Glutathione: Antioxidant Properties Dedicated to Nanotechnologies
Open accessAbstract
Which scientist has never heard of glutathione (GSH)? This well-known low-molecular-weight tripeptide is perhaps the most famous natural antioxidant. However, the interest in GSH should not be restricted to its redox properties. This multidisciplinary review aims to bring out some lesser-known aspects of GSH, for example, as an emerging tool in nanotechnologies to achieve targeted drug delivery. After recalling the biochemistry of GSH, including its metabolism pathways and redox properties, its involvement in cellular redox homeostasis and signaling is described. Analytical methods for the dosage and localization of GSH or glutathiolated proteins are also covered. Finally, the various therapeutic strategies to replenish GSH stocks are discussed, in parallel with its use as an addressing molecule in drug delivery.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Glutathione is a natural tripeptide (γ-l-glutamyl-l-cysteinylglycine) with a fundamental role in the regulation of redox homeostasis.
“Glutathione is a natural tripeptide, that is γ-l-glutamyl-l-cysteinylglycine, harbouring a fundamental role in the regulation of redox homeostasis [176].”
From The Role of Antioxidants in the Interplay between Oxidative Stress and Senescence (2022) · cites this paper as [176]
Both GSH levels and the GSH/GSSG ratio are tightly controlled through regulation of synthesis, metabolism, transport, and degradation.
“Being the main intracellular antioxidant buffer, both the levels of GSH and GSH/GSSH ratio are tightly controlled through a fine regulation of their synthesis, metabolism, transport, and degradation [176,177].”
From The Role of Antioxidants in the Interplay between Oxidative Stress and Senescence (2022) · cites this paper as [176]
GSH levels can be used as a biomarker for the oxidative status of the cell.
“As GSH levels can be used as a biomarker for the oxidative status of the cell [176,181,182,183]”
From The Role of Antioxidants in the Interplay between Oxidative Stress and Senescence (2022) · cites this paper as [176]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
The pathogenesis of atherosclerosis: a perspective for the 1990s
Ross, R. (1993) · Nature · doi:10.1038/362801a0 · Cited by 10,618 · see citing works
Improved method for the determination of blood glutathione.
Beutler, E., Duron, O., & KELLY, B. M. (1963) · PubMed · Cited by 6,932 · see citing works
Tietze, F. (1969) · Analytical Biochemistry · doi:10.1016/0003-2697(69)90064-5 · Cited by 6,077 · see citing works
Meister, A., & Anderson, M. E. (1983) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.52.070183.003431 · Cited by 5,694 · see citing works
Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587 · see citing works
Glutathione: overview of its protective roles, measurement, and biosynthesis
Forman, H. J., Zhang, H., & Rinna, A. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.08.006 · Cited by 2,636 · see citing works
TNF-mediated inflammatory disease
Bradley, Jr. (2008) · The Journal of Pathology · doi:10.1002/path.2287 · Cited by 2,094 · see citing works
The role of oxidized lipoproteins in atherogenesis
Berliner, J. A., & Heinecke, J. W. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)02173-6 · Cited by 1,365 · see citing works
Dual and multi-stimuli responsive polymeric nanoparticles for programmed site-specific drug delivery
Cheng, R., Meng, F., Deng, C., Klok, H., & Zhong, Z. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.01.084 · Cited by 1,356 · 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
Assessment of stress during handling and transport.
Grandin, T. (1997) · Journal of Animal Science · doi:10.2527/1997.751249x · Cited by 1,151 · see citing works
Cellular glutathione and thiols metabolism
Dickinson, D. A., & Forman, H. J. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01172-3 · Cited by 852 · see citing works
Glutathione and Related γ-Glutamyl Compounds: Biosynthesis and Utilization
Meister, A., & Tate, S. S. (1976) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.45.070176.003015 · Cited by 839 · see citing works
Levin, V. A. (1980) · Journal of Medicinal Chemistry · doi:10.1021/jm00180a022 · Cited by 815 · 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
Dual Redox Responsive Assemblies Formed from Diselenide Block Copolymers
Ma, N., Li, Y., Xu, H., Wang, Z., & Zhang, X. (2009) · Journal of the American Chemical Society · doi:10.1021/ja908124g · Cited by 722 · see citing works
Glutathione deficiency is associated with impaired survival in HIV disease
