Site-Specific Proteomic Mapping Identifies Selectively Modified Regulatory Cysteine Residues in Functionally Distinct Protein Networks

Structure, mechanism and regulation of peroxiredoxins

Wood, Z. A., Schröder, E., Harris, J. R., & Poole, L. B. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)00003-8 · Cited by 2,546

Signal transduction by reactive oxygen species

Finkel, T. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201102095 · Cited by 2,322

A tissue-specific atlas of mouse protein phosphorylation and expression

Huttlin, E. L., Jedrychowski, M. P., Elias, J. E., Goswami, T., Rad, R., Beausoleil, S. A., Villén, J., Haas, W., Sowa, M. E., & Gygi, S. P. (2010) · Cell · doi:10.1016/j.cell.2010.12.001 · Cited by 1,778

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

Specific and Reversible Inactivation of Protein Tyrosine Phosphatases by Hydrogen Peroxide: Evidence for a Sulfenic Acid Intermediate and Implications for Redox Regulation

Denu, J. M., & Tanner, K. G. (1998) · Biochemistry · doi:10.1021/bi973035t · Cited by 945

Hydrogen Sulfide-Linked Sulfhydration of NF-κB Mediates Its Antiapoptotic Actions

Sen, N., Paul, B. D., Gadalla, M. M., Mustafa, A. K., Sen, T., Xu, R., Kim, S., & Snyder, S. H. (2012) · Molecular Cell · doi:10.1016/j.molcel.2011.10.021 · Cited by 733

SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function

Krüger, M., Moser, M., Ussar, S., Thievessen, I., Luber, C. A., Forner, F., Schmidt, S., Zanivan, S., Fässler, R., & Mann, M. (2008) · Cell · doi:10.1016/j.cell.2008.05.033 · Cited by 680

Integrated proteomic analysis of post-translational modifications by serial enrichment

Mertins, P., Qiao, J., Patel, J., Udeshi, N. D., Clauser, K. R., Mani, D. R., Burgess, M. W., Gillette, M. A., Jaffe, J. D., & Carr, S. A. (2013) · Nature Methods · doi:10.1038/nmeth.2518 · Cited by 619

Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I

Chouchani, E. T., Methner, C., Nadtochiy, S. M., Logan, A., Pell, V. R., Ding, S., James, A. M., Cochemé, H. M., Reinhold, J., Lilley, K. S., et al. (2013) · Nature Medicine · doi:10.1038/nm.3212 · Cited by 619 · cited 1×

S-glutathionylation in protein redox regulation

Dalle‐Donne, I., Rossi, R., Giustarini, D., Colombo, R., & Milzani, A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.06.014 · Cited by 506

Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation

Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541

Sulfhydryl groups as targets of mercury toxicity

Ajsuvakova, O. P., Tinkov, A. A., Aschner, M., da Rocha, J. B. T., Michalke, B., Геннадиевна, С. М., Skalny, A. V., Butnariu, M., Dadar, M., Sărac, I., et al. (2020) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2020.213343 · Cited by 384

Protein S-Nitrosylation: Determinants of Specificity and Enzymatic Regulation of S-Nitrosothiol-Based Signaling

Stomberski, C. T., Hess, D. T., & Stamler, J. S. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7403 · Cited by 297

Chemical proteomics reveals new targets of cysteine sulfinic acid reductase

Akter, S., Fu, L., Jung, Y., Conte, M. L., Lawson, J. R., Lowther, W. T., Sun, R., Liu, K., Yang, J. H., & Carroll, K. S. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0116-2 · Cited by 235

Cysteine Sulfenylation Directs IRE-1 to Activate the SKN-1/Nrf2 Antioxidant Response

Hourihan, J. M., Mazzeo, L. E. M., Fernández-Cárdenas, L. P., & Blackwell, T. K. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.07.019 · Cited by 209

Cysteine Oxidation in Proteins: Structure, Biophysics, and Simulation

Ruiz, D. G., Sandoval‐Pérez, A., Rangarajan, A. V., Gunderson, E. L., & Jacobson, M. P. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00349 · Cited by 171

Dynamic Protein Acylation: New Substrates, Mechanisms, and Drug Targets

Lanyon‐Hogg, T., Faronato, M., Serwa, R. A., & Tate, E. W. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.04.004 · Cited by 149

