The basics of thiols and cysteines in redox biology and chemistry

A simple method for displaying the hydropathic character of a protein

Kyte, J., & Doolittle, R. F. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90515-0 · Cited by 22,694 · see citing works

Nitric Oxide and Peroxynitrite in Health and Disease

Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390 · see citing works

Hydroperoxide metabolism in mammalian organs.

Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827 · 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

Redefining Oxidative Stress

Jones, D. P. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.1865 · Cited by 1,726 · see citing works

Quantitative reactivity profiling predicts functional cysteines in proteomes

Weerapana, E., Wang, C., Simon, G. M., Richter, F., Khare, S., Dillon, M. B. D., Bachovchin, D. A., Mowen, K., Baker, D., & Cravatt, B. F. (2010) · Nature · doi:10.1038/nature09472 · Cited by 1,684 · see citing works

Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling

Wood, Z. A., Poole, L. B., & Karplus, P. A. (2003) · Science · doi:10.1126/science.1080405 · Cited by 1,369 · see citing works

Cysteine-Mediated Redox Signaling: Chemistry, Biology, and Tools for Discovery

Paulsen, C. E., & Carroll, K. S. (2013) · Chemical Reviews · doi:10.1021/cr300163e · Cited by 1,283 · see citing works

Thiol chemistry and specificity in redox signaling

Winterbourn, C. C., & Hampton, M. B. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.004 · Cited by 1,226 · see citing works

Hydrophobicity of Amino Acid Residues in Globular Proteins

Rose, G. D., Geselowitz, A., Lesser, G. J., Lee, R., & Zehfus, M. H. (1985) · Science · doi:10.1126/science.4023714 · Cited by 1,176 · see citing works

An Introduction to Organic Chemistry

(1922) · Nature · doi:10.1038/109039d0 · Cited by 1,029 · see citing works

ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin

Biteau, B., Labarre, J., & Tolédano, M. B. (2003) · Nature · doi:10.1038/nature02075 · Cited by 970 · see citing works

S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death

Gu, Z., Kaul, M., Yan, B., Kridel, S. J., Cui, J., Strongin, A., Smith, J. W., Liddington, R. C., & Lipton, S. A. (2002) · Science · doi:10.1126/science.1073634 · Cited by 950 · see citing works

A Thiol Peroxidase Is an H2O2 Receptor and Redox-Transducer in Gene Activation

Delaunay, A., Pflieger, D., Barrault, M., Vinh, J., & Tolédano, M. B. (2002) · Cell · doi:10.1016/s0092-8674(02)01048-6 · Cited by 902 · see citing works

Unraveling the biological roles of reactive oxygen species

Murphy, M. P., Holmgren, A., Larsson, N.-G., Halliwell, B., Chang, C. J., Kalyanaraman, B., Rhee, S. G., Thornalley, P. J., Partridge, L., Gems, D., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.010 · Cited by 836 · see citing works

Signaling Functions of Reactive Oxygen Species

Forman, H. J., Maiorino, M., & Ursini, F. (2010) · Biochemistry · doi:10.1021/bi9020378 · Cited by 827 · see citing works

Handbook of Biochemistry and Molecular Biology

(2010) · CRC Press eBooks · doi:10.1201/b10501 · Cited by 804 · 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

Redox-based regulation of signal transduction: principles, pitfalls, and promises

Janssen-Heininger, Y. M. W., Mossman, B. T., Heintz, N. H., Forman, H. J., Kalyanaraman, B., Finkel, T., Stamler, J. S., Rhee, S. G., & van der Vliet, A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.011 · Cited by 784 · see citing works

Surface and inside volumes in globular proteins

Janin, J. (1979) · Nature · doi:10.1038/277491a0 · Cited by 714 · see citing works

Redox compartmentalization in eukaryotic cells.

Go, Y., & Jones, D. P. (2008) · Biochimica et Biophysica Acta · doi:10.1016/j.bbagen.2008.01.011 · Cited by 635 · see citing works

Fundamentals of Biochemistry: Life at the Molecular Level

Voet, D., Voet, J. G., & Pratt, C. W. (2005) · Works - Scholarship, Research, & Creative Expression (Swarthmore College) · Cited by 616 · see citing works

Protein Sulfenic Acids in Redox Signaling

Poole, L. B., Karplus, P. A., & Claiborne, A. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.44.101802.121735 · Cited by 595 · see citing works

Structural Basis of the Redox Switch in the OxyR Transcription Factor

Choi, H., Kim, S.-J., Mukhopadhyay, P., Cho, S., Woo, J.-R., Storz, G., & Ryu, S.-E. (2001) · Cell · doi:10.1016/s0092-8674(01)00300-2 · Cited by 560 · see citing works

Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation

Woo, H. A., Chae, H. Z., Hwang, S. C., Yang, K., Kang, S. W., Kim, K., & Rhee, S. G. (2003) · Science · doi:10.1126/science.1080273 · Cited by 558 · see citing works

Mammalian Heme Peroxidases: From Molecular Mechanisms to Health Implications

Davies, M. J., Hawkins, C. L., Pattison, D. I., & Rees, M. D. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1927 · Cited by 556 · see citing works

Quantifying changes in the thiol redox proteome upon oxidative stress in vivo

Leichert, L. I. O., Gehrke, F., Gudiseva, H. V., Blackwell, T. W., Ilbert, M., Walker, A. K., Strahler, J. R., Andrews, P., & Jakob, U. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707723105 · Cited by 514 · see citing works

Nox enzymes and new thinking on reactive oxygen: A double-edged sword revisited

Lambeth, J. D., & Neish, A. S. (2014) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012513-104651 · Cited by 495 · see citing works

Kinetics and Mechanisms of Thiol–Disulfide Exchange Covering Direct Substitution and Thiol Oxidation-Mediated Pathways

Nagy, P. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4973 · Cited by 488 · see citing works

Hypochlorous Acid Oxygenates the Cysteine Switch Domain of Pro-matrilysin (MMP-7)

Fu, X., Kassim, S. Y., Parks, W. C., & Heinecke, J. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106958200 · Cited by 482 · see citing works

THE SULFHYDRYL GROUPS OF CRYSTALLINE PROTEINS

Benesch, R. E., Lardy, H. A., & Benesch, R. (1955) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81422-9 · Cited by 476 · see citing works

Orchestrating Redox Signaling Networks through Regulatory Cysteine Switches

Paulsen, C. E., & Carroll, K. S. (2009) · ACS Chemical Biology · doi:10.1021/cb900258z · Cited by 476 · see citing works

Endogenous generation of reactive oxidants and electrophiles and their reactions with DNA and protein

Marnett, L. J., Riggins, J. N., & West, J. D. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200318022 · Cited by 476 · see citing works

Enzymology of H 2 S Biogenesis, Decay and Signaling

Kabil, Ö., & Banerjee, R. V. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5339 · Cited by 474 · see citing works

Peroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity

Paulsen, C. E., Truong, T. H., García, F., Homann, A., Gupta, V., Leonard, S. E., & Carroll, K. S. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.736 · Cited by 473 · see citing works

Thiol redox control via thioredoxin and glutaredoxin systems

Holmgren, A., Johansson, C., Berndt, C., Lönn, M. E., Hudemann, C., & Lillig, C. H. (2005) · Biochemical Society Transactions · doi:10.1042/bst20051375 · Cited by 463 · see citing works

Cysteine Redox Sensor in PKGIa Enables Oxidant-Induced Activation

Burgoyne, J. R., Madhani, M., Cuello, F., Charles, R. L., Brennan, J. P., Schröder, E., Browning, D. D., & Eaton, P. (2007) · Science · doi:10.1126/science.1144318 · Cited by 457 · see citing works

Methods for detection and measurement of hydrogen peroxide inside and outside of cells

Rhee, S. G., Chang, T.-S., Jeong, W., & Kang, D. (2010) · Molecules and Cells · doi:10.1007/s10059-010-0082-3 · Cited by 433 · see citing works

Redox Potentials of Glutaredoxins and Other Thiol-Disulfide Oxidoreductases of the Thioredoxin Superfamily Determined by Direct Protein-Protein Redox Equilibria

Åslund, F., Berndt, K. D., & Holmgren, A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.49.30780 · Cited by 418 · see citing works

Redox control in trypanosomatids, parasitic protozoa with trypanothione-based thiol metabolism

Krauth‐Siegel, R. L., & Comini, M. A. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.03.006 · Cited by 414 · see citing works

Structure, Function, and Mechanism of Thioredoxin Proteins

Collet, J., & Messens, J. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3114 · Cited by 397 · see citing works

Cysteine Function Governs Its Conservation and Degeneration and Restricts Its Utilization on Protein Surfaces

Marino, S. M., & Gladyshev, V. N. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.09.027 · Cited by 394 · see citing works

Quantification of thiols and disulfides

Winther, J. R., & Thorpe, C. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.03.031 · Cited by 383 · see citing works

Thiol-based redox switches in eukaryotic proteins

Brandes, N., Schmitt, S., & Jakob, U. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2285 · Cited by 373 · see citing works

Thiol-Based Redox Switches and Gene Regulation

Antelmann, H., & Helmann, J. D. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3400 · Cited by 366 · see citing works

Cysteine-Based Redox Switches in Enzymes

Klomsiri, C., Karplus, P. A., & Poole, L. B. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3376 · Cited by 359 · see citing works