Herzenberg, L. A., Rosa, S. C. D., Dubs, J. G., Roederer, M., Anderson, M. T., Ela, S. W., Deresinski, S. C., & Herzenberg, L. A. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.5.1967 · Cited by 672 · see citing works
Schmidt, A. M., Hori, O., Brett, J., Yan, S. D., Wautier, J., & Stern, D. (1994) · Arteriosclerosis and Thrombosis A Journal of Vascular Biology · doi:10.1161/01.atv.14.10.1521 · Cited by 636 · see citing works
The Chemistry of the Sulfur–Gold Interface: In Search of a Unified Model
Pensa, E., Cortés, E., Corthey, G., et al. (2012) · Accounts of Chemical Research · doi:10.1021/ar200260p · Cited by 559 · see citing works
Mansoor, M. A., Svardal, A. M., & Ueland, P. M. (1992) · Analytical Biochemistry · doi:10.1016/0003-2697(92)90456-h · Cited by 505 · 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
Nagy, P. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4973 · Cited by 488 · see citing works
Ghosh, P., Kim, C., Han, G., Forbes, N. S., & Rotello, V. (2008) · ACS Nano · doi:10.1021/nn800507t · Cited by 431 · see citing works
Jones, D. P., Mody, V. C., Carlson, J. L., Lynn, M. J., & Sternberg, P. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01040-7 · Cited by 392 · see citing works
Pineda‐Molina, E., Klatt, P., Vázquez, J., Marina, A., de Lacoba, M. G., Pérez‐Sala, D., & Lamas, S. (2001) · Biochemistry · doi:10.1021/bi011459o · Cited by 389 · see citing works
Glutathione monoethyl ester: Preparation, uptake by tissues, and conversion to glutathione
Anderson, M. E., Powrie, F. M., Puri, R. N., & Meister, A. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90723-4 · Cited by 353 · see citing works
Cellular thiols and redox-regulated signal transduction
Sen, C. K. (2001) · Current topics in cellular regulation · doi:10.1016/s0070-2137(01)80001-7 · Cited by 345 · see citing works
Pharmacokinetics of N-acetylcysteine in man
Borgstr�m, L., K�gedal, B., & Paulsen, O. (1986) · European Journal of Clinical Pharmacology · doi:10.1007/bf00606662 · Cited by 343 · see citing works
Mungrue, I. N., Pagnon, J. C., Omid Kohannim, A., Gargalovic, P. S., & Lusis, A. J. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.182.1.466 · Cited by 336 · see citing works
Glutathione and modulation of cell apoptosis
Circu, M. L., & Aw, T. Y. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.06.019 · Cited by 333 · see citing works
Elevation of Glutathione as a Therapeutic Strategy in Alzheimer Disease
Pocernich, C., & Butterfield, D. (2011) · Biochimica et Biophysica Acta · doi:10.1016/j.bbadis.2011.10.003 · Cited by 333 · see citing works
Plasma membrane glutathione transporters and their roles in cell physiology and pathophysiology
Ballatori, N., Krance, S. M., Marchan, R., & Hammond, C. L. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.08.004 · Cited by 318 · see citing works
Glutathione—a review on its role and significance in Parkinson's disease
Martin, H. L., & Teismann, P. (2009) · The FASEB Journal · doi:10.1096/fj.08-125443 · Cited by 314 · 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
The systemic availability of oral glutathione
Witschi, A. T., Reddy, S. K., Stofer, B., & Lauterburg, B. H. (1992) · European Journal of Clinical Pharmacology · doi:10.1007/bf02284971 · Cited by 274 · see citing works
Gaillard, P. J., Appeldoorn, C. C. M., Dorland, R., van Kregten, J., Manca, F., Vugts, D. J., Windhorst, A. D., van Dongen, G. A. M. S., de Vries, H. E., Maussang, D., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0082331 · Cited by 273 · see citing works
Hanigan, M. H. (2014) · Advances in cancer research · doi:10.1016/b978-0-12-420117-0.00003-7 · Cited by 271 · 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
Pharmacokinetics of metallic nanoparticles
Lin, Z., Monteiro-Riviere, N. A., & Riviere, J. E. (2014) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1304 · Cited by 260 · see citing works
Bioreducible Polymers for Gene Silencing and Delivery
Son, S., Namgung, R., Kim, J., et al. (2011) · Accounts of Chemical Research · doi:10.1021/ar200248u · Cited by 248 · see citing works
Grinberg, L. N., Fibach, E., Amer, J., & Atlas, D. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.09.025 · Cited by 236 · see citing works
Glutamate Cysteine Ligase Catalysis
Chen, Y., Shertzer, H. G., Schneider, S. N., Nebert, D. W., & Dalton, T. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504604200 · Cited by 234 · see citing works
Glutathione redox imbalance in brain disorders
Gu, F., Chauhan, V. P. S., & Chauhan, A. (2014) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000134 · Cited by 233 · see citing works
Burford, N., Eelman, M. D., Mahony, D. E., et al. (2002) · Chemical Communications · doi:10.1039/b210570e · Cited by 229 · see citing works
Vascular endothelium: an integrator of pathophysiologic stimuli in atherosclerosis.
