Glutathione: An Old and Small Molecule with Great Functions and New Applications in the Brain and in Alzheimer's Disease

Ferroptosis: An Iron-Dependent Form of Nonapoptotic Cell Death

Dixon, S. J., Lemberg, K. M., Lamprecht, M. R., Skouta, R., Zaitsev, E. M., Gleason, C. E., Patel, D. N., Bauer, A. J., Cantley, A. M., Yang, W. S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.042 · Cited by 18,691 · see citing works

Ferroptosis: A Regulated Cell Death Nexus Linking Metabolism, Redox Biology, and Disease

Stockwell, B. R., Friedmann Angeli, J. P., Bayir, H., Bush, A. I., Conrad, M., Dixon, S. J., Fulda, S., Gascón, S., Hatzios, S. K., Kagan, V. E., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.021 · Cited by 7,695 · see citing works

Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes

Esterbauer, H., Schaur, R. J., & Zollner, H. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90192-6 · Cited by 6,672 · see citing works

Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple

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

Cell Survival Responses to Environmental Stresses Via the Keap1-Nrf2-ARE Pathway

Kensler, T. W., Wakabayashi, N., & Biswal, S. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141046 · Cited by 3,630 · see citing works

An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress

Harding, H. P., Zhang, Y., Zeng, H., Novoa, I., Lu, P. D., Calfon, M. A., Sadri, N., Yun, C., Popko, B., Paules, R. S., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,336 · see citing works

2020 Alzheimer's disease facts and figures

(2020) · Alzheimer's & Dementia · doi:10.1002/alz.12068 · Cited by 2,353 · see citing works

Oxidative stress and the amyloid beta peptide in Alzheimer’s disease

Cheignon, C., Tomas, M., Bonnefont-Rousselot, D., Faller, P., Hureau, C., & Collin, F. (2018) · Redox Biology · doi:10.1016/j.redox.2017.10.014 · Cited by 2,185 · see citing works

The thioredoxin antioxidant system

Lu, J., & Holmgren, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.036 · Cited by 2,055 · see citing works

Antioxidant and redox regulation of gene transcription

Sen, C. K., & Packer, L. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.7.8635688 · Cited by 1,996 · see citing works

THIOREDOXIN

Holmgren, A. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.001321 · Cited by 1,955 · see citing works

Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease

Butterfield, D. A., & Halliwell, B. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-019-0132-6 · Cited by 1,954 · cited 1× · see citing works

Mechanisms of ferroptosis

Cao, J. Y., & Dixon, S. J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2194-1 · Cited by 1,515 · see citing works

NAD ⁺ /NADH and NADP ⁺ /NADPH in Cellular Functions and Cell Death: Regulation and Biological Consequences

Ying, W. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1672 · Cited by 1,494 · see citing works

Glutathione Homeostasis and Functions: Potential Targets for Medical Interventions

Lushchak, V. I. (2012) · Journal of Amino Acids · doi:10.1155/2012/736837 · Cited by 1,266 · cited 1× · see citing works

ApoE4 markedly exacerbates tau-mediated neurodegeneration in a mouse model of tauopathy

Initiative, A. D. N., Shi, Y., Yamada, K., Liddelow, S. A., Smith, S. T., Zhao, L., Luo, W., Tsai, R. M., Spina, S., Grinberg, L. T., et al. (2017) · Nature · doi:10.1038/nature24016 · Cited by 1,220 · see citing works

13 reasons why the brain is susceptible to oxidative stress

Cobley, J. N., Fiorello, M. L., & Bailey, D. M. (2018) · Redox Biology · doi:10.1016/j.redox.2018.01.008 · Cited by 1,215 · see citing works

Oxidative stress and Alzheimer disease

Christen, Y. (2000) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/71.2.621s · Cited by 1,158 · see citing works

APOE and Alzheimer’s disease: Advances in genetics, pathophysiology, and therapeutic approaches

Serrano-Pozo, A., Das, S., & Hyman, B. T. (2021) · The Lancet Neurology · doi:10.1016/s1474-4422(20)30412-9 · Cited by 1,037 · see citing works

Glutamate toxicity in a neuronal cell line involves inhibition of cystine transport leading to oxidative stress

Murphy, T. H., Miyamoto, M., Sastre, A., Schnaar, R. L., & COYLE, J. T. (1989) · Neuron · doi:10.1016/0896-6273(89)90043-3 · Cited by 1,033 · see citing works

Imaging iron stores in the brain using magnetic resonance imaging

Haacke, E. M., Cheng, N. Y. C., House, M. J., Liu, Q., Neelavalli, J., Ogg, R. J., Khan, A., Ayaz, M., Kirsch, W., & Obenaus, A. (2005) · Magnetic Resonance Imaging · doi:10.1016/j.mri.2004.10.001 · Cited by 995 · see citing works

Mitochondrial Glutathione, a Key Survival Antioxidant

Marı́, M., Morales, A., Colell, A., García‐Ruiz, C., & Fernández-Checa, J. C. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2695 · Cited by 986 · see citing works

Apolipoprotein E isoform-dependent amyloid deposition and neuritic degeneration in a mouse model of Alzheimer's disease

Holtzman, D. M., Bales, K. R., Tenkova, T., Fagan, A. M., Parsadanian, M., Sartorius, L. J., Mackey, B., Olney, J., McKeel, D., Wozniak, D., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.050004797 · Cited by 937 · see citing works

Ablation of ferroptosis regulator glutathione peroxidase 4 in forebrain neurons promotes cognitive impairment and neurodegeneration

Hambright, W. S., Fonseca, R. S., Chen, L., Na, R., & Ran, Q. (2017) · Redox Biology · doi:10.1016/j.redox.2017.01.021 · Cited by 851 · see citing works

Flavonoids Protect Neuronal Cells from Oxidative Stress by Three Distinct Mechanisms

Ishige, K., Schubert, D., & Sagara, Y. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00498-6 · Cited by 841 · see citing works

Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease

Tebay, L. E., Robertson, H., Durant, S. T., Vitale, S. R., Penning, T. M., Dinkova-Kostova, A. T., & Hayes, J. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.021 · Cited by 837 · see citing works

Coordinate Regulation of Glutathione Biosynthesis and Release by Nrf2-Expressing Glia Potently Protects Neurons from Oxidative Stress

Shih, A. Y., Johnson, D. A., Wong, G., Kraft, A. D., Jiang, L., Erb, H., Johnson, J. A., & Murphy, T. H. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-08-03394.2003 · Cited by 786 · see citing works

Apoptosis and glutathione: beyond an antioxidant

Franco, R., & Cidlowski, J. A. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.107 · Cited by 749 · see citing works

GPx4, Lipid Peroxidation, and Cell Death: Discoveries, Rediscoveries, and Open Issues

Maiorino, M., Conrad, M., & Ursini, F. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7115 · Cited by 709 · see citing works

Glyoxalase I – structure, function and a critical role in the enzymatic defence against glycation

Thornalley, P. J. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311343 · Cited by 615 · see citing works

Oxidative stress in the progression of Alzheimer disease in the frontal cortex

Ansari, M. A., & Scheff, S. W. (2010) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181cb5af4 · Cited by 605 · see citing works

Synthesis of the Antioxidant Glutathione in Neurons: Supply by Astrocytes of CysGly as Precursor for Neuronal Glutathione

Dringen, R., Pfeiffer, B., & Hamprecht, B. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-02-00562.1999 · Cited by 589 · see citing works

Neurofibrillary Tangles, Amyloid, and Memory in Aging and Mild Cognitive Impairment

Guillozet-Bongaarts, A. L., Weıntraub, S., Mash, D. C., & Mesulam, M. M. (2003) · Archives of Neurology · doi:10.1001/archneur.60.5.729 · Cited by 572 · see citing works

The formation of methylglyoxal from triose phosphates

Phillips, S. A., & Thornalley, P. J. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17638.x · Cited by 565 · see citing works

Electrophile Response Element-mediated Induction of the Cystine/Glutamate Exchange Transporter Gene Expression

Sasaki, H., Sato, H., Kuriyama-Matsumura, K., Sato, K., Maebara, K., Wang, H., Tamba, M., Itoh, K., Yamamoto, M. P., & Bannai, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208704200 · Cited by 544 · see citing works

Regulation of lipid peroxidation and ferroptosis in diverse species

Conrad, M., Kagan, V. E., Bayir, H., Pagnussat, G. C., Head, B., Traber, M. G., & Stockwell, B. R. (2018) · Genes & Development · doi:10.1101/gad.314674.118 · Cited by 544 · see citing works

Exchange of cystine and glutamate across plasma membrane of human fibroblasts.

Bannai, S. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35926-4 · Cited by 543 · see citing works

Nuclear Factor E2-Related Factor 2-Dependent Antioxidant Response Element Activation by tert -Butylhydroquinone and Sulforaphane Occurring Preferentially in Astrocytes Conditions Neurons against Oxidative Insult

Kraft, A. D., Johnson, D. A., & Johnson, J. A. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.3817-03.2004 · Cited by 541 · see citing works

The Molecular Effects of Acrolein

Kehrer, J. P. (2000) · Toxicological Sciences · doi:10.1093/toxsci/57.1.6 · Cited by 532 · see citing works

Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling

Cox, A. G., Winterbourn, C. C., & Hampton, M. B. (2009) · Biochemical Journal · doi:10.1042/bj20091541 · Cited by 530 · 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

Synaptic NMDA receptor activity boosts intrinsic antioxidant defenses

Papadia, S., Soriano, F. X., Léveillé, F., Martel, M.-A., Dakin, K. A., Hansen, H. H., Kaindl, A., Sifringer, M., Fowler, J., Stefovska, V., et al. (2008) · Nature Neuroscience · doi:10.1038/nn2071 · Cited by 498 · see citing works

Striking while the iron is hot: Iron metabolism and ferroptosis in neurodegeneration

Masaldan, S., Bush, A. I., Devos, D., Rolland, A., & Moreau, C. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.033 · Cited by 485 · see citing works

Recent Trends in Glutathione Biochemistry—Glutathione–Protein Interactions: A Molecular Link between Oxidative Stress and Cell Proliferation?