Hsp70 in Redox Homeostasis

Zhang, H., Gong, W., Wu, S., & Perrett, S. (2022) · Cells · doi:10.3390/cells11050829 · Cited by 145

Molecular Basis for Redox Activation of Epidermal Growth Factor Receptor Kinase

Truong, T. H., Ung, P. M. U., Palde, P. B., Paulsen, C. E., Schlessinger, A., & Carroll, K. S. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.05.017 · Cited by 142

Protein S-glutathionlyation links energy metabolism to redox signaling in mitochondria

Mailloux, R. J., & Treberg, J. R. (2015) · Redox Biology · doi:10.1016/j.redox.2015.12.010 · Cited by 137

Redox Homeostasis in Photosynthetic Organisms: Novel and Established Thiol-Based Molecular Mechanisms

Zaffagnini, M., Fermani, S., Marchand, C. H., Costa, A., Sparla, F., Rouhier, N., Geigenberger, P., Lemaire, S. D., & Trost, P. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7617 · Cited by 133

KEAP1, a cysteine-based sensor and a drug target for the prevention and treatment of chronic disease

Naidu, S. D., & Dinkova‐Kostova, A. T. (2020) · Open Biology · doi:10.1098/rsob.200105 · Cited by 135

Diverse Redoxome Reactivity Profiles of Carbon Nucleophiles

Gupta, V., Yang, J. H., Liebler, D. C., & Carroll, K. S. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b01791 · Cited by 124

SPalmitoylC-PseAAC: A sequence-based model developed via Chou's 5-steps rule and general PseAAC for identifying S-palmitoylation sites in proteins

Hussain, W., Khan, Y. D., Rasool, N., Khan, S. A., & Chou, K. (2018) · Analytical Biochemistry · doi:10.1016/j.ab.2018.12.019 · Cited by 122

Oxidants, Antioxidants and Thiol Redox Switches in the Control of Regulated Cell Death Pathways

Benhar, M. (2020) · Antioxidants · doi:10.3390/antiox9040309 · Cited by 122

Non-enzymatic N-acetylation of lysine residues by acetylCoA often occurs via a proximal S-acetylated thiol intermediate sensitive to glyoxalase II

James, A. M., Hoogewijs, K., Logan, A., Hall, A. R., Ding, S., Fearnley, I. M., & Murphy, M. P. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.018 · Cited by 112

The Deep Thioredoxome in Chlamydomonas reinhardtii: New Insights into Redox Regulation

Pérez‐Pérez, M. E., Mauriès, A., Maes, A., Tourasse, N. J., Hamon, M., Lemaire, S. D., & Marchand, C. H. (2017) · Molecular Plant · doi:10.1016/j.molp.2017.07.009 · Cited by 110

The molecular era of protein S-acylation: spotlight on structure, mechanisms, and dynamics

Zaballa, M.-E., & van der Goot, F. G. (2018) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2018.1488804 · Cited by 109

Exercise redox biochemistry: Conceptual, methodological and technical recommendations

Cobley, J. N., Close, G. L., Bailey, D. M., & Davison, G. W. (2017) · Redox Biology · doi:10.1016/j.redox.2017.03.022 · Cited by 103

Going retro: Oxidative stress biomarkers in modern redox biology

Margaritelis, N. V., Cobley, J. N., Paschalis, V., Veskoukis, A. S., Theodorou, A. A., Kyparos, A., & Nikolaidis, M. G. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.02.005 · Cited by 84

Redox Systems Biology: Harnessing the Sentinels of the Cysteine Redoxome

Held, J. M. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7725 · Cited by 78

A global view of the human post-translational modification landscape

Kitamura, N., & Galligan, J. J. (2023) · Biochemical Journal · doi:10.1042/bcj20220251 · Cited by 81

Nitrosothiol formation and S-nitrosation signaling through nitric oxide synthases

Wynia‐Smith, S. L., & Smith, B. C. (2016) · Nitric Oxide · doi:10.1016/j.niox.2016.10.001 · Cited by 74

Principles for integrating reactive species into in vivo biological processes: Examples from exercise physiology

