Glutathione Homeostasis and Functions: Potential Targets for Medical Interventions
Open accessAbstract
Glutathione (GSH) is a tripeptide, which has many biological roles including protection against reactive oxygen and nitrogen species. The primary goal of this paper is to characterize the principal mechanisms of the protective role of GSH against reactive species and electrophiles. The ancillary goals are to provide up-to-date knowledge of GSH biosynthesis, hydrolysis, and utilization; intracellular compartmentalization and interorgan transfer; elimination of endogenously produced toxicants; involvement in metal homeostasis; glutathione-related enzymes and their regulation; glutathionylation of sulfhydryls. Individual sections are devoted to the relationships between GSH homeostasis and pathologies as well as to developed research tools and pharmacological approaches to manipulating GSH levels. Special attention is paid to compounds mainly of a natural origin (phytochemicals) which affect GSH-related processes. The paper provides starting points for development of novel tools and provides a hypothesis for investigation of the physiology and biochemistry of glutathione with a focus on human and animal health.
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The abundance of GSH is unusually high: cytosol concentration is ca 1-11 mM, mitochondria contain 6-10 mM, and nuclei 3-15 mM of GSH.
“The abundance of GSH is unusually high, the cytosol concentration is ca 1–11 mM, mitochondria contain 6–10 mM, and nuclei 3–15 mM of GSH.”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Lushchak 2012
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Cites
Colowick, S. P., Joshi, M. D., Jagannathan, & KAPLAN, N. O. (1966) · Cited by 26,137 · see citing works
Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178 · see citing works
Aging: a theory based on free radical and radiation chemistry
Harman, D. (1956) · Journal of Gerontology · doi:10.1093/geronj/11.3.298 · Cited by 8,567 · see citing works
Metals, Toxicity and Oxidative Stress
Valko, M., Morris, H., & Cronin, M. (2005) · Current Medicinal Chemistry · doi:10.2174/0929867053764635 · Cited by 5,018 · see citing works
Oxidative stress: oxidants and antioxidants
Sies, H. (1997) · Experimental Physiology · doi:10.1113/expphysiol.1997.sp004024 · Cited by 4,577 · see citing works
Environmentally induced oxidative stress in aquatic animals
Lushchak, V. I. (2011) · Aquatic Toxicology · doi:10.1016/j.aquatox.2010.10.006 · Cited by 2,729 · see citing works
Self-citationThe Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress
Nguyen, T., Nioi, P., & Pickett, C. B. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.r900010200 · Cited by 2,655 · see citing works
Regulation of glutathione synthesis
Lu, S. C.-L. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.05.005 · Cited by 2,131 · see citing works
The importance of glutathione in human disease
Townsend, D. M., Tew, K. D., & Tapiero, H. (2003) · Biomedicine & Pharmacotherapy · doi:10.1016/s0753-3322(03)00043-x · Cited by 2,009 · see citing works
The Biologic Clock: The Mitochondria?
Harman, D. (1972) · Journal of the American Geriatrics Society · doi:10.1111/j.1532-5415.1972.tb00787.x · Cited by 1,991 · see citing works
Glutathione and its role in cellular functions
Sies, H. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00177-x · Cited by 1,735 · see citing works
Griffith, O. W., & Meister, A. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35980-5 · Cited by 1,683 · see citing works
Nrf2:INrf2 (Keap1) signaling in oxidative stress
Kaspar, J. W., Niture, S. K., & Jaiswal, A. K. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.07.035 · Cited by 1,646 · see citing works
Akerboom, T. P. M., & Sies, H. (1981) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(81)77050-2 · Cited by 1,580 · see citing works
Glutathione, oxidative stress and neurodegeneration
Schulz, J. B., Lindenau, J. H., Seyfried, J., & DICHGANS, J. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01595.x · Cited by 1,215 · see citing works
Analysis of glutathione: implication in redox and detoxification
Pastore, A., Federici, G., Bertini, E., & Piemonte, F. (2003) · Clinica Chimica Acta · doi:10.1016/s0009-8981(03)00200-6 · Cited by 1,185 · see citing works
Storz, G., & Imlayt, J. A. (1999) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(99)80033-2 · Cited by 1,077 · see citing works
Modulation of natural killer cell activity by viruses
Lisnić, V. J., Krmpotić, A., & Jonjić, S. (2010) · Current Opinion in Microbiology · doi:10.1016/j.mib.2010.05.011 · Cited by 1,014 · see citing works
Oxidative Stress: Introductory Remarks
Sies, H. (1985) · Elsevier eBooks · doi:10.1016/b978-0-12-642760-8.50005-3 · Cited by 989 · see citing works
Mitochondrial Glutathione, a Key Survival Antioxidant
Marı́, M., Morales, A., Colell, A., García‐Ruiz, C., & Fernández-Checa, J. C. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2695 · Cited by 986 · 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
Arthur, J. R. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000664 · Cited by 949 · see citing works
Oxidative stress and regulation of glutathione in lung inflammation
Rahman, I., & MacNee, W. (2000) · European Respiratory Journal · doi:10.1034/j.1399-3003.2000.016003534.x · Cited by 923 · see citing works
A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
Liu, L., Hausladen, A., Zeng, M., Que, L., Heitman, J., & Stamler, J. S. (2001) · Nature · doi:10.1038/35068596 · Cited by 913 · see citing works
Kobayashi, M., & Yamamoto, M. P. (2006) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2006.01.007 · Cited by 855 · see citing works
[11] Redox potential of GSH/GSSG couple: Assay and biological significance
Jones, D. P. (2002) · Methods in Enzymology · doi:10.1016/s0076-6879(02)48630-2 · Cited by 812 · see citing works
Molecular mechanisms of Nrf2‐mediated antioxidant response
Li, W., & Kong, A. T. (2008) · Molecular Carcinogenesis · doi:10.1002/mc.20465 · Cited by 786 · see citing works
Surh, Y., Kundu, J. K., & Na, H. (2008) · Planta Medica · doi:10.1055/s-0028-1088302 · Cited by 759 · see citing works
Protein S-nitrosylation in health and disease: a current perspective
Foster, M. W., Hess, D. T., & Stamler, J. S. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.06.007 · Cited by 752 · see citing works
Dinkova‐Kostova, A. T., & Talalay, P. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.03.019 · Cited by 726 · see citing works
N-Acetylcysteine—a safe antidote for cysteine/glutathione deficiency
Atkuri, K. R., Mantovani, J. J., Herzenberg, L. A., & Herzenberg, L. A. (2007) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2007.04.005 · Cited by 721 · see citing works
Griffith, O. W. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33504-x · Cited by 701 · see citing works
Martı́n, D., Rojo, A. I., Salinas, M., Díaz, R. G., Gallardo, G., Alam, J., de Galarreta, C. M. R., & Cuadrado, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309660200 · Cited by 698 · see citing works
Lycopene is more bioavailable from tomato paste than from fresh tomatoes
Gärtner, C., Stahl, W., & Sies, H. (1997) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/66.1.116 · Cited by 694 · see citing works
Stahl, W., & Sies, H. (1992) · Journal of Nutrition · doi:10.1093/jn/122.11.2161 · Cited by 675 · see citing works
Keap1/Nrf2 Signaling Regulates Oxidative Stress Tolerance and Lifespan in Drosophila
Sykiotis, G. P., & Bohmann, D. (2008) · Developmental Cell · doi:10.1016/j.devcel.2007.12.002 · Cited by 675 · see citing works
Adaptive response to oxidative stress: Bacteria, fungi, plants and animals
Lushchak, V. I. (2010) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2010.10.004 · Cited by 670 · see citing works
Self-citationKobayashi, M., Li, L., Iwamoto, N., Nakajima‐Takagi, Y., Kaneko, H., Nakayama, Y., Eguchi, M., Wada, Y., Kumagai, Y., & Yamamoto, M. P. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01080-08 · Cited by 641 · see citing works
Glutathione peroxidase family – an evolutionary overview
Margis, R., Dunand, C., Teixeira, F. K., & Margis-Pinheiro, M. M. A. N. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06542.x · Cited by 611 · see citing works
The Role of Glutathione in Copper Metabolism and Toxicity
Freedman, J. H., Ciriolo, M. R., & Peisach, J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83589-x · Cited by 604 · see citing works
Glutathione: interorgan translocation, turnover, and metabolism.