Gimbrone, M. A. (1995) · The American Journal of Cardiology · doi:10.1016/0002-9149(95)80016-l · Cited by 225 · see citing works
Polavarapu, L., Manna, M., & Xu, Q. (2010) · Nanoscale · doi:10.1039/c0nr00458h · Cited by 221 · see citing works
Redox regulation of the G1 to S phase transition in the mouse embryo fibroblast cell cycle.
Menon, S. G., Sarsour, E. H., Spitz, D. R., Higashikubo, R., Sturm, M. T., Zhang, H., & Goswami, P. C. (2003) · PubMed · Cited by 218 · see citing works
Kumar, A., Tikoo, S., Maity, S., Sengupta, S., Sengupta, S., Kaur, A., & Bachhawat, A. K. (2012) · EMBO Reports · doi:10.1038/embor.2012.156 · Cited by 213 · see citing works
In vivo toxicity, biodistribution, and clearance of glutathione-coated gold nanoparticles
Simpson, C. A., Salleng, K. J., Cliffel, D. E., & Feldheim, D. L. (2012) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2012.06.002 · Cited by 202 · see citing works
Neuschwander‐Tetri, B. A., & Roll, F. J. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90121-8 · Cited by 201 · see citing works
Mandal, P. K., Tripathi, M., & Sugunan, S. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.11.047 · Cited by 199 · see citing works
Zhang, Z., Jia, J. T., Lai, Y., Ma, Y., Weng, J., & Sun, L. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.06.045 · Cited by 199 · see citing works
Paolicchi, A., Minotti, G., Tonarelli, P., Tongiani, R., Cesare, D. D., Mezzetti, A., Dominici, S., Comporti, M., & Alfonso Pompella, C. (1999) · PubMed · Cited by 197 · see citing works
Glutathione catabolism as a signaling mechanism
Paolicchi, A., Dominici, S., Pieri, L., Maellaro, E., & Alfonso Pompella, C. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01173-5 · Cited by 194 · see citing works
Gaillard, P. J., Appeldoorn, C. C. M., Rip, J., Dorland, R., van der Pol, S. M. A., Kooij, G., de Vries, H. E., & Reijerkerk, A. (2012) · Journal of Controlled Release · doi:10.1016/j.jconrel.2012.06.022 · Cited by 191 · see citing works
Evidence for carrier-mediated transport of glutathione across the blood-brain barrier in the rat.
Kannan, R., Kuhlenkamp, J., Jeandidier, É., Trinh, H., Ookhtens, M., & Kaplowitz, N. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114666 · Cited by 165 · see citing works
Rocha, C. R. R., Garcia, C. C. M., Vieira, D. B., Quinet, A., de Andrade-Lima, L. C., Munford, V., Belizário, J. E., & Menck, C. F. M. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.465 · Cited by 163 · see citing works
“Molecular Beacon”-Based Fluorescent Assay for Selective Detection of Glutathione and Cysteine
Xu, H., & Hepel, M. (2011) · Analytical Chemistry · doi:10.1021/ac102850y · Cited by 163 · see citing works
Beqa, L., Singh, A. K., Khan, S. A., et al. (2011) · ACS Applied Materials & Interfaces · doi:10.1021/am101118h · Cited by 162 · see citing works
The Incomplete Glutathione Puzzle: Just Guessing at Numbers and Figures?
Deponte, M. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7123 · Cited by 154 · see citing works
Trapani, A., Lopedota, A. A., Franco, M., et al. (2010) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2010.01.010 · Cited by 153 · see citing works
Rotman, M., Welling, M. M., Bunschoten, A., de Backer, M. E., Rip, J., Nabuurs, R. J. A., Gaillard, P. J., van Buchem, M. A., van der Maarel, S. M., & van der Weerd, L. (2015) · Journal of Controlled Release · doi:10.1016/j.jconrel.2015.02.012 · Cited by 152 · see citing works
Drożdż, R., Parmentier, C., Hachad, H., Leroy, P., Siest, G., & Wellman, M. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00127-0 · Cited by 151 · see citing works
Self-citationRip, J., Chen, L., Hartman, R., van den Heuvel, A., Reijerkerk, A., van Kregten, J., van der Boom, B. G., Appeldoorn, C. C. M., de Boer, M., Maussang, D., et al. (2014) · Journal of drug targeting · doi:10.3109/1061186x.2014.888070 · Cited by 149 · see citing works
Reversible 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
Brain-targeted delivery of paclitaxel using glutathione-coated nanoparticles for brain cancers
Geldenhuys, W. J., Mbimba, T., Bui, T., Harrison, K. A., & Sutariya, V. B. (2011) · Journal of drug targeting · doi:10.3109/1061186x.2011.589435 · Cited by 144 · see citing works