Margaritelis, N. V., Cobley, J. N., Paschalis, V., Veskoukis, A. S., Theodorou, A. A., Kyparos, A., & Nikolaidis, M. G. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.12.011 · Cited by 74

Spatial and temporal alterations in protein structure by EGF regulate cryptic cysteine oxidation

Behring, J. B., van der Post, S., Mooradian, A. D., Egan, M. J., Zimmerman, M. I., Clements, J. L., Bowman, G. R., & Held, J. M. (2020) · Science Signaling · doi:10.1126/scisignal.aay7315 · Cited by 69

Quantitative proteomic characterization of redox-dependent post-translational modifications on protein cysteines

Duan, J., Gaffrey, M. J., & Qian, W. (2017) · Molecular BioSystems · doi:10.1039/c6mb00861e · Cited by 71

Redox signaling in innate immunity and inflammation: focus on macrophages and neutrophils

Braunstein, I., Motohashi, H., Dallenga, T. K., Schaible, U. E., & Benhar, M. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.06.006 · Cited by 75

Global profiling of phosphorylation-dependent changes in cysteine reactivity

Kemper, E. K., Zhang, Y., Dix, M. M., & Cravatt, B. F. (2022) · Nature Methods · doi:10.1038/s41592-022-01398-2 · Cited by 61

Thiol-Based Redox Modulation of Soluble Guanylyl Cyclase, the Nitric Oxide Receptor

Beuve, A. V. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6591 · Cited by 61

Stress-induced Changes in the S-palmitoylation and S-nitrosylation of Synaptic Proteins*[S]

Zaręba-Kozioł, M., Bartkowiak-Kaczmarek, A., Figiel, I., Krzystyniak, A., Wójtowicz, T., Bijata, M., & Włodarczyk, J. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra119.001581 · Cited by 59

How widespread is stable protein S-nitrosylation as an end-effector of protein regulation?

Wolhuter, K., & Eaton, P. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.02.013 · Cited by 55

Exercise and Glycemic Control: Focus on Redox Homeostasis and Redox-Sensitive Protein Signaling

Parker, L., Shaw, C. S., Stepto, N. K., & Levinger, I. (2017) · Frontiers in Endocrinology · doi:10.3389/fendo.2017.00087 · Cited by 55

Mechanisms of Mitochondrial ROS Production in Assisted Reproduction: The Known, the Unknown, and the Intriguing

Cobley, J. N. (2020) · Antioxidants · doi:10.3390/antiox9100933 · Cited by 57

Stochiometric quantification of the thiol redox proteome of macrophages reveals subcellular compartmentalization and susceptibility to oxidative perturbations

Duan, J., Zhang, T., Gaffrey, M. J., Weitz, K., Moore, R., Li, X., Xian, M., Thrall, B. D., & Qian, W. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101649 · Cited by 53

Reactivity, Selectivity, and Stability in Sulfenic Acid Detection: A Comparative Study of Nucleophilic and Electrophilic Probes

Gupta, V., Paritala, H., & Carroll, K. S. (2016) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.6b00181 · Cited by 53

Systems Biology Approaches to Redox Metabolism in Stress and Disease States

Wang, R., Oldham, W. M., Maron, B. A., & Loscalzo, J. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7256 · Cited by 48

Proteome-Scale Analysis of Protein S-Acylation Comes of Age

Wang, Y., & Yang, W. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00409 · Cited by 46

Oxidative Stress in Preterm Infants: Overview of Current Evidence and Future Prospects

Falsaperla, R., Lombardo, F., Filosco, F., Romano, C., Saporito, M. A. N., Puglisi, F., Piro, E., Ruggieri, M., & Pavone, P. (2020) · Pharmaceuticals · doi:10.3390/ph13070145 · Cited by 44

Chemoproteomic Strategy to Quantitatively Monitor Transnitrosation Uncovers Functionally Relevant S -Nitrosation Sites on Cathepsin D and HADH2

Zhou, Y., Wynia‐Smith, S. L., Couvertier, S. M., Kalous, K., Marletta, M. A., Smith, B. C., & Weerapana, E. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.05.008 · Cited by 42