Griffith, O. W., & Meister, A. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.11.5606 · Cited by 603 · see citing works
Thioredoxin and thioredoxin reductase: Current research with special reference to human disease
Holmgren, A., & Lu, J. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.03.083 · Cited by 577 · see citing works
Fratelli, M., Demol, H., Puype, M., Casagrande, S., Eberini, I., Salmona, M., Bonetto, V., Mengozzi, M., Duffieux, F., Miclet, E., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052592699 · Cited by 556 · see citing works
Shehzad, A., Wahid, F., & Lee, Y. S. (2010) · Archiv der Pharmazie · doi:10.1002/ardp.200900319 · Cited by 542 · see citing works
Direct and indirect antioxidant properties of inducers of cytoprotective proteins
Dinkova‐Kostova, A. T., & Talalay, P. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700195 · Cited by 535 · see citing works
Molecular Mechanisms and Clinical Implications of Reversible Protein <i>S</i> -Glutathionylation
Mieyal, J. J., Gallogly, M. M., Qanungo, S., Sabens, E. A., & Shelton, M. D. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2089 · Cited by 523 · see citing works
Protein denitrosylation: enzymatic mechanisms and cellular functions
Benhar, M., Forrester, M. T., & Stamler, J. S. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2764 · Cited by 519 · see citing works
Methylglyoxal in living organisms
Kalapos, M. P. (1999) · Toxicology Letters · doi:10.1016/s0378-4274(99)00160-5 · Cited by 507 · see citing works
Glutathione metabolism and its role in hepatotoxicity
DeLeve, L. D., & Kaplowitz, N. (1991) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(91)90029-l · Cited by 495 · see citing works
Dean, O., Giorlando, F., & Berk, M. (2011) · Journal of Psychiatry and Neuroscience · doi:10.1503/jpn.100057 · Cited by 494 · see citing works
Regulation of PTP1B via Glutathionylation of the Active Site Cysteine 215
Barrett, W. C., DeGnore, J. P., König, S., Fales, H. M., Keng, Y., Zhang, Z., Yim, M. B., & Chock, P. B. (1999) · Biochemistry · doi:10.1021/bi990240v · Cited by 488 · see citing works
The Nrf2 System as a Potential Target for the Development of Indirect Antioxidants
Jung, K.-A., & Kwak, M. (2010) · Molecules · doi:10.3390/molecules15107266 · Cited by 476 · see citing works
Adams, J. D., Jr., Lauterburg, B. H., & Mitchell, J. R. (1983) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)22134-6 · Cited by 466 · see citing works
Eggler, A. L., Liu, G., Pezzuto, J. M., van Breemen, R. B., & Mesecar, A. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502402102 · Cited by 459 · see citing works
Methylglyoxal, glyoxalase 1 and the dicarbonyl proteome
Rabbani, N., & Thornalley, P. J. (2010) · Amino Acids · doi:10.1007/s00726-010-0783-0 · Cited by 431 · 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
Redox-Dependent Transcriptional Regulation
Liu, H., Colavitti, R., Rovira, I. I., & Finkel, T. (2005) · Circulation Research · doi:10.1161/01.res.0000188210.72062.10 · Cited by 427 · see citing works
The effects of stress and aging on glutathione metabolism
Maher, P. A. (2005) · Ageing Research Reviews · doi:10.1016/j.arr.2005.02.005 · Cited by 426 · see citing works
Endogenous Glutathione Conjugates: Occurrence and Biological Functions
Wang, W., & Ballatori, N. (1998) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01370-x · Cited by 414 · see citing works
Hong, F., Freeman, M. L., & Liebler, D. C. (2005) · Chemical Research in Toxicology · doi:10.1021/tx0502138 · Cited by 404 · 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
Redox-operated genetic switches: the SoxR and OxyR transcription factors
Pomposiello, P. J., & Demple, B. (2001) · Trends in biotechnology · doi:10.1016/s0167-7799(00)01542-0 · Cited by 403 · see citing works
Nrf2 signaling and cell survival
Niture, S. K., Kaspar, J. W., Shen, J., & Jaiswal, A. K. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.06.009 · Cited by 397 · see citing works
Feng, R., Lu, Y., Bowman, L. L., Qian, Y. R., Castranova, V., & Ding, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503347200 · Cited by 391 · see citing works
REGULATION OF BACTERIAL OXIDATIVE STRESS GENES
Demple, B. (1991) · Annual Review of Genetics · doi:10.1146/annurev.ge.25.120191.001531 · Cited by 382 · see citing works
Chromium genotoxicity: A double-edged sword
Nickens, K. P., Patierno, S. R., & Ceryak, S. M. (2010) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.04.018 · Cited by 376 · see citing works
Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme
Toppo, S., Flohé, L., Ursini, F., Vanin, S., & Maiorino, M. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.04.007 · Cited by 368 · see citing works
Glutathione peroxidases and redox-regulated transcription factors
Brigelius‐Flohé, R. (2006) · Biological Chemistry · doi:10.1515/bc.2006.166 · Cited by 361 · see citing works
Berry flavonoids and phenolics: bioavailability and evidence of protective effects
Rio, D. D., Borges, G., & Crozier, A. (2010) · British Journal Of Nutrition · doi:10.1017/s0007114510003958 · Cited by 360 · see citing works
Colell, A., García‐Ruiz, C., Miranda, M., Ardite, E., Marı́, M., Morales, A., Corrales, F. J., Kaplowitz, N., & Fernández-Checa, J. C. (1998) · Gastroenterology · doi:10.1016/s0016-5085(98)70034-4 · Cited by 351 · see citing works
Brigelius, R., Muckel, C., Akerboom, T. P. M., & Sies, H. (1983) · Biochemical Pharmacology · doi:10.1016/0006-2952(83)90014-x · Cited by 348 · see citing works
Mitochondrial carrier proteins
Palmieri, F. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00329-7 · Cited by 341 · see citing works
Glutathione revisited: a vital function in iron metabolism and ancillary role in thiol‐redox control
Kumar, C., Igbaria, A., D’Autréaux, B., Planson, A., Junot, C., Godat, E., Bachhawat, A. K., Delaunay, A., & Tolédano, M. B. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.105 · Cited by 324 · see citing works
Oxidative stress and beta-cell dysfunction
Drews, G., Krippeit-Drews, P., & Düfer, M. (2010) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-010-0862-9 · Cited by 315 · see citing works
Nomenclature for Mammalian Soluble Glutathione Transferases
Mannervik, B., Philip G. Board, Hayes, J. D., Listowsky, I., & Pearson, W. R. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)01001-3 · Cited by 313 · see citing works
Role of Glutathione S-Transferases in Protection against Lipid Peroxidation
Yang, Y., Cheng, J., Singhal, S. S., Saini, M. K., Pandya, U., Awasthi, S., & Awasthi, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100551200 · Cited by 312 · see citing works
Glutathione, Altruistic Metabolite in Fungi
Pócsi, I., Prade, R. A., & Penninckx, M. J. (2004) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(04)49001-8 · Cited by 311 · see citing works
Modulation of skeletal muscle antioxidant defense by exercise: Role of redox signaling
Ji, L. L. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.02.031 · Cited by 291 · see citing works
Hepatic mitochondrial glutathione: transport and role in disease and toxicity
Fernández-Checa, J. C., & Kaplowitz, N. (2004) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.10.001 · Cited by 289 · see citing works
Ecotoxicology of Hexavalent Chromium in Freshwater Fish: A Critical Review
Velma, V., Vutukuru, S. S., & Tchounwou, P. B. (2009) · Reviews on Environmental Health · doi:10.1515/reveh.2009.24.2.129 · Cited by 288 · see citing works
ROLE of MITOCHONDRIA in TOXIC OXIDATIVE STRESS
Fariss, M. W. (2005) · Molecular Interventions · doi:10.1124/mi.5.2.7 · Cited by 288 · see citing works
Mitochondrial glutathione transport: Physiological, pathological and toxicological implications
Lash, L. H. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2006.03.001 · Cited by 280 · see citing works
A nuclear glutathione cycle within the cell cycle
Díaz‐Vivancos, P., Wolff, T., Marković, J., Pallardó, F. V., & Foyer, C. H. (2010) · Biochemical Journal · doi:10.1042/bj20100409 · Cited by 277 · see citing works
Hu, J., Dong, L., & Outten, C. E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803028200 · Cited by 273 · see citing works
Nitric oxide and nitrosative stress tolerance in bacteria
Poole, R. K. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330176 · Cited by 269 · see citing works
Na, H., Kim, E., Jung, J., Lee, H., Hyun, J. W., & Surh, Y. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.04.003 · Cited by 268 · see citing works
Peroxiredoxin 1 and its role in cell signaling
Neumann, C. A., Cao, J., & Manevich, Y. (2009) · Cell Cycle · doi:10.4161/cc.8.24.10242 · Cited by 268 · see citing works
Regulation of 4-hydroxynonenal-mediated signaling by glutathione S-transferases
Awasthi, S., Yang, Y., Tiwari, N. K., Patrick, B., Sharma, A., Li, J., & Awasthi, S. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.05.033 · Cited by 268 · see citing works
Gilbert, H. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33682-2 · Cited by 264 · see citing works
Hepatic Glutathione Homeostasis in the Rat: Efflux Accounts for Glutathione Turnover
Lauterburg, B. H., Adams, J. D., Jr., & Mitchell, J. R. (1984) · Hepatology · doi:10.1002/hep.1840040402 · Cited by 261 · see citing works
Chen, C., Pung, D., Leong, V., Hebbar, V., Shen, G., Nair, S., Li, W., & Kong, A.-N. T. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.07.021 · Cited by 260 · see citing works
Yang, Y., Sharma, R., Sharma, A., Awasthi, S., & Awasthi, S. (2003) · Acta Biochimica Polonica · doi:10.18388/abp.2003_3689 · Cited by 258 · see citing works
