Glutathione and its role in cellular functions
Abstract
Glutathione (GSH) is the major cellular thiol participating in cellular redox reactions and thioether formation. This article serves as introduction to the FRBM Forum on glutathione and emphasizes cellular functions: What is GSH? Where does it come from? Where does it go? What does it do? What is new and noteworthy? Research tools, historical remarks, and links to current trends.
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Dunaliella sp. can produce high amounts of glutathione (GSH).
“Dunaliella sp. (Li et al., 2004, Sies, 1999) can produce high amounts of glutathione (GSH).”
From Microalgae Metabolites: A Rich Source for Food and Medicine (2019) · cites this paper as Sies, 1999
Cites
Habig, W. H., Pabst, M. J., & Jakoby, W. B. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42083-8 · Cited by 18,396 · see citing works
Selenium: Biochemical Role as a Component of Glutathione Peroxidase
Rotruck, J. T., Pope, A. L., Ganther, H. E., Swanson, A. B., Hafeman, D. G., & Hoekstra, W. G. (1973) · Science · doi:10.1126/science.179.4073.588 · Cited by 7,815 · 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
Wendel, A. (1981) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(81)77046-0 · Cited by 3,011 · see citing works
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
Hwang, C., Sinskey, A. J., & Lodish, H. F. (1992) · Science · doi:10.1126/science.1523409 · Cited by 1,968 · see citing works
ACETAMINOPHEN-INDUCED HEPATIC NECROSIS. IV. PROTECTIVE ROLE OF GLUTATHIONE
Mitchell, J. R., Jollow, D. J., Potter, W. Z., Gillette, J. R., & Brodie, B. B. (1973) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)29666-5 · Cited by 1,737 · see citing works
Hayes, J. D., & McLellan, L. I. (1999) · Free Radical Research · doi:10.1080/10715769900300851 · Cited by 1,528 · see citing works
Glutathione peroxidase: A selenoenzyme
Flohé, L., Günzler, W. A., & Schock, H. H. (1973) · FEBS Letters · doi:10.1016/0014-5793(73)80755-0 · Cited by 1,389 · see citing works
The Glutathione Status of Cells
Kosower, N. S., & Kosower, E. M. (1978) · International review of cytology · doi:10.1016/s0074-7696(08)60166-7 · Cited by 1,211 · see citing works
Biologic and pharmacologic regulation of mammalian glutathione synthesis
Griffith, O. W. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00176-8 · Cited by 1,195 · see citing works
Tissue-specific functions of individual glutathione peroxidases
Brigelius-Flohé, R. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00173-2 · Cited by 1,114 · see citing works
Glutathione: Metabolism and function
(1978) · Food and Cosmetics Toxicology · doi:10.1016/s0015-6264(78)80336-8 · Cited by 962 · see citing works
Leukotrienes are potent constrictors of human bronchi
Dahlén, S., Hedqvist, P., Hammarström, S., & Samuelsson, B. O. (1980) · Nature · doi:10.1038/288484a0 · Cited by 960 · see citing works
Dual Function of the Selenoprotein PHGPx During Sperm Maturation
Ursini, F., Heim, S., Kieß, M., Maiorino, M., Roveri, A., Wissing, J. B., & Flohé, L. (1999) · Science · doi:10.1126/science.285.5432.1393 · Cited by 902 · see citing works
Ursini, F., Maiorino, M., Valente, M., Ferri, L., & Gregolin, C. (1982) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(82)90150-3 · Cited by 884 · see citing works
ROLE OF REVERSIBLE OXIDATION-REDUCTION OF ENZYME THIOLS-DISULFIDES IN METABOLIC REGULATION
Ziegler, D. M. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.001513 · Cited by 838 · see citing works
Mills, G. C. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70608-x · Cited by 799 · see citing works
Fas-Induced Caspase Denitrosylation
Mannick, J. B., Hausladen, A., Liu, L., Hess, D. T., Zeng, M., Miao, Q., Kane, L. S., Gow, A. J., & Stamler, J. S. (1999) · Science · doi:10.1126/science.284.5414.651 · Cited by 743 · see citing works
Fairlamb, A. H., Blackburn, P., Ulrich, P. C., Chait, B. T., & Cerami, A. (1985) · Science · doi:10.1126/science.3883489 · Cited by 685 · 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
Functions of glutathione. Biochemical, physiological, toxicological and clinical aspects
(1984) · Analytical Biochemistry · doi:10.1016/0003-2697(84)90415-9 · Cited by 596 · see citing works
An enzyme from rat liver catalysing conjugations with glutathione
Booth, J., Boyland, E. J., & Sims, P. H. (1961) · Biochemical Journal · doi:10.1042/bj0790516 · Cited by 576 · see citing works
[2] Thiol/disulfide exchange equilibria and disulfidebond stability
Gilbert, H. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)51107-5 · Cited by 549 · see citing works
Gene expression and the thiol redox state
Arrigo, A. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00175-6 · Cited by 511 · see citing works
Glutathione levels in antigen-presenting cells modulate Th1 versus Th2 response patterns
Peterson, J. D., Herzenberg, L. A., Vasquez, K. O., & Waltenbaugh, C. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.3071 · Cited by 508 · see citing works
Glutathione Peroxidase Protects against Peroxynitrite-mediated Oxidations
Sies, H., Sharov, V. S., Klotz, L., & Briviba, K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.44.27812 · Cited by 488 · see citing works
Self-citationRegulation 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
Cotgreave, I. A., & Gerdes, R. G. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7812 · Cited by 481 · see citing works
Glutathione deficiency leads to mitochondrial damage in brain.