Thioredoxin reductase

Williams, C. H., Arscott, L. D., Müller, S., Lennon, B. W., Ludwig, M. L., Wang, P., Veine, D. M., Becker, K., & Schirmer, R. H. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01702.x · Cited by 343 · see citing works

Comparison of the chemical properties of selenocysteine and selenocystine with their sulfur analogs

Huber, R. E., & Criddle, R. S. (1967) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(67)90136-1 · Cited by 342 · see citing works

Biological roles for the NOX family NADPH oxidases

Nauseef, W. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r700045200 · Cited by 331 · see citing works

Cellular metabolic and autophagic pathways: Traffic control by redox signaling

Dodson, M. B., Darley-Usmar, V. M., & Zhang, J. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.014 · Cited by 325 · see citing works

Selenoproteins—What unique properties can arise with selenocysteine in place of cysteine?

Arnér, E. S. J. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.02.032 · Cited by 325 · 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

Ionisation of Cysteine Residues at the Termini of Model α-Helical Peptides. Relevance to Unusual Thiol pKaValues in Proteins of the Thioredoxin Family

Kortemme, T., & Creighton, T. E. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0592 · Cited by 319 · see citing works

Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis

Lind, C., Gerdes, R. G., Hamnell-Pamment, Y., Schuppe‐Koistinen, I., von Löwenhielm, H. B., Holmgren, A., & Cotgreave, I. A. (2002) · Archives of Biochemistry and Biophysics · doi:10.1016/s0003-9861(02)00468-x · Cited by 311 · see citing works

Selenium in chemistry and biochemistry in comparison to sulfur

Wessjohann, L. A., Schneider, A. R., Abbas, M., & Brandt, W. (2007) · Biological Chemistry · doi:10.1515/bc.2007.138 · Cited by 308 · 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

Mining the Thiol Proteome for Sulfenic Acid Modifications Reveals New Targets for Oxidation in Cells

Leonard, S. E., Reddie, K. G., & Carroll, K. S. (2009) · ACS Chemical Biology · doi:10.1021/cb900105q · Cited by 282 · see citing works

Mechanisms of S-nitrosothiol formation and selectivity in nitric oxide signaling

Smith, B. C., & Marletta, M. A. (2012) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2012.10.016 · Cited by 270 · see citing works

The redox proteome

Go, Y.-M., & Jones, D. P. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.464131 · Cited by 260 · see citing works

Identification of S-nitrosylation motifs by site-specific mapping of the S -nitrosocysteine proteome in human vascular smooth muscle cells

Greco, T. M., Hodara, R., Parastatidis, I., Heijnen, H. F. G., Dennehy, M. K., Liebler, D. C., & Ischiropoulos, H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600729103 · Cited by 255 · see citing works

Protein‐sulfenic acid stabilization and function in enzyme catalysis and gene regulation

Claiborne, A., Miller, H., Parsonage, D., & Ross, R. P. (1993) · The FASEB Journal · doi:10.1096/fasebj.7.15.8262333 · Cited by 251 · see citing works

Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases

Poole, L. B. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.09.006 · Cited by 246 · see citing works

Disparate proteome reactivity profiles of carbon electrophiles

Weerapana, E., Simon, G. M., & Cravatt, B. F. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.91 · Cited by 246 · see citing works

Reactivity and Ionization of the Active Site Cysteine Residues of DsbA, a Protein Required for Disulfide Bond Formation in vivo

Nelson, J. W., & Creighton, T. E. (1994) · Biochemistry · doi:10.1021/bi00185a039 · Cited by 242 · see citing works

The fairytale of the GSSG/GSH redox potential

Flohé, L. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.10.020 · Cited by 239 · see citing works

Rates of thiol-disulfide interchange reactions between mono- and dithiols and Ellman's reagent

Whitesides, G. M., Lilburn, J., & Szajewski, R. P. (1977) · The Journal of Organic Chemistry · doi:10.1021/jo00422a034 · Cited by 236 · see citing works

Mechanistic and Kinetic Details of Catalysis of Thiol-Disulfide Exchange by Glutaredoxins and Potential Mechanisms of Regulation

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

The peroxidase and peroxynitrite reductase activity of human erythrocyte peroxiredoxin 2

Manta, B., Hugo, M., Ortíz, C., Ferrer‐Sueta, G., Trujillo, M., & Denicola, A. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.11.017 · Cited by 213 · see citing works

Peroxide-Sensing Transcriptional Regulators in Bacteria

Dubbs, J. M., & Mongkolsuk, S. (2012) · Journal of Bacteriology · doi:10.1128/jb.00304-12 · Cited by 207 · see citing works

Novel Regulators in Photosynthetic Redox Control of Plant Metabolism and Gene Expression

Dietz, K., & Pfannschmidt, T. (2010) · PLANT PHYSIOLOGY · doi:10.1104/pp.110.170043 · Cited by 206 · see citing works

Glutathione analogs in prokaryotes.

