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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Self-citationInfluence of vitamin C and vitamin E on redox signaling: implications for exercise adaptations
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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 113 · see citing works
“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 108 · see citing works
“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 · see citing works
“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 · see citing works
“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 99 · see citing works
Kaya, A., Lee, B. C., & Gladyshev, V. N. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6385 · Cited by 96 · see citing works
“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 · see citing works
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 · see citing works
“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 · see citing works
“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 · see citing works
“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 · see citing works
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 81 · see citing works
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 · see citing works
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 72 · see citing works
Strempel, N., Nusser, M., Neidig, A., Brenner‐Weiß, G., & Overhage, J. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02311 · Cited by 65 · see citing works
“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 68 · see citing works
Singh, P., Barman, B., & Thakur, M. K. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.944697 · Cited by 69 · see citing works
“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 58 · see citing works
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 59 · see citing works
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 55 · see citing works
“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 55 · see citing works
Mandal, P. K., Roy, R. G., & Samkaria, A. (2022) · ACS Omega · doi:10.1021/acsomega.2c02760 · Cited by 53 · see citing works
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 50 · see citing works
“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 · see citing works
Makukhin, N., Tretyachenko, V., Moskovitz, J., & Míšek, J. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201605833 · Cited by 46 · see citing works
Protein Tyrosine Nitration in Plant Nitric Oxide Signaling
León, J. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.859374 · Cited by 43 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
“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 · see citing works
“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 36 · see citing works
“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., Ziberna, K., & Casadei, B. (2016) · Cardiovascular Research · doi:10.1093/cvr/cvw012 · Cited by 40 · see citing works
“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 · see citing works
“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 · see citing works
“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 · see citing works
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 · see citing works
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 · see citing works
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 35 · see citing works
“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 · see citing works
“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 · see citing works
“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 34 · see citing works
“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 · see citing works
Hentchel, K. L., & Escalante‐Semerena, J. C. (2014) · Journal of Bacteriology · doi:10.1128/jb.02311-14 · Cited by 32 · see citing works
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 32 · see citing works
“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 · see citing works
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 29 · see citing works
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 · see citing works
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 · see citing works
“…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 · see citing works
“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 · see citing works
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 · see citing works
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 · see citing works
“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 26 · see citing works
“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 · see citing works
Peng, T., Cheng, X., Chen, Y., & Yang, J. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.714899 · Cited by 25 · see citing works
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 · see citing works
“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 · see citing works
·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 · see citing works
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 · see citing works
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 · see citing works
“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 · see citing works
Sirota, F. L., Maurer‐Stroh, S., Eisenhaber, B., & Eisenhaber, F. (2015) · PROTEOMICS · doi:10.1002/pmic.201400633 · Cited by 20 · see citing works
“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 · see citing works
“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 · see citing works
“…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 19 · see citing works
“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 · see citing works
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 19 · see citing works
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 19 · see citing works
“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 19 · see citing works
“…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 · see citing works
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 · see citing works
Streptococcus pyogenes Metabolism
Pancholi, V., & Caparon, M. G. (2016) · Europe PMC (PubMed Central) · Cited by 18 · see citing works
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 17 · see citing works
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 16 · see citing works
Guo, J.-S., Tian, S., & Zhang, Y. T. (2023) · Physics of Plasmas · doi:10.1063/5.0139634 · Cited by 16 · see citing works
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 · see citing works
“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 · see citing works
“antibody function and immune response [34,35].”
BackgroundMakukhin, N., Havelka, V., Poláchová, E., Rampírová, P., Tarallo, V., Střı́šovský, K., & Míšek, J. (2019) · FEBS Journal · doi:10.1111/febs.14951 · Cited by 16 · see citing works
Porter, J. J., & Mehl, R. A. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/7607463 · Cited by 15 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
“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 · see citing works
- 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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