Competition of van der Waals and chemical forces on gold–sulfur surfaces and nanoparticles
Reimers, J. R., Ford, M. J., Marcuccio, S. M., Ulstrup, J., & Hush, N. S. (2017) · Nature Reviews Chemistry · doi:10.1038/s41570-017-0017 · Cited by 142 · 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
Characterization of the extracellular γ‐glutamyl transpeptidases, GGT1 and GGT2, in Arabidopsis
Ohkama‐Ohtsu, N., Radwan, S., Peterson, A. G., et al. (2007) · The Plant Journal · doi:10.1111/j.1365-313x.2006.03004.x · Cited by 136 · see citing works
γ‐Glutamyl Transpeptidase: Catalytic Mechanism and Gene Expression
Taniguchi, N., & Ikeda, Y. (1998) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123188.ch7 · Cited by 127 · see citing works
Inhibition of caspase-3 activity and activation by protein glutathionylation
Huang, Z., Pinto, J. T., Deng, H., & Richie, J. P. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.02.026 · Cited by 125 · see citing works
Birngruber, T., Raml, R., Gladdines, W., Gatschelhofer, C., Gander, E., Ghosh, A., Altendorfer‐Kroath, T., Gaillard, P. J., Pieber, T. R., & Sinner, F. M. (2014) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.23994 · Cited by 122 · see citing works
Bhattacharjee, A., Chakraborty, K., & Shukla, A. (2017) · Metallomics · doi:10.1039/c7mt00066a · Cited by 121 · see citing works
Stimuli‐Responsive Polymeric Nanoparticles
Liu, X., Yang, Y., & Urban, M. W. (2017) · Macromolecular Rapid Communications · doi:10.1002/marc.201700030 · Cited by 117 · see citing works
Baldelli, S., Aquilano, K., & Ciriolo, M. R. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.04.006 · Cited by 115 · see citing works
Rapid Activation of Glutamate Cysteine Ligase following Oxidative Stress
Krejsa, C. M., Franklin, C. C., White, C. C., Ledbetter, J. A., Schieven, G. L., & Kavanagh, T. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.116210 · Cited by 111 · see citing works
Assay of Biothiols by Regulating the Growth of Silver Nanoparticles with C-Dots as Reducing Agent
Shen, L., Chen, Q., Sun, Z.-Y., Chen, X., & Wang, J. (2014) · Analytical Chemistry · doi:10.1021/ac500601k · Cited by 109 · see citing works
Investigating the Causes for Decreased Levels of Glutathione in Individuals with Type II Diabetes
Lagman, M., Ly, J., Saing, T., Singh, M., Tudela, E. V., Morris, D., Chi, P.-T., Ochoa, C., Sathananthan, A., & Venketaraman, V. (2015) · PLoS ONE · doi:10.1371/journal.pone.0118436 · Cited by 108 · see citing works
Patel, S. P., Sullivan, P. G., Pandya, J. D., et al. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2014.04.026 · Cited by 108 · see citing works
Glutathione metabolism in sepsis
Biolo, G., Antonione, R., & Cicco, M. D. (2007) · Critical Care Medicine · doi:10.1097/01.ccm.0000278913.19123.13 · Cited by 105 · see citing works
Kannan, R., Chakrabarti, R., Tang, D., Kim, K. J., & Kaplowitz, N. (2000) · Brain Research · doi:10.1016/s0006-8993(99)02184-8 · Cited by 99 · see citing works
Redox-responsive theranostic nanoplatforms based on inorganic nanomaterials
Han, L., Zhang, X., Wang, Y., Li, X., Yang, X., Huang, M., Hu, K., Li, L., & Wei, Y. (2017) · Journal of Controlled Release · doi:10.1016/j.jconrel.2017.03.018 · Cited by 99 · see citing works
Hopkins, F. G., & Dixon, M. (1922) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)85719-2 · Cited by 98 · see citing works
ChaC2, an Enzyme for Slow Turnover of Cytosolic Glutathione
Kaur, A., Gautam, R., Srivastava, R., Chandel, A., Kumar, A., Karthikeyan, S., & Bachhawat, A. K. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.727479 · Cited by 97 · see citing works
Giustarini, D., Milzani, A., Dalle‐Donne, I., et al. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.09.010 · Cited by 96 · see citing works
Menon, S. G., Sarsour, E. H., Kalen, A. L., Venkataraman, S., Hitchler, M. J., Domann, F. E., Oberley, L. W., & Goswami, P. C. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0225 · Cited by 96 · see citing works
Protein Glutathionylation in Cardiovascular Diseases
Pastore, A., & Piemonte, F. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms141020845 · Cited by 94 · see citing works