Giudice, A., Arra, C., & Turco, M. C. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-738-9_3 · Cited by 254 · see citing works
Oxidative Stress and Autophagy in Cardiac Disease, Neurological Disorders, Aging and Cancer
Essick, E. E., & Sam, F. (2010) · Oxidative Medicine and Cellular Longevity · doi:10.4161/oxim.3.3.12106 · Cited by 249 · see citing works
Transcriptional responses to oxidative stress: Pathological and toxicological implications
Ma, Q. (2009) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.11.004 · Cited by 248 · see citing works
Mitochondrial changes associated with glutathione deficiency
Meister, A. (1995) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(95)00007-q · Cited by 242 · see citing works
The rise of antioxidant signaling—The evolution and hormetic actions of Nrf2
Maher, J. M., & Yamamoto, M. P. (2010) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2010.01.011 · Cited by 231 · see citing works
Maturation of Cytosolic Iron-Sulfur Proteins Requires Glutathione
Sipos, K., Lange, H., Fekete, Z., Ullmann, P., Lill, R., & Kispál, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200677200 · Cited by 228 · see citing works
Polyphenols and health: Update and perspectives
Sies, H. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.04.006 · Cited by 224 · see citing works
Green Tea: Nature's Defense against Malignancies
Butt, M. S., & Sultan, M. T. (2009) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408390802145310 · Cited by 219 · see citing works
Glutathione and Ascorbate During Ischemia and Postischemic Reperfusion in Rat Brain
Cooper, A. J. L., Pulsinelli, W. A., & Duffy, T. E. (1980) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1980.tb07882.x · Cited by 214 · see citing works
Dietz, B. M., Kang, Y., Liu, G., Eggler, A. L., Yao, P., Chadwick, L. R., Pauli, G. F., Farnsworth, N. R., Mesecar, A. D., van Breemen, R. B., et al. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050058x · Cited by 207 · see citing works
Redox characteristics of the eukaryotic cytosol
López-Mirabal, H. R., & Winther, J. R. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.10.013 · Cited by 207 · see citing works
Toxicological and pathophysiological roles of reactive oxygen and nitrogen species
Roberts, R. A., Smith, R. A., Safe, S. H., Szabó, C., Tjalkens, R. B., & Robertson, F. M. (2010) · Toxicology · doi:10.1016/j.tox.2010.07.009 · Cited by 206 · see citing works
S-Glutathionylation: Indicator of Cell Stress and Regulator of the Unfolded Protein Response
Townsend, D. M. (2007) · Molecular Interventions · doi:10.1124/mi.7.6.7 · Cited by 206 · see citing works
Geiler, J., Michaelis, M., Naczk, P., Leutz, A., Langer, K., Doerr, H.-W., & Cinatl, J. J. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2009.08.025 · Cited by 205 · see citing works
Nitric Oxide in Cell Survival: A Janus Molecule
Calabrese, V., Cornelius, C., Rizzarelli, E., Owen, J. B., Dinkova‐Kostova, A. T., & Butterfield, D. A. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2721 · Cited by 195 · see citing works
Pro-oxidant shift in glutathione redox state during aging
Rebrin, I., & Sohal, R. S. (2008) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2008.06.001 · Cited by 194 · see citing works
A Novel Role for Human Sulfiredoxin in the Reversal of Glutathionylation
Findlay, V. J., Townsend, D. M., Morris, T. E., Fraser, J. P., He, L., & Tew, K. D. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0484 · Cited by 193 · see citing works
McNally, S. J., Harrison, E. M., Ross, J. A., Garden, O. J., & Wigmore, S. J. (2007) · International Journal of Molecular Medicine · doi:10.3892/ijmm.19.1.165 · Cited by 192 · see citing works
Vanin, A. F., Malenkova, I. V., & Сереженков, В. А. (1997) · Nitric Oxide · doi:10.1006/niox.1997.0122 · Cited by 192 · see citing works
Sites of alkylation of human Keap1 by natural chemoprevention agents
Luo, Y., Eggler, A. L., Liu, D., Liu, G., Mesecar, A. D., & van Breemen, R. B. (2007) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2007.09.015 · Cited by 191 · see citing works
Skulachev, V. P. (2007) · Biochemistry (Moscow) · doi:10.1134/s0006297907120139 · Cited by 190 · see citing works
Lycopene: Antioxidant and Biological Effects and its Bioavailability in the Human
Sies, H., & Stahl, W. (1998) · Experimental Biology and Medicine · doi:10.3181/00379727-218-44285a · Cited by 187 · see citing works
Cheng, J.-Z., Sharma, R., Yang, Y., Singhal, S. S., Sharma, A., Saini, M. K., Singh, S. V., Zimniak, P., Awasthi, S., & Awasthi, Y. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106838200 · Cited by 185 · see citing works
Garg, R., Gupta, S., & Maru, G. B. (2008) · Carcinogenesis · doi:10.1093/carcin/bgn064 · Cited by 185 · see citing works
Chromium: celebrating 50 years as an essential element?
Vincent, J. B. (2010) · Dalton Transactions · doi:10.1039/b920480f · Cited by 182 · see citing works
Shen, G., Xu, C., Hu, R., Jain, M. R., Gopalkrishnan, A., Nair, S., Huang, M., Chan, J. Y., & Kong, A. T. (2006) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-05-0293 · Cited by 179 · see citing works
Queen, B., & Tollefsbol, T. O. (2010) · Current Aging Science · doi:10.2174/1874609811003010034 · Cited by 178 · see citing works
The Nrf2-Keap1-ARE Signaling Pathway: The Regulation and Dual Function of Nrf2 in Cancer
Zhang, D. D. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3301 · Cited by 177 · see citing works
Kalayarasan, S., Prabhu, P. N., Narayanan, S., Manikandan, R., Arumugam, M., & Sudhandiran, G. (2009) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2008.12.055 · Cited by 176 · see citing works
Wondrak, G. T., Villeneuve, N. F., Lamore, S. D., Bause, A. S., Jiang, T., & Zhang, D. D. (2010) · Molecules · doi:10.3390/molecules15053338 · Cited by 173 · see citing works
Signal transduction events elicited by cancer prevention compounds
Kong, A. T., Yu, R., Hebbar, V., Chen, C., Owuor, E. D., Hu, R., Ee, P. L. R., & Mandlekar, S. (2001) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(01)00182-8 · Cited by 169 · see citing works
Lian, F., & Wang, X. (2008) · International Journal of Cancer · doi:10.1002/ijc.23696 · Cited by 165 · see citing works
Rushworth, S. A., Ogborne, R. M., Charalambos, C., & O'Connell, M. A. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.01.065 · Cited by 164 · see citing works
Mitochondrial function, GSH and iron in neurodegeneration and Lewy body diseases
Gu, M., Owen, A., Toffa, S., Cooper, J. A. D., Dexter, D. T., Jenner, P. G., MARSDEN, C. D., & Schapira, A. H. V. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00095-1 · Cited by 164 · see citing works
Glutathione Binding to the Bcl-2 Homology-3 Domain Groove
Zimmermann, A. K., Loucks, F. A., Schroeder, E. K., Bouchard, R. J., Tyler, K. L., & Linseman, D. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702853200 · Cited by 163 · see citing works
Reactive oxygen species and endothelial function in diabetes
Fatehi‐Hassanabad, Z., Chan, C. B., & Furman, B. L. (2010) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2010.03.048 · Cited by 163 · see citing works
Bishayee, A., Barnes, K. F., Bhatia, D., Darvesh, A. S., & Carroll, R. T. (2010) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-09-0171 · Cited by 161 · see citing works
Ramasamy, R., Yan, S. F., & Schmidt, A. M. (2006) · Cell · doi:10.1016/j.cell.2006.01.002 · Cited by 159 · see citing works
Novel function of human RLIP76: ATP-dependent transport of glutathione conjugates and doxorubicin
Awasthi, S., Cheng, J., Singhal, S. S., Saini, M. K., Pandya, U., Pikula, S., Bandorowicz-Pikula, J., Singh, S. V., Zimniak, P., & Awasthi, Y. C. (2000) · Biochemistry · doi:10.1021/bi992964c · Cited by 159 · see citing works
Reconstitution of Cu,Zn-superoxide dismutase by the Cu(I).glutathione complex.
Ciriolo, M. R., Desideri, A., Paci, M., & Rotilio, G. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38552-7 · Cited by 158 · see citing works
Achkor, H., Dı́az, M., Fernández, M. R., Biosca, J. A., Parés, X., & Martı́nez, M. C. (2003) · PLANT PHYSIOLOGY · doi:10.1104/pp.103.022277 · Cited by 157 · see citing works
Liao, B., Hsieh, C., Liu, Y., Tzeng, T.-T., Sun, Y.-W., & Wung, B. (2008) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2008.01.021 · Cited by 154 · see citing works
Coll, O., Colell, A., García‐Ruiz, C., Kaplowitz, N., & Fernández-Checa, J. C. (2003) · Hepatology · doi:10.1053/jhep.2003.50351 · Cited by 151 · see citing works
Oxidative Stress and Mechanisms of Protection Against It in Bacteria
Lushchak, V. I. (2001) · Biochemistry (Moscow) · doi:10.1023/a:1010294415625 · Cited by 149 · see citing works
Self-citationReversible and irreversible protein glutathionylation: biological and clinical aspects
Cooper, A. J. L., Pinto, J., & Callery, P. (2011) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1517/17425255.2011.577738 · Cited by 148 · see citing works
Date, M., Morita, T., Yamashita, N., Nishida, K., Yamaguchi, O., Higuchi, Y., Hirotani, S., Matsumura, Y., Hori, M., Tada, M., et al. (2002) · Journal of the American College of Cardiology · doi:10.1016/s0735-1097(01)01826-5 · Cited by 147 · see citing works
Electrophiles in Foods: The Current Status of Isothiocyanates and Their Chemical Biology
NAKAMURA, Y., & MIYOSHI, N. (2010) · Bioscience, Biotechnology, and Biochemistry · doi:10.1271/bbb.90731 · Cited by 143 · see citing works
Glutathione Therapy: From Prodrugs to Genes
Anderson, M. E., & Luo, J. (1998) · Seminars in Liver Disease · doi:10.1055/s-2007-1007174 · Cited by 140 · see citing works
Redox regulation of gamma-glutamyl transpeptidase.
