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Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine).
Open accessAbstract
Buthionine sulfoximine (S-n-butyl homocysteine sulfoximine), the most potent of a series of analogs of methionine sulfoximine thus far studied (Griffith, O.W., Anderson, M.E., and Meister, A. (1979) J. Biol. Chem. 254, 1205-1210), inhibited gamma-glutamylcysteine synthetase about 20 times more effectively than did prothionine sulfoximine and at least 100 times more effectively than methionine sulfoximine. The findings support the conclusion that the S-alkyl moiety of the sulfoximine binds at the enzyme site that normally binds the acceptor amino acid. Thus, the affinity of the enzyme for the S-ethyl, S-n-propyl, and S-n-butyl sulfoximines increases in a manner which is parallel to those of the corresponding isosteric acceptor amino acid substrates, i.e. glycine, alanine, and alpha-aminobutyrate. Buthionine sulfoximine did not inhibit glutamine synthetase detectably, nor did it produce convulsions when injected into mice. Injection of buthionine sulfoximine into mice decreased the level of glutathione in the kidney to a greater extent (less than 20% of the control level) than found previously after giving prothionine sulfoximine. alpha-Methyl buthionine sulfoximine was also prepared and found to be almost as effective as buthionine sulfoximine; this compound would not be expected to undergo substantial degradative metabolism. Buthionine sulfoximine and alpha-methyl buthionine sulfoximine may be useful agents for inhibition of glutathione synthesis in various experimental systems.
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“eprenetapopt may be unique, triggering an increase in turnover of GSH rather than restraining de novo GSH synthesis, as imposed by erastin through its inhibition of cystine uptake or by l-buthionine sulfoximine through inhibition of glutamate-cysteine ligase (40).”
From Eprenetapopt triggers ferroptosis, inhibits NFS1 cysteine desulfurase, and synergizes with serine and glycine dietary restriction (2022) · cites this paper as [40]
In the citing paper
“buthionine sulfoximine (BSO), an inhibitor of glutamate cysteine ligase (GCL), the enzyme required for GSH synthesis, depletes GSH and exhibits anticancer activity”
From The Two Faces of Reactive Oxygen Species in Cancer (2017) · cites this paper as Griffith & Meister 1979
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Mechanism of inhibition of glutamine synthetase by methionine sulfoximine
Ronzio, R. A., Rowe, W. B., & Meister, A. (1969) · Biochemistry · doi:10.1021/bi00831a038 · Cited by 327
Self-citationGriffith, O. W., Anderson, M. E., & Meister, A. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34188-1 · Cited by 172
Self-citationManning, J. M., Moore, S., Rowe, W. B., & Meister, A. (1969) · Biochemistry · doi:10.1021/bi00834a066 · Cited by 166
Self-citationPhosphorylation of methionine sulfoximine by glutamine synthetase.
Ronzio, R. A., & Meister, A. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.59.1.164 · Cited by 156
Self-citationSekura, R. D., & Meister, A. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40500-x · Cited by 149
Self-citationGriffith, O. W., & Meister, A. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38077-8 · Cited by 101
Self-citationComputer analysis of the active site of glutamine synthetase
Gass, J. D., & Meister, A. (1970) · Biochemistry · doi:10.1021/bi00808a012 · Cited by 88
Self-citationBentley, H. R., McDermott, E. E., & Whitehead, J. K. (1951) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.1951.0021 · Cited by 47
New synthesis of S-alkyl- DL -homocysteines
Kolenbrander, H. M. (1969) · Canadian Journal of Chemistry · doi:10.1139/v69-542 · Cited by 16
Hayahsi, K. (1960) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.8.177 · Cited by 6
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SUMATHI, R., BASKARAN, G., & Varalakshmi, P. (1996) · Japanese Journal of Medical Science and Biology · doi:10.7883/yoken1952.49.39 · Cited by 43
Ying, W., Anderson, C. M., Chen, Y., Stein-Behrens, B., Fahlman, C. S., Copin, J., Chan, P. H., & Swanson, R. A. (2000) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200002000-00018 · Cited by 43
The role of glutathione turnover in the apparent renal secretion of cystine.