Fahey, R. C. (2013) · Biochimica et Biophysica Acta · doi:10.1016/j.bbagen.2012.10.006 · Cited by 205 · see citing works

The Genomics of Disulfide Bonding and Protein Stabilization in Thermophiles

Beeby, M., O’Connor, B. D., Ryttersgaard, C., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030309 · Cited by 201 · see citing works

Analysis of the Link between Enzymatic Activity and Oligomeric State in AhpC, a Bacterial Peroxiredoxin,

Parsonage, D., Youngblood, D. S., Sarma, G. N., Wood, Z. A., Karplus, P. A., & Poole, L. B. (2005) · Biochemistry · doi:10.1021/bi050448i · Cited by 201 · see citing works

Reactions of yeast thioredoxin peroxidases I and II with hydrogen peroxide and peroxynitrite: Rate constants by competitive kinetics

Ogusucu, R., Rettori, D., Munhoz, D. C., Netto, L. E. S., & Augusto, O. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.10.042 · Cited by 196 · see citing works

Structural Evidence that Peroxiredoxin Catalytic Power Is Based on Transition-State Stabilization

Hall, A., Parsonage, D., Poole, L. B., & Karplus, P. A. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.07.022 · Cited by 195 · see citing works

Effects of Buried Charged Groups on Cysteine Thiol Ionization and Reactivity in Escherichia coli Thioredoxin: Structural and Functional Characterization of Mutants of Asp 26 and Lys 57

Dyson, H. J., Jeng, M., Tennant, L. L., et al. (1997) · Biochemistry · doi:10.1021/bi961801a · Cited by 194 · see citing works

High-Throughput Identification of Catalytic Redox-Active Cysteine Residues

Fomenko, D. E., Xing, W., Adair, B. M., Thomas, D. J., & Gladyshev, V. N. (2007) · Science · doi:10.1126/science.1133114 · Cited by 187 · see citing works

Thiol peroxidases mediate specific genome-wide regulation of gene expression in response to hydrogen peroxide

Fomenko, D. E., Koç, A., Agisheva, N., Jacobsen, M. T., Kaya, A., Malinouski, M., Rutherford, J. C., Siu, K., Jin, D., Winge, D. R., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010721108 · Cited by 187 · see citing works

Introduction to organic chemistry

Lazonby, J. N. (1975) · Medical Entomology and Zoology · Cited by 184 · see citing works

The Inactivation of the Acyl Phosphatase Activity Catalyzed by the Sulfenic Acid Form of Glyceraldehyde 3-Phosphate Dehydrogenase by Dimedone and Olefins

Benitez, L. V., & Allison, W. S. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42244-8 · Cited by 179 · see citing works

Poplar Peroxiredoxin Q. A Thioredoxin-Linked Chloroplast Antioxidant Functional in Pathogen Defense

Rouhier, N., Gelhaye, É., Gualberto, J. M., et al. (2004) · PLANT PHYSIOLOGY · doi:10.1104/pp.103.035865 · Cited by 177 · see citing works

A Model of Redox Kinetics Implicates the Thiol Proteome in Cellular Hydrogen Peroxide Responses

Adimora, N. J., Jones, D. P., & Kemp, M. L. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2968 · Cited by 175 · see citing works

Characterization of Escherichia coli thioredoxin variants mimicking the active‐sites of other thiol/disulfide oxidoreductases

Mössner, E., Huber‐Wunderlich, M., & Glockshuber, R. (1998) · Protein Science · doi:10.1002/pro.5560070519 · Cited by 174 · see citing works

Chemical ‘omics’ approaches for understanding protein cysteine oxidation in biology

Leonard, S. E., & Carroll, K. S. (2010) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2010.11.012 · Cited by 172 · see citing works

The Saccharomyces cerevisiae Proteome of Oxidized Protein Thiols

Le Moan, N., Clement, G., Le Maout, S., Tacnet, F., & Toledano, M. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513346200 · Cited by 170 · see citing works

Quantitative In Vivo Redox Sensors Uncover Oxidative Stress as an Early Event in Life

Knoefler, D., Thamsen, M., Koniczek, M., Niemuth, N. J., Diederich, A.-K., & Jakob, U. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.06.016 · Cited by 169 · see citing works

Catalytic Mechanism of Thiol Peroxidase from Escherichia coli

Baker, L. M. S., & Poole, L. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209888200 · Cited by 165 · see citing works

Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin

Parsonage, D., Karplus, P. A., & Poole, L. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708308105 · Cited by 164 · see citing works

Microscopic pKa Values of Escherichia coli Thioredoxin

Chivers, P. T., Prehoda, K. E., Volkman, B. F., et al. (1997) · Biochemistry · doi:10.1021/bi970071j · Cited by 162 · see citing works

Hyperoxidation of Peroxiredoxins 2 and 3

Peskin, A. V., Dickerhof, N., Poynton, R. A., Paton, L. N., Pace, P., Hampton, M. B., & Winterbourn, C. C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.460881 · Cited by 160 · see citing works

Structure in Protein Chemistry

Kyte, J. (2006) · Garland Science eBooks · doi:10.4324/9780203833469 · Cited by 159 · see citing works

Low-Molecular-Weight Thiols in Thiol–Disulfide Exchange

Laer, K. V., Hamilton, C. J., & Messens, J. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4964 · Cited by 159 · see citing works

The Dual Functions of Thiol-Based Peroxidases in H 2 O 2 Scavenging and Signaling

Fourquet, S., Huang, M., D’Autréaux, B., & Tolédano, M. B. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2049 · Cited by 157 · see citing works

Post‐translational modification is essential for catalytic activity of nitrile hydratase

Murakami, T., Nojiri, M., Nakayama, H., Dohmae, N., Takio, K., Odaka, M., Endo, I., Nagamune, T., & Yohda, M. (2000) · Protein Science · doi:10.1110/ps.9.5.1024 · Cited by 156 · see citing works

Peroxide Stress Elicits Adaptive Changes in Bacterial Metal Ion Homeostasis

Faulkner, M. J., & Helmann, J. D. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3682 · Cited by 151 · see citing works

Cytosolic and Nuclear Protein Targets of Thiol-Reactive Electrophiles

Dennehy, M. K., Richards, K. A. M., Wernke, G. R., Shyr, Y., & Liebler, D. C. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050312l · Cited by 150 · see citing works

Oxidative protein folding: From thiol–disulfide exchange reactions to the redox poise of the endoplasmic reticulum

Hudson, D. A., Gannon, S. A., & Thorpe, C. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.07.037 · Cited by 149 · see citing works

Global Analysis of Protein Damage by the Lipid Electrophile 4-Hydroxy-2-nonenal

Codreanu, S. G., Zhang, B., Sobecki, S. M., Billheimer, D. D., & Liebler, D. C. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800070-mcp200 · Cited by 146 · see citing works

Structure-reactivity correlations for the thiol-disulfide interchange reaction

Wilson, J. M., Bayer, R. J., & HUPE, D. J. (1977) · Journal of the American Chemical Society · doi:10.1021/ja00466a027 · Cited by 141 · see citing works

Structural, redox, and mechanistic parameters for cysteine-sulfenic acid function in catalysis and regulation

Claiborne, A., Mallett, T. C., Yeh, J. I., Luba, J. P., & Parsonage, D. (2001) · Advances in protein chemistry · doi:10.1016/s0065-3233(01)58006-7 · Cited by 139 · see citing works

AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase

Poole, L. B., Reynolds, C. M., Wood, Z. A., Karplus, P. A., Ellis, H. R., & Calzi, M. L. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01704.x · Cited by 134 · see citing works

Redox Chemistry of Biological Thiols

Nagy, P., & Winterbourn, C. C. (2010) · Advances in molecular toxicology · doi:10.1016/s1872-0854(10)04006-3 · Cited by 125 · see citing works

Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid

Salsbury, F. R., Knutson, S. T., Poole, L. B., & Fetrow, J. S. (2008) · Protein Science · doi:10.1110/ps.073096508 · Cited by 125 · see citing works

Electrostatic Interactions in the Active Site of the N-Terminal Thioredoxin-like Domain of Protein Disulfide Isomerase

Kortemme, T., Darby, N. J., & Creighton, T. E. (1996) · Biochemistry · doi:10.1021/bi9617724 · Cited by 120 · see citing works

Using Quantitative Redox Proteomics to Dissect the Yeast Redoxome

Brandes, N., Reichmann, D., Tienson, H. L., Leichert, L. I. O., & Jakob, U. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.296236 · Cited by 116 · see citing works

Thiol‐blocking electrophiles interfere with labeling and detection of protein sulfenic acids

Reisz, J. A., Bechtold, E., King, S. B., et al. (2013) · FEBS Journal · doi:10.1111/febs.12535 · Cited by 115 · see citing works

Both Thioredoxin 2 and Glutaredoxin 2 Contribute to the Reduction of the Mitochondrial 2-Cys Peroxiredoxin Prx3

