Cysteine residues exposed on protein surfaces are the dominant intramitochondrial thiol and may protect against oxidative damage
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Cysteine plays a number of important roles in protecting the cell from oxidative damage through its thiol functional group. These defensive functions are generally considered to be carried out by the low molecular weight thiol glutathione and by cysteine residues in the active sites of proteins such as thioredoxin and peroxiredoxin. In addition, there are thiols exposed on protein surfaces that are not directly involved with protein function, although they can interact with the intracellular environment. In the present study, in subcellular fractions prepared from rat liver or heart, we show that the quantitatively dominant free thiols are those of cysteine residues exposed on protein surfaces and not those carried by glutathione. Within the mitochondrial matrix, the concentration of exposed protein thiols is 60–90 m m, which is approximately 26‐fold higher than the glutathione concentration in that compartment. This suggests that exposed protein thiols are of greater importance than glutathione for nonenzyme catalysed reactions of thiols with reactive oxygen and nitrogen species and with electrophiles within the cell. One such antioxidant role for exposed protein thiols may be to prevent protein oxidative damage. In the present study, in mitochondrial membranes and in complex I, we show that exposed protein thiols protect against tyrosine nitration and protein dysfunction caused by peroxynitrite. Therefore, exposed protein thiols are the dominant free thiol within the cell and may play a critical role in intracellular antioxidant defences against oxidative damage.
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Thiol groups can mediate nucleophilic attack at least as well as deprotonated amines and are abundant in the mitochondrial matrix.
“thiol residues are as capable as deprotonated amines of mediating nucleophilic attack, if not more so, and are found in large numbers in the mitochondrial matrix ((Requejo et al. 2010)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Requejo et al. 2010
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Cites
Measurement of protein using bicinchoninic acid
Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., & Klenk, D. C. (1985) · Analytical Biochemistry · doi:10.1016/0003-2697(85)90442-7 · Cited by 18,482 · see citing works
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works
Self-citationBeckman, J. S., Beckman, T. W., Chen, J., Marshall, P. A., & Freeman, B. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1620 · Cited by 7,029 · see citing works
Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587 · see citing works
Reconciling the chemistry and biology of reactive oxygen species
Winterbourn, C. C. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.85 · Cited by 2,504 · see citing works
Peroxynitrite oxidation of sulfhydryls.
Radí, R., Beckman, J. S., Bush, K., & Freeman, B. Α. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64313-7 · Cited by 2,499 · see citing works
Peroxynitrite: biochemistry, pathophysiology and development of therapeutics
Szabó, C., Ischiropoulos, H., & Radi, R. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2222 · Cited by 2,134 · see citing works
A new collection method for the evaluation of nasal mucus proteins
Ruocco, L. A., Fattori, Romanelli, Martelloni, L., Casani, Samolewska, & Rezzonico (1998) · Clinical & Experimental Allergy · doi:10.1046/j.1365-2222.1998.00312.x · Cited by 1,296 · see citing works
Extensive Nitration of Protein Tyrosines in Human Atherosclerosis Detected by Immunohistochemistry
Beckman, J. S., Ye, Y. Z., Anderson, P. G., Chen, J., Accavitti, M. A., Tarpey, M. M., & White, C. R. (1994) · Biological Chemistry Hoppe-Seyler · doi:10.1515/bchm3.1994.375.2.81 · Cited by 1,122 · see citing works
Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
Winterbourn, C. C., & Metodiewa, D. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00051-9 · Cited by 799 · see citing works
Molecular and Cellular Aspects of Thiol–Disulfide Exchange
Gilbert, H. (1990) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123096.ch2 · Cited by 759 · see citing works
Glutathione: Toxicological Implications
Reed, D. J. (1990) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.30.040190.003131 · Cited by 748 · see citing works
Levonen, A., Landar, A. L., Ramachandran, A., CEASER, E. K., Dickinson, D. A., Zanoni, G., Morrow, J. D., & Darley-Usmar, V. M. (2004) · Biochemical Journal · doi:10.1042/bj20031049 · Cited by 559 · see citing works
Methionine in proteins defends against oxidative stress
Luo, S., & Levine, R. L. (2008) · The FASEB Journal · doi:10.1096/fj.08-118414 · Cited by 462 · see citing works
Quantifying the global cellular thiol–disulfide status
Hansen, R. E., Roth, D., & Winther, J. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812149106 · Cited by 428 · see citing works
Beer, S. M., Taylor, E. R., Brown, S. E., Dahm, C. C., Costa, N. J., Runswick, M. J., & Murphy, M. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408011200 · Cited by 404 · see citing works
Self-citationProtein Sulfhydryls and Their Role in the Antioxidant Function of Protein S-Thiolation
Thomas, J. A., Poland, B. W., & Honzatko, R. B. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1261 · Cited by 399 · see citing works
Reversible Glutathionylation of Complex I Increases Mitochondrial Superoxide Formation
Taylor, E. R., Hurrell, F., Shannon, R. J., Lin, T., Hirst, J., & Murphy, M. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209359200 · Cited by 389 · see citing works
Self-citationSuperoxide as an intracellular radical sink
Winterbourn, C. C. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90512-s · Cited by 365 · see citing works
The chemistry of pernitrites. Part I. Kinetics of decomposition of pernitrous acid
Hughes, M., & Nicklin, H. G. (1968) · Journal of the Chemical Society A Inorganic Physical Theoretical · doi:10.1039/j19680000450 · Cited by 352 · see citing works
Methionine residues may protect proteins from critical oxidative damage
Levine, R. L., Berlett, B. S., Moskovitz, J., Mosoni, L., & Stadtman, E. R. (1999) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(98)00152-3 · Cited by 338 · see citing works
Cloning and Expression of a Novel Human Glutaredoxin (Grx2) with Mitochondrial and Nuclear Isoforms
Lundberg, M., Johansson, C., Chandra, J., Enoksson, M., Jacobsson, G., Lundström-Ljung, J., Johansson, M., & Holmgren, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011605200 · Cited by 335 · see citing works
Peroxynitrite rapidly permeates phospholipid membranes
Marla, S. S., Lee, J., & Groves, J. T. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14243 · Cited by 306 · see citing works
A precise method for the determination of whole blood and plasma sulfhydryl groups
Ellman, G. L., & Lysko, H. (1979) · Analytical Biochemistry · doi:10.1016/s0003-2697(79)80122-0 · Cited by 268 · see citing works
Identification and Characterization of a New Mammalian Glutaredoxin (Thioltransferase), Grx2
Gladyshev, V. N., Liu, A., Novoselov, S. V., Krysan, K., Sun, Q., Kryukov, V. M., Kryukov, G. V., & Lou, M. F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100020200 · Cited by 234 · see citing works
Ford, E., Hughes, M., & Wardman, P. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00850-x · Cited by 229 · see citing works
Gallogly, M. M., Starke, D. W., & Mieyal, J. J. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2291 · Cited by 224 · see citing works
