An evolving understanding of the S-glutathionylation cycle in pathways of redox regulation
Tóm tắt
Từ khóa
Tài liệu tham khảo
Grek, 2013, Causes and consequences of cysteine S-glutathionylation, J. Biol. Chem., 288, 26497, 10.1074/jbc.R113.461368
Bechtel, 2017, From structure to redox: the diverse functional roles of disulfides and implications in disease, Proteomics, 17, 10.1002/pmic.201600391
Hatahet, 2009, Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation, Antioxid. Redox Signal., 11, 2807, 10.1089/ars.2009.2466
Mailloux, 2014, S-glutathionylation reactions in mitochondrial function and disease, Front. Cell Dev. Biol., 2, 68, 10.3389/fcell.2014.00068
Gallogly, 2007, Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress, Curr. Opin. Pharmacol., 7, 381, 10.1016/j.coph.2007.06.003
Gilbert, 1995, Thiol/disulfide exchange equilibria and disulfide bond stability, Methods Enzymol., 251, 8, 10.1016/0076-6879(95)51107-5
Gilbert, 1990, Molecular and cellular aspects of thiol-disulfide exchange, Adv. Enzymol. Relat. Areas Mol. Biol., 63, 69
Klatt, 1999, Redox regulation of c-Jun DNA binding by reversible S-glutathiolation, FASEB J., 13, 1481, 10.1096/fasebj.13.12.1481
Arbault, 1997, Activation of the NADPH oxidase in human fibroblasts by mechanical intrusion of a single cell with an ultramicroelectrode, Carcinogenesis, 18, 569, 10.1093/carcin/18.3.569
Starke, 2003, Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase). Potential role in redox signal transduction, J. Biol. Chem., 278, 14607, 10.1074/jbc.M210434200
Gallogly, 2008, Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: implications for intracellular roles, Biochemistry, 47, 11144, 10.1021/bi800966v
Giustarini, 2005, S-nitrosation versus S-glutathionylation of protein sulfhydryl groups by S-nitrosoglutathione, Antioxid. Redox Signal., 7, 930, 10.1089/ars.2005.7.930
Townsend, 2006, A glutathione S-transferase pi-activated prodrug causes kinase activation concurrent with S-glutathionylation of proteins, Mol. Pharmacol., 69, 501, 10.1124/mol.105.018523
Townsend, 2009, Nitrosative stress-induced s-glutathionylation of protein disulfide isomerase leads to activation of the unfolded protein response, Cancer Res., 69, 7626, 10.1158/0008-5472.CAN-09-0493
Konorev, 2000, Modification of creatine kinase by S-nitrosothiols: s-nitrosation vs. S-thiolation, Free Radic. Biol. Med., 28, 1671, 10.1016/S0891-5849(00)00281-1
Manevich, 2004, Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST, Proc. Natl. Acad. Sci. USA, 101, 3780, 10.1073/pnas.0400181101
Ralat, 2006, Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes, Biochemistry, 45, 360, 10.1021/bi0520737
Townsend, 2009, Novel role for glutathione S-transferase pi. Regulator of protein S-Glutathionylation following oxidative and nitrosative stress, J. Biol. Chem., 284, 436, 10.1074/jbc.M805586200
Wetzelberger, 2010, Postischemic deactivation of cardiac aldose reductase: role of glutathione S-transferase P and glutaredoxin in regeneration of reduced thiols from sulfenic acids, J. Biol. Chem., 285, 26135, 10.1074/jbc.M110.146423
de Luca, 2011, Treatment of doxorubicin-resistant MCF7/Dx cells with nitric oxide causes histone glutathionylation and reversal of drug resistance, Biochem. J., 440, 175, 10.1042/BJ20111333
Klaus, 2013, Glutathione S-transferases interact with AMP-activated protein kinase: evidence for S-glutathionylation and activation in vitro, PLoS One, 8, e62497, 10.1371/journal.pone.0062497
Ye, 2017, Glutathione S-transferase P-mediated protein S-glutathionylation of resident endoplasmic reticulum proteins influences sensitivity to drug-induced unfolded protein response, Antioxid. Redox Signal., 26, 247, 10.1089/ars.2015.6486