Hanschmann, E.-M., Lönn, M. E., Schütte, L. D., Funke, M., Godoy, J. R., Eitner, S., Hudemann, C., & Lillig, C. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.185827 · Cited by 112 · see citing works

Thiol and Sulfenic Acid Oxidation of AhpE, the One-Cysteine Peroxiredoxin from Mycobacterium tuberculosis: Kinetics, Acidity Constants, and Conformational Dynamics

Hugo, M., Turell, L., Manta, B., Botti, H., Monteiro, G., Netto, L. E. S., Álvarez, B., Radí, R., & Trujillo, M. (2009) · Biochemistry · doi:10.1021/bi901221s · Cited by 109 · see citing works

The Non-flavin Redox Center of the Streptococcal NADH Peroxidase

Poole, L. B., & Claiborne, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63862-1 · Cited by 107 · see citing works

Cysteine p K a Values for the Bacterial Peroxiredoxin AhpC

Nelson, K. J., Parsonage, D., Hall, A., et al. (2008) · Biochemistry · doi:10.1021/bi801718d · Cited by 107 · see citing works

Proteomic approaches to the characterization of protein thiol modification

Chouchani, E. T., James, A. M., Fearnley, I. M., Lilley, K. S., & Murphy, M. P. (2010) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2010.11.003 · Cited by 106 · see citing works

Mechanism in Protein Chemistry

Kyte, J. (2024) · Garland Science eBooks · doi:10.1201/9781003573456 · Cited by 99 · see citing works

Integrated Redox Proteomics and Metabolomics of Mitochondria to Identify Mechanisms of Cd Toxicity

Go, Y., Roede, J. R., Orr, M. C., Liang, Y., & Jones, D. P. (2014) · Toxicological Sciences · doi:10.1093/toxsci/kfu018 · Cited by 98 · see citing works

Changing Paradigms in Thiology

Flohé, L. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)73001-9 · Cited by 96 · see citing works

Selective Targeting of the Cysteine Proteome by Thioredoxin and Glutathione Redox Systems

Go, Y., Roede, J. R., Walker, D. I., Duong, D. M., Seyfried, N. T., Orr, M. L., Liang, Y., Pennell, K. D., & Jones, D. P. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.030437 · Cited by 93 · see citing works

Lactoperoxidase: structural insights into the function,ligand binding and inhibition.

Sharma, S. P., Singh, A. K., Kaushik, S., Sinha, M., Singh, R. P., Sharma, P. K., Sirohi, H., Kaur, P., & Singh, T. P. (2013) · Europe PMC (PubMed Central) · Cited by 92 · see citing works

Thioredoxin and glutaredoxin-mediated redox regulation of ribonucleotide reductase

Sengupta, R. (2014) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v5.i1.68 · Cited by 90 · see citing works

Crystal Structures of the Reduced, Sulfenic Acid, and Mixed Disulfide Forms of SarZ, a Redox Active Global Regulator in Staphylococcus aureus

Poor, C. B., Chen, P. R., Duguid, E. M., Rice, P. A., & He, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.015826 · Cited by 89 · see citing works

Chemical approaches to detect and analyze protein sulfenic acids

Furdui, C. M., & Poole, L. B. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21384 · Cited by 85 · see citing works

Nox4- and Nox2-dependent oxidant production is required for VEGF-induced SERCA cysteine-674 S-glutathiolation and endothelial cell migration

Evangelista, A. M., Thompson, M. D., Bolotina, V. M., Tong, X., & Cohen, R. A. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.546 · Cited by 78 · see citing works

Glutathione Adducts on Sarcoplasmic/Endoplasmic Reticulum Ca2+ ATPase Cys-674 Regulate Endothelial Cell Calcium Stores and Angiogenic Function as Well as Promote Ischemic Blood Flow Recovery

Thompson, M. D., Mei, Y., Weisbrod, R. M., Silver, M., Shukla, P. C., Bolotina, V. M., Cohen, R. A., & Tong, X. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.554451 · Cited by 70 · see citing works

Mass spectrometry in studies of protein thiol chemistry and signaling: Opportunities and caveats

Devarie‐Baez, N. O., Reisz, J. A., & Furdui, C. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.09.016 · Cited by 64 · see citing works

Oxidative stress sensing by the iron–sulfur cluster in the transcription factor, SoxR

Kobayashi, K., Fujikawa, M., & Kozawa, T. (2013) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2013.11.008 · Cited by 63 · see citing works

Localized cysteine sulfenic acid formation by vascular endothelial growth factor: role in endothelial cell migration and angiogenesis

Kaplan, N., Urao, N., Furuta, E., Kim, S.-J., Razvi, M., Nakamura, Y., McKinney, R. D., Poole, L. B., Fukai, T., & Ushio‐Fukai, M. (2011) · Free Radical Research · doi:10.3109/10715762.2011.602073 · Cited by 63 · see citing works