Cotgreave, I. A., & Gerdes, R. G. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7812 · Cited by 481 · see citing works

Endogenous generation of reactive oxidants and electrophiles and their reactions with DNA and protein

Marnett, L. J., Riggins, J. N., & West, J. D. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200318022 · Cited by 476 · see citing works

Protein Disulfide Bond Formation in the Cytoplasm during Oxidative Stress

Cumming, R. C., Andon, N. L., Haynes, P. A., Park, M., Fischer, W. H., & Schubert, D. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312267200 · Cited by 463 · see citing works

Autopsy Samples of Alzheimer's Cortex Show Increased Peroxidation In Vitro

Subbarao, K. V., Richardson, J. S., & Ang, L. C. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb08858.x · Cited by 463 · see citing works

Constitutive and β-Naphthoflavone-induced Expression of the Human γ-Glutamylcysteine Synthetase Heavy Subunit Gene Is Regulated by a Distal Antioxidant Response Element/TRE Sequence

Mulcahy, R., Wartman, M. A., Bailey, H. H., & Gipp, J. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.11.7445 · Cited by 455 · see citing works

Peroxide detoxification by brain cells

Dringen, R., Pawlowski, P. G., & Hirrlinger, J. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20280 · Cited by 452 · see citing works

Lipid peroxidation in aging brain and Alzheimer’s disease1,2 1Guest Editors: Mark A. Smith and George Perry 2This article is part of a series of reviews on “Causes and Consequences of Oxidative Stress in Alzheimer’s Disease.” The full list of papers may be found on the homepage of the journal.

Montine, T. J., Neely, M. D., Quinn, J. F., Beal, M. F., Markesbery, W. R., Roberts, L. J., & Morrow, J. D. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00807-9 · Cited by 449 · see citing works

Acrolein is increased in Alzheimer’s disease brain and is toxic to primary hippocampal cultures

Lovell, M. A., Xie, C., & Markesbery, W. R. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00235-9 · Cited by 449 · see citing works

Ferroptosis-Induced Endoplasmic Reticulum Stress: Cross-talk between Ferroptosis and Apoptosis

Lee, Y., Lee, D.-H., Choudry, H. A., Bartlett, D. L., & Lee, Y. J. (2018) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-18-0055 · Cited by 434 · see citing works

Targeting Nrf2 to Suppress Ferroptosis and Mitochondrial Dysfunction in Neurodegeneration

Abdalkader, M., Lampinen, R., Kanninen, K. M., Malm, T., & Liddell, J. R. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00466 · Cited by 421 · see citing works

Unraveling the Truth About Antioxidants: Mitohormesis explains ROS-induced health benefits

Ristow, M. (2014) · Nature Medicine · doi:10.1038/nm.3624 · Cited by 417 · cited 1× · see citing works

Measurement of Oxidized/Reduced Glutathione Ratio

Owen, J. B., & Butterfield, D. A. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-756-3_18 · Cited by 411 · see citing works

Protein‐Bound Acrolein

Calingasan, N. Y., Uchida, K., & Gibson, G. E. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0720751.x · Cited by 400 · see citing works

Astrocytes as secretory cells of the central nervous system: idiosyncrasies of vesicular secretion

Verkhratsky, A., Matteoli, M., Parpura, V., Mothet, J., & Zorec, R. (2016) · The EMBO Journal · doi:10.15252/embj.201592705 · Cited by 397 · see citing works

Increased levels of 4-hydroxynonenal and acrolein, neurotoxic markers of lipid peroxidation, in the brain in Mild Cognitive Impairment and early Alzheimer's disease

Williams, T. I., Lynn, B. C., Markesbery, W. R., & Lovell, M. A. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.06.004 · Cited by 391 · see citing works

Neurohormetic phytochemicals: low-dose toxins that induce adaptive neuronal stress responses

Mattson, M. P., & Cheng, A. (2006) · Trends in Neurosciences · doi:10.1016/j.tins.2006.09.001 · Cited by 356 · see citing works

Recent advancements in liposomes targeting strategies to cross blood-brain barrier (BBB) for the treatment of Alzheimer's disease

Agrawal, M., Ajazuddin, Tripathi, D. K., Saraf, S., Saraf, S., Antimisiaris, S. G., Mourtas, S., Hammarlund-Udenaes, M., & Alexander, A. (2017) · Journal of Controlled Release · doi:10.1016/j.jconrel.2017.05.019 · Cited by 356 · see citing works

Metals and amyloid‐β in Alzheimer's disease

Maynard, C. J., Bush, A. I., Masters, C. L., Cappai, R., & Li, Q. (2005) · International Journal of Experimental Pathology · doi:10.1111/j.0959-9673.2005.00434.x · Cited by 353 · see citing works

The relationship of biliary glutathione disulfide efflux and intracellular glutathione disulfide content in perfused rat liver.

Akerboom, T. P. M., Bilzer, M., & Sies, H. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34713-6 · Cited by 342 · see citing works

Brain Glutathione Levels – A Novel Biomarker for Mild Cognitive Impairment and Alzheimer’s Disease

Mandal, P. K., Saharan, S., Tripathi, M., & Murari, G. (2015) · Biological Psychiatry · doi:10.1016/j.biopsych.2015.04.005 · Cited by 339 · see citing works

Cloning and Expression of a Novel Human Glutaredoxin (Grx2) with Mitochondrial and Nuclear Isoforms

Lundberg, M., Johansson, C., Chandra, J., Enoksson, M., Jacobsson, G., Lundström-Ljung, J., Johansson, M., & Holmgren, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011605200 · Cited by 335 · see citing works

Oxidative stress in blood in Alzheimer's disease and mild cognitive impairment: A meta-analysis

Schrag, M., Mueller, C., Zabel, M. K., Crofton, A. R., Kirsch, W. M., Ghribi, O., Squitti, R., & Perry, G. L. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.07.005 · Cited by 335 · 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

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 · see citing works

Compartmentation of Glutathione: Implications for the Study of Toxicity and Disease

Smith, C. V., Jones, D. P., Guenthner, T. M., Lash, L. H., & Lauterburg, B. H. (1996) · Toxicology and Applied Pharmacology · doi:10.1006/taap.1996.0191 · Cited by 331 · see citing works

Transport of cystine and cysteine in mammalian cells

Bannai, S. (1984) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(84)90014-5 · Cited by 329 · see citing works

Human Mitochondrial Glutaredoxin Reduces S-Glutathionylated Proteins with High Affinity Accepting Electrons from Either Glutathione or Thioredoxin Reductase

Johansson, C., Lillig, C. H., & Holmgren, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312719200 · Cited by 320 · see citing works

Molecular Basis of Electrophilic and Oxidative Defense: Promises and Perils of Nrf2

Ma, Q., & He, X. (2012) · Pharmacological Reviews · doi:10.1124/pr.110.004333 · Cited by 317 · see citing works

Characterization and proteomic analysis of ovarian cancer-derived exosomes

Liang, B., Peng, P., Chen, S., Li, L., Zhang, M., Cao, D., Yang, J., Li, H., Gui, T., Li, X., et al. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2012.12.029 · Cited by 309 · see citing works

The Nrf2–ARE cytoprotective pathway in astrocytes

Vargas, M. R., & Johnson, J. A. (2009) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399409001094 · Cited by 289 · see citing works

Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis

Morgan, B., Ezeriņa, D., Amoako, T. N. E., Riemer, J., Seedorf, M., & Dick, T. P. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1142 · Cited by 288 · see citing works

Pharmacokinetics, Brain Delivery, and Efficacy in Brain Tumor-Bearing Mice of Glutathione Pegylated Liposomal Doxorubicin (2B3-101)

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

Oxytosis/Ferroptosis—(Re-) Emerging Roles for Oxidative Stress-Dependent Non-apoptotic Cell Death in Diseases of the Central Nervous System

Lewerenz, J., Ates, G., Methner, A., Conrad, M., & Maher, P. A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00214 · Cited by 273 · see citing works

System xc− and Thioredoxin Reductase 1 Cooperatively Rescue Glutathione Deficiency

Mandal, P. K., Seiler, A., Perisic, T., Kölle, P., Banjac Canak, A., Förster, H., Weiss, N., Kremmer, E., Lieberman, M. W., Bannai, S., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.121327 · Cited by 269 · see citing works

Regulation of heat shock protein 70 release in astrocytes: Role of signaling kinases

Taylor, A. R., Robinson, M., Gifondorwa, D. J., Tytell, M., & Milligan, C. E. (2007) · Developmental Neurobiology · doi:10.1002/dneu.20559 · Cited by 261 · see citing works

Neuronal changes in normal human aging and Alzheimer's disease.