Prime, T. A., Blaikie, F. H., Evans, C., Nadtochiy, S. M., James, A. M., Dahm, C. C., Vitturi, D. A., Patel, R. P., Hiley, C. R., Abakumova, I., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903250106 · Cited by 222 · see citing works
Self-citationRapid and extensive uptake and activation of hydrophobic triphenylphosphonium cations within cells
Ross, M. F., Prime, T. A., Abakumova, I., James, A. M., Porteous, C. M., Smith, R. A. J., & Murphy, M. P. (2008) · Biochemical Journal · doi:10.1042/bj20080063 · Cited by 206 · see citing works
Self-citationDahm, C. C., Moore, K., & Murphy, M. P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512203200 · Cited by 194 · see citing works
Self-citationSharpley, M. S., Shannon, R. J., Draghi, F., & Hirst, J. (2005) · Biochemistry · doi:10.1021/bi051809x · Cited by 193 · see citing works
Bonini, M. G., & Augusto, O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008456200 · Cited by 191 · see citing works
Hurd, T. R., Requejo, R., Filipovska, A., Brown, S., Prime, T. A., Robinson, A. J., Fearnley, I. M., & Murphy, M. P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803432200 · Cited by 182 · see citing works
Self-citationMason, R. P. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.02.077 · Cited by 170 · see citing works
Overexpression of glutaredoxin 2 attenuates apoptosis by preventing cytochrome c release
Enoksson, M., Fernandes, A. P., Prast‐Nielsen, S., Lillig, C. H., Holmgren, A., & Orrenius, S. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.12.067 · Cited by 162 · see citing works
Covalent adduction of nucleophilic amino acids by 4-hydroxynonenal and 4-oxononenal
Doorn, J. A., & Petersen, D. R. (2003) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00178-3 · Cited by 147 · see citing works
Lillig, C. H., Lönn, M. E., Enoksson, M., Fernandes, A. P., & Holmgren, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401896101 · Cited by 147 · see citing works
Peroxynitrite causes calcium efflux from mitochondria which is prevented by Cyclosporin A
Packer, M. A., & Murphy, M. P. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00461-7 · Cited by 143 · see citing works
Self-citationPREPARATION OF MITOCHONDRIA FROM ANIMAL TISSUES AND YEASTS
Chappell, J., & Hansford, R. G. (1972) · Elsevier eBooks · doi:10.1016/b978-0-408-70360-4.50009-2 · Cited by 136 · see citing works
Redox Potential and Peroxide Reactivity of Human Peroxiredoxin 3
Cox, A. G., Peskin, A. V., Paton, L. N., Winterbourn, C. C., & Hampton, M. B. (2009) · Biochemistry · doi:10.1021/bi900558g · Cited by 130 · see citing works
Role of Protein -SH Groups in Redox Homeostasis— The Erythrocyte as a Model System
Simplicio, P. D., Cacace, M. G., Lusini, L., Giannerini, F., Giustarini, D., & Rossi, R. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0694 · Cited by 123 · see citing works
Liu, B., Tewari, A. K., Zhang, L., Green‐Church, K. B., Zweier, J. L., Chen, Y., & He, G. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.12.008 · Cited by 116 · see citing works
Madej, E., Folkes, L. K., Wardman, P., Czapski, G., & Goldstein, S. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.02.015 · Cited by 105 · see citing works
Yamamoto, T., Maruyama, W., Kato, Y., Yi, H. L., Shamoto‐Nagai, M., Tanaka, M., Sato, Y., & Naoi, M. (2002) · Journal of Neural Transmission · doi:10.1007/s702-002-8232-1 · Cited by 104 · see citing works
[2] Structural analysis of NADH: Ubiquinone oxidoreductase from bovine heart mitochondria
Walker, J. E., Skehel, M. J., & Buchanan, S. K. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)60127-9 · Cited by 87 · see citing works
Scarlett, J. L., Packer, M. A., Porteous, C. M., & Murphy, M. P. (1996) · Biochemical Pharmacology · doi:10.1016/0006-2952(96)99426-5 · Cited by 85 · see citing works
Self-citationZeng, J., Dunlop, R. A., Rodgers, K. J., & Davies, M. J. (2006) · Biochemical Journal · doi:10.1042/bj20060019 · Cited by 79 · see citing works