Zhang, H.-Q., & Forman, H. (2009) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2009-0169tr · Cited by 140 · see citing works
Inhibition of glutathione synthesis as a chemotherapeutic strategy for trypanosomiasis.
Arrick, B. A., Griffith, O. W., & Cerami, A. (1981) · The Journal of Experimental Medicine · doi:10.1084/jem.153.3.720 · Cited by 140 · see citing works
Regulation of Mitochondrial NADP+-dependent Isocitrate Dehydrogenase Activity by Glutathionylation
Kil, I. S., & Park, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411306200 · Cited by 137 · see citing works
In situ analysis of methylglyoxal metabolism in Saccharomyces cerevisiae
Martins, A. M., CORDEIRO, C. A., & Freire, A. P. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02519-4 · Cited by 133 · see citing works
Fisher, C. D., Augustine, L. M., Maher, J. M., Nelson, D. M., Slitt, A. L., Klaassen, C. D., Lehman‐McKeeman, L. D., & Cherrington, N. J. (2007) · Drug Metabolism and Disposition · doi:10.1124/dmd.106.014340 · Cited by 128 · see citing works
Diallyl sulfide induces heme oxygenase-1 through MAPK pathway
Gong, P., Hu, B., & Cederbaum, A. I. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.09.024 · Cited by 125 · see citing works
Current Concepts About Chromium Supplementation in Type 2 Diabetes and Insulin Resistance
Wang, Z. Q., & Cefalu, W. T. (2010) · Current Diabetes Reports · doi:10.1007/s11892-010-0097-3 · Cited by 121 · see citing works
Prodrug Approach for Increasing Cellular Glutathione Levels
Cacciatore, I., Cornacchia, C., Pinnen, F., Mollica, A., & Stefano, A. D. (2010) · Molecules · doi:10.3390/molecules15031242 · Cited by 121 · see citing works
AN OVERVIEW ON THE ROLE OF METHYLGLYOXAL AND GLYOXALASES IN PLANTS
Yadav, S. K., Singla-Pareek, S. L., & Sopory, S. K. (2008) · Drug metabolism and drug interactions · doi:10.1515/dmdi.2008.23.1-2.51 · Cited by 120 · see citing works
Joung, E.-J., Li, M., Lee, H. G., Somparn, N., Jung, Y. S., Na, H., Kim, S., Cha, Y., & Surh, Y. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1827 · Cited by 119 · see citing works
Mahagita, C., Grassl, S. M., Piyachaturawat, P., & Ballatori, N. (2007) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00075.2007 · Cited by 119 · see citing works
The use of thiols by ribonucleotide reductase
Holmgren, A., & Sengupta, R. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.09.005 · Cited by 116 · see citing works
Glutathione S‐Transferases as Regulators of Kinase Pathways and Anticancer Drug Targets
Townsend, D. M., Findlay, V. J., & Tew, K. D. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)01019-0 · Cited by 115 · see citing works
Kluth�, D., Banning, A., Paur, I., Blomhoff, R., & Brigelius‐Flohé, R. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.09.028 · Cited by 114 · see citing works
Transport of glutathione diethyl ester into human cells.
Levy, E. J., Anderson, M. E., & Meister, A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.19.9171 · Cited by 114 · see citing works
Nrf2–ARE signaling pathway and natural products for cancer chemoprevention
Zhao, C. R., Gao, Z. H., & Qu, X. J. (2010) · Cancer Epidemiology · doi:10.1016/j.canep.2010.06.012 · Cited by 114 · see citing works
Chai, Y.-C., Jung, C., Lii, C., Ashraf, S. M., Hendrich, S., Wolf, B. A., Sies, H., & Thomas, J. A. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90295-t · Cited by 110 · see citing works
Şahin, K., Tuzcu, M., Şahin, N., Ali, S., & Küçük, Ö. (2010) · Food and Chemical Toxicology · doi:10.1016/j.fct.2010.06.038 · Cited by 108 · see citing works
Oxidative stress in Parkinson's disease and other neurodegenerative disorders.
Jenner, P. G. (1996) · PubMed · Cited by 106 · see citing works
Townsend, D. M., Findlay, V. J., Fazilev, F., Ogle, M. E., Fraser, J. P., Saavedra, J. E., Ji, X., Keefer, L. K., & Tew, K. D. (2005) · Molecular Pharmacology · doi:10.1124/mol.105.018523 · Cited by 105 · see citing works
Critical Role of Mitochondrial Glutathione in the Survival of Hepatocytes during Hypoxia
Lluis, J. M., Morales, A., Blasco, C., Colell, A., Marı́, M., García‐Ruiz, C., & Fernández-Checa, J. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408244200 · Cited by 105 · see citing works
Cinnamoyl-based Nrf2-activators targeting human skin cell photo-oxidative stress
Wondrak, G. T., Cabello, C. M., Villeneuve, N. F., Zhang, S., Ley, S., Li, Y., Sun, Z., & Zhang, D. D. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.04.023 · Cited by 104 · see citing works
Antioxidant-Prooxidant Properties of a New Organoselenium Compound Library
Plano, D., Baquedano, Y., Ibáñez, E., Jiménez, I., Palop, J. A., Spallholz, J. E., & Sanmartín, C. (2010) · Molecules · doi:10.3390/molecules15107292 · Cited by 97 · see citing works
Chen, R., Wang, J., Zhang, X., Ren, J. M., & Zeng, C. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.12.033 · Cited by 96 · see citing works
The effect of cysteine oxidation on isolated hepatocytes
Viña, J., Sáez, G. T., Wiggins, D., Roberts, A. F. C., Hems, R., & Krebs, H. A. (1983) · Biochemical Journal · doi:10.1042/bj2120039 · Cited by 95 · see citing works
Meredith, M. J., Cusick, C. L., Soltaninassab, S. R., Sekhar, K. R., Lu, S. C.-L., & Freeman, M. L. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8998 · Cited by 94 · see citing works
O’Donovan, D. J., & Fernandes, C. J. (2000) · Molecular Genetics and Metabolism · doi:10.1006/mgme.2000.3063 · Cited by 93 · see citing works
Kinetic Analysis of Intracellular Concentrations of Reactive Nitrogen Species
Lim, C. H., Dedon, P. C., & Deen, W. M. (2008) · Chemical Research in Toxicology · doi:10.1021/tx800213b · Cited by 93 · see citing works
Lushchak, O. V., Kubrak, O. I., Nykorak, M. Z., Storey, K. B., & Lushchak, V. I. (2008) · Aquatic Toxicology · doi:10.1016/j.aquatox.2008.01.007 · Cited by 92 · see citing works
Self-citationSaavedra, J. E., Srinivasan, A., Buzard, G. S., Davies, K. M., Waterhouse, D. J., Inami, K., Wilde, T. C., Citro, M. L., Cuellar, M. E., Deschamps, J. R., et al. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm050700k · Cited by 92 · see citing works
METHYLGLYOXAL AND GLUCOSE METABOLISM: A HISTORICAL PERSPECTIVE AND FUTURE AVENUES FOR RESEARCH
Kalapos, M. P. (2008) · Drug metabolism and drug interactions · doi:10.1515/dmdi.2008.23.1-2.69 · Cited by 92 · see citing works
Bahadorani, S., Bahadorani, P., Phillips, J. P., & Hilliker, A. J. (2008) · The Journals of Gerontology Series A · doi:10.1093/gerona/63.1.35 · Cited by 91 · see citing works
Role of α Class Glutathione S-Transferases as Antioxidant Enzymes in Rodent Tissues
Yang, Y. (2002) · Toxicology and Applied Pharmacology · doi:10.1006/taap.2002.9450 · Cited by 90 · see citing works
Lü, Y., Su, M.-Y., Hai-ya, H., Lin-li, & Yuan, C.-G. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.07.078 · Cited by 89 · see citing works
CEASER, E. K., Moellering, D. R., Shiva, S., Ramachandran, A., Landar, A. L., Venkartraman, A., Crawford, J., Patel, R. P., Dickinson, D. A., Ulasova, E., et al. (2004) · Biochemical Society Transactions · doi:10.1042/bst0320151 · Cited by 87 · see citing works
Mitochondrial longevity pathways
Raffaello, A., & Rizzuto, R. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.10.007 · Cited by 87 · see citing works
Lash, L. H., Putt, D. A., & Matherly, L. H. (2002) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.102.040220 · Cited by 87 · see citing works
OATP8/1B3-mediated Cotransport of Bile Acids and Glutathione
Briz, Ó., Romero, M. R., Martinez-Becerra, P., Macı́as, R. I. R., Perez, M. J., Jimenez, F., Martin, F. G.-S., & Marı́n, J. J. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602048200 · Cited by 84 · see citing works
A Genetic Investigation of the Essential Role of Glutathione
Spector, D., Labarre, J., & Tolédano, M. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009814200 · Cited by 81 · see citing works
Dietary sulfur amino acid effects on fasting plasma cysteine/cystine redox potential in humans
Jones, D. P., Park, Y. H., Gletsu-Miller, N. A., Liang, Y., Yu, T., Accardi, C. J., & Ziegler, T. R. (2010) · Nutrition · doi:10.1016/j.nut.2010.01.014 · Cited by 81 · see citing works
Sulfiredoxin: a potential therapeutic agent?