Uylings, H., & de Brabander, J. D. (2002) · Brain and Cognition · doi:10.1006/brcg.2001.1500 · Cited by 260 · see citing works

Glutathione Metabolism during Aging and in Alzheimer Disease

LIU, H., Wang, H., Shenvi, S. V., Hagen, T. M., & LIU, R. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1297.059 · Cited by 258 · see citing works

The Enzymes of Glutathione Synthesis: γ‐Glutamylcysteine Synthetase

Griffith, O. W., & Mulcahy, R. (1999) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123195.ch7 · Cited by 254 · see citing works

Increased CSF F 2 -isoprostane concentration in probable AD

Montine, T. J., Beal, M. F., Cudkowicz, M., O’Donnell, H., Margolin, R. A., McFarland, L. L., Bachrach, A., Zackert, W. E., Roberts, L. J., & Morrow, J. D. (1999) · Neurology · doi:10.1212/wnl.52.3.562 · Cited by 251 · see citing works

Molecular mechanisms of reduced glutathione transport: role of the MRP/CFTR/ABCC and OATP/SLC21A families of membrane proteins

Ballatori, N., Hammond, C. L., Cunningham, J. B., Krance, S. M., & Marchan, R. (2004) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.09.008 · Cited by 247 · see citing works

Redox compartmentalization and cellular stress

Jones, D. P., & Go, Y.-M. (2010) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01266.x · Cited by 246 · see citing works

Isoprostanes and related products of lipid peroxidation in neurodegenerative diseases

Montine, K. S., Quinn, J. F., Zhang, J., Fessel, J. P., Roberts, L. J., Morrow, J. D., & Montine, T. J. (2003) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2003.10.010 · Cited by 242 · see citing works

Oxidative damage and protection by antioxidants in the frontal cortex of Alzheimer’s disease is related to the apolipoprotein E genotype

Ramassamy, C., Averill‐Bates, D. A., Beffert, U., Bastianetto, S., Théroux, L., Lussier‐Cacan, S., Cohn, J. S., Christen, Y., Davignon, J., Quirion, R., et al. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00102-1 · Cited by 240 · see citing works

Depletion of GSH in glial cells induces neurotoxicity: relevance to aging and degenerative neurological diseases

Lee, M., Cho, T., Jantaratnotai, N., Wang, Y. T., McGeer, E. G., & McGeer, P. L. (2010) · The FASEB Journal · doi:10.1096/fj.09-149997 · Cited by 239 · see citing works

Glutathione and Glutaredoxin Act as a Backup of Human Thioredoxin Reductase 1 to Reduce Thioredoxin 1 Preventing Cell Death by Aurothioglucose

Du, Y., Zhang, H., Lu, J., & Holmgren, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.392225 · Cited by 230 · see citing works

Hormesis, cellular stress response and vitagenes as critical determinants in aging and longevity

Calabrese, V., Cornelius, C., Cuzzocrea, S., Iavicoli, I., Rizzarelli, E., & Calabrese, E. J. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.10.007 · Cited by 225 · see citing works

BCL-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

Blood-Brain Barrier Restriction of Peptides and the Low Uptake of Enkephalins*

Cornford, E. M., Braun, L. D., Crane, P. D., & Oldendorf, W. H. (1978) · Endocrinology · doi:10.1210/endo-103-4-1297 · Cited by 220 · see citing works

Oxidative stress and aging: Is methylglyoxal the hidden enemy?This review is one of a selection of papers published in a Special Issue on Oxidative Stress in Health and Disease.

Desai, K. M., Chang, T., Wang, H., Banigesh, A., Dhar, A., Liu, J., Untereiner, A. A., & Wu, L. (2010) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y10-001 · Cited by 211 · see citing works

Oxidative stress factors in Parkinson’s disease

Dorszewska, J., Kowalska, M., Prendecki, M., Piekut, T., Kozłowska, J., & Kozubski, W. P. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.300980 · Cited by 211 · see citing works

Nrf2- and ATF4-Dependent Upregulation of xCT Modulates the Sensitivity of T24 Bladder Carcinoma Cells to Proteasome Inhibition

Ye, P., Mimura, J., Okada, T., Sato, H., Liu, T., Maruyama, A., Οhyama, C., & Itoh, K. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00221-14 · Cited by 209 · see citing works

Effects of N-acetylcysteine, oral glutathione (GSH) and a novel sublingual form of GSH on oxidative stress markers: A comparative crossover study.

Schmitt, B., Vicenzi, M., Garrel, C., & Denis, F. M. (2015) · Redox Biology · doi:10.1016/j.redox.2015.07.012 · Cited by 208 · see citing works

AGEs induce Alzheimer-like tau pathology and memory deficit via RAGE-mediated GSK-3 activation

Li, X., Lv, B.-L., Xie, J., Liu, J., Zhou, X., & Wang, J. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.02.003 · Cited by 207 · see citing works

Brain Iron Homeostasis: From Molecular Mechanisms To Clinical Significance and Therapeutic Opportunities

Singh, N., Haldar, S., Tripathi, A. K., Horback, K., Wong, J., Sharma, D., Beserra, A., Suda, S., Anbalagan, C., Dev, S., et al. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4931 · Cited by 205 · see citing works

Temporal Profile of Matrix Metalloproteinases and Their Inhibitors After Spontaneous Intracerebral Hemorrhage

Álvarez‐Sabín, J., Delgado, P., Abilleira, S., Molina, C. A., Arenillas, J. F., Ribó, M., Santamarina, E., Quintana, M., Monasterio, J., & Montaner, J. (2004) · Stroke · doi:10.1161/01.str.0000126827.69286.90 · Cited by 202 · see citing works

Human p53 Is Inhibited by Glutathionylation of Cysteines Present in the Proximal DNA-Binding Domain during Oxidative Stress,

Velu, C. S., Niture, S. K., Doneanu, C. E., Pattabiraman, N., & Srivenugopal, K. S. (2007) · Biochemistry · doi:10.1021/bi700425y · Cited by 201 · see citing works

Brain oxidative stress: Detection and mapping of anti-oxidant marker ‘Glutathione’ in different brain regions of healthy male/female, MCI and Alzheimer patients using non-invasive magnetic resonance spectroscopy

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

Evidence of an oxidative challenge in the Alzheimer's brain

Balázs, L., & Leon, M. (1994) · Neurochemical Research · doi:10.1007/bf00965146 · Cited by 196 · see citing works

Astrocyte NMDA receptors' activity sustains neuronal survival through a Cdk5–Nrf2 pathway

Jimenez-Blasco, D., Santofimia-Castaño, P., Gonzalez, A., Almeida, A., & Bolaños, J. P. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2015.49 · Cited by 196 · see citing works

Oxidative Insults Are Associated with Apolipoprotein E Genotype in Alzheimer's Disease Brain

Ramassamy, C., Averill‐Bates, D. A., Beffert, U., Théroux, L., Lussier‐Cacan, S., Cohn, J. S., Christen, Y., Schoofs, A. R., Davignon, J., & Poirier, J. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.1999.0273 · Cited by 194 · see citing works

Distribution of oxidized and reduced forms of glutathione and cysteine in rat plasma

Lash, L. H., & Jones, D. P. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90065-7 · Cited by 193 · see citing works

Loss of System xc−Does Not Induce Oxidative Stress But Decreases Extracellular Glutamate in Hippocampus and Influences Spatial Working Memory and Limbic Seizure Susceptibility

Bundel, D. D., Schallier, A., Loyens, E., Fernando, R. N., Miyashita, H., Liefferinge, J. V., Vermoesen, K., Bannai, S., Sato, H., Michotte, Y. M., et al. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.5465-10.2011 · Cited by 193 · see citing works

A Novel Role for Human Sulfiredoxin in the Reversal of Glutathionylation

Findlay, V. J., Townsend, D. M., Morris, T. E., Fraser, J. P., He, L., & Tew, K. D. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0484 · Cited by 193 · see citing works

Neuronal development is promoted by weakened intrinsic antioxidant defences due to epigenetic repression of Nrf2

Bell, K. F. S., Al-Mubarak, B., Martel, M.-A., McKay, S., Wheelan, N., Hasel, P., Márkus, N. M., Baxter, P., Deighton, R. F., Serio, A., et al. (2015) · Nature Communications · doi:10.1038/ncomms8066 · Cited by 191 · see citing works

Acrolein-induced oxygen radical formation

Adams, J. D., Jr., & Klaidman, L. K. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90058-3 · Cited by 191 · see citing works

Enhanced brain delivery of liposomal methylprednisolone improved therapeutic efficacy in a model of neuroinflammation

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

Proteomic identification of HNE-bound proteins in early Alzheimer disease: Insights into the role of lipid peroxidation in the progression of AD

Reed, T. T., Pierce, W. M., Markesbery, W. R., & Butterfield, D. A. (2009) · Brain Research · doi:10.1016/j.brainres.2009.04.009 · Cited by 190 · see citing works

Involvement of glutaredoxin-1 and thioredoxin-1 in β-amyloid toxicity and Alzheimer's disease

Akterin, S., Cowburn, R. F., Miranda‐Vizuete, A., Jiménez, A., Bogdanović, N., Winblad, B. G., & Cedazo-Mı́nguez, Á. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401818 · Cited by 182 · see citing works

Damage to Lipids, Proteins, DNA, and RNA in Mild Cognitive Impairment

Markesbery, W. R., & Lovell, M. A. (2007) · Archives of Neurology · doi:10.1001/archneur.64.7.954 · Cited by 182 · see citing works

Mitochondrial Glutathione: Regulation and Functions

Calabrese, G., Morgan, B., & Riemer, J. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7121 · Cited by 182 · see citing works