Zhang, H., Xu, Y., Joseph, J., & Kalyanaraman, B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504503200 · Cited by 76 · see citing works
Craig, C. L., & Weber, R. S. (1998) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a025981 · Cited by 71 · see citing works
Bharath, S., & Andersen, J. K. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.900 · Cited by 64 · see citing works
Sled, V. D., & Vinogradov, A. D. (1993) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(93)90051-g · Cited by 63 · see citing works
Jacob, M. H., Amir, D., Ratner, V., Gussakovsky, E. E., & Haas, E. (2005) · Biochemistry · doi:10.1021/bi051205t · Cited by 39 · see citing works
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The thiol pool in human plasma: The central contribution of albumin to redox processes
Turell, L., Radí, R., & Álvarez, B. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.050 · Cited by 712 · see citing works
Lavie, L. (2014) · Sleep Medicine Reviews · doi:10.1016/j.smrv.2014.07.003 · Cited by 692 · see citing works
Biochemistry of Peroxynitrite and Protein Tyrosine Nitration
Ferrer‐Sueta, G., Campolo, N., Trujillo, M., Bartesaghi, S., Carballal, S., Romero, N., Álvarez, B., & Radí, R. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00568 · Cited by 645 · see citing works
Heger, M., van Golen, R. F., Broekgaarden, M., & Michel, M. C. (2013) · Pharmacological Reviews · doi:10.1124/pr.110.004044 · Cited by 581 · see citing works
A Quantitative Tissue-Specific Landscape of Protein Redox Regulation during Aging
Xiao, H., Jedrychowski, M. P., Schweppe, D. K., Huttlin, E. L., Yu, Q., Heppner, D. E., Li, J., Long, J., Mills, E. L., Szpyt, J., et al. (2020) · Cell · doi:10.1016/j.cell.2020.02.012 · Cited by 399 · see citing works
Murphy, M. P. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4289 · Cited by 341 · see citing works
Self-citationCarrico, C., Meyer, J. G., He, W., Gibson, B. W., & Verdin, E. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.01.016 · Cited by 331 · see citing works
Cell signalling by reactive lipid species: new concepts and molecular mechanisms
Higdon, A. N., Diers, A. R., Oh, J. Y., Landar, A. L., & Darley-Usmar, V. M. (2012) · Biochemical Journal · doi:10.1042/bj20111752 · Cited by 320 · see citing works
Causes and consequences of cysteine S-glutathionylation
Grek, C. L., Zhang, J., Manevich, Y., Townsend, D. M., & Tew, K. D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.461368 · Cited by 312 · see citing works
Redox regulation of mitochondrial function with emphasis on cysteine oxidation reactions
Mailloux, R. J., Jin, X., & Willmore, W. G. (2013) · Redox Biology · doi:10.1016/j.redox.2013.12.011 · Cited by 312 · see citing works
Marzia Perluigi, A., Domenico, F. D., & Butterfield, D. A. (2023) · Physiological Reviews · doi:10.1152/physrev.00030.2022 · Cited by 306 · see citing works
Factors Affecting Protein Thiol Reactivity and Specificity in Peroxide Reduction
Ferrer‐Sueta, G., Manta, B., Botti, H., Radí, R., Trujillo, M., & Denicola, A. (2011) · Chemical Research in Toxicology · doi:10.1021/tx100413v · Cited by 286 · see citing works
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van der Reest, J., Lilla, S., Zheng, L., Zanivan, S. R., & Gottlieb, E. (2018) · Nature Communications · doi:10.1038/s41467-018-04003-3 · Cited by 267 · see citing works
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Sousa, J. S., D’Imprima, E., & Vonck, J. (2018) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-10-7757-9_7 · Cited by 239 · see citing works
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Baba, S. P., & Bhatnagar, A. (2018) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2018.03.005 · Cited by 230 · see citing works
Protein Oxidative Modifications: Beneficial Roles in Disease and Health.