Zhang, 2014, Glutathione S-transferase P influences redox and migration pathways in bone marrow, PLoS One, 9, e107478, 10.1371/journal.pone.0107478
Kamada, 2004, Nuclear glutathione S-transferase pi prevents apoptosis by reducing the oxidative stress-induced formation of exocyclic DNA products, Free Radic. Biol. Med., 37, 1875, 10.1016/j.freeradbiomed.2004.09.002
Goto, 2009, Glutathione S-transferase pi localizes in mitochondria and protects against oxidative stress, Free Radic. Biol. Med., 46, 1392, 10.1016/j.freeradbiomed.2009.02.025
Tajc, 2004, Direct determination of thiol pKa by isothermal titration microcalorimetry, J. Am. Chem. Soc., 126, 10508, 10.1021/ja047929u
Dirr, 1994, X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function, Eur. J. Biochem., 220, 645, 10.1111/j.1432-1033.1994.tb18666.x
Tew, 2011, The role of glutathione S-transferase P in signaling pathways and S-glutathionylation in cancer, Free Radic. Biol. Med., 51, 299, 10.1016/j.freeradbiomed.2011.04.013
Xiong, 2011, S-glutathionylation: from molecular mechanisms to health outcomes, Antioxid. Redox Signal., 15, 233, 10.1089/ars.2010.3540
Mannervik, 1980, Role of cytoplasmic thioltransferase in cellular regulation by thiol-disulphide interchange, Biochem. J., 190, 125, 10.1042/bj1900125
Gladyshev, 2001, Identification and characterization of a new mammalian glutaredoxin (thioltransferase), Grx2, J. Biol. Chem., 276, 30374, 10.1074/jbc.M100020200
Lundberg, 2001, Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms, J. Biol. Chem., 276, 26269, 10.1074/jbc.M011605200
Pai, 2007, What is the functional significance of the unique location of glutaredoxin 1 (GRx1) in the intermembrane space of mitochondria?, Antioxid. Redox Signal., 9, 2027, 10.1089/ars.2007.1642
Gallogly, 2009, Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulation, Antioxid. Redox Signal., 11, 1059, 10.1089/ars.2008.2291
Gravina, 1993, Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase, Biochemistry, 32, 3368, 10.1021/bi00064a021
Peltoniemi, 2006, Insights into deglutathionylation reactions. Different intermediates in the glutaredoxin and protein disulfide isomerase catalyzed reactions are defined by the gamma-linkage present in glutathione, J. Biol. Chem., 281, 33107, 10.1074/jbc.M605602200
Jensen, 2014, The pKa value and accessibility of cysteine residues are key determinants for protein substrate discrimination by glutaredoxin, Biochemistry, 53, 2533, 10.1021/bi4016633
Menon, 2013, A role for glutathione transferase Omega 1 (GSTO1-1) in the glutathionylation cycle, J. Biol. Chem., 288, 25769, 10.1074/jbc.M113.487785
Findlay, 2006, A novel role for human sulfiredoxin in the reversal of glutathionylation, Cancer Res., 66, 6800, 10.1158/0008-5472.CAN-06-0484
Park, 2009, Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin, J. Biol. Chem., 284, 23364, 10.1074/jbc.M109.021394
Board, 2000, Identification, characterization, and crystal structure of the Omega class glutathione transferases, J. Biol. Chem., 275, 24798, 10.1074/jbc.M001706200
Board, 2016, Structure, function and disease relevance of Omega-class glutathione transferases, Arch. Toxicol., 90, 1049, 10.1007/s00204-016-1691-1
Kim, 2012, Glutathione s-transferase omega 1 activity is sufficient to suppress neurodegeneration in a Drosophila model of Parkinson disease, J. Biol. Chem., 287, 6628, 10.1074/jbc.M111.291179
Chen, 2017, Glycosylation of KEAP1 links nutrient sensing to redox stress signaling, EMBO J., 36, 2233, 10.15252/embj.201696113
Uys, 2011, Nitrosative stress-induced S-glutathionylation of protein disulfide isomerase, Methods Enzymol., 490, 321, 10.1016/B978-0-12-385114-7.00018-0
Ghezzi, 2005, Regulation of protein function by glutathionylation, Free Radic. Res., 39, 573, 10.1080/10715760500072172
