GLUTATHIONE

Free radicals, antioxidants and functional foods: impact on human health

Lobo, V, Patil, A., Phatak, A., & Chandra, N. (2010) · Pharmacognosy Reviews · doi:10.4103/0973-7847.70902 · Cited by 5,435

Reactive oxygen species, cellular redox systems, and apoptosis

Circu, M. L., & Aw, T. Y. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.022 · Cited by 3,340

Oxidative Stress: An Essential Factor in the Pathogenesis of Gastrointestinal Mucosal Diseases

Bhattacharyya, A., Chattopadhyay, R., Mitra, S., & Crowe, S. E. (2014) · Physiological Reviews · doi:10.1152/physrev.00040.2012 · Cited by 2,484

Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production

Powers, S. K., & Jackson, M. J. (2008) · Physiological Reviews · doi:10.1152/physrev.00031.2007 · Cited by 2,459

Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean?

Halliwell, B., & Whiteman, M. (2004) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705776 · Cited by 2,238

DNA damage and oxygen radical toxicity

Imlay, J. A., & Linn, S. (1988) · Science · doi:10.1126/science.3287616 · Cited by 1,974

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

Metabolism and functions of glutathione in brain

Dringen, R. (2000) · Progress in Neurobiology · doi:10.1016/s0301-0082(99)00060-x · Cited by 1,702

Drug delivery strategy utilizing conjugation via reversible disulfide linkages: Role and site of cellular reducing activities

Saito, G., Swanson, J. A., & Lee, K.-D. (2003) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00179-5 · Cited by 1,407

Selective Modification of Glutathione Metabolism

Meister, A. (1983) · Science · doi:10.1126/science.6836290 · Cited by 1,267

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

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

Role 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

Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia

Sian, J., Dexter, D. T., Lees, A. J., Daniel, S., Agid, Y., Javoy‐Agid, F., Jenner, P., & Marsden, C. D. (1994) · Annals of Neurology · doi:10.1002/ana.410360305 · Cited by 1,161

Glutathione in Cancer Biology and Therapy

Estrela, J. M., Ortega, A., & Obrador, E. (2006) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360500523878 · Cited by 1,041

Nitric oxide in immunity and inflammation

Coleman, J. W. (2001) · International Immunopharmacology · doi:10.1016/s1567-5769(01)00086-8 · Cited by 945

Mitochondrial damage induced by conditions of oxidative stress

Kowaltowski, A. J., & Vercesi, A. E. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00216-0 · Cited by 866

Identification and characterization of Ref‐1, a nuclear protein that facilitates AP‐1 DNA‐binding activity.

Xanthoudakis, S., & Curran, T. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05097.x · Cited by 708

Metabolic zonation of the liver: Regulation and implications for liver function

Gebhardt, R. (1992) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(92)90055-5 · Cited by 607

Antioxidant Therapy in Acute Central Nervous System Injury: Current State

Gilgun-Sherki, Y., Rosenbaum, Z., Melamed, E., & Offen, D. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.2.271 · Cited by 568

N-Acetyl Cysteine as a Glutathione Precursor for Schizophrenia—A Double-Blind, Randomized, Placebo-Controlled Trial

Berk, M., Copolov, D., Dean, O., Lu, K., Jeavons, S., Schapkaitz, I., Anderson-Hunt, M., Judd, F., Katz, F., Katz, P., et al. (2008) · Biological Psychiatry · doi:10.1016/j.biopsych.2008.03.004 · Cited by 552

Schizophrenia: glutathione deficit in cerebrospinal fluid and prefrontal cortex in vivo

Do, K. Q., Trabesinger, A. H., Kirsten‐Krüger, M., Lauer, C. J., Dydak, U., Hell, D., Holsboer, F., Boesiger, P., & Cuénod, M. (2000) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2000.00229.x · Cited by 540

Structure of the Blood–Brain Barrier and Its Role in the Transport of Amino Acids

Hawkins, R. A., O’Kane, R. L., Simpson, I. A., & Viña, J. R. (2006) · The Journal of Nutrition · doi:10.1093/jn/136.1.218s · Cited by 453