Cai, Z., & Yan, L. (2013) · PubMed · Cited by 226 · see citing works
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Schwarzländer, M., & Finkemeier, I. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5104 · Cited by 192 · see citing works
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Musatov, A., & Robinson, N. C. (2012) · Free Radical Research · doi:10.3109/10715762.2012.717273 · Cited by 180 · see citing works
Storkey, C., Davies, M. J., & Pattison, D. I. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.04.024 · Cited by 165 · see citing works
Glutathione and Glutaredoxin—Key Players in Cellular Redox Homeostasis and Signaling
Chai, Y.-C., & Mieyal, J. J. (2023) · Antioxidants · doi:10.3390/antiox12081553 · Cited by 162 · see citing works
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Dröse, S., Brandt, U., & Wittig, I. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.02.006 · Cited by 153 · see citing works
Bazylewski, P. F., Divigalpitiya, R., & Fanchini, G. (2017) · RSC Advances · doi:10.1039/c6ra25879d · Cited by 153 · see citing works
Targeting Stimulator of Interferon Genes (STING): A Medicinal Chemistry Perspective
Zhang, H., You, Q., & Xu, X. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01039 · Cited by 152 · see citing works
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Activity-Based Sensing for Site-Specific Proteomic Analysis of Cysteine Oxidation
Shi, Y., & Carroll, K. S. (2019) · Accounts of Chemical Research · doi:10.1021/acs.accounts.9b00562 · Cited by 145 · see citing works
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Piantadosi, C. A. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.03.008 · Cited by 144 · see citing works
Chouchani, E. T., Hurd, T. R., Nadtochiy, S. M., Brookes, P. S., Fearnley, I. M., Lilley, K. S., Smith, R. A. J., & Murphy, M. P. (2010) · Biochemical Journal · doi:10.1042/bj20100633 · Cited by 137 · see citing works
Self-citationRedox regulation of the actin cytoskeleton and its role in the vascular system
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Chen, H., Qi, H., & Xiong, P. (2022) · Marine Drugs · doi:10.3390/md20070450 · Cited by 129 · see citing works
Musaogullari, A., & Chai, Y.-C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218113 · Cited by 116 · see citing works
McDonagh, B., Sakellariou, G. K., Smith, N. T., Brownridge, P., & Jackson, M. J. (2014) · Journal of Proteome Research · doi:10.1021/pr5006394 · Cited by 110 · see citing works
Proteomic approaches to the characterization of protein thiol modification
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Held, J. M., & Gibson, B. W. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r111.013037 · Cited by 103 · see citing works
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STING palmitoylation as a therapeutic target
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Pleonsil, P., Soogarun, S., & Suwanwong, Y. (2013) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2013.06.016 · Cited by 93 · see citing works
Batchelor‐McAuley, C., Tschulik, K., Neumann, C., Laborda, E., & Compton, R. G. (2014) · International Journal of Electrochemical Science · doi:10.1016/s1452-3981(23)07783-0 · Cited by 91 · see citing works
Giardia secretome highlights secreted tenascins as a key component of pathogenesis
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Møller, I. M., Igamberdiev, A. U., Bykova, N. V., Finkemeier, I., Rasmusson, A. G., & Schwarzländer, M. (2020) · The Plant Cell · doi:10.1105/tpc.19.00535 · Cited by 89 · see citing works
Zhu, Z., Umehara, T., Okazaki, T., Goto, M., Fujita, Y., Hoque, S. A. M., Kawai, T., Zeng, W., & Shimada, M. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00252 · Cited by 88 · see citing works
Redox signaling pathways in unilateral ureteral obstruction (UUO)-induced renal fibrosis
Aranda‐Rivera, A. K., Cruz‐Gregorio, A., Aparicio‐Trejo, O. E., Ortega-Lozano, A. J., & Pedraza‐Chaverrí, J. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.05.034 · Cited by 87 · see citing works