Maussang, D., Rip, J., van Kregten, J., van den Heuvel, A., van der Pol, S. M. A., van der Boom, B. G., Reijerkerk, A., Chen, L., de Boer, M., Gaillard, P. J., et al. (2016) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2016.09.003 · Cited by 88 · see citing works
Conour, J. E., Graham, W., & Gaskins, H. (2004) · Physiological Genomics · doi:10.1152/physiolgenomics.00058.2004 · Cited by 86 · see citing works
Engineering triiodothyronine (T3) nanoparticle for use in ischemic brain stroke
Mdzinarishvili, A., Sutariya, V. B., Talasila, P. K., et al. (2012) · Drug Delivery and Translational Research · doi:10.1007/s13346-012-0117-8 · Cited by 84 · see citing works
Park, S. K., Boulton, R. B., & Noble, A. C. (2000) · Food Chemistry · doi:10.1016/s0308-8146(99)00227-7 · Cited by 83 · see citing works
Fabrication of basil seed gum nanoparticles as a novel oral delivery system of glutathione
Naji‐Tabasi, S., Razavi, S. M. A., & Mehditabar, H. (2016) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2016.11.052 · Cited by 83 · see citing works
Glutathione monoethyl ester provides neuroprotection in a rat model of stroke
Anderson, M. F., Nilsson, M., Eriksson, P. S., et al. (2003) · Neuroscience Letters · doi:10.1016/j.neulet.2003.09.067 · Cited by 82 · see citing works
Williams, S. R., Lepene, B. S., Thatcher, C. D., & Long, T. E. (2008) · Biomacromolecules · doi:10.1021/bm801058j · Cited by 81 · see citing works
Parmentier, C., Leroy, P., Wellman, M., et al. (1998) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(98)00414-9 · Cited by 81 · see citing works
Self-citationZarka, M. H., & Bridge, W. J. (2017) · Redox Biology · doi:10.1016/j.redox.2017.01.014 · Cited by 79 · see citing works
Mena, S., Benlloch, M., Ortega, Á., Carretero, J., Obrador, E., Asensi, M. A., Petschen, I., Brown, B. D., & Estrela, J. M. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-2642 · Cited by 78 · see citing works
Baek, M., Choy, J., & Choi, S. (2012) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2012.01.015 · Cited by 78 · see citing works
Prooxidant Reactions Promoted by Soluble and Cell‐Bound γ‐Glutamyltransferase Activity
Dominici, S., Paolicchi, A., Corti, A., et al. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)01029-3 · Cited by 77 · see citing works
Comparative efficacies of 2 cysteine prodrugs and a glutathione delivery agent in a colitis model
Oz, H. S., Chen, T. S., & Nagasawa, H. T. (2007) · Translational research · doi:10.1016/j.trsl.2006.12.010 · Cited by 77 · see citing works
Serru, V., Baudin, B., Ziegler, F., et al. (2001) · Clinical Chemistry · doi:10.1093/clinchem/47.7.1321 · Cited by 75 · see citing works
Stimuli-Responsive Block Copolymer-Based Assemblies for Cargo Delivery and Theranostic Applications
Yin, J., Chen, Y., Zhang, Z., & Han, X. H. (2016) · Polymers · doi:10.3390/polym8070268 · Cited by 75 · see citing works
S-Adenosyl-l-methionine and alcoholic liver disease in animal models
Lieber, C. S. (2002) · Alcohol · doi:10.1016/s0741-8329(02)00230-6 · Cited by 74 · see citing works
Elimination of Ehrlich tumours by ATP-induced growth inhibition, glutathione depletion and X-rays
Estrela, J. M., Obrador, E., Navarro, J., et al. (1995) · Nature Medicine · doi:10.1038/nm0195-84 · Cited by 74 · see citing works
Trapani, A., Laquintana, V., Denora, N., Lopedota, A. A., Cutrignelli, A., Franco, M., Trapani, G., & Liso, G. (2006) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2006.10.003 · Cited by 72 · see citing works
Brain-Targeted Delivery of Docetaxel by Glutathione-Coated Nanoparticles for Brain Cancer
Grover, A., Hirani, A., Pathak, Y. V., & Sutariya, V. B. (2014) · AAPS PharmSciTech · doi:10.1208/s12249-014-0165-0 · Cited by 68 · see citing works
Recent Advances in Redox Active Plant and Microbial Products
Burkholz, T., Winyard, P. G., Slusarenko, A. J., Kirsch, G., & Jacob, C. (2014) · Springer eBooks · doi:10.1007/978-94-017-8953-0 · Cited by 68 · see citing works
Pitfalls of assays devoted to evaluation of oxidative stress induced by inorganic nanoparticles
Tournebize, J., Sapin‐Minet, A., Bartosz, G., Leroy, P., & Boudier, A. (2013) · Talanta · doi:10.1016/j.talanta.2013.07.077 · Cited by 67 · see citing works
Self-citationCrossing the blood-brain barrier: Glutathione-conjugated poly(ethylene imine) for gene delivery