Jain, A., Mårtensson, J., Stole, E., Auld, P. A. M., & Meister, A. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.5.1913 · Cited by 428 · see citing works
Åslund, F., Berndt, K. D., & Holmgren, A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.49.30780 · Cited by 418 · see citing works
Protein Sulfhydryls and Their Role in the Antioxidant Function of Protein S-Thiolation
Thomas, J. A., Poland, B. W., & Honzatko, R. B. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1261 · Cited by 399 · see citing works
Glutathione : metabolism and physiological functions
Viña, J. (1990) · CRC Press eBooks · Cited by 377 · see citing works
Functions of Glutathione in Liver and Kidney
Sies, H., & Wendel, A. (1978) · Proceedings in life sciences · doi:10.1007/978-3-642-67132-6 · Cited by 351 · see citing works
Self-citationRapid and Specific Efflux of Reduced Glutathione during Apoptosis Induced by Anti-Fas/APO-1 Antibody
van den Dobbelsteen, D. J., Nobel, S., Schlegel, J., Cotgreave, I. A., Orrenius, S., & Slater, A. F. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.26.15420 · Cited by 343 · see citing works
[11] Diamide: An oxidant probe for thiols
Kosower, N. S., & Kosower, E. M. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)51116-4 · Cited by 340 · see citing works
Bertini, R., Howard, O. M. Z., Dong, H., Oppenheim, J. J., Bizzarri, C., Sergi, R., Caselli, G., Pagliei, S., Romines, B., Wilshire, J. A., et al. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.11.1783 · Cited by 337 · see citing works
Lipoic acid increases de novo synthesis of cellular glutathione by improving cystine utilization
Han, D., Handelman, G. J., Marcocci, L., Sen, C. K., Roy, S., Kobuchi, H., Tritschler, H., Flohé, L., & Packer, L. (1997) · BioFactors · doi:10.1002/biof.5520060303 · Cited by 334 · see citing works
Competition between glutathione and protein thiols for disulphide-bond formation
Cuozzo, J. W., & Kaiser, C. A. (1999) · Nature Cell Biology · doi:10.1038/11047 · Cited by 310 · see citing works
Mohr, S., Hallak, H., de Boitte, A., Lapetina, E. G., & Brüne, B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9427 · Cited by 309 · see citing works
Structure of leukotriene C identification of the amino acid part
Hammarström, S., Murphy, R. C., Samuelsson, B. O., Clark, D. A., Mioskowski, C., & Corey, E. J. (1979) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(79)91203-8 · Cited by 305 · see citing works
Glutathione S-transferases and drug resistance
Morrow, C. S., & Cowan, K. H. (1991) · International Journal of Biochemistry · doi:10.1016/0020-711x(91)90023-g · Cited by 305 · see citing works
Bcl-2 expression causes redistribution of glutathione to the nucleus
Voehringer, D. W., McConkey, D. J., McDonnell, T. J., Brisbay, S. M., & Meyn, R. E. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.2956 · Cited by 300 · see citing works
Glutathione conjugation: Mechanisms and biological significance
(1989) · Comparative Biochemistry and Physiology Part A Physiology · doi:10.1016/0300-9629(89)90661-0 · Cited by 264 · see citing works
Dringen, R., Kußmaul, L., Gutterer, J. M., Hirrlinger, J., & Hamprecht, B. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0722523.x · Cited by 243 · see citing works
Ebselen as a Glutathione Peroxidase Mimic and as a Scavenger of Peroxynitrite
Sies, H., & Masumoto, H. (1996) · Advances in pharmacology · doi:10.1016/s1054-3589(08)60986-2 · Cited by 230 · see citing works
Self-citationBCL-2 and glutathione: alterations in cellular redox state that regulate apoptosis sensitivity
Voehringer, D. W. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00174-4 · Cited by 224 · see citing works
Demonstration of nuclear compartmentalization of glutathione in hepatocytes.