Gene expression profiling reveals a signaling role of glutathione in redox regulation

Fratelli, M., Goodwin, L. O., Ørom, U. A., Lombardi, S., Tonelli, R., Mengozzi, M., & Ghezzi, P. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504398102 · Cited by 180 · see citing works

Thiol redox homeostasis in neurodegenerative disease

McBean, G. J., Aslan, M., Griffiths, H. R., & Torrão, R. C. (2015) · Redox Biology · doi:10.1016/j.redox.2015.04.004 · Cited by 178 · see citing works

Disruption of mitochondrial redox circuitry in oxidative stress

Jones, D. P. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2006.07.008 · Cited by 176 · see citing works

Transcriptional control of cystine/glutamate transporter gene by amino acid deprivation

Sato, H., Nomura, S., Maebara, K., Sato, K., Tamba, M., & Bannai, S. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.10.009 · Cited by 176 · see citing works

The cytosolic redox state of astrocytes: Maintenance, regulation and functional implications for metabolite trafficking

Hirrlinger, J., & Dringen, R. (2009) · Brain Research Reviews · doi:10.1016/j.brainresrev.2009.10.003 · Cited by 171 · see citing works

Effects of Oral Glutathione Supplementation on Systemic Oxidative Stress Biomarkers in Human Volunteers

Allen, J., & Bradley, R. D. (2011) · The Journal of Alternative and Complementary Medicine · doi:10.1089/acm.2010.0716 · Cited by 170 · see citing works

Repeated‐Dose Oral N‐Acetylcysteine in Parkinson's Disease: Pharmacokinetics and Effect on Brain Glutathione and Oxidative Stress

Coles, L. D., Tuite, P. J., Öz, G., Mishra, U. R., Kartha, R. V., Sullivan, K. M., Cloyd, J. C., & Terpstra, M. (2018) · The Journal of Clinical Pharmacology · doi:10.1002/jcph.1008 · Cited by 170 · see citing works

Distribution of Cystine/Glutamate Exchange Transporter, System xc−, in the Mouse Brain

Sato, H., Tamba, M., Okuno, S., Sato, K., Keino‐Masu, K., Masu, M., & Bannai, S. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-18-08028.2002 · Cited by 167 · see citing works

Peripheral levels of glutathione and protein oxidation as markers in the development of Alzheimer's disease from Mild Cognitive Impairment

Bermejo‐Bescós, P., Martín‐Aragón, S., Benedı́, J., Susín, C., Felici, E., Gil, P., Ribera, J. M., & Villar, Á. (2008) · Free Radical Research · doi:10.1080/10715760701861373 · Cited by 167 · see citing works

An increase in S‐glutathionylated proteins in the Alzheimer's disease inferior parietal lobule, a proteomics approach

Newman, S. F., Rukhsana Sultana, A., Marzia Perluigi, A., Coccia, R., Cai, J., Pierce, W. M. J., Klein, J. B., Turner, D. M., & Butterfield, D. A. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21275 · Cited by 166 · 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

Role of By-Products of Lipid Oxidation in Alzheimer's Disease Brain: A Focus on Acrolein

Singh, M., Nam, D. T., Arseneault, M., & Ramassamy, C. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100405 · Cited by 162 · see citing works

AGEs/RAGE complex upregulates BACE1 via NF-κB pathway activation

Guglielmotto, M., Aragno, M., Tamagno, E., Vercellinatto, I., Visentin, S., Medana, C., Catalano, M. G., Smith, M. A., Perry, G. L., Danni, O., et al. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.05.026 · Cited by 162 · see citing works

Fisetin Lowers Methylglyoxal Dependent Protein Glycation and Limits the Complications of Diabetes

Maher, P. A., Dargusch, R., Ehren, J. L., Okada, S., Sharma, K., & Schubert, D. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021226 · Cited by 161 · see citing works

Actin Glutathionylation Increases in Fibroblasts of Patients with Friedreich's Ataxia

Pastore, A., Tozzi, G., Gaeta, L. M., Bertini, E., Serafini, V., Cesare, S. D., Bonetto, V., Casoni, F., Carrozzo, R., Federici, G., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301872200 · Cited by 161 · see citing works

Apolipoprotein E Is Present in Hippocampal Neurons without Neurofibrillary Tangles in Alzheimer's Disease and in Age-Matched Controls

Han, S., Hulette, C., Saunders, A. M., Einstein, G., Pericak‐Vance, M. A., Strittmatter, W. J., Roses, A. D., & Schmechel, D. E. (1994) · Experimental Neurology · doi:10.1006/exnr.1994.1108 · Cited by 155 · see citing works

Enhanced glutathione PEGylated liposomal brain delivery of an anti-amyloid single domain antibody fragment in a mouse model for Alzheimer's disease

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

Advanced glycation end product level, diabetes, and accelerated cognitive aging

Yaffe, K. S., Lindquist, K. J., Schwartz, A. V., Vitartas, C., Vittinghoff, E., Satterfield, S., Simonsick, E. M., Launer, L. J., Rosano, C., Cauley, J. A., et al. (2011) · Neurology · doi:10.1212/wnl.0b013e3182315a56 · Cited by 151 · see citing works

Mitochondrial Cholesterol Loading Exacerbates Amyloid β Peptide-Induced Inflammation and Neurotoxicity

Fernández, A., Llacuna, L., Fernández-Checa, J. C., & Colell, A. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4909-08.2009 · Cited by 150 · see citing works

Glutathione PEGylated liposomes: pharmacokinetics and delivery of cargo across the blood–brain barrier in rats

Rip, 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

Amyloid‐β induces disulfide bonding and aggregation of GAPDH in Alzheimer's disease

Cumming, R. C., & Schubert, D. A. (2005) · The FASEB Journal · doi:10.1096/fj.05-4195fje · Cited by 147 · see citing works

Serum concentration of an inflammatory glycotoxin, methylglyoxal, is associated with increased cognitive decline in elderly individuals

Beeri, M. S., Moshier, E. L., Schmeidler, J., Godbold, J., Uribarri, J., Reddy, S., Sano, M. C., Grossman, H. T., Cai, W., Vlassara, H., et al. (2011) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2011.10.007 · Cited by 145 · see citing works

Glutathione release from cultured brain cells: Multidrug resistance protein 1 mediates the release of GSH from rat astroglial cells

Hirrlinger, J., Schulz, J. B., & Dringen, R. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10308 · Cited by 142 · see citing works

Heat shock proteins and hormesis in the diagnosis and treatment of neurodegenerative diseases

Dattilo, S., Mancuso, C., Koverech, G., Mauro, P. D., Ontario, M. L., Petralia, C. C. T., Petralia, A., Maiolino, L., Serra, A., Calabrese, E. J., et al. (2015) · Immunity & Ageing · doi:10.1186/s12979-015-0046-8 · Cited by 140 · see citing works

Effect of antioxidants on cultured human diploid fibroblasts exposed to cystine-free medium

Bannai, S., Tsukeda, H., & Okumura, H. (1977) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(77)90623-4 · Cited by 139 · see citing works

Synaptic NMDA receptor activity is coupled to the transcriptional control of the glutathione system

Baxter, P. S., Bell, K. F. S., Hasel, P., Kaindl, A. M., Fricker, M., Thomson, D., Cregan, S. P., Gillingwater, T. H., & Hardingham, G. E. (2015) · Nature Communications · doi:10.1038/ncomms7761 · Cited by 139 · see citing works

Redox status in mammalian cells and stem cells during culture in vitro: Critical roles of Nrf2 and cystine transporter activity in the maintenance of redox balance

Ishii, T., & Mann, G. E. (2014) · Redox Biology · doi:10.1016/j.redox.2014.04.008 · Cited by 137 · see citing works

Reactive Metabolites and AGE/RAGE-Mediated Cellular Dysfunction Affect the Aging Process – A Mini-Review

Fleming, T. H., Humpert, P. M., Nawroth, P. P., & Bierhaus, A. (2010) · Gerontology · doi:10.1159/000322087 · Cited by 135 · see citing works

The selection between apoptosis and necrosis is differentially regulated in hydrogen peroxide-treated and glutathione-depleted human promonocytic cells

Troyano, A., Sancho, P., Fernández, C., de Blas, E., Bernardi, P., & Aller, P. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401249 · Cited by 133 · see citing works

Lipidomic and proteomic characterization of platelet extracellular vesicle subfractions from senescent platelets

Pienimaeki‐Roemer, A., Kuhlmann, K., Böttcher, A., Konovalova, T., Black, A., Orsó, E., Liebisch, G., Ahrens, M., Eisenacher, M., Meyer, H. E., et al. (2014) · Transfusion · doi:10.1111/trf.12874 · Cited by 126 · see citing works

Randomized controlled trial of oral glutathione supplementation on body stores of glutathione

Richie, J. P., Nichenametla, S. N., Neidig, W., Calcagnotto, A., Haley, J. S., Schell, T. D., & Muscat, J. E. (2014) · European Journal of Nutrition · doi:10.1007/s00394-014-0706-z · Cited by 124 · see citing works

Amino acids, glutathione, and glutathione transferase activity in the brains of patients with Alzheimer's disease

Perry, T. L., Yong, V. W., Bergeron, C., Hansen, S., & Jones, K. L. (1987) · Annals of Neurology · doi:10.1002/ana.410210403 · Cited by 121 · see citing works