Englert, C., Trützschler, A., Raasch, M., Buś, T., Borchers, P., Mosig, A. S., Traeger, A., & Schubert, U. S. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2016.08.039 · Cited by 67 · see citing works
Chen, Z., Wang, Z., Chen, J., Wang, S., & Huang, X. (2012) · The Analyst · doi:10.1039/c2an35405e · Cited by 64 · see citing works
Shen, C., Tseng, W., & Hsieh, M. (2008) · Journal of Chromatography A · doi:10.1016/j.chroma.2008.11.044 · Cited by 63 · see citing works
Evidence for Transcapillary Transport of Reduced Glutathione in Vascular Perfused Guinea-Pig Brain
Zloković, B. V., Mačkić, J. B., McComb, J. G., Weiss, M. H., Kaplowitz, N., & Kannan, R. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1715 · Cited by 63 · see citing works
Brain-targeted delivery of doxorubicin using glutathione-coated nanoparticles for brain cancers
Geldenhuys, W. J., Wehrung, D., Groshev, A., Hirani, A., & Sutariya, V. B. (2014) · Pharmaceutical Development and Technology · doi:10.3109/10837450.2014.892130 · Cited by 63 · see citing works
Assessment of the genotoxic risk from laxative senna products
Brusick, D., & Mengs, U. (1997) · Environmental and Molecular Mutagenesis · doi:10.1002/(sici)1098-2280(1997)29:1 · Cited by 59 · see citing works
Label-free colorimetric detection of biothiols utilizing SAM and unmodified Au nanoparticles
Li, Z., Zheng, X., Zhang, L., Liang, R., Li, Z., & Qiu, J. (2015) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2015.01.062 · Cited by 59 · see citing works
Tortiglione, C., Quarta, A., Tino, A., et al. (2007) · Bioconjugate Chemistry · doi:10.1021/bc060355t · Cited by 57 · see citing works
Impact of gold nanoparticle coating on redox homeostasis
Tournebize, J., Boudier, A., Joubert, O., et al. (2012) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2012.07.026 · Cited by 56 · see citing works
Self-citationSinha, P. K., Hütter, G., Köttgen, E., Dietel, M., Schadendorf, D., & Lage, H. (1999) · Electrophoresis · doi:10.1002/(sici)1522-2683(19991001)20:14 · Cited by 55 · see citing works
Zampagni, M., Wright, D., Cascella, R., D’Adamio, G., Casamenti, F., Evangelisti, E., Cardona, F., Goti, A., Nacmias, B., Sorbi, S., et al. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.01.012 · Cited by 54 · see citing works
Rosenblat, M., Volkova, N., Coleman, R., & Aviram, M. (2007) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2007.05.012 · Cited by 53 · see citing works
Nutritional and hormonal regulation of glutathione homeostasis
Taylor, C. G., Nagy, L. E., & Bray, T. Μ. (1996) · Current topics in cellular regulation · doi:10.1016/s0070-2137(96)80007-0 · Cited by 52 · see citing works
Raval, N. J., Mistry, T., Acharya, N. S., & Acharya, S. R. (2015) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.12460 · Cited by 52 · see citing works
Tournebize, J., Boudier, A., Sapin‐Minet, A., et al. (2012) · ACS Applied Materials & Interfaces · doi:10.1021/am3012752 · Cited by 51 · see citing works
Self-citationHuang, G. G., Hossain, M. K., Han, X. X., et al. (2009) · The Analyst · doi:10.1039/b914976g · Cited by 50 · see citing works
Straightforward Method To Quantify GSH, GSSG, GRP, and Hydroxycinnamic Acids in Wines by UPLC-MRM-MS
Vallverdú‐Queralt, A., Verbaere, A., Meudec, E., et al. (2014) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf504383g · Cited by 46 · see citing works
Belcastro, E., Gaucher, C., Corti, A., Leroy, P., Lartaud, I., & Alfonso Pompella, C. (2017) · Biological Chemistry · doi:10.1515/hsz-2017-0150 · Cited by 46 · see citing works
Self-citationPiccoli, G., Fiorani, M., Biagiarelli, B., Palma, F., Potenza, L., Amicucci, A., & Stocchi, V. (1994) · Journal of Chromatography A · doi:10.1016/0021-9673(94)80465-6 · Cited by 45 · see citing works
Recent Advances in Nanomaterial Probes for Optical Biothiol Sensing: A Review
Tsogas, G. Z., Kappi, F. A., Vlessidis, A. G., & Giokas, D. L. (2017) · Analytical Letters · doi:10.1080/00032719.2017.1329833 · Cited by 44 · see citing works
Mandracchia, D., Denora, N., Franco, M., Pitarresi, G. L., Giammona, G., & Trapani, G. (2010) · Journal of Biomaterials Science Polymer Edition · doi:10.1163/092050609x12609582084086 · Cited by 42 · see citing works