Findlay, V. J., Tapiero, H., & Townsend, D. M. (2005) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2005.07.003 · Cited by 80 · see citing works
Fimognari, C., Lenzi, M., & Hrelia, P. (2008) · Current Medicinal Chemistry · doi:10.2174/092986708783503168 · Cited by 79 · see citing works
Transcriptional regulation of mammalian selenoprotein expression
Stoytcheva, Z., & Berry, M. J. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.05.012 · Cited by 75 · see citing works
Inhibition of AP-1 and MAPK signaling and activation of Nrf2/ARE pathway by quercitrin.
Ding, M., Zhao, J., Bowman, L. L., Lu, Y., & Shi, X. (2010) · PubMed · Cited by 73 · see citing works
Lushchak, V., Semchyshyn, H., Lushchak, O., & Mandryk, S. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.10.147 · Cited by 72 · see citing works
Self-citationJiang, F., Robin, A. M., Katakowski, M., Tong, L., Espiritu, M., Singh, G., & Chopp, M. (2003) · Lasers in Medical Science · doi:10.1007/s10103-003-0269-3 · Cited by 71 · see citing works
Lushchak, V. I., Semchyshyn, H. M., Mandryk, S., & Lushchak, O. V. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.06.010 · Cited by 69 · see citing works
Self-citationTan, X., & Spivack, S. D. (2009) · Lung Cancer · doi:10.1016/j.lungcan.2009.01.002 · Cited by 69 · see citing works
Kalyanaraman, B., Karoui, H., Singh, R. J., & Felix, C. C. (1996) · Analytical Biochemistry · doi:10.1006/abio.1996.0380 · Cited by 67 · see citing works
Natarajan, V. T., Singh, A. K., Kumar, A. A., Sharma, P., Kar, H. K., Marrot, L., Meunier, J., Natarajan, K., Rani, R., & Gokhale, R. S. (2010) · Journal of Investigative Dermatology · doi:10.1038/jid.2010.201 · Cited by 66 · see citing works
Demkiv, O. M., Smutok, O. V., Paryzhak, S. Y., Gayda, G. Z., SULTANOV, Y. M., Guschin, D. A., Shkil, H., Schuhmann, W. W., & Gonchar, M. V. (2008) · Talanta · doi:10.1016/j.talanta.2008.04.040 · Cited by 65 · see citing works
Lushchak, V. I. (2010) · Biochemistry (Moscow) · doi:10.1134/s0006297910030041 · Cited by 64 · see citing works
Self-citationZhong, Q. P. W., Putt, D. A., Xu, F., & Lash, L. H. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.03.008 · Cited by 63 · see citing works
Regulation of glutathione transferase P: A tumor marker of hepatocarcinogenesis
Sakai, M., & Muramatsu, M. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.03.174 · Cited by 63 · see citing works
Tsai, C.-W., Chen, H., Yang, J., Sheen, L., & Lii, C. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf061874t · Cited by 63 · see citing works
The glutathione-dependent glyoxalase pathway in the yeast Saccharomyces cerevisiae.
Penninckx, M. J., Jaspers, C. J., & Legrain, M. J. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32368-8 · Cited by 62 · see citing works
Murray, A. R., Kisin, E. R., Castranova, V., Kommineni, C., Gunther, M. R., & Shvedova, A. A. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700201z · Cited by 61 · see citing works
PI3K, RSK, and mTOR Signal Networks for the GST Gene Regulation
Kim, S. G., & Lee, S. (2006) · Toxicological Sciences · doi:10.1093/toxsci/kfl175 · Cited by 61 · see citing works
Kaczmarek, M. Z., Timofeeva, O. A., Karaczyn, A. A., Malyguine, A. M., Kasprzak, K. S., & Salnikow, K. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.01.026 · Cited by 60 · see citing works
Li, Y., Cohenford, M. A., Dutta, U., & Dain, J. A. (2007) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-007-1682-4 · Cited by 60 · see citing works
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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
Free radicals, reactive oxygen species, oxidative stress and its classification
Lushchak, V. I. (2014) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2014.10.016 · Cited by 1,665 · see citing works
Self-citationOxidative Stress in Neurodegenerative Diseases
Simonian, N. A., & Coyle, J. T. (1996) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.36.040196.000503 · Cited by 1,377 · see citing works
Mitochondrial energetics in the kidney
Bhargava, P., & Schnellmann, R. G. (2017) · Nature Reviews Nephrology · doi:10.1038/nrneph.2017.107 · Cited by 1,363 · see citing works
Glutathione metabolism in cancer progression and treatment resistance
Bansal, A., & Simon, M. C. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201804161 · Cited by 1,234 · see citing works
“Apart from the classical antioxidant role, GSH also has several organelle-specific functions discussed in detail by Lushchak (2012).”
BackgroundRole of Glutathione in Cancer Progression and Chemoresistance
Traverso, N., Ricciarelli, R., Nitti, M., Marengo, B., Furfaro, A. L., Pronzato, M. A., Marinari, U. M., & Domenicotti, C. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/972913 · Cited by 1,208 · see citing works
Niu, B., Liao, K., Zhou, Y., Wen, T., Quan, G., Pan, X., & Wu, C. (2021) · Biomaterials · doi:10.1016/j.biomaterials.2021.121110 · Cited by 1,168 · see citing works
Oxidative Stress in Neurodegenerative Diseases
Niedzielska, E., Smaga, I., Gawlik, M., Moniczewski, A., Stankowicz, P., Pera, J., & Filip, M. (2016) · Molecular Neurobiology · doi:10.1007/s12035-015-9337-5 · Cited by 800 · see citing works
Chemical biology of anticancer gold( iii ) and gold( i ) complexes
Zou, T., Lum, C. T., Lok, C., Zhang, J., & Che, C. (2015) · Chemical Society Reviews · doi:10.1039/c5cs00132c · Cited by 628 · see citing works
Endogenous non-enzymatic antioxidants in the human body
Mirończuk-Chodakowska, I., Witkowska, A. M., & Zujko, M. E. (2017) · Advances in Medical Sciences · doi:10.1016/j.advms.2017.05.005 · Cited by 620 · see citing works
Srinivasarao, M., & Low, P. S. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00013 · Cited by 616 · see citing works
Lushchak, V. I., Matviishyn, T. M., Hušák, V., Storey, J. M., & Storey, K. B. (2018) · EXCLI journal · doi:10.17179/excli2018-1710 · Cited by 578 · see citing works
“In this case, changes in the levels of different glutathione forms (either reduced GSH or oxidized GSSG) may indicate a shift in the prooxidant-antioxidant balance, which often takes place under pesticide-induced stress conditions (Atamaniuk et al., 2013; Lushchak, 2012; Maher, 2005).”
BackgroundMethodInfluentialSelf-citationSilymarin as Supportive Treatment in Liver Diseases: A Narrative Review
Gillessen, A., & Schmidt, H. (2020) · Advances in Therapy · doi:10.1007/s12325-020-01251-y · Cited by 494 · see citing works
TGF-β Promotes Heterogeneity and Drug Resistance in Squamous Cell Carcinoma
Oshimori, N., Oristian, D., & Fuchs, E. (2015) · Cell · doi:10.1016/j.cell.2015.01.043 · Cited by 471 · see citing works
Altered amino acid concentrations in NAFLD: Impact of obesity and insulin resistance
Gaggini, M., Carli, F., Rosso, C., Buzzigoli, E., Marietti, M., Latta, V. D., Ciociaro, D., Abate, M. L., Gambino, R., Cassader, M., et al. (2017) · Hepatology · doi:10.1002/hep.29465 · Cited by 467 · see citing works
“GSH is an antioxidant molecule produced by several tissues in response to oxidative stress and increased production of reactive oxygen species (ROS).((41,42)) Oxidative stress is one of the mechanisms responsible for liver damage and is characterized by mitochondrial dysfunction, impaired oxidation, and production of…”
BackgroundThe promise of N-acetylcysteine in neuropsychiatry
Berk, M., Malhi, G. S., Gray, L. J., & Dean, O. M. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.01.001 · Cited by 434 · see citing works
Effector T Cells Abrogate Stroma-Mediated Chemoresistance in Ovarian Cancer
Wang, W., Kryczek, I., Dostál, L., Lin, H., Tan, L., Zhao, L., Lu, F., Wei, S., Maj, T., Peng, D., et al. (2016) · Cell · doi:10.1016/j.cell.2016.04.009 · Cited by 423 · see citing works
Antioxidants of Edible Mushrooms
Kozarski, M., Klaus, A., Jakovljevic, D., Todorovic, N., Vunduk, J., Petrović, P., Niksic, M., Vrvic, M., & Van Griensven, L. (2015) · Molecules · doi:10.3390/molecules201019489 · Cited by 413 · see citing works
“Under high intensity oxidative stress perturbations of mitochondrial permeability transition pore, activation of apoptosis cascade, destruction of electron transporters take place, which may culminate in apoptosis and/or necrosis [23,69].”