The Cerebrocortical Areas in Normal Brain Aging and in Alzheimer's Disease: Noticeable Differences in the Lipid Peroxidation Level and in Antioxidant Defense

Karelson, E., Bogdanović, N., Garlind, A., Winblad, B. G., Zilmer, K., Kullisaar, T., Vihalemm, T., Kairane, C., & Zilmer, M. (2001) · Neurochemical Research · doi:10.1023/a:1010942929678 · Cited by 114 · see citing works

F 2 -Isoprostanes in Alzheimer and Other Neurodegenerative Diseases

Montine, T. J., Montine, K. S., McMahan, W., Markesbery, W. R., Quinn, J. F., & Morrow, J. D. (2004) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.269 · Cited by 113 · see citing works

Gamma-glutamyltransferase activity in exosomes as a potential marker for prostate cancer

Kawakami, K., Fujita, Y., Matsuda, Y., Arai, T., Horie, K., Kameyama, K., Kato, T., Masunaga, K., Kasuya, Y., Tanaka, M., et al. (2017) · BMC Cancer · doi:10.1186/s12885-017-3301-x · Cited by 113 · see citing works

Oral supplementation with liposomal glutathione elevates body stores of glutathione and markers of immune function

Sinha, R., Sinha, I., Calcagnotto, A., Trushin, N., Haley, J. S., Schell, T. D., & Richie, J. P. (2017) · European Journal of Clinical Nutrition · doi:10.1038/ejcn.2017.132 · Cited by 111 · see citing works

Metabolism of selenium compounds catalyzed by the mammalian selenoprotein thioredoxin reductase

Lu, J., Berndt, C., & Holmgren, A. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.04.013 · Cited by 108 · see citing works

Age- and stage-dependent glyoxalase I expression and its activity in normal and Alzheimer's disease brains

Kuhla, B., Boeck, K., Schmidt, A., Ogunlade, V., Arendt, T., Münch, G., & Lüth, H.-J. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.11.007 · Cited by 108 · see citing works

Insights into Deglutathionylation Reactions

Peltoniemi, M. J., Karala, A., Jurvansuu, J. K., Kinnula, V. L., & Ruddock, L. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605602200 · Cited by 107 · see citing works

Free radical-mediated damage to brain in Alzheimer's disease and its transgenic mouse models

Sonnen, J. A., Breitner, J. C. S., Lovell, M. A., Markesbery, W. R., Quinn, J. F., & Montine, T. J. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.04.022 · Cited by 103 · see citing works

Potentiation of glutathione loss and nerve cell death by the transition metals iron and copper: Implications for age-related neurodegenerative diseases

Maher, P. A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.11.015 · Cited by 102 · see citing works

Role of microglial redox balance in modulation of neuroinflammation

Innamorato, N. G., Lastres‐Becker, I., & Cuadrado, A. (2009) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32832a3225 · Cited by 100 · see citing works

Enhanced Brain Delivery of the Opioid Peptide DAMGO in Glutathione PEGylated Liposomes: A Microdialysis Study

Lindqvist, A., Rip, J., Gaillard, P. J., Björkman, S. E., & Hammarlund‐Udenaes, M. (2012) · Molecular Pharmaceutics · doi:10.1021/mp300272a · Cited by 100 · see citing works

Competition between transport of glutathione disulfide (GSSG) and glutathione S‐conjugates from perfused rat liver into bile

Akerboom, T. P. M., Bilzer, M., & Sies, H. (1982) · FEBS Letters · doi:10.1016/0014-5793(82)80523-1 · Cited by 100 · see citing works

Oxidative stress and hippocampal synaptic protein levels in elderly cognitively intact individuals with Alzheimer’s disease pathology

Scheff, S. W., Ansari, M. A., & Mufson, E. J. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.02.030 · Cited by 100 · see citing works

Lipid peroxidation in neurodegeneration

Peña‐Bautista, C., Vento, M., Baquero, M., & Cháfer‐Pericás, C. (2019) · Clinica Chimica Acta · doi:10.1016/j.cca.2019.07.037 · Cited by 100 · see citing works

GSH transport in human cerebrovascular endothelial cells and human astrocytes: evidence for luminal localization of Na+-dependent GSH transport in HCEC1Portions of this work were presented at the annual meeting of the Federation of the American Societies of Experimental Biology, April 17–21, 1999, Washington, DC [FASEB J. 13(4), 571.4A (1999)].1

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

Targeting glycogen synthase kinase-3 for oxidative stress and neuroinflammation: Opportunities, challenges and future directions for cerebral stroke management

Rana, A. K., & Singh, D. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.07.006 · Cited by 99 · see citing works

Neuronal activity regulates astrocytic Nrf2 signaling

Habas, A., Hahn, J., Wang, X., & Margeta, M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208764110 · Cited by 97 · see citing works

Potential Role of Acrolein in Neurodegeneration and in Alzheimers Disease

Nam, D. T., Arseneault, M., Murthy, V., & Ramassamy, C. (2010) · Current Molecular Pharmacology · doi:10.2174/1874-470211003020066 · Cited by 97 · see citing works

Hydrogen peroxide-induced apoptosis mediated by p53 protein in glial cells

Kitamura, Y., Ota, T., Matsuoka, Y., Tooyama, I., Kimura, H., Shimohama, S., Nomura, Y., Gebicke‐Haerter, P. J., & Taniguchi, T. (1999) · Glia · doi:10.1002/(sici)1098-1136(19990115)25:2 · Cited by 96 · see citing works

Age-dependent changes of glyoxalase I expression in human brain

Kuhla, B., Boeck, K., Lüth, H., Schmidt, A., Weigle, B., Schmitz, M., Ogunlade, V., Münch, G. W., & Arendt, T. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.04.006 · Cited by 95 · see citing works

Posttranslational Modification of Human Glyoxalase 1 Indicates Redox-Dependent Regulation

Birkenmeier, G., Stegemann, C., Hoffmann, R., Günther, R., Huse, K., & Birkemeyer, C. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010399 · Cited by 95 · see citing works

Peripheral markers in neurodegenerative patients and their first-degree relatives

Cristalli, D. O., Arnal, N., Marra, F. A., de Alaniz, M. J. T., & Marra, C. A. (2011) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2011.11.001 · Cited by 92 · see citing works

Crosslinking of Apolipoprotein E by Products of Lipid Peroxidation

Montine, T. J., Huang, D. Y., Valentine, W. M., Amaranath, V., Saunders, A. M., Weisgraber, K. H., Graham, D. G., & Strittmatter, W. J. (1996) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199602000-00009 · Cited by 90 · see citing works

Two-photon Imaging of Glutathione Levels in Intact Brain Indicates Enhanced Redox Buffering in Developing Neurons and Cells at the Cerebrospinal Fluid and Blood-Brain Interface

Sun, X., Shih, A. Y., Johannssen, H. C., Erb, H., Li, P., & Murphy, T. H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601567200 · Cited by 89 · see citing works

Acrolein induces Alzheimer's disease-like pathologies in vitro and in vivo

Huang, Y., Jin, M.-H., Pi, R., Zhang, J., Ouyang, Y., Chao, X., Chen, M.-H., Liu, P., Yu, J., Ramassamy, C., et al. (2013) · Toxicology Letters · doi:10.1016/j.toxlet.2012.12.023 · Cited by 88 · see citing works

Glutathione conjugation dose-dependently increases brain-specific liposomal drug delivery in vitro and in vivo

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

The cystine‐glutamate exchanger (xCT, Slc7a11) is expressed in significant concentrations in a subpopulation of astrocytes in the mouse brain

Ottestad‐Hansen, S., Hu, Q. X., Follin‐Arbelet, V. V., Bentea, E., Sato, H., Massie, A., Zhou, Y., & Danbolt, N. C. (2018) · Glia · doi:10.1002/glia.23294 · Cited by 88 · see citing works

Selective Recognition of Glutathiolated Aldehydes by Aldose Reductase

Ramana, K. V., Dixit, B. L., Srivastava, S., Balendiran, G. K., Sk, S., & Bhatnagar, A. (2000) · Biochemistry · doi:10.1021/bi000796e · Cited by 87 · see citing works

Knockdown of Glutamate-Cysteine Ligase by Small Hairpin RNA Reveals That Both Catalytic and Modulatory Subunits Are Essential for the Survival of Primary Neurons

Diaz-Hernandez, J. I., Almeida, A., Delgado-Esteban, M., Fernandez, E., & Bolaños, J. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507065200 · Cited by 82 · see citing works

Oral administration of γ-glutamylcysteine increases intracellular glutathione levels above homeostasis in a randomised human trial pilot study

Zarka, M. H., & Bridge, W. J. (2017) · Redox Biology · doi:10.1016/j.redox.2017.01.014 · Cited by 79 · see citing works

Scavenging of H2O2 by mouse brain mitochondria

Starkov, A. A., Andreyev, A. Y., Zhang, S. F., Starkova, N. N., Korneeva, M., Syromyatnikov, M., & Popov, V. N. (2014) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-014-9581-9 · Cited by 78 · see citing works

Glutathione transport system in human small intestine epithelial cells

lantomasi, T., Favilli, F., Marraccini, P., Magaldi, T., Bruni, P., & VINCENZINI, M. T. (1997) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(97)00097-7 · Cited by 77 · see citing works

Glutathionylation of the Pro-apoptotic Protein p53 in Alzheimer’s Disease Brain: Implications for AD Pathogenesis