Griffith, O. W. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43264-4 · Cited by 43
Self-citationYoshida, T., Oguro, T., Numazawa, S., & Kuroiwa, Y. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)91349-0 · Cited by 43
Laursen, J. B., Boesgaard, S., Trautner, S., Rubin, I., Poulsen, H. E., & Aldershvile, J. (2001) · Free Radical Research · doi:10.1080/10715760100300901 · Cited by 42
Redpath, C. J., Khalil, M. B., Drozdzal, G., Radisic, M., & McBride, H. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069165 · Cited by 49
Sharpe, P. C., Yue, K. K. M., Catherwood, M. A., McMaster, D., & Trimble, E. R. (1998) · Diabetologia · doi:10.1007/s001250051054 · Cited by 42
In vivo regulation by glutathione of methionine adenosyltransferase S-nitrosylation in rat liver
Corrales, F. J., Ruiz, F. A., & Mato, J. M. (1999) · Journal of Hepatology · doi:10.1016/s0168-8278(99)80291-8 · Cited by 42
Mayer, R., Lee, K.-E., & Cockett, A. T. �. (1987) · Cancer Chemotherapy and Pharmacology · doi:10.1007/bf00570486 · Cited by 42
Sun, J. D. (1985) · Fundamental and Applied Toxicology · doi:10.1016/0272-0590(85)90173-3 · Cited by 42
Haddad, J. J., Saadé, N. E., & Safieh‐Garabedian, B. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(01)00233-9 · Cited by 42
Guo, Z., Nakagawara, S., Sumitani, K., & Ohta, Y. (1993) · PLANT PHYSIOLOGY · doi:10.1104/pp.102.1.45 · Cited by 42
Effect of glutathione depletion by buthionine sulfoximine on rat embryonic development in vitro
Slott, V. L., & Hales, B. F. (1987) · Biochemical Pharmacology · doi:10.1016/0006-2952(87)90719-2 · Cited by 42
Selective glutathione depletion on function and structure of the isolated perfused rat kidney
Brezis, M., Rosen, S., Silva, P., Epstein, F. H., & Epstein, F. H. (1983) · Kidney International · doi:10.1038/ki.1983.142 · Cited by 42
Cheff, D. M., Cheng, Q., Guo, H., Travers, J., Klumpp-Thomas, C. A., Shen, M., Arnér, E. S. J., & Hall, M. D. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102719 · Cited by 40
Increased glucose availability sensitizes pancreatic cancer to chemotherapy
Gohar, A. V., Hue, J. J., Abbas, A., Graor, H. J., Hajihassani, O., Zarei, M., Titomihelakis, G., Feczko, J., Rathore, M. G., Chełstowska, S., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38921-8 · Cited by 45
Magalh�es, J., Soares, J. M. C., Neuparth, M. J., Ferreira, R. M., Oliveira, J., Amado, F. M. L., Duarte, J. A., & Ascens�o, A. (2004) · European Journal of Applied Physiology · doi:10.1007/s00421-003-0972-6 · Cited by 41
Protective role of melatonin on retinal ganglionar cell: In vitro an in vivo evidences
Bessone, C. D. V., Fajreldines, H. D., de Barboza, G. D., de Talamoni, N. G. T., Allemandi, D. A., Carpentieri, A. R., & Quinteros, D. A. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.12.053 · Cited by 41
Mechanisms of suppression of neoplastic transformation in vitro by low doses of low LET radiation
Pant, M. C. (2003) · Carcinogenesis · doi:10.1093/carcin/bgg172 · Cited by 41
The possible role of endogenous glutathione as an anticonvulsant in mice
Abe, K., Nakanishi, K., & Saitō, H. (2000) · Brain Research · doi:10.1016/s0006-8993(99)02269-6 · Cited by 41
Delneste, Y., Jeannin, P., Potier, L., Romero, P. J., & Bonnefoy, J. (1997) · Blood · doi:10.1182/blood.v90.3.1124 · Cited by 41
Almagor, M., Kahane, I., Gilon, C., & Yatziv, S. (1986) · Infection and Immunity · doi:10.1128/iai.52.1.240-244.1986 · Cited by 41
Woods, J. S., Ellis, M. E., Dieguez-Acuña, F. J., & Corral, J. (1999) · Toxicology and Applied Pharmacology · doi:10.1006/taap.1998.8583 · Cited by 41
Reaction of glutathione with a free radical metabolite of carbon tetrachloride.