BackgroundReactive Oxygen Species‐Regulating Strategies Based on Nanomaterials for Disease Treatment
Zhang, C., Wang, X., Du, J., Gu, Z., & Zhao, Y. (2020) · Advanced Science · doi:10.1002/advs.202002797 · Cited by 404 · see citing works
RONS and Oxidative Stress: An Overview of Basic Concepts
Aranda‐Rivera, A. K., Cruz‐Gregorio, A., Arancibia‐Hernández, Y. L., Cruz, E. Y. H., & Pedraza‐Chaverrí, J. (2022) · Oxygen · doi:10.3390/oxygen2040030 · Cited by 406 · see citing works
“For example, the conjugation of GSH by the enzyme GST with xenobiotic compounds produces non-toxic products, which affects their detoxification [269].”
BackgroundContaminant-induced oxidative stress in fish: a mechanistic approach
Lushchak, V. I. (2015) · Fish Physiology and Biochemistry · doi:10.1007/s10695-015-0171-5 · Cited by 376 · see citing works
Self-citationGlutathione-Related Enzymes and Proteins: A Review
Vašková, J., Kočan, L., Vaško, L., & Perjési, P. (2023) · Molecules · doi:10.3390/molecules28031447 · Cited by 363 · see citing works
“As Lushchak [60] discussed, inhibition of glutathione reductase, phosphofructokinase, fatty acid synthase, or activation of fructose-1,6-bisphosphatase by CoASSG was shown.”
BackgroundJanaszak-Jasiecka, A., Płoska, A., Wierońska, J. M., Dobrucki, L. W., & Kalinowski, L. (2023) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-023-00423-2 · Cited by 358 · see citing works
“Glutathione is produced ubiquitously in eukaryotes, and its intracellular concentration is in the millimolar range [153].”
BackgroundClinical perspective on oxidative stress in sporadic amyotrophic lateral sclerosis
D’Amico, E., Factor-Litvak, P. R., Santella, R. M., & Mitsumoto, H. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.06.029 · Cited by 324 · see citing works
Targeting Glutamine Metabolism for Cancer Treatment
Choi, Y., & Park, K. (2017) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2017.178 · Cited by 321 · see citing works
“GSH can be regenerated from its oxidized form (GSSG), along with the conversion of NADPH to NADP+ (Gorrini et al., 2013).”
BackgroundChanges in Glutathione Content in Liver Diseases: An Update
Vairetti, M., Pasqua, L. G. D., Cagna, M., Richelmi, P., Ferrigno, A., & Berardo, C. (2021) · Antioxidants · doi:10.3390/antiox10030364 · Cited by 323 · see citing works
“From these considerations, it emerges that GSH cannot be considered a mere free radical scavenger but that it has a weighty role in the network governing the choice between survival, necrosis and apoptosis [9,10] as well as in cell signaling [10,11] and metabolism [3,12].”
BackgroundInfluentialRecent Progress in Bioconjugation Strategies for Liposome-Mediated Drug Delivery
Almeida, B., Nag, O. K., Rogers, K. E., & Delehanty, J. B. (2020) · Molecules · doi:10.3390/molecules25235672 · Cited by 299 · see citing works
“Utilization of the strong reducing conditions of the cellular cytosol, where glutathione (GSH) concentrations are 10 mM [45], has become a very effective way to mediate the release of drugs through the intracellular reduction of disulfide linkages.”
BackgroundNatasha, N., Shahid, M. A. R., Khalid, S., Bibi, I., Bundschuh, J., Niazi, N. K., & Dumat, C. (2019) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2019.134749 · Cited by 292 · see citing works
RetractedSadiq, I. Z. (2021) · Current Molecular Medicine · doi:10.2174/1566524022666211222161637 · Cited by 284 · see citing works
Oxidative Stress in Pulmonary Fibrosis
Otoupalova, E., Smith, S., Cheng, G., & Thannickal, V. J. (2020) · Comprehensive physiology · doi:10.1002/cphy.c190017 · Cited by 309 · see citing works
Mitochondria in Sepsis-Induced AKI
Sun, J., Zhang, J., Tian, J., Virzì, G. M., Digvijay, K., Bravo, L. C., Yin, Y., Rosner, M. H., & Ronco, C. (2019) · Journal of the American Society of Nephrology · doi:10.1681/asn.2018111126 · Cited by 262 · see citing works
The Necroptosis Adaptor RIPK3 Promotes Injury-Induced Cytokine Expression and Tissue Repair
Moriwaki, K., Balaji, S., McQuade, T. J., Malhotra, N., Kang, J., & Chan, F. K.-M. (2014) · Immunity · doi:10.1016/j.immuni.2014.09.016 · Cited by 251 · see citing works
Ashok, A., Andrabi, S. S., Mansoor, S., Kuang, Y., Kwon, B. K., & Labhasetwar, V. D. (2022) · Antioxidants · doi:10.3390/antiox11020408 · Cited by 262 · see citing works
“GSH can directly neutralize ROS and is an important factor in the xenobiotic metabolism [140].”
BackgroundThe Multifaceted Role of Glutathione S-Transferases in Health and Disease
Mazari, A. M. A., Zhang, L., Ye, Z., Zhang, J., Tew, K. D., & Townsend, D. M. (2023) · Biomolecules · doi:10.3390/biom13040688 · Cited by 247 · see citing works
Formaldehyde in brain: an overlooked player in neurodegeneration?
Tulpule, K., & Dringen, R. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12356 · Cited by 238 · see citing works
Mitochondrial Glutathione in Cellular Redox Homeostasis and Disease Manifestation
Chen, T., Wang, H., Chang, C.-J., & Lee, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25021314 · Cited by 243 · see citing works
“The dicarboxylate carrier and 2-oxoglutarate carrier were identified as the main transporters of GSH [65].”
BackgroundSrikanth, K., Pereira, E., Duarte, A. C., & Ahmad, I. (2013) · Environmental Science and Pollution Research · doi:10.1007/s11356-012-1459-y · Cited by 229 · see citing works
Soldevila‐Barreda, J. J., & Metzler‐Nolte, N. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00493 · Cited by 218 · see citing works
The mechanism of ferroptosis and its related diseases
Feng, S., Tang, D., Wang, Y., Li, X., Bao, H., Tang, C., Dong, X., Li, X., Yang, Q., Yan, Y., et al. (2023) · Molecular Biomedicine · doi:10.1186/s43556-023-00142-2 · Cited by 224 · see citing works
Metabolic cell death in cancer: ferroptosis, cuproptosis, disulfidptosis, and beyond
Mao, C., Wang, M., Zhuang, L., & Gan, B. (2024) · Protein & Cell · doi:10.1093/procel/pwae003 · Cited by 225 · see citing works
“Cysteine, in turn, serves as the essential precursor for the synthesis of glutathione (GSH), a tripeptide of paramount importance in maintaining redox homeostasis (Lushchak, 2012).”
BackgroundCopper signalling: causes and consequences
Kardos, J., Héja, L., Simon, Á., Jablonkai, I., Kovács, R., & Jemnitz, K. (2018) · Cell Communication and Signaling · doi:10.1186/s12964-018-0277-3 · Cited by 214 · see citing works
“Redox propensity of chelates between copper and pertinent peptides (tripeptide glutathione (γ-L-glutamyl-L-cysteinylglycine: GSH) [116, 117]; peptide fragments of matricellular calcium-binding glycoprotein (secreted protein, acidic and rich in cysteine: SPARC) Gly-His-Lys (GHK) (for a recent review see [118] and prote…”
Glutathione in Brain Disorders and Aging
Iskusnykh, I. Y., Zakharova, A. A., & Pathak, D. (2022) · Molecules · doi:10.3390/molecules27010324 · Cited by 213 · see citing works
“Redox reactions Neutralizes charges on ROS, RNS, and other reactive species [4]”
BackgroundTan, M., Yin, Y., Ma, X., Zhang, J., Pan, W., Tan, M., Zhao, Y., Yang, T., Jiang, T., & Li, H. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05645-y · Cited by 214 · see citing works
“Glutathione synthetase (GS) then catalyzes the combination of glycine residues and gammaglutamyl-cysteine to form GSH [31].”
BackgroundDNA damage by lipid peroxidation products: Implications in cancer, inflammation and autoimmunity
Gentile, F., Arcaro, A., Pizzimenti, S., Daga, M., Cetrangolo, G. P., Dianzani, C., Lepore, A., Graf, M., Ames, P. R. J., & Barrera, G. (2017) · AIMS Genetics · doi:10.3934/genet.2017.2.103 · Cited by 205 · see citing works
Optical imaging of localized chemical events using programmable diamond quantum nanosensors
Rendler, T., Neburková, J., Zemek, O., Kotek, J., Zappe, A., Chu, Z., Cígler, P., & Wrachtrup, J. (2017) · Nature Communications · doi:10.1038/ncomms14701 · Cited by 202 · see citing works
“Similarly, the intracellular GSH concentrations usually range from 0.5 to 10 mM, whereas extracellular values are almost three orders of magnitude lower 51 .”