Bellomo, G., Vairetti, M., Stivala, L. A., et al. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.10.4412 · Cited by 221 · see citing works
ON GLUTATHIONE: A REINVESTIGATION
Hopkins, F. G. (1929) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77062-2 · Cited by 215 · see citing works
Glutathione and trypanothione in parasitic hydroperoxide metabolism
Flohé, L., Hecht, H., & Steinert, P. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00172-0 · Cited by 211 · see citing works
[3] Kinetic factors that control the fate of thiyl radicals in cells
Wardman, P., & von Sonntag, C. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)51108-3 · Cited by 204 · see citing works
Reduced and oxidized glutathione efflux from liver
Bartoli, G. M., & Sies, H. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)80105-7 · Cited by 194 · see citing works
Self-citationGlutathione and glutathione-related enzymes in reproduction
Knapen, M. F. C. M., Zusterzeel, P. L. M., Peters, W. H. M., et al. (1999) · European Journal of Obstetrics & Gynecology and Reproductive Biology · doi:10.1016/s0301-2115(98)00242-5 · Cited by 189 · see citing works
Wahlländer, A., Soboll, S., Sies, H., Linke, I. M., & Monika, M. (1979) · FEBS Letters · doi:10.1016/0014-5793(79)80069-1 · Cited by 189 · see citing works
Self-citationLest I Forget Thee, Glutathione …
Kosower, E. M., & Kosower, N. S. (1969) · Nature · doi:10.1038/224117a0 · Cited by 188 · see citing works
Activity of thiols as singlet molecular oxygen quenchers
Devasagayam, T. P. A., Sundquist, A. R., Di Mascio, P., Kaiser, S., & Sies, H. (1991) · Journal of Photochemistry and Photobiology B: Biology · doi:10.1016/1011-1344(91)80008-6 · Cited by 175 · see citing works
Self-citationS-Nitrosylation and S-Glutathiolation of Protein Sulfhydryls byS-Nitroso Glutathione
Ji, Y., Akerboom, T. P. M., Sies, H., & Thomas, J. A. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.1013 · Cited by 173 · see citing works
Self-citationGlutathione S-transferases and carcinogenesis
Mantle, T. J., Pickett, C. B., & Hayes, J. D. (1987) · Taylor & Francis eBooks · Cited by 168 · see citing works
Hydroperoxides and Thiol Oxidants in the Study of Oxidative Stress in Intact Cells and Organs
Sies, H. (1985) · Elsevier eBooks · doi:10.1016/b978-0-12-642760-8.50008-9 · Cited by 166 · see citing works
Self-citationBlackburn, R. V., Spitz, D. R., Liu, X. Z., Galoforo, S., Sim, J. E., Ridnour, L. A., Chen, J. C., Davis, B. H., Corry, P. M., & Lee, Y. J. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00217-2 · Cited by 158 · see citing works
Nitric Oxide Inhibits c-Jun DNA Binding by Specifically TargetedS-Glutathionylation
Klatt, P., Pineda‐Molina, E., & Lamas, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.22.15857 · Cited by 156 · see citing works
Stephenson, D. T., Rash, K. S., Smalstig, B., Roberts, E. F., Johnstone, E., Sharp, J., Panetta, J., Little, S. P., Kramer, R. M., & Clemens, J. A. (1999) · Glia · doi:10.1002/(sici)1098-1136(199908)27:2 · Cited by 152 · see citing works
Creighton, T. (1997) · Biological Chemistry · doi:10.1515/bchm.1997.378.8.731 · Cited by 150 · see citing works
Export pumps for glutathione S-conjugates
KEPPLER, D. O. R. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00171-9 · Cited by 147 · see citing works
Winterbourn, C. C., & Brennan, S. O. (1997) · Biochemical Journal · doi:10.1042/bj3260087 · Cited by 146 · see citing works
Leukotrienes: a new group of biologically active compounds.