Domenico, F. D., Cenini, G., Rukhsana Sultana, A., Marzia Perluigi, A., Uberti, D. L., Memo, M., & Butterfield, D. A. (2009) · Neurochemical Research · doi:10.1007/s11064-009-9924-9 · Cited by 77 · see citing works

Potential Role of Acrolein in Neurodegeneration and in Alzheimers Disease

Nam, D. T., Arseneault, M., Murthy, V., et al. (2010) · Current Molecular Pharmacology · doi:10.2174/1874467211003020066 · Cited by 77 · see citing works

Impaired cross-talk between the thioredoxin and glutathione systems is related to ASK-1 mediated apoptosis in neuronal cells exposed to mercury

Branco, V., Coppo, L., Solá, S., Lu, J., Rodrigues, C. M. P., Holmgren, A., & Carvalho, C. M. L. (2017) · Redox Biology · doi:10.1016/j.redox.2017.05.024 · Cited by 76 · see citing works

Methylglyoxal Induces Tau Hyperphosphorylation via Promoting AGEs Formation

Li, X., Xie, J., Jiang, X., Lv, B.-L., Cheng, X., Du, L., Zhang, J. Y., Wang, J., & Zhou, X. (2012) · NeuroMolecular Medicine · doi:10.1007/s12017-012-8191-0 · Cited by 72 · see citing works

Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae

Greetham, D., Vickerstaff, J., Shenton, D., Perrone, G. G., Dawes, I. W., & Grant, C. M. (2010) · BMC Biochemistry · doi:10.1186/1471-2091-11-3 · Cited by 72 · see citing works

Supplementation with γ-glutamylcysteine (γ-GC) lessens oxidative stress, brain inflammation and amyloid pathology and improves spatial memory in a murine model of AD

Liu, Y., Chen, Z., Li, B., Yao, H., Zarka, M., Welch, J., Sachdev, P., Bridge, W., & Braidy, N. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2020.104931 · Cited by 69 · see citing works

Quantitation of in vivo brain glutathione conformers in cingulate cortex among age‐matched control, MCI, and AD patients using MEGA‐PRESS

Shukla, D., Mandal, P. K., Tripathi, M., Vishwakarma, G., Mishra, R., & Sandal, K. (2019) · Human Brain Mapping · doi:10.1002/hbm.24799 · Cited by 67 · see citing works

Glutathione (GSH) Peptide Conjugated Magnetic Nanoparticles As Blood–Brain Barrier Shuttle for MRI-Monitored Brain Delivery of Paclitaxel

Nosrati, H., Tarantash, M., Bochani, S., Charmi, J., Bagheri, Z., Fridoni, M., Abdollahifar, M., Davaran, S., Danafar, H., & Manjili, H. K. (2019) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.8b01420 · Cited by 66 · see citing works

Mannose receptor is present in a functional state in rat microglial cells

Marzolo, M., Rommy von Bernhardi, M., & Inestrosa, N. C. (1999) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19991101)58:3 · Cited by 65 · see citing works

Glycation affects fibril formation of Aβ peptides

Emendato, A., Milordini, G., Zacco, E., Sicorello, A., Dal Piaz, F., Guerrini, R., Thorogate, R., Picone, D., & Pastore, A. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002275 · Cited by 65 · 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

Posttranslational modification and regulation of glutamate–cysteine ligase by the α,β-unsaturated aldehyde 4-hydroxy-2-nonenal

Backos, D. S., Fritz, K. S., Roede, J. R., Petersen, D. R., & Franklin, C. C. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.10.694 · Cited by 62 · see citing works

Optimization of Curcumin-Loaded PEG-PLGA Nanoparticles by GSH Functionalization: Investigation of the Internalization Pathway in Neuronal Cells

Paka, G. D., & Ramassamy, C. (2016) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.6b00738 · Cited by 62 · see citing works

Alteration of Thioredoxin and Glutaredoxin in the Progression of Alzheimer's Disease

Arodin, L., Lamparter, H., Karlsson, H., Nennesmo, I., Björnstedt, M., Schröder, J., & Fernandes, A. P. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131814 · Cited by 61 · see citing works

RAGE and AGEs in Mild Cognitive Impairment of Diabetic Patients: A Cross-Sectional Study

Wang, P., Huang, R., Lu, S., Xia, W., Cai, R., Sun, H., & Wang, S. (2016) · PLoS ONE · doi:10.1371/journal.pone.0145521 · Cited by 55 · see citing works

Effect of orally administered glutathione on glutathione levels in some organs of rats: role of specific transporters

Favilli, F., Marraccini, P., Iantomasi, T., & VINCENZINI, M. T. (1997) · British Journal Of Nutrition · doi:10.1079/bjn19970147 · Cited by 54 · see citing works

AGEs Induce Cell Death via Oxidative and Endoplasmic Reticulum Stresses in Both Human SH-SY5Y Neuroblastoma Cells and Rat Cortical Neurons

Yin, Q., Dong, C., Dong, S., Dong, X.-L., Yan, H., Hou, X., Luo, D., Pei, J.-J., & Liu, X. (2012) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-012-9856-9 · Cited by 53 · see citing works

Memantine protects thalamocortical hyper‐glutamatergic transmission induced by NMDA receptor antagonism via activation of system xc−

Okada, M., Fukuyama, K., Kawano, Y., Shiroyama, T., & Ueda, Y. (2019) · Pharmacology Research & Perspectives · doi:10.1002/prp2.457 · Cited by 51 · see citing works

Protein glutathionylation in human central nervous system: Potential role in redox regulation of neuronal defense against free radicals

Sparaco, M., Gaeta, L. M., Tozzi, G., Bertini, E., Pastore, A., Simonati, A., Santorelli, F. M., & Piemonte, F. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20729 · Cited by 49 · see citing works

Time sequence of oxidative stress in the brain from transgenic mouse models of Alzheimer's disease related to the amyloid-β cascade

Belkacemi, A., & Ramassamy, C. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.11.020 · Cited by 49 · see citing works

Alterations in Acrolein Metabolism Contribute to Alzheimer’s Disease

Tsou, H., Hsu, W.-C., Fuh, J., Chen, S., Liu, T., & Wang, H. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170736 · Cited by 47 · see citing works

Modulation of Hydrogen Peroxide and Acrolein-Induced Oxidative Stress, Mitochondrial Dysfunctions and Redox Regulated Pathways by the Bacopa Monniera Extract: Potential Implication in Alzheimer's Disease

Singh, M., Murthy, V., & Ramassamy, C. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-091729 · Cited by 46 · see citing works

Circulating and Extracellular Vesicles Levels of N-(1-Carboxymethyl)-L-Lysine (CML) Differentiate Early to Moderate Alzheimer’s Disease

Haddad, M., Perrotte, M., Landri, S., Page, A. Y. L., Fülöp, T., & Ramassamy, C. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-181272 · Cited by 44 · see citing works

Oxidative Stress Occurs Prior to Amyloid Aβ Plaque Formation and Tau Phosphorylation in Alzheimer’s Disease: Role of Glutathione and Metal Ions

Roy, R. G., Mandal, P. K., & Maroon, J. C. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00486 · Cited by 194 · see citing works

Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery

Buccellato, F. R., D’Anca, M., Fenoglio, C., Scarpini, E., & Galimberti, D. (2021) · Antioxidants · doi:10.3390/antiox10091353 · Cited by 179 · see citing works

Blood-Based Biomarkers for Alzheimer’s Disease Diagnosis and Progression: An Overview

Varesi, A., Carrara, A., Pires, V. G., Floris, V., Pierella, E., Savioli, G., Prasad, S., Esposito, C., Ricevuti, G., Chirumbolo, S., et al. (2022) · Cells · doi:10.3390/cells11081367 · Cited by 142 · see citing works

The mechanisms of ferroptosis and its role in alzheimer’s disease

Ma, H., Dong, Y., Chu, Y., Guo, Y., & Li, L. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.965064 · Cited by 115 · see citing works

Molecular pathways associated with oxidative stress and their potential applications in radiotherapy (Review)

Liu, R., Bian, Y., Liu, L., Liu, L., Liu, X., & Ma, S. (2022) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2022.5121 · Cited by 112 · see citing works

Oxidative stress–mediated neuroinflammation in Alzheimer’s disease

Firdous, S. M., Khan, S. A., & Maity, A. (2024) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-024-03188-3 · Cited by 85 · see citing works

The Effects of Dietary Advanced Glycation End-Products on Neurocognitive and Mental Disorders

D'Cunha, N. M., Sergi, D., Lane, M. M., Naumovski, N., Gamage, E., Rajendran, A., Kouvari, M., Gauci, S., Dissanayaka, T. D., Marx, W., et al. (2022) · Nutrients · doi:10.3390/nu14122421 · Cited by 80 · see citing works

Critical Roles of the Cysteine–Glutathione Axis in the Production of γ-Glutamyl Peptides in the Nervous System

Fujii, J., Osaki, T., Soma, Y., & Matsuda, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24098044 · Cited by 54 · see citing works

Electron transfer-based antioxidant nanozymes: Emerging therapeutics for inflammatory diseases

Zhao, J., Guo, F., Hou, L., Zhao, Y., & Sun, P. (2023) · Journal of Controlled Release · doi:10.1016/j.jconrel.2023.01.068 · Cited by 47 · see citing works

Glutathione and glutathione disulfide – their biomedical and pharmaceutical applications

Guan, X. (2023) · Medicinal Chemistry Research · doi:10.1007/s00044-023-03116-9 · Cited by 43 · see citing works