Castro, H., Teixeira, F., Romão, S., Santos, M., Cruz, T., Flórido, M., Appelberg, R., Oliveira, P., Ferreira‐da‐Silva, F., & Tomás, A. M. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002325 · Cited by 83 · see citing works
Respiratory chain complex II as general sensor for apoptosis
Grimm, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.09.009 · Cited by 82 · see citing works
Selective Inhibition of Deactivated Mitochondrial Complex I by Biguanides
Matsuzaki, S., & Humphries, K. M. (2015) · Biochemistry · doi:10.1021/bi501473h · Cited by 81 · see citing works
Studying the Effects of Cysteine Residues on Protein Interactions with Silver Nanoparticles
Siriwardana, K., Wang, A., Gadogbe, M., Collier, W. E., Fitzkee, N. C., & Zhang, D. (2015) · The Journal of Physical Chemistry C · doi:10.1021/jp512440z · Cited by 80 · see citing works
Watanabe, H., Imafuku, T., Otagiri, M., & Maruyama, T. (2017) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2017.03.002 · Cited by 79 · see citing works
Selective and reversible photochemical derivatization of cysteine residues in peptides and proteins
Arumugam, S., Guo, J., Mbua, N. E., Friscourt, F., Lin, N., Nekongo, E. E., Boons, G., & Popik, V. V. (2014) · Chemical Science · doi:10.1039/c3sc51691a · Cited by 76 · see citing works
Horowitz, M. P., Milanese, C., Maio, R. D., Hu, X., Montero, L. M., Sanders, L. H., Tapias, V., Sepe, S., van Cappellen, W. A., Burton, E. A., et al. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3629 · Cited by 75 · see citing works
Chemical Forms of Mercury in Human Hair Reveal Sources of Exposure
Manceau, A., Enescu, M., Simionovici, A., Lanson, M., González-Rey, M., Rovezzi, M., Tucoulou, R., Glatzel, P., Nagy, K. L., & Bourdineaud, J. (2016) · Environmental Science & Technology · doi:10.1021/acs.est.6b03468 · Cited by 75 · see citing works
Redox regulation of mitochondrial proteins and proteomes by cysteine thiol switches
Nietzel, T., Mostertz, J., Hochgräfe, F., & Schwarzländer, M. (2016) · Mitochondrion · doi:10.1016/j.mito.2016.07.010 · Cited by 74 · see citing works
de Groot, A., Roche, D., Fernandez, B., Ludanyi, M., Cruveiller, S., Pignol, D., Vallenet, D., Armengaud, J., & Blanchard, L. (2014) · Genome Biology and Evolution · doi:10.1093/gbe/evu069 · Cited by 72 · see citing works
Souza, C. F., Baldissera, M. D., Verdi, C. M., Santos, R. C. V., da Rocha, M. I. D. U. M., da Veiga, M. L., Silva, A. S. D., & Baldisserotto, B. (2019) · Microbial Pathogenesis · doi:10.1016/j.micpath.2019.04.007 · Cited by 72 · see citing works
Menger, K. E., James, A. M., Cochemé, H. M., Harbour, M. E., Chouchani, E. T., Ding, S., Fearnley, I. M., Partridge, L., & Murphy, M. P. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.05.033 · Cited by 72 · see citing works
Self-citationTargeting Non-Catalytic Cysteine Residues Through Structure-Guided Drug Discovery
Hallenbeck, K. K., Turner, D., Renslo, A. R., & Arkin, M. R. (2016) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026616666160719163839 · Cited by 71 · see citing works
Donida, B., Marchetti, D. P., Biancini, G. B., Deon, M., Manini, P. R., da Rosa, H. T., Moura, D. J., Saffi, J., Bender, F., Burin, M. G., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.02.004 · Cited by 68 · see citing works
Fernandes, C. G., Borges, C. G., Seminotti, B., Amaral, A. U., Knebel, L. A., Eichler, P., de Oliveira, A. B., Leipnitz, G., & Wajner, M. (2011) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-011-9675-4 · Cited by 67 · see citing works
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Schopfer, F. J., & Khoo, N. K. H. (2019) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2019.04.009 · Cited by 67 · see citing works
Shu, N., Lorentzen, L. G., & Davies, M. J. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.04.026 · Cited by 63 · see citing works
Siriwardana, K., Wang, A., Vangala, K., Fitzkee, N. C., & Zhang, D. (2013) · Langmuir · doi:10.1021/la402239h · Cited by 61 · see citing works
Oyagbemi, A. A., Omóbòwálé, T. O., Saba, A. B., Olowu, E. R., Dada, R. O., & Akinrinde, A. S. (2015) · Journal of Dietary Supplements · doi:10.3109/19390211.2015.1103827 · Cited by 60 · see citing works