InfluentialLushchak, O. V., Piroddi, M., Galli, F., & Lushchak, V. I. (2013) · Redox Report · doi:10.1179/1351000213y.0000000073 · Cited by 195 · see citing works
Self-citationCellular and subcellular oxidative stress parameters following severe spinal cord injury
Visavadiya, N. P., Patel, S. P., VanRooyen, J. L., Sullivan, P. G., & Rabchevsky, A. G. (2015) · Redox Biology · doi:10.1016/j.redox.2015.12.011 · Cited by 191 · see citing works
Redox Imbalance in Inflammation: The Interplay of Oxidative and Reductive Stress
Bellanti, F., Coda, A. R. D., Trecca, M. I., Buglio, A. L., Serviddio, G., & Vendemiale, G. (2025) · Antioxidants · doi:10.3390/antiox14060656 · Cited by 212 · see citing works
“The GSH/GSSG ratio is crucial for maintaining redox balance [67].”
The Glutathione System: A New Drug Target in Neuroimmune Disorders
Morris, G., Anderson, G., Dean, O. M., Berk, M., Gałecki, P., Martín-Subero, M., & Maes, M. H. J. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8705-x · Cited by 187 · see citing works
Rizvi, S. A. A., Einstein, G. P., Tulp, O. L., Sainvil, F., & Branly, R. (2022) · Biomolecules · doi:10.3390/biom12101442 · Cited by 181 · see citing works
“removal from the body, is of great physiological importance as it is produced from the metabolism of choline, methanol, sarcosine, xenobiotics, and methionine [91].”
BackgroundChromium(VI) Toxicity in Legume Plants: Modulation Effects of Rhizobial Symbiosis
Stambulska, U. Y., Bayliak, M. M., & Lushchak, V. I. (2018) · BioMed Research International · doi:10.1155/2018/8031213 · Cited by 178 · see citing works
“In particular, Cr can form highly stable complexes with organic compounds such as peptides (glutathione), carbohydrates (especially pentoses), NADH, FADH2, and possibly also organic acids, and these complexes are stored in vacuoles of root cells [37, 43].”
BackgroundSelf-citationVitamin C and Cardiovascular Disease: An Update
Morelli, M. B., Gambardella, J., Castellanos, V., Trimarco, V., & Santulli, G. (2020) · Antioxidants · doi:10.3390/antiox9121227 · Cited by 169 · see citing works
Cee, V. J., Volak, L. P., Chen, Y., Bartberger, M. D., Tegley, C. M., Arvedson, T., McCarter, J. D., Tasker, A. S., & Fotsch, C. H. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01018 · Cited by 164 · see citing works
Sexual dimorphism in glutathione metabolism and glutathione-dependent responses
Wang, L., Ahn, Y. J., & Asmis, R. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101410 · Cited by 159 · see citing works
Farokhnia, M., Azarkolah, A., Adinehfar, F., Khodaie-Ardakani, M.-R., Hosseini, S.-M.-R., Yekehtaz, H., Tabrizi, M., Rezaei, F., Salehi, B., Sadeghi, S.-M.-H., et al. (2013) · Clinical Neuropharmacology · doi:10.1097/wnf.0000000000000001 · Cited by 155 · see citing works
Dwivedi, D., Megha, K., Mishra, R., & Mandal, P. K. (2020) · Neurochemical Research · doi:10.1007/s11064-020-03030-1 · Cited by 154 · see citing works
Exercise-Induced Oxidative Stress and Dietary Antoxidative
Yavari, A., Javadi, M., Mirmiran, P., & Bahadoran, Z. (2015) · Asian Journal of Sports Medicine · doi:10.5812/asjsm.24898 · Cited by 156 · see citing works
Kung, H., Lin, K.-J., Kung, C., & Lin, T. (2021) · Biomedicines · doi:10.3390/biomedicines9080918 · Cited by 160 · see citing works
“Two molecules of GSH are oxidized into glutathione disulfide (GSSG) in order to eliminate H2O2 by GSH peroxidase (GPX) isozymes (GPX1 and GPX2) in the mitochondria [58,60].”
BackgroundInfluentialApproaches to the design of catalytic metallodrugs
Soldevila‐Barreda, J. J., & Sadler, P. J. (2015) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2015.01.024 · Cited by 152 · see citing works
Sappington, D. R., Siegel, E. R., Hiatt, G., Desai, A., Penney, R. B., Jamshidi-Parsian, A., Griffin, R. J., & Boysen, G. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.01.021 · Cited by 143 · see citing works
“Glutathione, the most abundant thiol-compound, (i) functions as an antioxidant, (ii) is a precursor for conjugation reactions, (iii) participates in maintenance of the cysteine pool and (iv) contributes to the regulation of cellular processes, including apoptosis [20].”
BackgroundThe role of glutathione redox imbalance in autism spectrum disorder: A review
Bjørklund, G., Tinkov, A. A., Hosnedlová, B., Kizek, R., Ajsuvakova, O. P., Chirumbolo, S., Геннадиевна, С. М., Peana, M., Dadar, M., El-Ansary, A. K., et al. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.07.017 · Cited by 150 · see citing works
Glutathione Participation in the Prevention of Cardiovascular Diseases
Matuz‐Mares, D., Riveros‐Rosas, H., Vilchis‐Landeros, M. M., & Vázquez‐Meza, H. (2021) · Antioxidants · doi:10.3390/antiox10081220 · Cited by 149 · see citing works
“It is four times more effective than GSH monoester [61].”
BackgroundManchope, M. F., Calixto-Campos, C., Coelho-Silva, L., Zarpelon, A. C., Pinho-Ribeiro, F. A., Georgetti, S. R., Baracat, M. M., Casagrande, R., & Verri, W. A., Jr. (2016) · PLoS ONE · doi:10.1371/journal.pone.0153015 · Cited by 147 · see citing works
“GSH is an important redox cellular system, with efficacy partly driven by the direct interactions of sulfhydryl groups (-SH) with ROS, thereby promoting a direct detox reaction [50].”
BackgroundGlutathione: Role in Oxidative/Nitrosative Stress, Antioxidant Defense, and Treatments
Raj, S. R., Bhattacharyya, C., Sarkar, A., Chakraborty, S., Sircar, E., Dutta, S., & Sengupta, R. (2021) · ChemistrySelect · doi:10.1002/slct.202100773 · Cited by 147 · see citing works
Labarrere, C. A., & Kassab, G. S. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.1007816 · Cited by 146 · see citing works
Potential Role of Sulfur-Containing Antioxidant Systems in Highly Oxidative Environments
Mukwevho, E., Ferreira, Z., & Ayeleso, A. O. (2014) · Molecules · doi:10.3390/molecules191219376 · Cited by 143 · see citing works
Smart Targeting To Improve Cancer Therapeutics
Morales‐Cruz, M., Delgado, Y., Castillo, B., Figueroa, C. M., Molina, A., Torres, A., Milián, M., & Griebenow, K. H. (2019) · Drug Design Development and Therapy · doi:10.2147/dddt.s219489 · Cited by 144 · see citing works
Zare, I., Chevrier, D. M., Cifuentes‐Rius, A., Moradi, N., Xianyu, Y., Ghosh, S., Trapiella‐Alfonso, L., Tian, Y., Shourangiz-Haghighi, A., Mukherjee, S., et al. (2021) · Materials Today · doi:10.1016/j.mattod.2020.10.027 · Cited by 138 · see citing works
miR-145 micelles mitigate atherosclerosis by modulating vascular smooth muscle cell phenotype
Chin, D. D., Poon, C. J., Wang, J., Joo, J., Ong, V., Jiang, Z., Cheng, K., Plotkin, A., Magee, G. A., & Chung, E. J. (2021) · Biomaterials · doi:10.1016/j.biomaterials.2021.120810 · Cited by 135 · see citing works
The Implication of Reactive Oxygen Species and Antioxidants in Knee Osteoarthritis
Tudorachi, N. B., Totu, E. E., Fifere, A., Ardeleanu, V., Mocanu, V., Mircea, C., Işıldak, İ., Smilkov, K., & Cărăușu, E. M. (2021) · Antioxidants · doi:10.3390/antiox10060985 · Cited by 135 · see citing works
“Nonenzymatic Antioxidants Comprise Compounds such as GSH, Carotenoids, Vitamin C, Vitamin E, or Coenzyme Q10 GSH- is an antioxidant of endogenous source; it is a tripeptide comprising amino acids such as glycine, L-glutamic acid, or L-cysteine [44].”
BackgroundImpact of Supplementary Amino Acids, Micronutrients, and Overall Diet on Glutathione Homeostasis
Gould, R. L., & Pazdro, R. (2019) · Nutrients · doi:10.3390/nu11051056 · Cited by 134 · see citing works
“It is synthesized from the amino acids glutamate, cysteine, and glycine, produced exclusively in the cytosol [2], and transported to other subcellular organelles, including mitochondria [3], endoplasmic reticulum [4], and the nucleus [5].”
BackgroundResponsive Nanocarriers as an Emerging Platform for Cascaded Delivery of Nucleic Acids to Cancer
Liu, Y., Xu, C., Iqbal, S., Yang, X., & Wang, J. (2017) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2017.03.004 · Cited by 130 · see citing works
“glutathione (GSH) in the cytoplasm [105] and high levels of reactive oxygen species [106].”