Potential role and therapeutic implications of glutathione peroxidase 4 in the treatment of Alzheimer’s disease

Shen, Y., Zhang, G., Wei, C., Zhao, P., Wang, Y., Li, M., & Sun, L. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01343 · Cited by 44 · see citing works

Ferroptosis and its contribution to cognitive impairment in Alzheimer’s disease: mechanisms and therapeutic potential

Khan, G., Hussain, M. S., Khan, Y., Fatima, R., Ahmad, S., Sultana, A., & Alam, P. (2025) · Brain Research · doi:10.1016/j.brainres.2025.149776 · Cited by 33 · see citing works

Alzheimer's Disease: A Review of Pathology, Current Treatments, and the Potential Therapeutic Effect of Decreasing Oxidative Stress by Combined Vitamin D and l -Cysteine Supplementation

Jain, S. K., Stevens, C. M., Margret, J. J., & Levine, S. N. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0245 · Cited by 27 · see citing works

Curculigoside, a traditional Chinese medicine monomer, ameliorates oxidative stress in Alzheimer's disease mouse model via suppressing ferroptosis

Gong, Y., Wang, Y., Li, Y., Weng, F., Chen, T., & He, L. (2024) · Phytotherapy Research · doi:10.1002/ptr.8152 · Cited by 25 · see citing works

Oral delivery of glutathione: antioxidant function, barriers and strategies

Wei, T., Thakur, S. S., Liu, M., & Wen, J. (2022) · Acta Materia Medica · doi:10.15212/amm-2022-0005 · Cited by 25 · see citing works

Current Status of Alzheimer’s Disease and Pathological Mechanisms Investigating the Therapeutic Molecular Targets

Bagga, S., & Kumar, M. (2022) · Current Molecular Medicine · doi:10.2174/1566524022666220404112843 · Cited by 25 · see citing works

Therapeutic nanotechnologies for Alzheimer’s disease: A critical analysis of recent trends and findings

Delbreil, P., Rabanel, J., Banquy, X., & Brambilla, D. (2022) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2022.114397 · Cited by 25 · see citing works

Exploring the complexities of 1C metabolism: implications in aging and neurodegenerative diseases

Ghanem, A. B., Hussayni, Y., Kadbey, R., Ratel, Y., Yehya, S., Khouzami, L., Ghadieh, H. E., Kanaan, A., Azar, S. T., & Harb, F. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1322419 · Cited by 22 · see citing works

The Neuropharmacological Evaluation of Seaweed: A Potential Therapeutic Source

Jannat, K., Balakrishnan, R., Han, J., Yu, Y.-J., Kim, G.-W., & Choi, D. (2023) · Cells · doi:10.3390/cells12222652 · Cited by 21 · see citing works

Redox Imbalance in Neurological Disorders in Adults and Children

Rey, F., Berardo, C., Maghraby, E., Mauri, A., Messa, L., Esposito, L., Casili, G., Ottolenghi, S., Bonaventura, E., Cuzzocrea, S., et al. (2023) · Antioxidants · doi:10.3390/antiox12040965 · Cited by 23 · see citing works

Brain glutathione and GABA + levels in autistic children

Song, Y., Hupfeld, K. E., Davies‐Jenkins, C. W., Zöllner, H. J., Murali‐Manohar, S., Mumuni, A. N., Crocetti, D., Yedavalli, V. S., Oeltzschner, G., Alessi, N., et al. (2024) · Autism Research · doi:10.1002/aur.3097 · Cited by 20 · see citing works

The role of ferroptosis in epilepsy: mechanisms and targeted therapies

Shen, D., Zhao, Z., Ji, Y., Zhang, J., Yao, X., Qi, L., & Sun, H. (2026) · Biochemical Pharmacology · doi:10.1016/j.bcp.2026.117912 · Cited by 19 · see citing works

Antioxidant and Antibacterial Properties of a Functional Sports Beverage Formulation

Kolonas, A., Vareltzis, P. K., Kyroglou, S., Goutzourelas, N., Stagos, D., Trachana, V., Tsadila, C., Mossialos, D., Mourtakos, S., & Gortzi, O. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043558 · Cited by 22 · see citing works

Dietary advanced glycation end products (AGEs): A modifiable risk factor in the prevention of chronic diseases associated with aging?

Ávila, F., Cruz, N., González, M. A., Eduardo Fuentes, Q., Wehinger, S., & Mariane Lutz, R. (2025) · Biochimie · doi:10.1016/j.biochi.2025.06.001 · Cited by 15 · see citing works

Normal-Tension Glaucoma and Potential Clinical Links to Alzheimer’s Disease

Ho, K., Bodi, N. E., & Sharma, T. P. (2024) · Journal of Clinical Medicine · doi:10.3390/jcm13071948 · Cited by 14 · see citing works

Nicotinamide, an acetylcholinesterase uncompetitive inhibitor, protects the blood‒brain barrier and improves cognitive function in rats fed a hypercaloric diet

Ramírez-Cruz, A., Gómez‐González, B., Baiza-Gutman, L. A., Manuel‐Apolinar, L., Mejía, S. Á., López-Cervantes, S. P., Ortega‐Camarillo, C., Cruz, M., Gómez‐Olivares, J. L., & Díaz-Flores, M. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.176068 · Cited by 12 · see citing works

Perspectives on Alzheimer’s Disease Treatment Based on Counteracting Oxidative Stress

Bilski, R., Dąbkowski, S., Kozieł, I., Kozicki, M., Małachowska, A., Przygocki, M., & Tyska, O. (2025) · Biomolecules · doi:10.3390/biom15091345 · Cited by 12 · see citing works

Effects of natural source polysaccharides on neurological diseases: A review

Yang, L., Hou, H., Lu, L., Sun, Y. H., Chen, R., Deng, Q., & Chen, H. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.139697 · Cited by 11 · see citing works

Therapeutic effect and mechanism of Anemarrhenae Rhizoma on Alzheimer’s disease based on multi-platform metabolomics analyses

Wang, H., Dai, J., He, Y.-Z., Xia, Z.-W., Chen, X., Hong, Z., & Chai, Y. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.940555 · Cited by 11 · see citing works

Lysosome as a Chemical Reactor

Dharmasivam, M., & Kaya, B. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262311581 · Cited by 11 · see citing works

Taurine alleviated paraquat-induced oxidative stress and gut-liver axis damage in weaned piglets by regulating the Nrf2/Keap1 and TLR4/NF-κB signaling pathways

Chen, C., Qi, M., Zhang, W., Chen, F., Sun, Z., Sun, W., Tang, W., Yang, Z., Zhao, X., & Tang, Z. (2025) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-025-01244-3 · Cited by 10 · see citing works

MPV17 Prevents Myocardial Ferroptosis and Ischemic Cardiac Injury through Maintaining SLC25A10-Mediated Mitochondrial Glutathione Import

Xu, T., & Chen, G. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910832 · Cited by 9 · see citing works

Advances in the application of manganese dioxide and its composites for theranostics

Hao, J., Zhao, Y., Ma, Y., Liu, B., Luo, Y., Alfaifi, S., Sun, X., & Wu, M. C. (2023) · Inorganic Chemistry Frontiers · doi:10.1039/d3qi00978e · Cited by 8 · see citing works

Novel insights into the activating transcription factor 4 in Alzheimer’s disease and associated aging-related diseases: Mechanisms and therapeutic implications

Zhang, N., Nao, J., Zhang, S., & Dong, X. (2024) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2024.101144 · Cited by 8 · see citing works

The α-MG exhibits neuroprotective potential by reducing amyloid beta peptide-induced inflammation, oxidative stress, and tau aggregation in human neural stem cells

Chiang, M., Nicol, C. J. B., Yang, Y., Chiang, T., & Yen, C. (2025) · Brain Research · doi:10.1016/j.brainres.2025.149506 · Cited by 7 · see citing works

Postprandial Glucose Response in Type 2 Diabetes Mellitus Patients and Possible Antioxidant Properties of a Plant-Based Snack Bar

Dimopoulou, M., Bargiota, Α., Barmpa, E., Outskouni, Z., Stagos, D., Trachana, V., Androutsos, O., & Gortzi, O. (2024) · Foods · doi:10.3390/foods13244123 · Cited by 6 · see citing works

Unlocking the Potential of Taste and Taste-active Peptides: Bridging Structural Characteristics and Biological Activities with Food and Pharmaceutical Applications

Xiang, H., Song, W., Hao, S., & Sun‐Waterhouse, D. (2026) · Journal of Future Foods · doi:10.1016/j.jfutfo.2025.12.020 · Cited by 5 · see citing works

Interplay of oxidative stress and neuroinflammation in alzheimer’s: insights into age-driven pathogenesis

Firdous, S. M., Chakrabortty, S., Undale, V., Mallik, S., & Gouda, M. (2026) · Inflammopharmacology · doi:10.1007/s10787-026-02169-7 · Cited by 6 · see citing works

Voltammetric studies of glutathione transfer across arrays of liquid–liquid microinterfaces for sensing applications

Poklonnov, V., Martynov, L. Y., Astafiev, A. A., & Зайцев, Н. К. (2022) · Amino Acids · doi:10.1007/s00726-022-03166-0 · Cited by 5 · see citing works

Genetic Disruption of the γ-Glutamylcysteine Ligase in PDAC Cells Induces Ferroptosis-Independent Cell Death In Vitro without Affecting In Vivo Tumor Growth