Connor, H. D., Lacagnin, L. B., Knecht, K. T., Thurman, R. G., & Mason, R. P. (1990) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10824-9 · Cited by 41
The role of glutathione detoxification pathway in MCLR-induced hepatotoxicity in SD rats
Li, S., Chen, J., Xie, P., Guo, X., Fan, H., Yu, D., Zeng, C. C., & Chen, L. (2014) · Environmental Toxicology · doi:10.1002/tox.22017 · Cited by 40
Jaleel, C. A., Gopi, R., & Panneerselvam, R. (2009) · Cited by 40
Chowdhury, A. A., Chaudhuri, J., Biswas, N., Manna, A., Chatterjee, S., Mahato, S. K., Chaudhuri, U., Jaisankar, P., & Bandyopadhyay, S. K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073672 · Cited by 40
RetractedIida, A., Sasaki, E., Yano, A., Tsuneyama, K., Fukami, T., Nakajima, M., & Yokoi, T. (2015) · Drug Metabolism and Disposition · doi:10.1124/dmd.115.063370 · Cited by 41
Dotsey, E. Y., Jung, K., Basit, A., Don, W., Daglian, J. M., Vacondio, F., Armirotti, A., Mor, M., & Piomelli, D. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.04.013 · Cited by 42
Hojati, M., Modarres‐Sanavy, S. A. M., Ghanati, F., & Mehdi, P. (2011) · Journal of Plant Physiology · doi:10.1016/j.jplph.2010.11.009 · Cited by 40
Hansen, J. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00751-1 · Cited by 40
Will, O. (1999) · Carcinogenesis · doi:10.1093/carcin/20.2.333 · Cited by 40
Masini, A., Gallesi, D., Giovannini, F., Trenti, T., & Ceccarelli, D. (1997) · Hepatology · doi:10.1002/hep.510250221 · Cited by 40
A histone-like protein (HTa) from Thermoplasma acidophilum. I. Purification and properties.
DeLange, R. J., Green, G. R., & Searcy, D. G. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70064-7 · Cited by 40
Frenzel, J., Richter, J. P., & Eschrich, K. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(01)00169-0 · Cited by 40
Oncogenic Basis of Radiation Resistance
Kasid, U. N., Pirollo, K. F., Dritschilo, A., & Chang, E. H. (1993) · Advances in cancer research · doi:10.1016/s0065-230x(08)60959-8 · Cited by 40
Oxidative stress in fish cells:In vitro studies
Babich, H., Palace, M. R., & Stern, A. (1993) · Archives of Environmental Contamination and Toxicology · doi:10.1007/bf01141344 · Cited by 40
Wang, F., Wang, L. Y., Wright, D. E., & Parmely, M. J. (1999) · Infection and Immunity · doi:10.1128/iai.67.10.5409-5416.1999 · Cited by 40
Henmi, K., Tsuboi, S., Demura, T., Fukuda, H., Iwabuchi, M., & Ogawa, K. (2001) · Plant and Cell Physiology · doi:10.1093/pcp/pce072 · Cited by 40
Variation in sensitizing efficiency for SR 2508 in human cells dependent on glutathione content
Phillips, T. L., Mitchell, J. B., Graff, W., Russo, A. J., & GLATSTEIN, E. J. (1986) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/0360-3016(86)90289-0 · Cited by 40
Ochi, H., Morita, I., & Murota, S. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90704-z · Cited by 40
Comparative responses of two species of marine phytoplankton to metolachlor exposure
Thakkar, M., Randhawa, V., & Wei, L. (2012) · Aquatic Toxicology · doi:10.1016/j.aquatox.2012.10.002 · Cited by 40
Methionine and Buthionine Sulfoximines: Syntheses under Mild and Safe Imidation/Oxidation Conditions
Buglioni, L., Bizet, V., & Bolm, C. (2014) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.201400354 · Cited by 39
Majid, A. S. A., Majid, A. M. S. A., Yin, Z., & Ji, D. (2013) · Neurochemical Research · doi:10.1007/s11064-013-1034-z · Cited by 39