Watanabe, 2014, Methods of measuring protein disulfide isomerase activity: a critical overview, Front. Chem., 2, 73, 10.3389/fchem.2014.00073
Xiong, 2012, S-glutathionylation of protein disulfide isomerase regulates estrogen receptor alpha stability and function, Int. J. Cell Biol., 2012, 273549, 10.1155/2012/273549
Hofmann, 2002, Peroxiredoxins, Biol. Chem., 383, 347
Ralat, 2008, Characterization of the complex of glutathione S-transferase pi and 1-cysteine peroxiredoxin, Arch. Biochem. Biophys., 474, 109, 10.1016/j.abb.2008.02.043
Mieyal, 1991, Thioltransferase in human red blood cells: purification and properties, Biochemistry, 30, 6088, 10.1021/bi00239a002
Manevich, 2013, Allelic variants of glutathione S-transferase P1-1 differentially mediate the peroxidase function of peroxiredoxin VI and alter membrane lipid peroxidation, Free Radic. Biol. Med., 54, 62, 10.1016/j.freeradbiomed.2012.10.556
Choi, 1998, Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution, Nat. Struct. Biol., 5, 400, 10.1038/nsb0598-400
Manevich, 2014, Peroxiredoxin VI oxidation in cerebrospinal fluid correlates with traumatic brain injury outcome, Free Radic. Biol. Med., 72, 210, 10.1016/j.freeradbiomed.2014.04.002
Zhang, 2014, Pleiotropic functions of glutathione S-transferase P, Adv. Cancer Res., 122, 143, 10.1016/B978-0-12-420117-0.00004-9
Murphy, 2012, Mitochondrial thiols in antioxidant protection and redox signaling: distinct roles for glutathionylation and other thiol modifications, Antioxid. Redox Signal., 16, 476, 10.1089/ars.2011.4289
O'Brien, 2017, Protein S-glutathionylation alters superoxide/hydrogen peroxide emission from pyruvate dehydrogenase complex, Free Radic. Biol. Med., 106, 302, 10.1016/j.freeradbiomed.2017.02.046
Kil, 2005, Regulation of mitochondrial NADP+-dependent isocitrate dehydrogenase activity by glutathionylation, J. Biol. Chem., 280, 10846, 10.1074/jbc.M411306200
Applegate, 2008, Reversible inhibition of alpha-ketoglutarate dehydrogenase by hydrogen peroxide: glutathionylation and protection of lipoic acid, Biochemistry, 47, 473, 10.1021/bi7017464
Eaton, 2002, Purification of proteins susceptible to oxidation at cysteine residues: identification of malate dehydrogenase as a target for S-glutathiolation, Ann. N. Y. Acad. Sci., 973, 529, 10.1111/j.1749-6632.2002.tb04694.x
Garcia, 2010, Regulation of mitochondrial glutathione redox status and protein glutathionylation by respiratory substrates, J. Biol. Chem., 285, 39646, 10.1074/jbc.M110.164160
Han, 2005, Sites and mechanisms of aconitase inactivation by peroxynitrite: modulation by citrate and glutathione, Biochemistry, 44, 11986, 10.1021/bi0509393
Baradaran, 2013, Crystal structure of the entire respiratory complex I, Nature, 494, 443, 10.1038/nature11871
Passarelli, 2010, GSSG-mediated Complex I defect in isolated cardiac mitochondria, Int. J. Mol. Med., 26, 95
Hurd, 2008, Complex I within oxidatively stressed bovine heart mitochondria is glutathionylated on Cys-531 and Cys-704 of the 75-kDa subunit: potential role of CYS residues in decreasing oxidative damage, J. Biol. Chem., 283, 24801, 10.1074/jbc.M803432200
Kumar, 2013, Redox proteomics of thiol proteins in mouse heart during ischemia/reperfusion using ICAT reagents and mass spectrometry, Free Radic. Biol. Med., 58, 109, 10.1016/j.freeradbiomed.2013.01.021
Mailloux, 2014, Glutaredoxin-2 is required to control oxidative phosphorylation in cardiac muscle by mediating deglutathionylation reactions, J. Biol. Chem., 289, 14812, 10.1074/jbc.M114.550574
Grivennikova, 2001, Catalytic activity of NADH-ubiquinone oxidoreductase (complex I) in intact mitochondria. evidence for the slow active/inactive transition, J. Biol. Chem., 276, 9038, 10.1074/jbc.M009661200
