Ouellette, D. R., Garofalo, R., Zhu, K., Xu, J., Oloo, E. O., Negron, C., & Ihnat, P. M. (2022) · PLoS ONE · doi:10.1371/journal.pone.0279689 · Cited by 22
“The sulfur in methionine, present as a thioether (R-S-R), has a low oxidation potential and therefore a large number of oxidizing species can oxidize this residue [11].”
BackgroundBuchert, F. E., Bailleul, B., & Hisabori, T. (2017) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2017.09.001 · Cited by 22
Sirota, F. L., Maurer‐Stroh, S., Eisenhaber, B., & Eisenhaber, F. (2015) · PROTEOMICS · doi:10.1002/pmic.201400633 · Cited by 20
“The localization of methionine within structures seems to be important in determining its accessibility to oxidants, contributing to complex redox-regulation mechanisms of protein function, as well as eventually preventing other functionally relevant amino acids from being oxidized [122].”
BackgroundChang, Y., He, B., Wang, C., Li, W., Tao, S., Chen, J., Wang, Y., Yang, L., Wu, Y., Wu, Z., et al. (2025) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2025.2491638 · Cited by 23
“The oxidation of methionine can be catalytically regenerated by methionine sulfoxide reductase to reform methionine (Drazic and Winter 2014).”
Kim, J., Lee, H., Roh, Y. J., Kim, H.-U., Shin, D., Kim, S., Son, J., Lee, A., Kim, M., Park, J., et al. (2019) · IUCrJ · doi:10.1107/s2052252519015409 · Cited by 20
“…enzymes are involved in several metabolic processes, including the biosynthesis of hormones and vitamins, the inactivation of signaling molecules, the excretion of xenobiotic substrates and the guidance of axons (Kaya et al., 2015; Drazic & Winter, 2014; Lee et al., 2013; Nadella et al., 2005).”
BackgroundTrmB Family Transcription Factor as a Thiol-Based Regulator of Oxidative Stress Response
Mondragon, P., Hwang, S., Kasirajan, L., Oyetoro, R. O., Nasthas, A., Winters, E., Couto-Rodríguez, R. L., Schmid, A., & Maupin-furlow, J. A. (2022) · mBio · doi:10.1128/mbio.00633-22 · Cited by 21
“These switches can turn TF function on or off in coordinating gene co-expression networks associated with electron flow, antioxidant systems and other pathways (6-8).”
BackgroundMendoza, C., Emmanuel, N., Martínez, C. P., Dreesen, L., Monbaliu, J. M., & Heinrichs, B. (2017) · Journal of Photochemistry and Photobiology A Chemistry · doi:10.1016/j.jphotochem.2017.12.028 · Cited by 19
Cysteine Sulfur Chemistry in Transcriptional Regulators at the Host–Bacterial Pathogen Interface
Luebke, J. L., & Giedroc, D. P. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00085 · Cited by 20
Rao, R. S. P., Møller, I. M., Thelen, J. J., & Miernyk, J. A. (2014) · Cell Stress and Chaperones · doi:10.1007/s12192-014-0544-1 · Cited by 20
“The roles of reversible Met-oxidation in controlling cellular functions have been previously reviewed (Levine et al. 2000; Drazic and Winter 2014; Kim et al. 2014a, b), and will not be further elaborated herein.”
Madeira, J.-P., Alpha‐Bazin, B., Armengaud, J., & Duport, C. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.01342 · Cited by 21
“…transcription units, (ii) msrA and msrB cistrons are organized as an operon, (iii) msrA and msrB cistrons form a single open reading frame (ORF) to produce a two domain protein, and (iv) trx, msrA, and msrB cistrons form a single ORF to produce a three domain protein (Drazic and Winter, 2014).”