Samuelsson, B. O., Borgeat, P., Hammarström, S., et al. (1980) · PubMed · Cited by 142 · see citing works
Harington, C. R., & Mead, T. H. (1935) · Biochemical Journal · doi:10.1042/bj0291602 · Cited by 140 · see citing works
Akerboom, T. P. M., Narayanaswami, V., Kunst, M., et al. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98817-4 · Cited by 132 · 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
Maiorino, M., Wissing, J. B., Brigelius‐Flohé, R., Calabrese, F., Roveri, A., Steinert, P., Ursini, F., & Flohé, L. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.13.1359 · Cited by 127 · see citing works
Isolation, characterization, and turnover of glutathionylspermidine from Escherichia coli.
Tabor, H., & Tabor, C. W. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41651-7 · Cited by 119 · see citing works
[12] Bromobimane probes for thiols
Kosower, E. M., & Kosower, N. S. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)51117-2 · Cited by 118 · see citing works
Synthesis of Glutathione in the Preimplantation Mouse Embryo
Gardiner, C. S., & Reed, D. J. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1200 · Cited by 117 · see citing works
[42] Protein S-thiolation and dethiolation
Thomas, J. A., Chai, Y.-C., & Jung, C. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(94)33045-x · Cited by 114 · see citing works
Barnes, M. M., James, S. P., & Wood, P. B. (1959) · Biochemical Journal · doi:10.1042/bj0710680 · Cited by 112 · see citing works
Sulfhydryl Oxidase from Egg White
Hoober, K. L., Sheasley-O’Neill, S. L., Gilbert, H., & Thorpe, C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.32.22147 · Cited by 112 · 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
Self-citationRegulation of HIV-1 Protease Activity through Cysteine Modification
Davis, D. A., Dorsey, K. E., Wingfield, P. T., Stahl, S. J., Kaufman, J. D., Fales, H. M., & Levine, R. L. (1996) · Biochemistry · doi:10.1021/bi951525k · Cited by 99 · see citing works
Review of the current status of calcium and thiols in cellular injury
Reed, D. J. (1990) · Chemical Research in Toxicology · doi:10.1021/tx00018a002 · Cited by 97 · 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
Labadarios, D., Davis, M. R., Portmann, B. C., et al. (1977) · Biochemical Pharmacology · doi:10.1016/0006-2952(77)90126-5 · Cited by 91 · see citing works
Jaffe, M. (1879) · Berichte der deutschen chemischen Gesellschaft · doi:10.1002/cber.187901201286 · Cited by 88 · see citing works
Bojes, H. K., Datta, K., Xu, J., Chin, A. J., Simonian, P. L., Núñez, G., & Kehrer, J. P. (1997) · Biochemical Journal · doi:10.1042/bj3250315 · Cited by 86 · see citing works
Ueber Bromphenylmercaptursäure
Baumann, E., & Preusse, C. (1879) · Berichte der deutschen chemischen Gesellschaft · doi:10.1002/cber.187901201225 · Cited by 86 · see citing works
Antioxidant and redox regulation of genes
Sen, C. K., Sies, H., & Baeuerle, P. A. (1999) · Cited by 84 · see citing works
Self-citationThe formation of mercapturic acids. 2. The possible role of glutathionase
Bray, H. G., Franklin, T. J., & James, S. P. (1959) · Biochemical Journal · doi:10.1042/bj0710690 · Cited by 83 · see citing works
Kaplowitz, N., Fernández-Checa, J. C., Kannan, R., García‐Ruiz, C., Ookhtens, M., & Yi, J. (1996) · Biological Chemistry Hoppe-Seyler · doi:10.1515/bchm3.1996.377.5.267 · Cited by 80 · see citing works
Glutathione Centennial : molecular perspectives and clinical implications
Centennial, G., 谷口, 直., 日本生化学会, et al. (1989) · Academic Press eBooks · Cited by 78 · see citing works
Soboll, S., GRÜNDEL, S., Harris, J. M., Kolb-Bachofen, V., KETTERER, B., & Sies, H. (1995) · Biochemical Journal · doi:10.1042/bj3110889 · Cited by 73 · see citing works
Self-citationHausladen, A., & Stamler, J. S. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)00143-3 · Cited by 72 · see citing works
Protein mixed-disulfides in cardiac cells.S-thiolation of soluble proteins in response to diamide
Grimm, L. M., Collison, M. W., Fisher, R. A., et al. (1985) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(85)90232-0 · Cited by 62 · see citing works
Dafré, A. L., Sies, H., & Akerboom, T. P. M. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0344 · Cited by 61 · see citing works
Self-citationMiller, R. M., Sies, H., Park, E., et al. (1990) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(90)90732-e · Cited by 57 · see citing works
Self-citationBriviba, K., Fraser, G. R., Sies, H., & KETTERER, B. (1993) · Biochemical Journal · doi:10.1042/bj2940631 · Cited by 55 · see citing works
Self-citationPeinado, J., Sies, H., & Akerboom, T. P. M. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90497-9 · Cited by 54 · see citing works
Self-citationRole of cysteine and glutathione in signal transduction, immunopathology and cachexia
Dröge, W., Hack, V., Breitkreutz, R., Holm, E., Shubinsky, G., Schmid, E., & Galter, D. (1998) · BioFactors · doi:10.1002/biof.5520080117 · Cited by 53 · see citing works
Stoll, V. S., Simpson, S. J., Krauth‐Siegel, R. L., et al. (1997) · Biochemistry · doi:10.1021/bi963074p · Cited by 52 · see citing works
Different sites of acivicin binding and inactivation of gamma-glutamyl transpeptidases.