Structural Basis for the Retroreduction of Inactivated Peroxiredoxins by Human Sulfiredoxin,

Jönsson, T. J., Murray, M. S., Johnson, L. C., Poole, L. B., & Lowther, W. T. (2005) · Biochemistry · doi:10.1021/bi050131i · Cited by 60 · see citing works

Structure in protein chemistry

Wood, E. (1996) · Biochemical Education · doi:10.1016/s0307-4412(96)80028-8 · Cited by 56 · see citing works

Kinetic and Thermodynamic Features Reveal That Escherichia coli BCP Is an Unusually Versatile Peroxiredoxin

Reeves, S. A., Parsonage, D., Nelson, K. J., & Poole, L. B. (2011) · Biochemistry · doi:10.1021/bi200935d · Cited by 53 · see citing works

An NADH-Dependent Bacterial Thioredoxin Reductase-like Protein in Conjunction with a Glutaredoxin Homologue Form a Unique Peroxiredoxin (AhpC) Reducing System in Clostridium pasteurianum

Reynolds, C. M., Meyer, J., & Poole, L. B. (2002) · Biochemistry · doi:10.1021/bi011802p · Cited by 53 · see citing works

Endosomal H2O2 production leads to localized cysteine sulfenic acid formation on proteins during lysophosphatidic acid-mediated cell signaling

Klomsiri, C., Rogers, L. C., Soito, L., McCauley, A. K., King, S. B., Nelson, K. J., Poole, L. B., & Daniel, L. W. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.017 · Cited by 49 · see citing works

Biosynthesis of the methanogenic cofactors

White, R. H. (2001) · Vitamins and hormones · doi:10.1016/s0083-6729(01)61010-0 · Cited by 48 · see citing works

Mildly oxidized GAPDH: the coupling of the dehydrogenase and acyl phosphatase activities

Schmalhausen, E. V., Nagradova, N. K., Boschi‐Müller, S., et al. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00627-4 · Cited by 44 · see citing works

Structural Basis for Catalytic Activation of Thiocyanate Hydrolase Involving Metal-Ligated Cysteine Modification

Arakawa, T., Kawano, Y., Katayama, Y., Nakayama, H., Dohmae, N., Yohda, M., & Odaka, M. (2009) · Journal of the American Chemical Society · doi:10.1021/ja903979s · Cited by 44 · see citing works

Influence of Acidic Residues and the Kink in the Active-site Helix on the Properties of the Disulfide Oxidoreductase DsbA

Hennecke, J., Spleiss, C., & Glockshuber, R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.189 · Cited by 42 · see citing works

Characterization by tandem mass spectrometry of stable cysteine sulfenic acid in a cysteine switch peptide of matrix metalloproteinases

Shetty, V., Spellman, D. S., & Neubert, T. A. (2007) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2007.05.013 · Cited by 41 · see citing works

Broad Phenotypic Changes Associated with Gain of Radiation Resistance in Head and Neck Squamous Cell Cancer

Bansal, N., Mims, J., Kuremsky, J. G., Olex, A. L., Zhao, W., Yin, L.-M., Wani, R., Qian, J. X., Marrs, G. S., Porosnicu, M., et al. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5690 · Cited by 40 · see citing works

Oxidation of 2-Cys-peroxiredoxins by Arachidonic Acid Peroxide Metabolites of Lipoxygenases and Cyclooxygenase-2

Cordray, P., Doyle, K. J., Edes, K., Moos, P. J., & Fitzpatrick, F. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704369200 · Cited by 37 · see citing works

Forgotten Radicals in Biology

Laboratoire De Physiopathologie Et Pharmacologie Cardiovasculaires Experimentales, F. D. M. E. P., Vergely, C., & Luc, R. (2008) · International Journal of Biomedical Science · doi:10.59566/ijbs.2008.4255 · Cited by 33 · see citing works

Analysis of the Kinetic Mechanism of Enterococcal NADH Peroxidase Reveals Catalytic Roles for NADH Complexes with both Oxidized and Two-Electron-Reduced Enzyme Forms

Crane, E. J., Parsonage, D., Poole, L. B., et al. (1995) · Biochemistry · doi:10.1021/bi00043a016 · Cited by 32 · see citing works

Forgotten radicals in biology.