The role of oxidative stress in the pathophysiology of hypertension

Rodrigo, R., González, J., & Paoletto, F. (2011) · Hypertension Research · doi:10.1038/hr.2010.264 · Cited by 436

Redox state is a central modulator of the balance between self-renewal and differentiation in a dividing glial precursor cell

Smith, J., Ladi, E., Mayer-Pröschel, M., & Noble, M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.170209797 · Cited by 399

Glutathione Precursor, N-Acetyl-Cysteine, Improves Mismatch Negativity in Schizophrenia Patients

Lavoie, S., Murray, M. M., Deppen, P., Knyazeva, M. G., Berk, M., Boulat, O., Bovet, P., Bush, A. I., Conus, P., Copolov, D., et al. (2008) · Neuropsychopharmacology · doi:10.1038/sj.npp.1301624 · Cited by 371

Reaction between S-Nitrosothiols and Thiols: Generation of Nitroxyl (HNO) and Subsequent Chemistry

Wong, P. S.-Y., Hyun, J., Fukuto, J. M., Shirota, F. N., DeMaster, E. G., Shoeman, D. W., & Nagasawa, H. T. (1998) · Biochemistry · doi:10.1021/bi973153g · Cited by 363

Cysteine Metabolism in Neuronal Redox Homeostasis

Paul, B. D., Sbodio, J. I., & Snyder, S. H. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2018.02.007 · Cited by 356

Autocatalytic, bistable, oscillatory networks of biologically relevant organic reactions

Semenov, S. N., Kraft, L. J., Ainla, A., Zhao, M., Baghbanzadeh, M., Campbell, V. E., Kang, K., Fox, J. M., & Whitesides, G. M. (2016) · Nature · doi:10.1038/nature19776 · Cited by 350

Systemic multicompartmental effects of the gut microbiome on mouse metabolic phenotypes

Claus, S. P., Tsang, T. M., Wang, Y., Cloarec, O., Skordi, E., Martin, F., Rezzi, S., Ross, A., Kochhar, S., Holmes, E., et al. (2008) · Molecular Systems Biology · doi:10.1038/msb.2008.56 · Cited by 334

The chemistry of nitroxyl (HNO) and implications in biology

Miranda, K. M. (2005) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2004.08.010 · Cited by 339

Glutathione: Antioxidant Properties Dedicated to Nanotechnologies

Gaucher, C., Boudier, A., Bonetti, J., Clarot, I., Leroy, P., & Parent, M. (2018) · Antioxidants · doi:10.3390/antiox7050062 · Cited by 332

A malarial cysteine proteinase is necessary for hemoglobin degradation by Plasmodium falciparum

Rosenthal, P. J., McKerrow, J. H., Aikawa, M., Nagasawa, H., & Leech, J. H. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113766 · Cited by 331

Defining Physiological Normoxia for Improved Translation of Cell Physiology to Animal Models and Humans

Keeley, T. P., & Mann, G. E. (2019) · Physiological Reviews · doi:10.1152/physrev.00041.2017 · Cited by 329

Unraveling the Potential Role of Glutathione in Multiple Forms of Cell Death in Cancer Therapy

Lv, H., Zhen, C., Liu, J., Yang, P., Hu, L., & Shang, P. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/3150145 · Cited by 320

Catalytic organometallic anticancer complexes

Dougan, S. J., Habtemariam, A., McHale, S. E., Parsons, S., & Sadler, P. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800076105 · Cited by 303

A biochemical rationale for the discrete behavior of nitroxyl and nitric oxide in the cardiovascular system

Miranda, K. M., Paolocci, N., Katori, T., Thomas, D. D., Ford, E., Bartberger, M. D., Espey, M. G., Kass, D. A., Feelisch, M., Fukuto, J. M., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1430507100 · Cited by 283

Astrocytes Provide Cysteine to Neurons by Releasing Glutathione

Wang, X. F., & Cynader, M. S. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0741434.x · Cited by 281