Proteomics of the heart

Karpov, O. A., Stotland, A. B., Raedschelders, K., Chazarin, B., Ai, L., Murray, C. I., & Eyk, J. E. V. (2024) · Physiological Reviews · doi:10.1152/physrev.00026.2023 · Cited by 43

DHHC5 Mediates β-Adrenergic Signaling in Cardiomyocytes by Targeting Gα Proteins

Chen, J. J., Marsden, A. N., Scott, C. A., Akimzhanov, A. M., & Boehning, D. F. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.08.018 · Cited by 42

Cy-preds: An algorithm and a web service for the analysis and prediction of cysteine reactivity

Soylu, İ., & Marino, S. M. (2015) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24978 · Cited by 41

Computational Structural Biology of S-nitrosylation of Cancer Targets

Bignon, E., Allega, M. F., Lucchetta, M., Tiberti, M., & Papaleo, E. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00272 · Cited by 39

The Cys Sense: Thiol Redox Switches Mediate Life Cycles of Cellular Proteins

Radzinski, M., Oppenheim, T., Metanis, N., & Reichmann, D. (2021) · Biomolecules · doi:10.3390/biom11030469 · Cited by 38

MDD-Palm: Identification of protein S-palmitoylation sites with substrate motifs based on maximal dependence decomposition

Weng, S., Kao, H.-J., Huang, C., & Lee, T.-Y. (2017) · PLoS ONE · doi:10.1371/journal.pone.0179529 · Cited by 39

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 40

Redox Post-translational Modifications of Protein Thiols in Brain Aging and Neurodegenerative Conditions—Focus on S-Nitrosation

Finelli, M. J. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00254 · Cited by 38

Proximal Cysteines that Enhance Lysine N-Acetylation of Cytosolic Proteins in Mice Are Less Conserved in Longer-Living Species

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

Thioredoxin and glutaredoxin regulate metabolism through different multiplex thiol switches

López-Grueso, M. J., González, R., Requejo-Aguilar, R., McDonagh, B., Fuentes-Almagro, C. A., Muntané, J., Bárcena, J. A., & Padilla, C. A. (2018) · Redox Biology · doi:10.1016/j.redox.2018.11.007 · Cited by 37

Pinpointing cysteine oxidation sites by high-resolution proteomics reveals a mechanism of redox-dependent inhibition of human STING

Cuervo, N. Z., Fortin, A., Caron, E., Chartier, S., & Grandvaux, N. (2021) · Science Signaling · doi:10.1126/scisignal.aaw4673 · Cited by 36

Mitoproteomics: Tackling Mitochondrial Dysfunction in Human Disease

Gómez‐Serrano, M., Camafeita, E., Loureiro, M., & Peral, B. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1435934 · Cited by 38

Redox regulation of proteostasis

Duy, D. L., West, J. D., & Morano, K. A. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107977 · Cited by 39

Oxidative Post-Translational Modifications: A Focus on Cysteine S- Sulfhydration and the Regulation of Endothelial Fitness

Bibli, S., & Fleming, I. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0162 · Cited by 33

Structure/function of the soluble guanylyl cyclase catalytic domain

Childers, K. C., & Garcin, E. D. (2018) · Nitric Oxide · doi:10.1016/j.niox.2018.04.008 · Cited by 34

MinOmics, an Integrative and Immersive Tool for Multi-Omics Analysis

Maes, A., Martinez, X., Druart, K., Laurent, B., Guégan, S., Marchand, C. H., Lemaire, S. D., & Baaden, M. (2018) · Berichte aus der medizinischen Informatik und Bioinformatik/Journal of integrative bioinformatics · doi:10.1515/jib-2018-0006 · Cited by 33

Immunological Techniques to Assess Protein Thiol Redox State: Opportunities, Challenges and Solutions

Cobley, J. N., & Husi, H. (2020) · Antioxidants · doi:10.3390/antiox9040315 · Cited by 33

The redox-responsive roles of intermediate filaments in cellular stress detection, integration and mitigation

Pérez‐Sala, D., & Quinlan, R. A. (2023) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2023.102283 · Cited by 29

Emerging chemistry and biology in protein glutathionylation

Kukulage, D. S. K., Don, N. N. J. M., & Ahn, Y. (2022) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2022.102221 · Cited by 30