Ma, H.-C., Liu, Y., Wang, C., Strauss, M., Rehage, N., Chen, Y.-H., Altan‐Bonnet, N., Hogle, J. M., Wimmer, E., Mueller, S., et al. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004052 · Cited by 39
Compound profiling for ABCC2 (MRP2) using a fluorescent microplate assay system
Förster, F., Volz, A., & Fricker, G. (2007) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2007.10.003 · Cited by 39
Apoptosis vs. necrosis: glutathione-mediated cell death during rewarming of rat hepatocytes
Vairetti, M., Ferrigno, A., Bertone, R., Richelmi, P., Bertè, F., & Freitas, I. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.11.022 · Cited by 39
Harnessing drug resistance: Using ABC transporter proteins to target cancer cells
Leitner, H., Kachadourian, R., & Day, B. J. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.05.014 · Cited by 42
Zechmann, B., Müller, M., & Zellnig, G. (2006) · PROTOPLASMA · doi:10.1007/s00709-005-0129-z · Cited by 39
Differential utilisation of sulfur compounds for H2S liberation by nitrogen-starved wine yeasts
HALLINAN, C. P., Saul, D. J., & Jiranek, V. (1999) · Australian Journal of Grape and Wine Research · doi:10.1111/j.1755-0238.1999.tb00291.x · Cited by 39
Broquist, H. P. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.1992.tb01298.x · Cited by 39
Yoon, I., Lee, K. H., & Cho, J. (2004) · Archives of Pharmacal Research · doi:10.1007/bf02980089 · Cited by 37
Shrieve, D. C., & Harris, J. (1985) · International Journal of Radiation Biology and Related Studies in Physics Chemistry and Medicine · doi:10.1080/09553008514551131 · Cited by 39
Buthionine sulfoximine-induced glutathione depletion
Thanislass, J., Raveendran, M., & Devaraj, H. (1995) · Biochemical Pharmacology · doi:10.1016/0006-2952(95)00123-h · Cited by 39
Viarengo, A. (1994) · Advances in comparative and environmental physiology · doi:10.1007/978-3-642-78598-6_3 · Cited by 39
Singlet Oxygen-Mediated Oxidation during UVA Radiation Alters the Dynamic of Genomic DNA Replication
Graindorge, D., Martineau, S., Machon, C., Arnoux, P., Guitton, J., Francesconi, S., Frochot, C., Sage, É., & Girard, P.-M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0140645 · Cited by 42
Liu, T., Xiong, C., Zhang, L., Jiao, G., Shi, H., Feng, J. X., & Zhang, X. (2022) · Advanced Healthcare Materials · doi:10.1002/adhm.202202045 · Cited by 38
Role for PKC-ε in neuronal death induced by oxidative stress
Jung, Y.-S., Ryu, B., Lee, B., Mook-Jung, I., Kim, S., Lee, S. H., Baik, E., & Moon, C. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.05.217 · Cited by 38
Frade, J. G., Pope, S. A. S., Schmidt, M., Dringen, R., Barbosa, R. M., Pocock, J. M., Laranjinha, J. A. N., & Heales, S. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05216.x · Cited by 38
Gabryel, B., & Małecki, A. (2006) · PubMed · Cited by 38
Stimulation of H2S Emission from Pumpkin Leaves by Inhibition of Glutathione Synthesis
Rennenberg, H., & Filner, P. (1982) · PLANT PHYSIOLOGY · doi:10.1104/pp.69.4.766 · Cited by 38
Treatment of Advanced Malignancies with High-Dose Acetaminophen and N-Acetylcysteine Rescue
Kobrinsky, N. L., Hartfield, D. S., Horner, H., Maksymiuk, A. W., Minuk, G. Y., White, D. F., & Feldstein, T. J. (1996) · Cancer Investigation · doi:10.3109/07357909609012140 · Cited by 38
Mechanism of renal peritubular extraction of plasma glutathione
Inoue, M., Shinozuka, S., & Morino, Y. (1986) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1986.tb09708.x · Cited by 38
Glutathione depletion greatly reduces neocarzinostatin cytotoxicity in Chinese hamster V79 cells.