Glutathione activates virulence gene expression of an intracellular pathogen

Reniere, M. L., Whiteley, A. T., Hamilton, K. L., John, S. M., Lauer, P., Brennan, R. G., & Portnoy, D. A. (2015) · Nature · doi:10.1038/nature14029 · Cited by 277

Initial Characterization of the Glutamate-Cysteine Ligase Modifier Subunit Gclm(−/−) Knockout Mouse

Yang, Y., Dieter, M. Z., Chen, Y., Shertzer, H. G., Nebert, D. W., & Dalton, T. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209372200 · Cited by 269

Exploiting cancer cell vulnerabilities to develop a combination therapy for ras-driven tumors

De Raedt, T., Walton, Z., Yecies, J. L., Li, D., Chen, Y., Malone, C. F., Maertens, O., Jeong, S. M., Bronson, R. T., Lebleu, V., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.08.014 · Cited by 258

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

Glutathione and glutathione-dependent enzymes: From biochemistry to gerontology and successful aging

Lapenna, D. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102066 · Cited by 239

Schizophrenia and Oxidative Stress: Glutamate Cysteine Ligase Modifier as a Susceptibility Gene

Tosic, M., Ott, J., Barral, S., Bovet, P., Deppen, P., Gheorghita, F., Matthey, M.-L., Parnas, J., Preisig, M., Saraga, M., et al. (2006) · The American Journal of Human Genetics · doi:10.1086/507566 · Cited by 234

Polymeric micelles from poly (ethylene glycol)–poly (amino acid) block copolymer for drug and gene delivery

Osada, K., Christie, R. J., & Kataoka, K. (2009) · Journal of The Royal Society Interface · doi:10.1098/rsif.2008.0547.focus · Cited by 218

Impact of CHO Metabolism on Cell Growth and Protein Production: An Overview of Toxic and Inhibiting Metabolites and Nutrients

Pereira, S., Kildegaard, H. F., & Andersen, M. R. (2018) · Biotechnology Journal · doi:10.1002/biot.201700499 · Cited by 214

The Diverse Functions of Non-Essential Amino Acids in Cancer

Choi, B.-H., & Coloff, J. L. (2019) · Cancers · doi:10.3390/cancers11050675 · Cited by 213

Glutathione in Brain Disorders and Aging

Iskusnykh, I. Y., Zakharova, A. A., & Pathak, D. (2022) · Molecules · doi:10.3390/molecules27010324 · Cited by 213

Lipopolysaccharide Stimulates Mitochondrial Biogenesis via Activation of Nuclear Respiratory Factor-1

Suliman, H. B., Carraway, M. S., Welty-Wolf, K. E., Whorton, A. R., & Piantadosi, C. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304719200 · Cited by 189

Sex differences in inflammation, redox biology, mitochondria and autoimmunity

Di Florio, D. N., Sin, J., Coronado, M. J., Atwal, P. S., & Fairweather, D. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101482 · Cited by 185

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

Neuroprotective and Neurorescue Effects of a Novel Polymeric Nanoparticle Formulation of Curcumin (NanoCurc™) in the Neuronal Cell Culture and Animal Model: Implications for Alzheimer's disease

Ray, B., Bisht, S., Maitra, A., Maitra, A., & Lahiri, D. K. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-101374 · Cited by 177

IL-6 promotes nonthyroidal illness syndrome by blocking thyroxine activation while promoting thyroid hormone inactivation in human cells

Wajner, S. M., Goemann, I. M., Bueno, A. L., Larsen, P. R., & Maia, A. L. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44678 · Cited by 168

Glutamine drives glutathione synthesis and contributes to radiation sensitivity of A549 and H460 lung cancer cell lines

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

Substrate specificity of human ABCC4 (MRP4)-mediated cotransport of bile acids and reduced glutathione

Rius, M., Hummel-Eisenbeiss, J., Hofmann, A. F., & Keppler, D. (2006) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00354.2005 · Cited by 144

Age and sex differences in human skeletal muscle: Role of reactive oxygen species

Pansarasa, O., Castagna, L., Colombi, B., Vecchiet, J., Felzani, G., & Marzatico, F. (2000) · Free Radical Research · doi:10.1080/10715760000301451 · Cited by 135