Proteomic strategies to unravel age-related redox signalling defects in skeletal muscle

Cobley, J. N., Sakellariou, G. K., Husi, H., & McDonagh, B. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.012 · Cited by 32

Comparative and integrative metabolomics reveal that S-nitrosation inhibits physiologically relevant metabolic enzymes

Bruegger, J. J., Smith, B. C., Wynia-Smith, S. L., & Marletta, M. A. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.817700 · Cited by 27

Regulation of Cell Proliferation and Nrf2-Mediated Antioxidant Defense: Conservation of Keap1 Cysteines and Nrf2 Binding Site in the Context of the Evolution of KLHL Family

Shilovsky, G. A., & Dibrova, D. V. (2023) · Life · doi:10.3390/life13041045 · Cited by 27

Exercise stress leads to an acute loss of mitochondrial proteins and disruption of redox control in skeletal muscle of older subjects: An underlying decrease in resilience with aging?

Pugh, J. N., Stretton, C., McDonagh, B., Brownridge, P., McArdle, A., Jackson, M. J., & Close, G. L. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.10.003 · Cited by 26

Chalcone suppresses tumor growth through NOX4-IRE1α sulfonation-RIDD-miR-23b axis

Kim, H., Lee, H.-Y., Riaz, T. A., Bhattarai, K. R., Chaudhary, M., Ahn, J. H., Jeong, J., Kim, H.-R., & Chae, H. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101853 · Cited by 25

An Isozyme-specific Redox Switch in Human Brain Glycogen Phosphorylase Modulates Its Allosteric Activation by AMP

Mathieu, C., Duval, R., Cocaign, A., Petit, E., Bui, L. C., Haddad, I., Vinh, J., Etchebest, C., Dupret, J., & Rodrigues‐Lima, F. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.757062 · Cited by 24

Features of reactive cysteines discovered through computation: from kinase inhibition to enrichment around protein degrons

Fowler, N. J., Blanford, C. F., de Visser, S. P., & Warwicker, J. (2017) · Scientific Reports · doi:10.1038/s41598-017-15997-z · Cited by 24

Improved integrative analysis of the thiol redox proteome using filter-aided sample preparation

Bonzón‐Kulichenko, E., Camafeita, E., López, J. A., Gómez‐Serrano, M., Jorge, I., Calvo, E., Núñez, E., Trevisán-Herraz, M., Bagwan, N., Bárcena, J. A., et al. (2019) · Journal of Proteomics · doi:10.1016/j.jprot.2019.103624 · Cited by 23

Click chemistry-based thiol redox proteomics reveals significant cysteine reduction induced by chronic ethanol consumption

Harris, P. S., McGinnis, C. D., Michel, C. R., Marentette, J., Reisdorph, R. M., Roede, J. R., & Fritz, K. S. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102792 · Cited by 21

50 shades of oxidative stress: A state-specific cysteine redox pattern hypothesis

Cobley, J. N. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102936 · Cited by 24

Trapping redox partnerships in oxidant-sensitive proteins with a small, thiol-reactive cross-linker

Allan, K. M., Loberg, M. A., Chepngeno, J., Hurtig, J. E., Tripathi, S., Kang, M. G., Allotey, J. K., Widdershins, A., Pilat, J. M., Sizek, H., et al. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.506 · Cited by 23

Endogenous S-nitrosocysteine proteomic inventories identify a core of proteins in heart metabolic pathways

Lau, B., Fazelinia, H., Mohanty, I., Raimo, S., Τενοπούλου, Μ., Doulias, P., & Ischiropoulos, H. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102153 · Cited by 20

ZDHHC9-mediated CD38 palmitoylation stabilizes CD38 expression and promotes pancreatic cancer growth

Guo, H., Lin, Z., Zhang, D., Qin, Q., Li, Z., Yin, Y., Chen, J., & Guo, W. M. (2025) · Communications Biology · doi:10.1038/s42003-025-07897-0 · Cited by 19

Palm Oil-Rich Diet Affects Murine Liver Proteome and S-Palmitoylome

Ziemlińska, E., Sobocińska, J., Świątkowska, A., Hromada‐Judycka, A., Traczyk, G., Malinowska, A., Świderska, B., Mietelska‐Porowska, A., Ciesielska, A., & Kwiatkowska, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222313094 · Cited by 19