Drose, 2014, Mitochondrial respiratory chain complexes as sources and targets of thiol-based redox-regulation, Biochim. Biophys. Acta, 1844, 1344, 10.1016/j.bbapap.2014.02.006
Galkin, 2008, Identification of the mitochondrial ND3 subunit as a structural component involved in the active/deactive enzyme transition of respiratory complex I, J. Biol. Chem., 283, 20907, 10.1074/jbc.M803190200
Chen, 2007, Mitochondrial complex II in the post-ischemic heart: oxidative injury and the role of protein S-glutathionylation, J. Biol. Chem., 282, 32640, 10.1074/jbc.M702294200
Wang, 2011, Redox regulation of mitochondrial ATP synthase: implications for cardiac resynchronization therapy, Circ. Res., 109, 750, 10.1161/CIRCRESAHA.111.246124
Mailloux, 2011, Uncoupling proteins and the control of mitochondrial reactive oxygen species production, Free Radic. Biol. Med., 51, 1106, 10.1016/j.freeradbiomed.2011.06.022
Mailloux, 2011, Glutathionylation acts as a control switch for uncoupling proteins UCP2 and UCP3, J. Biol. Chem., 286, 21865, 10.1074/jbc.M111.240242
Queiroga, 2010, Glutathionylation of adenine nucleotide translocase induced by carbon monoxide prevents mitochondrial membrane permeabilization and apoptosis, J. Biol. Chem., 285, 17077, 10.1074/jbc.M109.065052
Kramer, 2015, The measurement of reversible redox dependent post-translational modifications and their regulation of mitochondrial and skeletal muscle function, Front. Physiol., 6, 347, 10.3389/fphys.2015.00347
Zhang, 2018, S-Glutathionylation of estrogen receptor alpha affects dendritic cell function, J. Biol. Chem.
Hwang, 1992, Oxidized redox state of glutathione in the endoplasmic reticulum, Science, 257, 1496, 10.1126/science.1523409
Coe, 2009, Calcium binding chaperones of the endoplasmic reticulum, Gen. Physiol. Biophys. 28 Spec. No Focus, F96
Carreras-Sureda, 2017, Calcium signaling at the endoplasmic reticulum: fine-tuning stress responses, Cell Calcium
Aracena-Parks, 2006, Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1, J. Biol. Chem., 281, 40354, 10.1074/jbc.M600876200
Aracena, 2005, Effects of S-glutathionylation and S-nitrosylation on calmodulin binding to triads and FKBP12 binding to type 1 calcium release channels, Antioxid. Redox Signal., 7, 870, 10.1089/ars.2005.7.870
Zima, 2016, Functional impact of ryanodine receptor oxidation on intracellular calcium regulation in the heart, Rev. Physiol. Biochem. Pharmacol., 171, 39, 10.1007/112_2016_2
Sanchez, 2005, Tachycardia increases NADPH oxidase activity and RyR2 S-glutathionylation in ventricular muscle, J. Mol. Cell Cardiol., 39, 982, 10.1016/j.yjmcc.2005.08.010
Lock, 2012, Protein S-glutathionylation enhances Ca2+-induced Ca2+ release via the IP3 receptor in cultured aortic endothelial cells, J. Physiol., 590, 3431, 10.1113/jphysiol.2012.230656
Viner, 1996, The oxidative inactivation of sarcoplasmic reticulum Ca(2+)-ATPase by peroxynitrite, Free Radic. Res., 24, 243, 10.3109/10715769609088022
Adachi, 2004, S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide, Nat. Med., 10, 1200, 10.1038/nm1119
Vangheluwe, 2005, Modulating sarco(endo)plasmic reticulum Ca2+ ATPase 2 (SERCA2) activity: cell biological implications, Cell Calcium, 38, 291, 10.1016/j.ceca.2005.06.033
Wang, 2016, Formation and reversibility of BiP Protein cysteine oxidation facilitate cell survival during and post oxidative stress, J. Biol. Chem., 291, 7541, 10.1074/jbc.M115.694810
Ali-Osman, 1997, Molecular cloning, characterization, and expression in Escherichia coli of full-length cDNAs of three human glutathione S-transferase Pi gene variants. Evidence for differential catalytic activity of the encoded proteins, J. Biol. Chem., 272, 10004, 10.1074/jbc.272.15.10004