Turell, L., Vitturi, D. A., Coitiño, E. L., Lebrato, L., Möller, M. N., Sagasti, C., Salvatore, S. R., Woodcock, S. R., Álvarez, B., & Schopfer, F. J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.756288 · Cited by 60 · see citing works
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Tomás, A. M., & Castro, H. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4948 · Cited by 59 · see citing works
Huang, Z., Wang, H., & Yang, W. (2015) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5b01552 · Cited by 57 · see citing works
New indole-based chalconoids as tubulin-targeting antiproliferative agents
Mirzaei, H., Shokrzadeh, M., Modanloo, M., Ziar, A., Riazi, G. H., & Emami, S. (2017) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2017.09.005 · Cited by 57 · see citing works
Serien, D., & Sugioka, K. (2018) · Opto-Electronic Advances · doi:10.29026/oea.2018.180008 · Cited by 57 · see citing works
An injectable PEG hydrogel controlling neurotrophin-3 release by affinity peptides
Wang, J., Youngblood, R. L., Cassinotti, L. R., Skoumal, M., Corfas, G., & Shea, L. D. (2020) · Journal of Controlled Release · doi:10.1016/j.jconrel.2020.12.045 · Cited by 57 · see citing works
Cobley, J. N. (2020) · Antioxidants · doi:10.3390/antiox9100933 · Cited by 56 · see citing works
Dual regulation of SLC25A39 by AFG3L2 and iron controls mitochondrial glutathione homeostasis
Shi, X., DeCiucis, M., Grabinska, K. A., Kanyo, J., Liu, A., Lam, T. T., & Shen, H. (2024) · Molecular Cell · doi:10.1016/j.molcel.2023.12.008 · Cited by 54 · see citing works
Benavides, G. A., Liang, Q., Dodson, M. B., Darley-Usmar, V. M., & Zhang, J. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.09.006 · Cited by 52 · see citing works
Go, Y. (2011) · Journal of Proteomics & Bioinformatics · doi:10.4172/jpb.1000190 · Cited by 52 · see citing works
Photoactivatable protein labeling by singlet oxygen mediated reactions
To, T., Medzihradszky, K. F., Burlingame, A. L., DeGrado, W. F., Jo, H., & Shu, X. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.05.034 · Cited by 51 · see citing works
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Hansen, S. H., & Grunnet, N. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-6093-0_1 · Cited by 48 · see citing works
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Castro, H., Romão, S., Carvalho, S., Teixeira, F., Sousa, C. F., & Tomás, A. M. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012607 · Cited by 48 · see citing works
Why does mitochondrial complex I have so many subunits?
Hirst, J. (2011) · Biochemical Journal · doi:10.1042/bj20110918 · Cited by 48 · see citing works
Sundqvist, M., Christenson, K., Björnsdóttir, H., Osla, V., Karlsson, A., Dahlgren, C., Speert, D. P., Fasth, A. L., Brown, K. L., & Bylund, J. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01828 · Cited by 47 · see citing works
Vanzin, C. S., Biancini, G. B., Sitta, Â., Wayhs, C. A. Y., Pereira, I. N., Rockenbach, F. J., García, S. C., Wyse, Â. T. D. S., Schwartz, I. V. D., Wajner, M., et al. (2011) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2011.06.013 · Cited by 46 · see citing works
Lumpuy‐Castillo, J., Amador‐Martínez, I., Díaz-Rojas, M., Lorenzo, Ó., Pedraza-Chaverrí, J., Sánchez‐Lozada, L. G., & Aparicio‐Trejo, O. E. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103340 · Cited by 44 · see citing works
The properties of human disease mutations at protein interfaces
Livesey, B., & Marsh, J. A. (2022) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1009858 · Cited by 42 · see citing works
Sun, Q., Sun, D., Song, L., Chen, Z., Chen, Z., Zhang, W., & Qian, J. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b00178 · Cited by 40 · see citing works
Storkey, C., Pattison, D. I., Ignasiak, M. T., Schiesser, C. H., & Davies, M. J. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.10.424 · Cited by 40 · see citing works
Davis, D. A., Bulut, H., Shrestha, P., Yaparla, A., Jaeger, H. K., Hattori, S.-I., Wingfield, P. T., Mieyal, J. J., Mitsuya, H., & Yarchoan, R. (2021) · mBio · doi:10.1128/mbio.02094-21 · Cited by 39 · see citing works