Rochette, L., & Vergely, C. (2008) · Europe PMC (PubMed Central) · Cited by 27 · see citing works

Studies on the enhancement of the reactivity of the (Cys-25)-S-/(His159)-Im+H ion-pair of papain by deprotonation across pKa 4

Pinitglang, S., Noble, M., Verma, C. S., Thomas, E. W., & Brocklehurst, K. (1996) · Biochemical Society Transactions · doi:10.1042/bst024468s · Cited by 8 · see citing works

Reactive oxygen species (ROS) as pleiotropic physiological signalling agents

Sies, H., & Jones, D. P. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0230-3 · Cited by 5,335 · see citing works

Oxidative Stress

Sies, H., Berndt, C., & Jones, D. P. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045037 · Cited by 3,520 · see citing works

Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging

Jomova, K., Raptova, R., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03562-9 · Cited by 2,638 · see citing works

Hydrogen peroxide as a central redox signaling molecule in physiological oxidative stress: Oxidative eustress

Sies, H. (2017) · Redox Biology · doi:10.1016/j.redox.2016.12.035 · Cited by 2,148 · see citing works

Functions of ROS in Macrophages and Antimicrobial Immunity

Herb, M., & Schramm, M. (2021) · Antioxidants · doi:10.3390/antiox10020313 · Cited by 633 · see citing works

ROS in Cancer: The Burning Question

Chio, I. I. C., & Tuveson, D. A. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.03.004 · Cited by 532 · see citing works

Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases

Kehm, R., Baldensperger, T., Raupbach, J., & Höhn, A. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101901 · Cited by 348 · see citing works

Prebiotic synthesis of cysteine peptides that catalyze peptide ligation in neutral water

Foden, C. S., Islam, S., Fernández-García, C., Maugeri, L., Sheppard, T. D., & Powner, M. W. (2020) · Science · doi:10.1126/science.abd5680 · Cited by 205 · see citing works

The phagocyte NOX2 NADPH oxidase in microbial killing and cell signaling

Nauseef, W. M. (2019) · Current Opinion in Immunology · doi:10.1016/j.coi.2019.05.006 · Cited by 188 · see citing works

Signaling and stress: The redox landscape in NOS2 biology

Thomas, D. D., Heinecke, J. L., Ridnour, L. A., Cheng, R. Y., Kesarwala, A. H., Switzer, C. H., McVicar, D. W., Roberts, D. D., Glynn, S., Fukuto, J. M., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.002 · Cited by 150 · see citing works

Fragment-based covalent ligand discovery

Lu, W., Kostic, M., Zhang, T., Che, J., Patricelli, M. P., Jones, L. H., Chouchani, E. T., & Gray, N. S. (2021) · RSC Chemical Biology · doi:10.1039/d0cb00222d · Cited by 136 · see citing works

The 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

The basic chemistry of exercise-induced DNA oxidation: oxidative damage, redox signaling, and their interplay

Cobley, J. N., Margaritelis, N. V., Morton, J. P., Close, G. L., Nikolaidis, M. G., & Malone, J. K. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00182 · Cited by 43 · see citing works

Curcumin induces secretion of glucagon-like peptide-1 through an oxidation-dependent mechanism

Alli-Oluwafuyi, A.-M., Luis, P. B., Nakashima, F., Giménez-Bastida, J. A., Presley, S. H., Duvernay, M. T., Iwalewa, E. O., & Schneider, C. (2019) · Biochimie · doi:10.1016/j.biochi.2019.08.013 · Cited by 28 · see citing works

Methionine oxidation products as biomarkers of oxidative damage to proteins and modulators of cellular metabolism and toxicity

Davies, M. J. (2025) · Redox Biochemistry and Chemistry · doi:10.1016/j.rbc.2025.100052 · Cited by 11 · see citing works

A hemicyanine complex for the detection of thiol biomolecules by fluorescence

Nhan, D. T., Hien, N. K., Đức, H. V., et al. (2016) · Dyes and Pigments · doi:10.1016/j.dyepig.2016.03.050 · Cited by 21 · see citing works

A novel pathway for formation of thiol metabolites and cysteine conjugates from cysteine conjugate sulphoxides

Tomisawa, H., Hayashi, M., Fukushima, M., et al. (1993) · Biochemical Pharmacology · doi:10.1016/0006-2952(93)90457-8 · Cited by 5 · see citing works

The Reactivity of Silylsulfides with Disulfides: A New Aspect of the Thiol-Disulfide Interchange

Capozzi, G., Menichetti, S., & Rosi, A. (1993) · Phosphorus, sulfur, and silicon and the related elements · doi:10.1080/10426509308038124 · Cited by 1 · see citing works

Colorimetric detection of thiol-containing amino acids using gold nanoparticles

Zhang, F. X., Han, L., Israel, L. B., et al. (2002) · The Analyst · doi:10.1039/b200007e · Cited by 190 · see citing works

[45] Affinity chromatography of cysteine peptidases

Buttle, D. J. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(94)44047-6 · Cited by 7 · see citing works