Harries, 1997, Identification of genetic polymorphisms at the glutathione S-transferase Pi locus and association with susceptibility to bladder, testicular and prostate cancer, Carcinogenesis, 18, 641, 10.1093/carcin/18.4.641
Harris, 1998, Polymorphism of the Pi class glutathione S-transferase in normal populations and cancer patients, Pharmacogenetics, 8, 27, 10.1097/00008571-199802000-00004
Grek, 2014, S-glutathionylation of buccal cell proteins as biomarkers of exposure to hydrogen peroxide, BBA Clin., 2, 31, 10.1016/j.bbacli.2014.08.003
Karihtala, 2003, Peroxiredoxins in breast carcinoma, Clin. Cancer Res., 9, 3418
Chang, 2007, Identification of the functional role of peroxiredoxin 6 in the progression of breast cancer, Breast Cancer Res., 9, R76, 10.1186/bcr1789
Manevich, 2004, Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST, Proc. Natl. Acad. Sci. USA, 101, 3780, 10.1073/pnas.0400181101
Manevich, 2005, Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism, Free Radic. Biol. Med., 38, 1422, 10.1016/j.freeradbiomed.2005.02.011
Townsend, 2007, S-glutathionylation: indicator of cell stress and regulator of the unfolded protein response, Mol. Interv., 7, 313, 10.1124/mi.7.6.7
Morgan, 1996, Isozyme-specific glutathione S-transferase inhibitors potentiate drug sensitivity in cultured human tumor cell lines, Cancer Chemother. Pharmacol., 37, 363, 10.1007/s002800050398
Raza, 2012, A phase 2 randomized multicenter study of 2 extended dosing schedules of oral ezatiostat in low to intermediate-1 risk myelodysplastic syndrome, Cancer, 118, 2138, 10.1002/cncr.26469
Mahadevan, 2015, Ezatiostat hydrochloride for the treatment of myelodysplastic syndromes, Expert Opin. Investig. Drugs, 24, 725, 10.1517/13543784.2015.1021003
Quddus, 2010, Oral Ezatiostat HCl (TLK199) and Myelodysplastic syndrome: a case report of sustained hematologic response following an abbreviated exposure, J. Hematol. Oncol., 3, 16, 10.1186/1756-8722-3-16
Lyons, 2011, Oral ezatiostat HCl (Telintra(R), TLK199) and idiopathic chronic neutropenia (ICN): a case report of complete response of a patient with G-CSF resistant ICN following treatment with ezatiostat, a glutathione S-transferase P1-1 (GSTP1-1) inhibitor, J. Hematol. Oncol., 4, 43, 10.1186/1756-8722-4-43
Flatgaard, 1993, Isozyme specificity of novel glutathione-S-transferase inhibitors, Cancer Chemother. Pharmacol., 33, 63, 10.1007/BF00686025
Lyttle, 1994, Isozyme-specific glutathione-S-transferase inhibitors: design and synthesis, J. Med. Chem., 37, 189, 10.1021/jm00027a024
Gate, 2004, Increased myeloproliferation in glutathione S-transferase pi-deficient mice is associated with a deregulation of JNK and Janus kinase/STAT pathways, J. Biol. Chem., 279, 8608, 10.1074/jbc.M308613200
McMillan, 2016, Attenuation of lung fibrosis in mice with a clinically relevant inhibitor of glutathione-S-transferase pi, JCI Insight, 1, 10.1172/jci.insight.85717
Zhang, 2017, Hydrogen polysulfide biosignal-responsive polymersomes as a nanoplatform for distinguishing intracellular reactive sulfur species (RSS), Small
Cortese-Krott, 2017, The reactive species interactome: evolutionary emergence, biological significance, and opportunities for redox metabolomics and personalized medicine, Antioxid. Redox Signal., 27, 684, 10.1089/ars.2017.7083
Paulsen, 2013, Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery, Chem. Rev., 113, 4633, 10.1021/cr300163e
Casas, 2015, Reactive oxygen-related diseases: therapeutic targets and emerging clinical indications, Antioxid. Redox Signal., 23, 1171, 10.1089/ars.2015.6433
Sparaco, 2009, Friedreich's ataxia: oxidative stress and cytoskeletal abnormalities, J. Neurol. Sci., 287, 111, 10.1016/j.jns.2009.08.052