BackgroundOrabi, E. A., & English, A. M. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c8cp03277g · Cited by 18
Ji, C., Zhang, N., Jiang, H., Meng, X., Ge, H., Yang, X., Xu, X., Qian, K., Park, Y., Yang, Z., et al. (2021) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2021.103546 · Cited by 18
Streptococcus pyogenes Metabolism
Pancholi, V., & Caparon, M. G. (2016) · Europe PMC (PubMed Central) · Cited by 18
Signal-regulated oxidation of proteins via MICAL
Salas, C. O., Schneider, K., Lillig, C. H., & Gellert, M. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190866 · Cited by 16
Advances in hydrogel systems for bone regeneration: trends, innovations, and prospects
Han, Y., Liu, J., Hu, C., Wang, Y., & He, C. (2025) · Journal of Materials Chemistry B · doi:10.1039/d5tb02041g · Cited by 18
Guo, J.-S., Tian, S., & Zhang, Y. T. (2023) · Physics of Plasmas · doi:10.1063/5.0139634 · Cited by 16
Copper(I)-nitrene platform for chemoproteomic profiling of methionine
Sahu, S., Emenike, B., Beusch, C. M., Bagchi, P., Gordon, D. E., & Raj, M. (2024) · Nature Communications · doi:10.1038/s41467-024-48403-0 · Cited by 16
“The redox cycle between methionine and methionine sulfoxide provides an excellent anti-oxidant defense platform against various oxidizing species in cells 8 – 10 .”
BackgroundMethodInfluentialYao, S., & Udenigwe, C. C. (2018) · Royal Society Open Science · doi:10.1098/rsos.172425 · Cited by 17
“antibody function and immune response [34,35].”
BackgroundMakukhin, N., Havelka, V., Poláchová, E., Rampírová, P., Tarallo, V., Stříšovský, K., & Míšek, J. (2019) · FEBS Journal · doi:10.1111/febs.14951 · Cited by 16
Porter, J. J., & Mehl, R. A. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/7607463 · Cited by 15
Nojima, Y., Takeda, Y., Maeda, Y., Bamba, T., Fukusaki, E., Itoh, M. N., Mizuguchi, K., & Kumanogoh, A. (2020) · FEBS Open Bio · doi:10.1002/2211-5463.12982 · Cited by 15
Chen, X., Yang, S., Ruan, X.-J., Ding, H., Wang, N.-X., Liu, F., Li, J., & Li, Y. (2021) · Cell Transplantation · doi:10.1177/09636897211053203 · Cited by 15
Methionine and Antioxidant Potential
Yin, J., Li, T., & Yin, Y. (2016) · Journal of Antioxidant Activity · doi:10.14302/issn.2471-2140.jaa-16-1378 · Cited by 14
“However, the recent experimental models suggested that Met oxidation involves in activation or inactivation of protein function and is now established as a novel mode of redoxregulation of protein function similar with thiol-based redox-regulation of protein function [8].”
BackgroundTheoretical Evaluation of Sulfur-Based Reactions as a Model for Biological Antioxidant Defense
Sciscio, M. L. D., D’Annibale, V., & D’Abramo, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314515 · Cited by 13
Metadata
- Authors
- Drazic, A., & Winter, J.
- Affiliations
- Center for Integrated Protein Science Munich (DE)
- Corresponding author
- Winter, Jeannette
- ORCID
- Drazic, Adrian
- Venue
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- Publisher
- Elsevier BV
- Published
- 2014-08
- Volume
- 1844
- Issue
- 8
- Pages
- 1367-1382
- ISSN
- 1570-9639 (ISSN-L)
- OpenAlex
- W2039213528
- Cited by
- 198
- References
- 187
- Citations by year
- 2026: 8 · 2025: 13 · 2024: 19 · 2023: 11 · 2022: 22 · 2021: 14 · 2020: 15 · 2019: 17 · 2018: 12 · 2017: 18 · 2016: 15 · 2015: 20 · 2014: 13
- FWCI
- 2.08
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- methionine sulfoxide, methionine sulfoxide reductase, post-translational modification, protein inactivation, cysteine oxidation, sulfur-containing amino acids
- MeSH terms
- Animals, Cell Physiological Phenomena, Humans, Methionine, Oxidation-Reduction, Signal Transduction
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