Arsenic induces oxidative DNA damage in mammalian cells

Kessel, M., Liu, S. X., Xu, A., Santella, R., & Hei, T. K. (2002) · Molecular and Cellular Biochemistry · doi:10.1023/a:1015927406142 · Cited by 135

Protein glutathiolation by nitric oxide: An intracellular mechanism regulating redox protein modification

West, M. B., Hill, B. G., Xuan, Y.-T., Bhatnagar, A., West, M. B., Hill, B. G., Xuan, Y.-T., & Bhatnagar, A. (2006) · The FASEB Journal · doi:10.1096/fj.06-5843fje · Cited by 116

Glutathione deficit impairs myelin maturation: relevance for white matter integrity in schizophrenia patients

Monin, A., Baumann, P. S., Griffa, A., Xin, L., Mekle, R., Fournier, M., Butticaz, C., Klaey, M., Cabungcal, J. H., Steullet, P., et al. (2015) · Molecular Psychiatry · doi:10.1038/mp.2014.88 · Cited by 113

Oxidative stress and genetic markers of suboptimal antioxidant defense in the aging brain: A theoretical review

Salminen, L. E., & Paul, R. H. (2014) · Reviews in the Neurosciences · doi:10.1515/revneuro-2014-0046 · Cited by 113

Discriminating formation of HNO from other reactive nitrogen oxide species

Donzelli, S., Espey, M. G., Thomas, D. D., Mancardi, D., Tocchetti, C. G., Ridnour, L. A., Paolocci, N., King, S. B., Miranda, K. M., Lazzarino, G., et al. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.10.058 · Cited by 112

The role of mitochondria in aging of skeletal muscle

Figueiredo, P. A., Mota, M. P., Appell, H. J., & Duarte, J. A. (2008) · Biogerontology · doi:10.1007/s10522-007-9121-7 · Cited by 109

Protein oxidation of cytochrome c by reactive halogen species enhances its peroxidase activity

Chen, Y.-R., Deterding, L. J., Sturgeon, B. E., Tomer, K. B., & Mason, R. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200709200 · Cited by 110

New insights toward the acute non-thyroidal illness syndrome

Wajner, S. M., & Maia, A. L. (2012) · Frontiers in Endocrinology · doi:10.3389/fendo.2012.00008 · Cited by 105

Targeting multidrug resistance-associated protein 1 (MRP1)-expressing cancers: Beyond pharmacological inhibition

Hanssen, K. M., Haber, M., & Fletcher, J. I. (2021) · Drug Resistance Updates · doi:10.1016/j.drup.2021.100795 · Cited by 102

Aminopeptidase N mediates the utilization of the GSH precursor CysGly by cultured neurons

Dringen, R., Gutterer, J. M., Gros, C., & Hirrlinger, J. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.10042 · Cited by 104

Visualization of the compartmentalization of glutathione and protein‐glutathione mixed disulfides in cultured cells

Söderdahl, T., Enoksson, M., Lundberg, M., Holmgren, A., Ottersen, O. P., Orrenius, S., Bolcsfoldi, G., & Cotgreave, I. A. (2003) · The FASEB Journal · doi:10.1096/fj.02-0259fje · Cited by 99

Inducing the cell cycle arrest and apoptosis of oral KB carcinoma cells by hydroxychavicol: roles of glutathione and reactive oxygen species

Chang, M. C., Uang, B. J., Wu, H. L., Lee, J. J., Hahn, L. J., & Jeng, J. H. (2002) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0704492 · Cited by 99

Glutathione deficit during development induces anomalies in the rat anterior cingulate GABAergic neurons: Relevance to schizophrenia

Cabungcal, J.-H., Nicolas, D., Kraftsik, R., Cuénod, M., Do, K. Q., & Hornung, J.-P. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.01.003 · Cited by 96

Cellular Compartmentalization, Glutathione Transport and Its Relevance in Some Pathologies