Molecular Mechanisms of Allosteric Inhibition of Brain Glycogen Phosphorylase by Neurotoxic Dithiocarbamate Chemicals

Mathieu, C., Bui, L. C., Petit, E., Haddad, I., Agbulut, O., Vinh, J., Dupret, J., & Rodrigues‐Lima, F. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.766725 · Cited by 19

Oxidative post-translational modification of βeta 2-glycoprotein I in the pathophysiology of the anti-phospholipid syndrome

Weaver, J. C., Krilis, S. A., & Giannakopoulos, B. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.03.048 · Cited by 18

Soluble guanylyl cyclase mediates noncanonical nitric oxide signaling by nitrosothiol transfer under oxidative stress

Cui, C., Wu, C., Shu, P., Liu, T., Hong Li, A., & Beuve, A. V. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102425 · Cited by 17

Protein S-Nitrosylation: A Chemical Modification with Ubiquitous Biological Activities

Aboalroub, A. A., & Azzam, K. M. A. (2024) · The Protein Journal · doi:10.1007/s10930-024-10223-y · Cited by 18

Proteome-wide identification of palmitoylated proteins in mouse testis

Gao, J., Li, W., Zhang, Z., Gao, W., & Kong, E. (2022) · Reproductive Sciences · doi:10.1007/s43032-022-00919-w · Cited by 16

Experimental Approaches for Investigating Disulfide-Based Redox Relays in Cells

West, J. D. (2022) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.2c00123 · Cited by 16

PRESS: PRotEin S-Sulfenylation server

Sakka, M., Tzortzis, G., Mantzaris, M. D., Bekas, N., Kellici, T. F., Likas, A. C., Galaris, D., Gerothanassis, I. P., & Tzakos, A. G. (2016) · Bioinformatics · doi:10.1093/bioinformatics/btw301 · Cited by 16

Redox proteomics screening cellular factors associated with oxidative stress in hepatocarcinogenesis

Zhou, L., Ji, W., Huang, Z., Nice, E. C., Huang, C., Zhang, H., & Li, Q. (2016) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201600089 · Cited by 16

S-palmitoylation Is Required for the Control of Growth Cone Morphology of DRG Neurons by CNP-Induced cGMP Signaling

Dumoulin, A., Dagane, A., Dittmar, G. A. G., & Rathjen, F. G. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00345 · Cited by 16

Regulation of Death Receptor Signaling by S-Palmitoylation and Detergent-Resistant Membrane Micro Domains—Greasing the Gears of Extrinsic Cell Death Induction, Survival, and Inflammation

Fritsch, J., Särchen, V., & Schneider‐Brachert, W. (2021) · Cancers · doi:10.3390/cancers13112513 · Cited by 15

Regulation of hyperoxia-induced neonatal lung injury via post-translational cysteine redox modifications

Zhang, T., Day, N., Gaffrey, M. J., Weitz, K., Attah, K., Mimche, P. N., Paine, R., Qian, W., & Helms, M. N. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102405 · Cited by 15

Residue Modification and Mass Spectrometry for the Investigation of Structural and Metalation Properties of Metallothionein and Cysteine-Rich Proteins

Irvine, G. W., & Stillman, M. J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18050913 · Cited by 14

Lipoxin A4 yields an electrophilic 15-oxo metabolite that mediates FPR2 receptor-independent anti-inflammatory signaling

Koudelka, A., Buchan, G. J., Cechova, V., O’Brien, J. P., Stevenson, E. R., Uvalle, C. E., Liu, H., Woodcock, S. R., Mullett, S. J., Zhang, C., et al. (2024) · Journal of Lipid Research · doi:10.1016/j.jlr.2024.100705 · Cited by 13

Protein S-glutathionylation and the regulation of cellular functions

Mailloux, R. J., Gill, R., & Young, A. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-818606-0.00013-4 · Cited by 15

Redox signaling in cell fate: Beyond damage

Lamontagne, F., Paz‐Trejo, C., Cuervo, N. Z., & Grandvaux, N. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119722 · Cited by 14