Gaillard, P. J., Kerklaan, B. M., Aftimos, P. G., et al. (2014) · Cancer Research · doi:10.1158/1538-7445.am2014-ct216 · Cited by 39 · see citing works
Belcastro, E., Wu, W., Fries, I., et al. (2017) · Nitric Oxide · doi:10.1016/j.niox.2017.07.004 · Cited by 38 · see citing works
Hunter, G., & Eagles, B. A. (1927) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)84368-x · Cited by 37 · see citing works
Preparation, Characteristics, and Stability of Glutathione-Loaded Nanoparticles
Koo, S. H., Lee, J.-S., Kim, G., et al. (2011) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf2024648 · Cited by 36 · see citing works
Brandsma, D., Kerklaan, B. M., Dieras, V. C., Altıntaş, S., Anders, C. K., Ballester, M. A., Gelderblom, H. A. J., Soetekouw, P. M. M. B., Gladdines, W., Lonnqvist, F., et al. (2014) · Annals of Oncology · doi:10.1093/annonc/mdu331.32 · Cited by 35 · see citing works
Mucoadhesive polymers-based film as a carrier system for sublingual delivery of glutathione
Chen, G., Bunt, C. R., & Wen, J. (2014) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.12313 · Cited by 34 · see citing works
Lewicki, K., Marchand, S., Matoub, L., et al. (2006) · Talanta · doi:10.1016/j.talanta.2006.02.009 · Cited by 33 · see citing works
Redox regulation by thioredoxin and thioredoxin reductase
Holmgren, A. (2000) · BioFactors · doi:10.1002/biof.5520110117 · Cited by 32 · see citing works
Evidence for the transport of glutathione through ryanodine receptor channel type 1
Bánhegyi, G., Csala, M., Nagy, G., et al. (2003) · Biochemical Journal · doi:10.1042/bj20031419 · Cited by 31 · see citing works
Li, J., Huang, P., & Wu, F. (2016) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2016.09.018 · Cited by 31 · see citing works
Kanhai, K. M. S., Zuiker, R. G. J. A., Stavrakaki, I., et al. (2018) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.13525 · Cited by 31 · see citing works
Patel, P. J., Acharya, N. S., & Acharya, S. R. (2013) · Drug Delivery · doi:10.3109/10717544.2013.801050 · Cited by 30 · see citing works
N-acetyl-cysteine in the therapy of HIV-positive patients
Dröge, W., & Breitkreutz, R. (1999) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-199911000-00011 · Cited by 29 · see citing works
Biotin and Glutathione Targeting of Solid Nanoparticles to Cross Human Brain Endothelial Cells
Veszelka, S., Mészáros, M., Kiss, L., Kóta, Z., Páli, T., Hoyk, Z., Bozsó, Z., Fülöp, L., Toth, A., Rákhely, G., et al. (2017) · Current Pharmaceutical Design · doi:10.2174/1381612823666170727144450 · Cited by 29 · see citing works
A Complete Physicochemical Identity Card of S-nitrosoglutathione
Parent, M., Dahboul, F., Schneider, R., et al. (2013) · Current Pharmaceutical Analysis · doi:10.2174/157341213804806098 · Cited by 28 · see citing works
Self-citationDetection of Glutathione by Glutathione-S-Transferase-Nanoconjugate Ensemble Electrochemical Device
Barman, U., Mukhopadhyay, G., Goswami, N., Ghosh, S. S., & Paily, R. P. (2017) · IEEE Transactions on NanoBioscience · doi:10.1109/tnb.2017.2698241 · Cited by 27 · see citing works
Minhas, H. S., & Thornalley, P. J. (1995) · Biochemical Pharmacology · doi:10.1016/0006-2952(94)00518-q · Cited by 25 · see citing works
Shibui, Y., Sakai, R., Manabe, Y., et al. (2017) · Journal of Toxicologic Pathology · doi:10.1293/tox.2017-0002 · Cited by 25 · see citing works
Bioavailability Study of an Innovative Orobuccal Formulation of Glutathione
Buonocore, D., Grosini, M., Giardina, S., Michelotti, A., Carrabetta, M. E., Seneci, A., Verri, M., Dossena, M., & Marzatico, F. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/3286365 · Cited by 24 · see citing works
Han, H., He, Z., & Zeng, Y. (2006) · Microchimica Acta · doi:10.1007/s00604-006-0513-1 · Cited by 24 · see citing works
Greene, S. C., Noonan, P. K., Sanabria, C. R., et al. (2016) · Current Therapeutic Research · doi:10.1016/j.curtheres.2016.06.001 · Cited by 23 · see citing works
Kappi, F. A., Papadopoulos, G. A., Tsogas, G. Z., & Giokas, D. L. (2017) · Talanta · doi:10.1016/j.talanta.2017.05.014 · Cited by 23 · see citing works
Wen, J., Du, Y., Li, D., et al. (2013) · Pharmaceutical Development and Technology · doi:10.3109/10837450.2012.734518 · Cited by 22 · see citing works