DeGraff, W., Russo, A., & Mitchell, J. B. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39472-3 · Cited by 38
Nuclear Glutathione and Oxygen Enhancement of Radiosensitivity
Edgren, M. (1987) · International Journal of Radiation Biology and Related Studies in Physics Chemistry and Medicine · doi:10.1080/09553008714550431 · Cited by 38
Henderson, P. T., Li, T., He, M., Zhang, H., Malfatti, M. A., Gandara, D. R., Grimminger, P., Danenberg, K. D., Beckett, L. A., White, R. D., et al. (2010) · International Journal of Cancer · doi:10.1002/ijc.25814 · Cited by 39
Development of an invasively monitored porcine model of acetaminophen-induced acute liver failure
Newsome, P. N., Henderson, N. C., Nelson, L. J., Dabos, C., Filippi, C., Bellamy, C. O. C., Howie, F. A., Clutton, R. E., King, T., Lee, A., et al. (2010) · BMC Gastroenterology · doi:10.1186/1471-230x-10-34 · Cited by 37
Sasaki, E., Matsuo, K., Iida, A., Tsuneyama, K., Fukami, T., Nakajima, M., & Yokoi, T. (2013) · Toxicological Sciences · doi:10.1093/toxsci/kft184 · Cited by 37
Calviño, E., Estañ, M. C., Sànchez‐Martìn, C., Brea, R., de Blas, E., Boyano-Adánez, M. D. C., Rial, E., & Aller, P. (2013) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.113.206714 · Cited by 37
Wu, C., Gong, M.-Q., Liu, B., Zhuo, R., & Cheng, S. (2016) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2016.10.029 · Cited by 37
The brain response to 2-deoxy glucose is blocked by a glial drug
Young, J. K., Baker, J. H., & Montes, M. I. (2000) · Pharmacology Biochemistry and Behavior · doi:10.1016/s0091-3057(00)00315-4 · Cited by 37
Moreira, D. D. S., do Monte‐Neto, R. L., Andrade, J. M., Santi, A. M. M., dos Reis, P. G., Frézard, F., & Murta, S. M. F. (2013) · International Journal for Parasitology Drugs and Drug Resistance · doi:10.1016/j.ijpddr.2013.08.001 · Cited by 36
Toxicogenomics and Metabolomics of Pentamethylchromanol (PMCol)-Induced Hepatotoxicity
Parman, T., Bunin, D. I., Ng, H. H., McDunn, J. E., Wulff, J. E., Wang, A., Swezey, R. R., Rasay, L., Fairchild, D. G., Kapetanović, I. M., et al. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfr238 · Cited by 36
Fraxin Prevents Chemically Induced Hepatotoxicity by Reducing Oxidative Stress
Chang, B. Y., Jung, Y. J., Yoon, C., Oh, J. S., Hong, J. H., Kim, Y., & Kim, S. H. (2017) · Molecules · doi:10.3390/molecules22040587 · Cited by 36
Muri, J., Thut, H., Heer, S., Krueger, C. C., Bornkamm, G. W., Bachmann, M. F., & Köpf, M. (2019) · European Journal of Immunology · doi:10.1002/eji.201848044 · Cited by 37
Glutathione levels in human platelets display a circadian rhythm in vitro
Radha, E., Hill, T. D., Rao, G. H. R., & White, J. G. (1985) · Thrombosis Research · doi:10.1016/0049-3848(85)90319-6 · Cited by 36
Ji, L., Shen, K., Jiang, P., Morahan, G., & Wang, Z. (2011) · Molecular Carcinogenesis · doi:10.1002/mc.20741 · Cited by 36
Bitar, M. S., & Al‐Mulla, F. (2012) · Disease Models & Mechanisms · doi:10.1242/dmm.007872 · Cited by 36
Relationship between gluconeogenesis and glutathione redox state in rabbit kidney-cortex tubules
Winiarska, K., Dr⊙ak, J., Węgrzynowicz, M., Jagielski, A. K., & Bryła, J. (2003) · Metabolism · doi:10.1016/s0026-0495(03)00035-0 · Cited by 36
Role of glutathione in nitric oxide-mediated injury to rat gastric mucosal cells
Wakulich, C. A., & Tepperman, B. L. (1997) · European Journal of Pharmacology · doi:10.1016/s0014-2999(96)00865-5 · Cited by 36
Depletion of glutathione in the kidney and the renal disposition of administered inorganic mercury.