Chemoproteomic strategy identified p120-catenin glutathionylation regulates E-cadherin degradation and cell migration

Kukulage, D. S. K., Abeywardana, M. Y., Don, N. N. J. M., Ren-ming, H., Shishikura, K., Matthews, M. L., & Ahn, Y. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.08.004 · Cited by 12

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Rafea, R., Siragusa, M., & Fleming, I. (2025) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.70029 · Cited by 12

Cpipe: a comprehensive computational platform for sequence and structure-based analyses of Cysteine residues

Soylu, İ., & Marino, S. M. (2017) · Bioinformatics · doi:10.1093/bioinformatics/btx181 · Cited by 11

Ageing-dependent thiol oxidation reveals early oxidation of proteins with core proteostasis functions

Jonak, K., Suppanz, I., Bender, J., Chacińska, A., Warscheid, B., & Topf, U. (2024) · Life Science Alliance · doi:10.26508/lsa.202302300 · Cited by 9

Cysteine Alkylation in Enzymes and Transcription Factors: A Therapeutic Strategy for Cancer

Andrés, C. M. C., Lobo, F., de la Lastra, J. M. P., Munguira, E. B., Andrés, C., & Pérez‐Lebeña, E. (2025) · Cancers · doi:10.3390/cancers17111876 · Cited by 9

Gasotransmitter-Mediated Cysteinome Oxidative Posttranslational Modifications: Formation, Biological Effects, and Detection

Li, Z., Huang, Y., Lv, B., Du, J., Yang, J. H., Fu, L., & Jin, H. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0407 · Cited by 9

SNOs Differ

Seth, D., & Stamler, J. S. (2015) · Circulation Research · doi:10.1161/circresaha.115.307551 · Cited by 9

Understanding the chemically-reactive proteome

Jones, L. H. (2015) · Molecular BioSystems · doi:10.1039/c5mb00760g · Cited by 8

S-acylation regulates the membrane association and activity of Calpain-5

Gal, J., Bondada, V., Mashburn, C. B., Rodgers, D. W., Croall, D. E., & Geddes, J. W. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119298 · Cited by 8

Protein phosphatase PP2Cα S-glutathionylation regulates cell migration

Kukulage, D. S. K., Samarasinghe, K. T. G., Don, N. N. J. M., Shivamadhu, M. C., Shishikura, K., Schiff, W., Ramezani, F. M., Padmavathi, R., Matthews, M. L., & Ahn, Y. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107784 · Cited by 7

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Rajczewski, A. T., Ndreu, L., Pujari, S. S., Griffin, T. J., Törnqvist, M., Karlsson, I. B., & Tretyakova, N. Y. (2021) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.1c00111 · Cited by 7

Analysis of Cysteine Post Translational Modifications Using Organic Mercury Resin

Doulias, P., & Gould, N. S. (2018) · Current Protocols in Protein Science · doi:10.1002/cpps.69 · Cited by 7

Activation of hepatic acetyl-CoA carboxylase by S-nitrosylation in response to diet

Venetos, N. M., Stomberski, C. T., Qian, Z., Premont, R. T., & Stamler, J. S. (2024) · Journal of Lipid Research · doi:10.1016/j.jlr.2024.100542 · Cited by 6

Site-Specific Proteomic Mapping of Modified Cysteine Residues

Gould, N. S. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9187-7_11 · Cited by 3

Regulation of protein function and signaling by reversible cysteine S-nitrosylation

Gould, N., Doulias, P.-T., Tenopoulou, M., Raju, K., & Ischiropoulos, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.460261 · Cited by 274

Global, in situ, site-specific analysis of protein S-sulfenylation

Yang, J. H., Gupta, V., Tallman, K. A., Porter, N. A., Carroll, K. S., & Liebler, D. C. (2015) · Nature Protocols · doi:10.1038/nprot.2015.062 · Cited by 139

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Majmudar, J. D., Konopko, A. M., Labby, K. J., Tom, C. T. M. B., Crellin, J. E., Prakash, A., & Martin, B. R. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.5b06806 · Cited by 51

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Weerapana, E. (2015) · The FASEB Journal · doi:10.1096/fasebj.29.1_supplement.370.1