Day, B. J. (2005) · CHEST Journal · doi:10.1378/chest.127.1.12 · Cited by 20 · see citing works
Adsorption and Reduction of Glutathione Disulfide on α-Al2O3 Nanoparticles: Experiments and Modeling
Dringen, R., Koehler, Y., Derr, L., et al. (2011) · Langmuir · doi:10.1021/la201856p · Cited by 20 · see citing works
Csala, M., Fulceri, R., Mandl, J., Benedetti, A., & Bánhegyi, G. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5648 · Cited by 18 · see citing works
Muanprasat, C., Wongborisuth, C., Pathomthongtaweechai, N., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055685 · Cited by 17 · see citing works
Rezaei, B., Khosropour, H., Ensafi, A. A., et al. (2014) · IEEE Sensors Journal · doi:10.1109/jsen.2014.2343152 · Cited by 17 · see citing works
Dominici, S., Pieri, L., Comporti, M., & Alfonso Pompella, C. (2003) · Cancer Cell International · doi:10.1186/1475-2867-3-7 · Cited by 16 · see citing works
Cardiovascular and renal manifestations of glutathione depletion induced by buthionine sulfoximine
Vargas, F., Rodríguez‐Gómez, I., Pérez-Abud, R., et al. (2012) · American Journal of Hypertension · doi:10.1038/ajh.2011.240 · Cited by 16 · see citing works
Gold Nanoparticles Grafted by Reduced Glutathione With Thiol Function Preservation
Luo, M., Boudier, A., Clarot, I., et al. (2016) · Colloids and Interface Science Communications · doi:10.1016/j.colcom.2016.07.002 · Cited by 15 · see citing works
Self-citationGrattagliano, I., Wieland, P., Schranz, C., et al. (1994) · Pharmacology & Toxicology · doi:10.1111/j.1600-0773.1994.tb00372.x · Cited by 14 · see citing works
Valušová, E., Švec, P., Sr., & Antalı́k, M. (2009) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-009-0476-x · Cited by 14 · see citing works
Jp, F., Schiller, B., Jiang, R., et al. (1997) · PubMed · Cited by 7 · see citing works
Simoni, R., Hill, R. L., & Vaughan, M. M. (2002) · PubMed · Cited by 7 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Glutamine: Metabolism and Immune Function, Supplementation and Clinical Translation
Cruzat, V., Macedo Rogero, M., Noel Keane, K., Curi, R., & Newsholme, P. (2018) · Nutrients · doi:10.3390/nu10111564 · Cited by 1,261 · 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
Janaszak-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
Glutamine: Metabolism and Immune Function, Supplementation and Clinical Translation
Cruzat, V., Macedo Rogero, M., Noel Keane, K., Curi, R., & Newsholme, P. (2018) · doi:10.20944/preprints201809.0459.v1 · Cited by 1,261 · see citing works
The Role of Antioxidants in the Interplay between Oxidative Stress and Senescence
Varesi, A., Chirumbolo, S., Campagnoli, L. I. M., Pierella, E., Piccini, G. B., Carrara, A., Ricevuti, G., Scassellati, C., Bonvicini, C., & Pascale, A. (2022) · Antioxidants · doi:10.3390/antiox11071224 · Cited by 145 · see citing works
Haddad, M., Hervé, V., Ben Khedher, M. R., Rabanel, J.-M., & Ramassamy, C. (2021) · Antioxidants & Redox Signaling · doi:10.1089/ars.2020.8129 · Cited by 68 · see citing works
Hamidi, S. H., Kadamboor Veethil, S., & Hamidi, S. H. (2021) · Pharmacological Reports · doi:10.1007/s43440-021-00255-x · Cited by 50 · see citing works
- Authors
- Gaucher, C., Boudier, A., Bonetti, J., Clarot, I., Leroy, P., & Parent, M.
- Affiliations
- Cibles thérapeutiques, formulation et expertise préclinique du médicament (FR)
- Corresponding author
- Gaucher, Caroline
- Venue
- Antioxidants
- Publisher
- MDPI AG
- Published
- 2018-04-27
- Volume
- 7
- Issue
- 5
- Pages
- 62
- ISSN
- 2076-3921 (ISSN-L)
- PMC
- PMC5981248
- OpenAlex
- W2801663757
- Cited by
- 332
- References
- 165
- Citations by year
- 2026: 24 · 2025: 43 · 2024: 51 · 2023: 53 · 2022: 59 · 2021: 41 · 2020: 30 · 2019: 23 · 2018: 8
- FWCI
- 2.49
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Antioxidants (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Funders
- Agence Nationale de la Recherche (ANR-15-IDEX-0004)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- glutathione, redox homeostasis, glutathione metabolism, glutathione quantification, targeted drug delivery, nanotechnology
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review