Zalups, R. K., & Lash, L. H. (1997) · PubMed · Cited by 36
Glutathione Efflux Induced by NMDA and Kainate
Wallin, C., Weber, S. G., & Sandberg, M. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0731566.x · Cited by 36
Effects of buthionine sulfoximine and diethyl maleate on glutathione turnover in the channel catfish
Gallagher, E. P., Hasspieler, B. M., & Glulio, R. T. D. (1992) · Biochemical Pharmacology · doi:10.1016/0006-2952(92)90180-q · Cited by 36
Meister, A. (1984) · Springer eBooks · doi:10.1007/978-3-642-69754-8_1 · Cited by 36
Self-citationSuttorp, N., Kästle, S., & Neuhof, H. (1991) · Lung · doi:10.1007/bf02714155 · Cited by 36
DeGraff, W., & Mitchell, J. B. (1985) · PubMed · Cited by 36
Glutathione-conferred resistance to antineoplastics: Approaches toward its reduction
Somfai-Relle, S., Suzukake, K., Vistica, B. P., & Vistica, D. T. (1984) · Cancer Treatment Reviews · doi:10.1016/0305-7372(84)90042-2 · Cited by 36
Boesgaard, S., Poulsen, H. E., Aldershvile, J., Loft, S. H., Anderson, M. E., & Meister, A. (1993) · Circulation · doi:10.1161/01.cir.87.2.547 · Cited by 36
Self-citationChepikova, O. E., Malin, D., Strekalova, E., Lukasheva, E. V., Zamyatnin, A. A., & Cryns, V. L. (2020) · Breast Cancer Research and Treatment · doi:10.1007/s10549-020-05801-4 · Cited by 36
Redox regulation of DUBs and its therapeutic implications in cancer
Tyagi, A., Haq, S., & Ramakrishna, S. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102194 · Cited by 35
Faúndez, M., López‐Muñoz, R., Torres, G., Morello, A., Ferreira, J., Kemmerling, U., Myriam Orellana, B., & Maya, J. D. (2008) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01454-07 · Cited by 35
Effects of Cadmium Stress on Hairy Roots of Daucus carota
di Toppi, L. S., Lambardi, M., Pecchion, N., Pazzagli, L., Durante, M., & Gabbrielli, R. (1999) · Journal of Plant Physiology · doi:10.1016/s0176-1617(99)80185-0 · Cited by 35
Ochi, T., Suzuki, T., Isono, H., Schlagenhaufen, C., Goessler, W., & Tsutsui, T. (2003) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(03)00137-4 · Cited by 35
Redox Control of Ion Channel Activity in Vascular Endothelial Cells by Glutathione
Elliott, S. J., & Koliwad, S. K. (1997) · Microcirculation · doi:10.3109/10739689709146798 · Cited by 35
Tokutake, N., Hiratake, J., Katoh, M., Irie, T., Kato, H., & Oda, J. (1998) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(98)00142-4 · Cited by 35
Glial and neuronal glutamate transport following glutamine synthetase inhibition
Rothstein, J. D., & Tabakoff, B. (1985) · Biochemical Pharmacology · doi:10.1016/0006-2952(85)90102-9 · Cited by 35
Diah, S. K., Smitherman, P. K., Townsend, A. J., & Morrow, C. S. (1999) · Toxicology and Applied Pharmacology · doi:10.1006/taap.1999.8672 · Cited by 35
Effects of glutathione depletion on gluconeogenesis in isolated hepatocytes
Sáez, G. T., Romero, F. J., & Viña, J. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90363-7 · Cited by 35
Jevtović‐Todorović, V., & Guenthner, T. M. (1992) · Biochemical Pharmacology · doi:10.1016/0006-2952(92)90540-y · Cited by 35
How is rat liver S‐adenosylmethionine synthetase regulated?
Pajares, M. A., Corrales, F. J., Durán, C., Mato, J. M., & Álvarez, L. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80726-w · Cited by 35
Metadata
- Authors
- Griffith, O. W., & Meister, A.
- Affiliations
- Cornell University (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1979-08
- Volume
- 254
- Issue
- 16
- Pages
- 7558-7560
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1535828429
- Cited by
- 1,683
- References
- 10
- Citations by year
- 2026: 12 · 2025: 25 · 2024: 33 · 2023: 30 · 2022: 33 · 2021: 34 · 2020: 26 · 2019: 27 · 2018: 28 · 2017: 25 · 2016: 33 · 2015: 35 · 2014: 38 · 2013: 36 · 2012: 29
- FWCI
- 3.97
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- 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 › Biochemistry › Amino Acid Enzymes and Metabolism
- Keywords
- buthionine sulfoximine, glutathione synthesis inhibition, gamma-glutamylcysteine synthetase, enzyme inhibition, glutathione, glutamine synthetase
- MeSH terms
- Glutamate-Cysteine Ligase, Glutathione, Kinetics, Methionine Sulfoximine, Peptide Synthases, Structure-Activity Relationship
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