Vázquez-Meza, H., Vilchis-Landeros, M. M., Vázquez-Carrada, M., Uribe-Ramírez, D., & Matuz-Mares, D. (2023) · Antioxidants · doi:10.3390/antiox12040834 · Cited by 94

Ferrous Fumarate Deteriorated Plasma Antioxidant Status in Patients with Crohn Disease

Erichsen, K., Hausken, T., Ulvik, R. J., Svardal, A., Berstad, A., & Berge, R. K. (2003) · Scandinavian Journal of Gastroenterology · doi:10.1080/00365520310000771 · Cited by 91

Asiaticoside: Attenuation of neurotoxicity induced by MPTP in a rat model of Parkinsonism via maintaining redox balance and up-regulating the ratio of Bcl-2/Bax

Xu, C.-L., Wang, Q.-Z., Sun, L.-M., Li, X.-M., Deng, J.-M., Li, L.-F., Zhang, J., Xu, R., & Ma, S.-P. (2012) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2011.09.014 · Cited by 85

Neuroprotective effects of madecassoside in early stage of Parkinson's disease induced by MPTP in rats

Xu, C.-L., Qu, R., Zhang, J., Li, L.-F., & Ma, S.-P. (2013) · Fitoterapia · doi:10.1016/j.fitote.2013.07.009 · Cited by 84

Redox remodeling as an immunoregulatory strategy

Yan, Z., & Banerjee, R. (2010) · Biochemistry · doi:10.1021/bi902022n · Cited by 82

Attenuation of doxorubicin-induced cardiac injury by mitochondrial glutaredoxin 2

Diotte, N. M., Xiong, Y., Gao, J., Chua, B. H. L., & Ho, Y.-S. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.10.014 · Cited by 78

Design of reversibly core cross-linked micelles sensitive to reductive environment

Cajot, S., Lautram, N., Passirani, C., & Jérôme, C. (2011) · Journal of Controlled Release · doi:10.1016/j.jconrel.2011.03.026 · Cited by 76

Decreased glutathione levels and altered antioxidant defense in an animal model of schizophrenia: Long-term effects of perinatal phencyclidine administration

Radonjić, N. V., Knežević, I. D., Vilimanovich, U., Kravić-Stevović, T., Marina, L. V., Nikolić, T., Todorović, V., Bumbaširević, V., & Petronijević, N. D. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2009.12.009 · Cited by 75

Role of peroxisome proliferator-activated receptor-α in fasting-mediated oxidative stress

Abdelmegeed, M. A., Moon, K.-H., Hardwick, J. P., Gonzalez, F. J., & Song, B.-J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.06.017 · Cited by 74

Development of Mesoporous Silica Nanomaterials As a Vehicle for Anticancer Drug Delivery

Yanes, R. E., & Tamanoi, F. (2012) · Therapeutic Delivery · doi:10.4155/tde.12.9 · Cited by 68

Direct correlation of glutathione and ascorbate and their dependence on age and season in human lymphocytes

Lenton, K. J., Therriault, H., Cantin, A. M., Fülöp, T., Payette, H., & Wagner, J. R. (2000) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/71.5.1194 · Cited by 67

Concurrent analysis of intracellular glutathione content and gap junctional intercellular communication

Barhoumi, R., Bowen, J. A., Stein, L. S., Echols, J., & Burghardt, R. C. (1993) · Cytometry · doi:10.1002/cyto.990140707 · Cited by 67

Amino Acids, Peptides, and Proteins

Dietzen, D. J. (2018) · Principles and Applications of Molecular Diagnostics · doi:10.1016/b978-0-12-816061-9.00013-8 · Cited by 82

Enzyme-cleavable polymeric micelles for the intracellular delivery of proapoptotic peptides

Kern, H. B., Srinivasan, S., Convertine, A. J., Hockenbery, D., Press, O. W., & Stayton, P. S. (2017) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.6b01178 · Cited by 63

Astrocyte control of fetal cortical neuron glutathione homeostasis: up‐regulation by ethanol

Rathinam, M. L., Watts, L. T., Stark, A. A., Mahimainathan, L., Stewart, J., Schenker, S., & Henderson, G. I. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03674.x · Cited by 60