Daher, B., Meira, W., Durivault, J., Gotorbe, C., Pouysségur, J., & Vučetić, M. (2022) · Cancers · doi:10.3390/cancers14133154 · Cited by 5 · see citing works

Rlip76 in ageing and Alzheimer’s disease: Focus on oxidative stress and mitochondrial mechanisms

Bandaru, M., Sultana, O. F., Islam, M. A., Alvir, R. V., & Reddy, P. H. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102600 · Cited by 4 · see citing works

Bilirubin: a game-changer in alzheimer’s therapy? Unveiling its neuroprotective and disease-modifying potential

Sidhu, R. K., Mittal, Y., & Aran, K. R. (2025) · Metabolic Brain Disease · doi:10.1007/s11011-025-01653-3 · Cited by 4 · see citing works

Serine metabolism in the central nervous system: advances and challenges on a conditionally essential amino acid

Kustrimovic, N., Rabattoni, V., Riva, D., Motta, Z., Sacchi, S., & Pollegioni, L. (2025) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2025.101438 · Cited by 6 · see citing works

Deciphering the Mysterious Relationship between the Cross-Pathogenetic Mechanisms of Neurodegenerative and Oncological Diseases

Aleksandrova, Y. R., & Неганова, М. Е. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914766 · Cited by 4 · see citing works

Untargeted urine metabolomics reveals dynamic metabolic differences and key biomarkers across different stages of Alzheimer’s disease

Feng, X., & Zhao, S. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1530046 · Cited by 4 · see citing works

Antioxidant dynamics and mRNA abundance alterations in dromedary camels during the transition period

Ahmadpour, A., & Zarrin, M. (2025) · Tropical Animal Health and Production · doi:10.1007/s11250-025-04486-5 · Cited by 2 · see citing works

State-of-the-Art Oxidation Mechanisms of Sulfur-Containing Amino Acids: Insights into Redox Chemistry, Metal-Ion Catalysis, and Biomedical Implications

Nagaraj, K., Kaliyaperumal, R., Gokulan, R., Nakshatra, U., Abhirami, J., Selvaraj, S., Sam, S., Balasubramaniam, L. M., Preetham, M., Varshini, C., et al. (2025) · Topics in Catalysis · doi:10.1007/s11244-025-02133-9 · Cited by 2 · see citing works

Hypermethylation of GSTM5 and its effect on oxidation in myelodysplastic syndrome

Wang, C., Yu, Y., Chang, Q., Dong, T., Wang, L., & Li, M. (2024) · iLABMED · doi:10.1002/ila2.47 · Cited by 2 · see citing works

Causal associations between chronic heart failure and the cerebral cortex: results from Mendelian randomization study and integrated bioinformatics analysis

Peng, L., Cai, H., Tang, Y., Zhou, F., Liu, Y., Xu, Z., Chen, Q.-Y., & Chen, X. (2024) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2024.1396311 · Cited by 2 · see citing works

Simultaneous Mapping of the Nanoscale Organization and Redox State of Extracellular Space in Living Brain Tissue

Chen, H., Zhao, L., Wang, L., Wang, Z., Pang, D., & Liu, S. (2024) · ACS Nano · doi:10.1021/acsnano.4c06059 · Cited by 2 · see citing works

Glutathione: synthesis, mechanism of action, antioxidant and detoxifying role

Геруш, І. В., Grigorieva, N. P., & Ferenchuk, Y. O. (2023) · Reports of Vinnytsia National Medical University · doi:10.31393/reports-vnmedical-2023-27(4)-25 · Cited by 1 · see citing works

Electrochemical sensor for glutathione reductase based on screen-printed electrodes coated with 3,5-dinitrobenzoic acid-modified carbon nanotubes

Villalonga, A., López-López, D., García-Díez, E., Sánchez, A., Villalonga, R., & Ojeda, I. (2024) · Microchimica Acta · doi:10.1007/s00604-024-06728-z · Cited by 1 · see citing works

Hypnea musciformis Seaweed Extract Protected Human Mesenchymal Stem Cells From Oxidative Stress Through NRF2 Activation

Goutas, A., Goutzourelas, N., Kevrekidou, A., Kevrekidis, D. P., Malea, P., Virgiliou, C., Assimopoulou, A. N., Trachana, V., Kollatos, N., Moustafa, T., et al. (2024) · Food Science & Nutrition · doi:10.1002/fsn3.4615 · Cited by 4 · see citing works

Modulation of mitochondrial quality by exercise mimetics: A potential strategy for the prevention and treatment of Alzheimer's disease

Ke, Z., Wang, B., & Liang, R. (2026) · Journal of Alzheimer s Disease · doi:10.1177/13872877261424276 · Cited by 1 · see citing works

Glutathione-conjugated gold nanoparticles mitigate amyloid-beta-induced neuroinflammation and tauopathy through inhibition of NF-κB, the NLRP3 inflammasome axis in 3D human neural stem cell models

Yang, Y., Nicol, C. J. B., Yen, C., & Chiang, M. (2026) · Experimental Cell Research · doi:10.1016/j.yexcr.2026.115030 · Cited by 1 · see citing works

Disulfide‐Driven Pore Functionalization of Metal–Organic Frameworks

Moore, J. M., Crom, A. B., Feldblyum, J. I., & Genna, D. T. (2023) · Chemistry - A European Journal · doi:10.1002/chem.202302144 · Cited by 1 · see citing works

The Role of Antioxidants in the Treatment of Alzheimer’s Disease

Tahiroğlu, V. (2024) · doi:10.69860/nobel.9786053359333.9

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Raghuvanshi, S., Mazumder, A., & Das, S. (2025) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/0118715273378092250623064748

Artificial intelligence inspired redox homeostasis of cardiovascular system: next-gen drug therapy

Sunny, S., & Thomas, S. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-40441-2.00006-8

DNA-Protective Effects of Crocus sativus Stamen Extracts and Their Safety Assessment for Use as Natural Bioactive Agents

Mamri, S., Baddaoui, S., Khibech, O., Ouahhoud, S., Khoulati, A., Choukri, M. A., Asehraou, A., & Saalaoui, E. (2026) · Preventive Nutrition and Food Science · doi:10.3746/pnf.2025.258

Patterning of an in situ gel of oxytocin – albumin-stabilized selenium nanoparticles as a new guided neuroprotective combination in chemobrain

Ramzy, L., Elmowafy, E. M., Osman, R., & Awad, G. A. S. (2026) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2026.108450

In silico dysbiosis-associated neuroprotective metabolite insufficiency in Alzheimer’s disease

Shaer, N. A., & Al-Abbas, N. S. (2026) · Open Medicine · doi:10.1515/med-2026-1484

Peptide Redox Networks in Human Cells

de la Lastra, J. M. P., Andrés, C. M. C., Munguira, E. B., Juan, C. A., & Pérez‐Lebeña, E. (2026) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-026-10855-x

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Mandal, P. K., Perry, G. L., Maroon, J. C., Corby, P., Patira, R., & López, O. L. (2026) · Journal of Alzheimer s Disease · doi:10.1177/13872877261474009

Dual channel detection of GSH based on AgNTs colorimetry and coupled plasmonic SERS

Dong, X., Song, Z., Liu, W., Gao, C., Deng, Y., Ni, M., Zhang, D., & Wang, Q. (2026) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2026.128648

Nanomedicine for Neurological Disorders: Advanced Nanotherapeutic Strategies, Blood–Brain Barrier Targeting, and Translational Perspectives

Khalid, S., Amjad, W., Nisar, U., Iqbal, L. Z., & Khan, S. (2026) · doi:10.68050/jams.2026.169

Astrocytic timekeepers and their influence on brain waste clearance in Alzheimer's disease

Koenders, C. L., Chiu, R. K., Medeiros-Furquim, T., & Bergink, S. (2026) · Neurobiology of Sleep and Circadian Rhythms · doi:10.1016/j.nbscr.2026.100155

Fe/Co dual-doped carbon dots@MOF nanozymes with synergistically enhanced colorimetric/fluorescent dual-mode detection for highly sensitive analysis of glutathione

Hong, J., Xiang, J., Gao, Y., Wang, J., Ma, Y., & Zheng, Y. (2026) · Nanoscale · doi:10.1039/d6nr02410f

Elevated glutathione as a therapeutic strategy in Alzheimer's disease

Butterfield, D. A., Pocernich, C. B., & Drake, J. (2002) · Drug Development Research · doi:10.1002/ddr.10095 · Cited by 51 · see citing works

Glutathione in Brain: Overview of Its Conformations, Functions, Biochemical Characteristics, Quantitation and Potential Therapeutic Role in Brain Disorders

Dwivedi, D., Megha, K., Mishra, R., & Mandal, P. K. (2020) · Neurochemical Research · doi:10.1007/s11064-020-03030-1 · Cited by 154 · see citing works

Therapeutic Approaches to Modulating Glutathione Levels as a Pharmacological Strategy in Alzheimer’s Disease

Braidy, N., Zarka, M. H., Welch, J. H., & Bridge, W. J. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666150302160308 · Cited by 43 · see citing works

The emerging role of glutathione in Alzheimer’s disease

Saharan, S., & Mandal, P. K. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132483 · Cited by 168 · see citing works

Oral glutathione administration inhibits the oxidative stress and the inflammatory responses in AppNL−G-F/NL−G-F knock-in mice

Izumi, H., Sato, K., Kojima, K., Saito, T., Saido, T. C., & Fukunaga, K. (2020) · Neuropharmacology · doi:10.1016/j.neuropharm.2020.108026 · Cited by 37 · see citing works