Smith, T., Ikeda, Y., Fujii, J., et al. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.6.2360 · Cited by 52 · see citing works
Subcellular glutathione contents in isolated hepatocytes treated with L-buthionine sulfoximine
Romero, F. J., & Sies, H. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80248-x · Cited by 50 · see citing works
Self-citationKing, J. S. (1968) · Experimental Biology and Medicine · doi:10.3181/00379727-129-33461 · Cited by 50 · see citing works
Glutathione s-transferases and drug resistance
(1991) · Comparative Biochemistry and Physiology Part A Physiology · doi:10.1016/0300-9629(91)90616-k · Cited by 47 · see citing works
Protein folding coupled to disulphide-bond formation
Creighton, T. E. (2000) · doi:10.1093/oso/9780199637898.003.0009 · Cited by 44 · see citing works
Han, D., Handelman, G. J., & Packer, L. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)51134-2 · Cited by 43 · see citing works
Ji, Y., Akerboom, T. P. M., & Sies, H. (1996) · Biochemical Journal · doi:10.1042/bj3130377 · Cited by 35 · see citing works
Self-citationProtein S-thiolation and redox regulation of membrane-bound glutathione transferase
Sies, H., Dafré, A. L., Ji, Y., & Akerboom, T. P. M. (1998) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(97)00160-9 · Cited by 35 · see citing works
Self-citationSulfur and sulfur amino acids.
Jakoby, W. B., & Griffith, O. W. (1987) · PubMed · Cited by 33 · see citing works
Glutathione and the mitochondrial reduction of hydroperoxides
Jocelyn, P. C., & DICKSON, J. C. (1980) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(80)90141-3 · Cited by 30 · see citing works
[49] Preparation and use of glutathione monoesters
Anderson, M. E., Levy, E. J., & Meister, A. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(94)34120-6 · Cited by 25 · see citing works
Anderson, M. T., Trudell, J. R., Voehringer, D. W., et al. (1999) · Analytical Biochemistry · doi:10.1006/abio.1999.4153 · Cited by 22 · see citing works
Treatment of Cystinuria with Alpha-Mercaptopropionylglycine
Johansen, K., Gammelgård, P. A., & Jørgensen, F. S. (1980) · Scandinavian Journal of Urology and Nephrology · doi:10.3109/00365598009179559 · Cited by 20 · see citing works
An evolutionary approach to the design of glutathione-linked enzymes
Mannervik, B., Cameron, A. D., Fernandez, E., et al. (1998) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(97)00147-6 · Cited by 18 · see citing works
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- Authors
- Sies, H.
- Affiliations
- Heinrich Heine University Düsseldorf (DE)
- Corresponding author
- Sies, Helmut
- ORCID
- Sies, Helmut
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 1999-11
- Volume
- 27
- Issue
- 9-10
- Pages
- 916-921
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2073703119
- Cited by
- 1,735
- References
- 114
- Citations by year
- 2026: 24 · 2025: 38 · 2024: 47 · 2023: 78 · 2022: 63 · 2021: 58 · 2020: 75 · 2019: 69 · 2018: 74 · 2017: 92 · 2016: 60 · 2015: 86 · 2014: 113 · 2013: 76 · 2012: 100
- FWCI
- 3.69
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- 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 reactions, thioether formation, glutathione metabolism
- MeSH terms
- Animals, Free Radicals, Glutathione, Humans, Oxidation-Reduction, History, 19th Century, History, 20th Century
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