Powerhouse down: Complex II dissociation in the respiratory chain
Hwang, M., Rohlena, J., Dong, L., Neužil, J., & Grimm, S. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.06.001 · Cited by 39 · see citing works
The Causes and Consequences of Nonenzymatic Protein Acylation
James, A. M., Smith, C. L., Smith, A. C., Robinson, A. J., Hoogewijs, K., & Murphy, M. P. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.07.002 · Cited by 39 · see citing works
Self-citationMiljković, J. L., Burger, N., Gawel, J. M., Mulvey, J. F., Norman, A. A. I., Nishimura, T., Tsujihata, Y., Logan, A., Sauchanka, O., Caldwell, S. T., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102429 · Cited by 39 · see citing works
Self-citationND3 Cys39 in complex I is exposed during mitochondrial respiration
Burger, N., James, A. M., Mulvey, J. F., Hoogewijs, K., Ding, S., Fearnley, I. M., Loureiro, M., Norman, A. A. I., Arndt, S., Mottahedin, A., et al. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.10.010 · Cited by 38 · see citing works
Self-citationImproved prediction of accessible surface area results in efficient energy function application
Iqbal, S., Mishra, A., & Hoque, M. T. (2015) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2015.06.012 · Cited by 38 · see citing works
Cherdkiatikul, T., & Suwanwong, Y. (2014) · SLAS DISCOVERY · doi:10.1177/1087057113520565 · Cited by 37 · see citing works
Quantification and identification of mitochondrial proteins containing vicinal dithiols
Requejo-Aguilar, R., Chouchani, E. T., James, A. M., Prime, T. A., Lilley, K. S., Fearnley, I. M., & Murphy, M. P. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.09.003 · Cited by 36 · see citing works
Self-citationN-Acetyl-l-Cysteine Protects Astrocytes against Proteotoxicity without Recourse to Glutathione
Gleixner, A. M., Hutchison, D. F., Sannino, S., Bhatia, T. N., Leak, L. C., Flaherty, P. T., Wipf, P., Brodsky, J. L., & Leak, R. K. (2017) · Molecular Pharmacology · doi:10.1124/mol.117.109926 · Cited by 36 · see citing works
James, A. M., Smith, A. C., Smith, C. L., Robinson, A. J., & Murphy, M. P. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.07.007 · Cited by 36 · see citing works
Self-citationNedoboy, P. E., Morgan, P. E., Mocatta, T. J., Richards, M., Winterbourn, C. C., & Davies, M. J. (2014) · Free Radical Research · doi:10.3109/10715762.2014.947286 · Cited by 35 · see citing works
Carroll, L., Davies, M. J., & Pattison, D. I. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1018247 · Cited by 35 · see citing works
Convenient detection of the thiol functional group using H/D isotope sensitive Raman spectroscopy
Bandyopadhyay, S., & Dey, A. (2014) · The Analyst · doi:10.1039/c3an02166a · Cited by 34 · see citing works
- Authors
- Requejo, R., Hurd, T. R., Costa, N. J., & Murphy, M. P.
- Affiliations
- MRC Mitochondrial Biology Unit (GB)
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2010-02-24
- Volume
- 277
- Issue
- 6
- Pages
- 1465-1480
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- PMC
- PMC2847196
- OpenAlex
- W1524076404
- Cited by
- 231
- References
- 52
- Citations by year
- 2026: 7 · 2025: 7 · 2024: 14 · 2023: 12 · 2022: 15 · 2021: 13 · 2020: 11 · 2019: 13 · 2018: 20 · 2017: 11 · 2016: 14 · 2015: 18 · 2014: 24 · 2013: 16 · 2012: 14
- FWCI
- 6.77
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- FEBS Journal (publishedVersion)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Ministerio de Ciencia y Tecnología
- Medical Research Council
- 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
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- cysteine residues, mitochondrial matrix, glutathione, oxidative damage, antioxidant defense, peroxynitrite, tyrosine nitration, protein oxidation, mitochondrial complex I, reactive oxygen species, reactive nitrogen species, electrophiles, rat liver, rat heart
- MeSH terms
- Animals, Cells, Cultured, Cysteine, Glutathione, Membrane Proteins, Mitochondria, Heart, Mitochondria, Liver, Sulfhydryl Compounds, Oxidative Stress, Rats
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