Antimicrobial Compounds in Food Packaging
Duda‐Chodak, A., Tarko, T., & Petka, K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032457 · Cited by 135 · see citing works
Moura, R. P., Martins, C., Pinto, S. F. T., Sousa, F., & Sarmento, B. F. C. C. (2019) · Expert Opinion on Drug Delivery · doi:10.1080/17425247.2019.1583205 · Cited by 127 · see citing works
Redox-sensitive nanoscale drug delivery systems for cancer treatment
Mirhadi, E., Mashreghi, M., Maleki, M. F., Alavizadeh, S. H., Arabi, L., Badiee, A., & Jaafari, M. R. (2020) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2020.119882 · Cited by 122 · see citing works
Streptococcus pneumoniae Uses Glutathione To Defend against Oxidative Stress and Metal Ion Toxicity
Potter, A. J., Trappetti, C., & Paton, J. C. (2012) · Journal of Bacteriology · doi:10.1128/jb.01393-12 · Cited by 123 · see citing works
Bhattacharjee, A., Chakraborty, K., & Shukla, A. (2017) · Metallomics · doi:10.1039/c7mt00066a · Cited by 121 · see citing works
Mons, E., Jansen, I., Loboda, J., van Doodewaerd, B. R., Hermans, J., Verdoes, M., Boeckel, C. V. V., van Veelen, P. V., Turk, B., Turk, D., et al. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b11027 · Cited by 96 · see citing works
“Glutathione (GSH), a tripeptide with a cellular concentration of 0.5 − 10 mM, 39 is a commonly used biological thiol to assess the risk of iodiosyncratic toxicity.”
InfluentialPotęga, A. (2022) · Molecules · doi:10.3390/molecules27165252 · Cited by 119 · see citing works
“, it has a direct impact on DNA biosynthesis and the related proliferation process [8].”
BackgroundInfluentialeIF4A supports an oncogenic translation program in pancreatic ductal adenocarcinoma
Chan, K., Robert, F., Oertlin, C., Kapeller-Libermann, D., Avizonis, D., Gutierrez, J., Handly-Santana, A., Doubrovin, M., Park, J., Schoepfer, C., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13086-5 · Cited by 106 · see citing works
Nonenzymatic Exogenous and Endogenous Antioxidants
Moussa, Z., Judeh, Z. M. A., & Ahmed, S. A. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.87778 · Cited by 123 · see citing works
Shahcheraghi, S. H., Salemi, F., Small, S., Syed, S., Salari, F., Alam, W., Cheang, W. S., Saso, L., & Khan, H. Z. (2023) · Phytotherapy Research · doi:10.1002/ptr.7754 · Cited by 116 · see citing works
“These findings may benefit the development of resveratrol in the prevention and intervention of human HCC (Bishayee, Barnes, Bhatia, Darvesh, & Carroll, 2010; Lushchak, 2012).”
BackgroundOxidative stress concept updated: Definitions, classifications and regulatory pathways implicated
Lushchak, V. I., & Storey, K. B. (2021) · EXCLI journal · doi:10.17179/excli2021-3596 · Cited by 124 · see citing works
“Sulfenic acid derivatives may be returned to their initial form by several reductases such as thioredoxin and glutaredoxin (Lushchak, 2012).”
BackgroundSelf-citationPasserieux, E., Hayot, M., Jaussent, A., Carnac, G., Gouzi, F., Pillard, F., Picot, M., Böcker, K. B. E., Hugon, G., Pincemail, J., et al. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.09.014 · Cited by 114 · see citing works
Pleiotropic effects of alpha-ketoglutarate as a potential anti-ageing agent
Bayliak, M. M., & Lushchak, V. I. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101237 · Cited by 115 · see citing works
Self-citationWong, C. Y. J., Al‐Salami, H., & Dass, C. R. (2020) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.13359 · Cited by 112 · see citing works
Mitochondrial Dysfunction and Kidney Stone Disease
Chaiyarit, S., & Thongboonkerd, V. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.566506 · Cited by 109 · see citing works
“GSSG can be reversed to mGSH by glutathione reductase that requires NADPH from the pentose phosphate pathway (Baudouin-Cornu et al., 2012; Lushchak, 2012; Bajic et al., 2019).”
BackgroundZhang, T., Hu, Y., Tang, M. X., Kong, L., Ying, J., Wu, T., Xue, Y., & Pu, Y. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161023279 · Cited by 107 · see citing works
“Meanwhile, the liver is an important biosynthetic organ where ROS are produced in substantial amounts as side products of energy production in the mitochondrial electron transport chain or as the result of biosyntheses involving diverse oxygenases [34].”
BackgroundUllah, S., Li, Z., Hasan, Z., Khan, S. U., & Fahad, S. (2018) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2018.06.002 · Cited by 107 · see citing works
Nuhu, F., Gordon, A. D., Sturmey, R. G., Seymour, A. L., & Bhandari, S. (2020) · Molecules · doi:10.3390/molecules25184196 · Cited by 105 · see citing works
“GSH is synthesised de novo from glutamate, cysteine and glycine [13] with a γ-carboxyl linkage between glutamate and cysteine of GSH, which is only susceptible to hydrolysis by γ glutamyltranspeptidase, [14] rather than the usual α-carboxyl group.”
BackgroundThe Universal Soldier: Enzymatic and Non-Enzymatic Antioxidant Functions of Serum Albumin
Belinskaia, D. A., Voronina, P. A., Shmurak, V. I., Vovk, M. A., Batalova, A. A., Jenkins, R. O., & Goncharov, N. V. (2020) · Antioxidants · doi:10.3390/antiox9100966 · Cited by 105 · see citing works
“5) oxidise their substrates to organic acids using GSH as a coenzyme [43].”
MethodItsumi, M., Inoue, S., Elia, A., Murakami, K., Sasaki, M., Lind, E. F., Brenner, D., Harris, I. S., Chio, I. I. C., Afzal, S., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.38 · Cited by 106 · see citing works
Amine, R. E., Germini, D., Zakharova, V., Tsfasman, T., Sheval, E. V., Louzada, R. A. N., Dupuy, C., Bilhou‐Nabera, C., Hamadé, A., Najjar, F., et al. (2017) · Redox Biology · doi:10.1016/j.redox.2017.11.024 · Cited by 104 · see citing works
Amino acids and the regulation of oxidative stress and immune function in dairy cattle
Coleman, D. N., Lopreiato, V., Alharthi, A. S., & Loor, J. J. (2020) · Journal of Animal Science · doi:10.1093/jas/skaa138 · Cited by 104 · see citing works
Liang, C., Zheng, D., Lee, Y. H., Chan, T. K., Kumar, Y., Ho, W. E., Chen, J. Z., Tannenbaum, S. R., & Ong, C. N. (2016) · Scientific Reports · doi:10.1038/srep26076 · Cited by 99 · see citing works
How to Increase Cellular Glutathione
Giustarini, D., Milzani, A., Dalle‐Donne, I., & Rossi, R. (2023) · Antioxidants · doi:10.3390/antiox12051094 · Cited by 99 · see citing works
“The most important chemical functionality of GSH is its cysteinyl moiety, which can act as a radical scavenger and reducing agent via its sulfhydryl group (SH) or participate in detoxification reactions through its addition to the electrophilic center of xenobiotics [1].”
BackgroundThe Role of microRNAs in Metabolic Syndrome-Related Oxidative Stress
Włodarski, A., Strycharz, J., Wróblewski, A. M., Kasznicki, J., Drzewoski, J., & Śliwińska, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186902 · Cited by 99 · see citing works
“, glyoxalases) along with reducing, and thus, regenerating vast antioxidants such as vitamins C and E [41,42].”
BackgroundMetal- and metalloid-based compounds to target and reverse cancer multidrug resistance
Valente, A., Podolski-Renić, A., Poetsch, I., Filipović, N. R., López, Ó., Turel, I., & Heffeter, P. (2021) · Drug Resistance Updates · doi:10.1016/j.drup.2021.100778 · Cited by 98 · see citing works
Hashem, H. A. (2013) · Botany · doi:10.1139/cjb-2013-0164 · Cited by 98 · see citing works
The Biochemistry and Effectiveness of Antioxidants in Food, Fruits, and Marine Algae
Pruteanu, L.-L., Bailey, D. S., Grădinaru, A. C., & Jäntschi, L. (2023) · Antioxidants · doi:10.3390/antiox12040860 · Cited by 114 · see citing works
“It is mainly synthesized by the body [88], and it can increase the level of cytotoxic T cells in lymphocytes and neutralize free radicals [89,90].”
Background
- Authors
- Lushchak, V. I.
- Affiliations
- Vasyl Stefanyk Carpathian National University (UA)
- Corresponding author
- Lushchak, Volodymyr I.
- Venue
- Journal of Amino Acids
- Publisher
- Wiley
- Published
- 2012-02-28
- Volume
- 2012
- Pages
- 1-26
- ISSN
- 2090-0104 (ISSN-L)
- 2090-0112
- PMC
- PMC3303626
- OpenAlex
- W2043037824
- Cited by
- 1,266
- References
- 283
- Citations by year
- 2026: 70 · 2025: 117 · 2024: 119 · 2023: 126 · 2022: 125 · 2021: 131 · 2020: 110 · 2019: 79 · 2018: 76 · 2017: 93 · 2016: 64 · 2015: 64 · 2014: 52 · 2013: 29 · 2012: 7
- FWCI
- 20.84
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Journal of Amino Acids (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Ministry of Education and Science of Ukraine (0106U002245)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- glutathione, glutathione homeostasis, reactive oxygen species, reactive nitrogen species, glutathione synthesis, glutathione metabolism, metal homeostasis, glutathionylation, sulfhydryl groups, phytochemicals, disease pathology
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