Mileo, 2009, Human papillomavirus-16 E7 interacts with glutathione S-transferase P1 and enhances its role in cell survival, PLoS One, 4, e7254, 10.1371/journal.pone.0007254
Trujillo, 2014, The cellular redox environment alters antigen presentation, J. Biol. Chem., 289, 27979, 10.1074/jbc.M114.573402
Butturini, 2018, S-glutathionylation exerts opposing roles in the regulation of STAT1 and STAT3 signaling in reactive microglia, Free Radic. Biol. Med., 117, 191, 10.1016/j.freeradbiomed.2018.02.005
Hoffman, 2016, Ablation of the thiol transferase Glutaredoxin-1 augments protein S-glutathionylation and modulates type 2 inflammatory responses and IL-17 in a house dust mite model of allergic airway disease in mice, Ann. Am. Thorac. Soc., 13, S97, 10.1513/AnnalsATS.201510-656MG
Kovats, 2012, Estrogen receptors regulate an inflammatory pathway of dendritic cell differentiation: mechanisms and implications for immunity, Horm. Behav., 62, 254, 10.1016/j.yhbeh.2012.04.011
Michalek, 2011, Estrogen-related receptor-alpha is a metabolic regulator of effector T-cell activation and differentiation, Proc. Natl. Acad. Sci. USA, 108, 18348, 10.1073/pnas.1108856108
Mitchell, 2017, Glutathionylation of Yersinia pestis LcrV and its effects on plague pathogenesis, MBio, 8, 10.1128/mBio.00646-17
Gu, 2016, Proteomic approaches to quantify cysteine reversible modifications in aging and neurodegenerative diseases, Proteom. Clin. Appl., 10, 1159, 10.1002/prca.201600015
Yang, 2016, The expanding landscape of the thiol redox proteome, Mol. Cell. Proteom., 15, 1, 10.1074/mcp.O115.056051
Su, 2014, Proteomic identification and quantification of S-glutathionylation in mouse macrophages using resin-assisted enrichment and isobaric labeling, Free Radic. Biol. Med., 67, 460, 10.1016/j.freeradbiomed.2013.12.004
Guo, 2014, Resin-assisted enrichment of thiols as a general strategy for proteomic profiling of cysteine-based reversible modifications, Nat. Protoc., 9, 64, 10.1038/nprot.2013.161
Lind, 2002, Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis, Arch. Biochem. Biophys., 406, 229, 10.1016/S0003-9861(02)00468-X
Reynaert, 2006, In situ detection of S-glutathionylated proteins following glutaredoxin-1 catalyzed cysteine derivatization, Biochim. Biophys. Acta, 1760, 380, 10.1016/j.bbagen.2006.01.006
Abo, 2015, Electrophilic probe for global analysis of cysteine reactivity in living cells, J. Am. Chem. Soc., 137, 7087, 10.1021/jacs.5b04350
Hurd, 2007, Detection of reactive oxygen species-sensitive thiol proteins by redox difference gel electrophoresis: implications for mitochondrial redox signaling, J. Biol. Chem., 282, 22040, 10.1074/jbc.M703591200
Comini, 2016, Measurement and meaning of cellular thiol: disufhide redox status, Free Radic. Res., 50, 246, 10.3109/10715762.2015.1110241
Pan, 2014, Mass spectrometry-based quantitative proteomics for dissecting multiplexed redox cysteine modifications in nitric oxide-protected cardiomyocyte under hypoxia, Antioxid. Redox Signal., 20, 1365, 10.1089/ars.2013.5326
Forrester, 2009, Proteomic analysis of S-nitrosylation and denitrosylation by resin-assisted capture, Nat. Biotechnol., 27, 557, 10.1038/nbt.1545
Michelet, 2008, In vivo targets of S-thiolation in Chlamydomonas reinhardtii, J. Biol. Chem., 283, 21571, 10.1074/jbc.M802331200
Brennan, 2006, The utility of N,N-biotinyl glutathione disulfide in the study of protein S-glutathiolation, Mol. Cell. Proteom., 5, 215, 10.1074/mcp.M500212-MCP200
Yang, 2010, Oxidative stress inhibits vascular K(ATP) channels by S-glutathionylation, J. Biol. Chem., 285, 38641, 10.1074/jbc.M110.162578
Samarasinghe, 2014, Metabolic synthesis of clickable glutathione for chemoselective detection of glutathionylation, J. Am. Chem. Soc., 136, 11566, 10.1021/ja503946q