Mixed Ligand Cu 2+ Complexes of a Model Therapeutic with Alzheimer’s Amyloid-β Peptide and Monoamine Neurotransmitters

Kenche, V. B., Zawisza, I., Masters, C. L., Bal, W., Barnham, K. J., & Drew, S. C. (2013) · Inorganic Chemistry · doi:10.1021/ic302289r · Cited by 59

Glutathione Reductase and a Mitochondrial Thioredoxin Play Overlapping Roles in Maintaining Iron-Sulfur Enzymes in Fission Yeast

Song, J.-Y., Cha, J., Lee, J., & Roe, J.-H. (2006) · Eukaryotic Cell · doi:10.1128/ec.00244-06 · Cited by 55

Dual regulation of SLC25A39 by AFG3L2 and iron controls mitochondrial glutathione homeostasis

Shi, X., DeCiucis, M., Grabinska, K. A., Kanyo, J., Liu, A., Lam, T. T., & Shen, H. (2024) · Molecular Cell · doi:10.1016/j.molcel.2023.12.008 · Cited by 54

Glutathione biosynthesis in the yeast pathogens Candida glabrata and Candida albicans: Essential in C. glabrata, and essential for virulence in C. albicans

Yadav, A. K., Desai, P. R., Rai, M. N., Kaur, R., Ganesan, K., & Bachhawat, A. K. (2011) · Microbiology · doi:10.1099/mic.0.045054-0 · Cited by 49

Ibuprofen and Glutathione Conjugate as a Potential Therapeutic Agent for Treating Alzheimer's Disease

Pinnen, F., Sozio, P., Cacciatore, I., Cornacchia, C., Mollica, A., Iannitelli, A., D′Aurizio, E., Cataldi, A., Zara, S., Nasuti, C., et al. (2011) · Archiv der Pharmazie · doi:10.1002/ardp.201000209 · Cited by 49

Role of glutathione in the oxidative stress response in the fungal pathogen Candida glabrata

Gutiérrez-Escobedo, G., Orta-Zavalza, E., Castaño, I., & De Las Peñas, A. (2013) · Current Genetics · doi:10.1007/s00294-013-0390-1 · Cited by 47

Changes in glutathione-dependent redox status and mitochondrial energetic strategies are part of the adaptive response during the filamentation process in Candida albicans

Guedouari, H., Gergondey, R., Bourdais, A., Vanparis, O., Bulteau, A. L., Camadro, J. M., & Auchère, F. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.07.006 · Cited by 45

Protective effect of centella triterpene saponins against cyclophosphamide-induced immune and hepatic system dysfunction in rats: its possible mechanisms of action

Duggina, P., Kalla, C. M., Varikasuvu, S. R., Bukke, S., & Tartte, V. (2015) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-015-0423-y · Cited by 44

Nuclear Factor-κB modulates cellular glutathione and prevents oxidative stress in cancer cells

Meng, Q., Peng, Z., Chen, L., Si, J., Dong, Z., & Xia, Y. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.08.002 · Cited by 39

Supplementation with n-acetylcysteine and taurine failed to restore glutathione content in liver of streptozotocin-induced diabetics rats but protected from oxidative stress

Patriarca, S., Furfaro, A. L., Domenicotti, C., Odetti, P., Cottalasso, D., Marinari, U. M., Pronzato, M. A., & Traverso, N. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2005.04.003 · Cited by 41

Protective role of bacillithiol in superoxide stress and Fe–S metabolism in Bacillus subtilis

Fang, Z., & Dos Santos, P. C. (2015) · MicrobiologyOpen · doi:10.1002/mbo3.267 · Cited by 38

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Control of angiogenesis dictated by picomolar superoxide levels

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Early onset senescence occurs when fibroblasts lack the glutamate–cysteine ligase modifier subunit

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Roles of Amino Acid Derivatives in the Regulation of Obesity

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An investigation of the effects of the antioxidants, ebselen or N-acetyl cysteine on human peripheral blood mononuclear cells and T cells

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