The DOI matches its Crossref record; 139 of the 140 references it cites were found in a registry or an index.
Neurodegenerative diseases and oxidative stress
Abstract
Oxidative stress has been implicated in the progression of Alzheimer's disease, Parkinson's disease and amyotrophic lateral sclerosis. Oxygen is vital for life but is also potentially dangerous, and a complex system of checks and balances exists for utilizing this essential element. Oxidative stress is the result of an imbalance in pro-oxidant/antioxidant homeostasis that leads to the generation of toxic reactive oxygen species. The systems in place to cope with the biochemistry of oxygen are complex, and many questions about the mechanisms of oxygen regulation remain unanswered. However, this same complexity provides a number of therapeutic targets, and different strategies, including novel metal-protein attenuating compounds, aimed at a variety of targets have shown promise in clinical studies.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Thus, these metal ions have been shown to promote Aβ40 aggregation,23–27,29–32”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [24]
In the citing paper
“Remarkably high concentrations of Zn, Cu, and Fe have been found within the amyloid deposits in AD-affected brains,23,24”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [24]
In the citing paper
“For example, the non-specific chelator clioquinol (CQ) showed decreased Aβ aggregate formation that resulted in improved cognition in clinical trials.24,25,43–45”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [24]
In the citing paper
“This is in contrast with a large number of reports showing the aggregation-promoting effect of metal ions on the Aβ peptide.23–27,29–32,37,38”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [24]
In the citing paper
“Chronic oxidative stress and the resultant oxidative damage have been implicated in many human diseases including cardiovascular disease, neurodegenerative diseases, diabetes, cancer, and the aging process [18,19,20,21,22].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [22]
In the citing paper
“The link between oxidative stress and the pathogenesis of neurodegenerative diseases is well-established [22,105].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [22]
Citations
Cites
Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178
Free Radicals in Biology and Medicine
Halliwell, B., & Gutteridge, J. M. C. (2015) · doi:10.1093/acprof:oso/9780198717478.001.0001 · Cited by 8,990
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382
Dauer, W., & Przedborski, S. (2003) · Neuron · doi:10.1016/s0896-6273(03)00568-3 · Cited by 5,469
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Self-citationAmyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
Self-citationMotor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation
Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H.-X., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143
Friedreich's Ataxia: Autosomal Recessive Disease Caused by an Intronic GAA Triplet Repeat Expansion
Campuzano, V., Montermini, L., Moltò, M. D., Pianese, L., Cossée, M., Cavalcanti, F., Monros, E., Rodius, F., Duclos, F., Monticelli, A., et al. (1996) · Science · doi:10.1126/science.271.5254.1423 · Cited by 2,786
A Controlled Trial of Selegiline, Alpha-Tocopherol, or Both as Treatment for Alzheimer's Disease
Sano, M., Ernesto, C., Thomas, R. G., Klauber, M. R., Schafer, K., Grundman, M., Woodbury, P., Growdon, J., Cotman, C. W., Pfeiffer, E., et al. (1997) · New England Journal of Medicine · doi:10.1056/nejm199704243361704 · Cited by 2,380
Flagged first, then by citations
1 of the 140 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Ferrari, C. K. B. Free radicals, lipid peroxidation and antioxidents in apoptosis: implications in cancer, cardiovascular and neurological diseases. Biologia 55, 581–590 (2000).
Cited by
Sorted by citations
Items 401–500 of 1,020
Zucca, F. A., Bellei, C., Giannelli, S. G., Terreni, M., Gallorini, M., Rizzio, E., Pezzoli, G., Albertini, A., & Zecca, L. (2006) · Journal of Neural Transmission · doi:10.1007/s00702-006-0453-2 · Cited by 132
“The neuroprotection obtained in animal models treated with iron chelators indicates that iron-chelation therapy could be a good neuroprotective approach for the management of neurodegenerative diseases associated with loss of iron homeostasis (Barnham et al., 2004).”
BackgroundNakamura, T., Cieplak, P., Cho, D., Godzik, A., & Lipton, S. A. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.04.007 · Cited by 138
“neuronal cell injury and death via a series of redox reactions (Barnham et al., 2004; Beal, 2001; Emerit et al., 2004; Lin and Beal, 2006; Muchowski, 2002).”
BackgroundA benzothiazole-based fluorescent probe for distinguishing and bioimaging of Hg 2+ and Cu 2+
Gu, B., Huang, L., Su, W., Duan, X., Li, H., & Yao, S. (2016) · Analytica Chimica Acta · doi:10.1016/j.aca.2016.11.044 · Cited by 131
Ramdass, A., Sathish, V., Babu, E., Velayudham, M., Thanasekaran, P., & Rajagopal, S. (2017) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2017.06.002 · Cited by 131
Ferritin as an important player in neurodegeneration
Friedman, A., Arosio, P., Finazzi, D., Koziorowski, D., & Gałązka-Friedman, J. (2011) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2011.03.016 · Cited by 131
“malonic dialdehyde [2] and thymine glycol [3].”
Biometals and Their Therapeutic Implications in Alzheimer's Disease
Ayton, S., Lei, P., & Bush, A. I. (2014) · Neurotherapeutics · doi:10.1007/s13311-014-0312-z · Cited by 134
“the potential for copper induced toxicity in AD [164–166].”
BackgroundSelf-citationKalinowski, D. S., Stefani, C., Toyokuni, S., Ganz, T., Anderson, G. J., Subramaniam, V. N., Trinder, D., Olynyk, J. K., Chua, A. C. G., Jansson, P. J., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.01.026 · Cited by 131
“Notably, ROS react rapidly with biological molecules, such as proteins, lipids and DNA [11, 12].”
BackgroundInfluentialTang, J., Liu, J., Zheng, Q., Li, W., Sheng, J., Mao, L., & Wang, M. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202105634 · Cited by 131
Motion of VAPB molecules reveals ER–mitochondria contact site subdomains
Obara, C. J., Nixon‐Abell, J., Moore, A. S., Riccio, F., Hoffman, D. P., Shtengel, G. E., Xu, C. S., Schaefer, K., Pasolli, H. A., Masson, J., et al. (2024) · Nature · doi:10.1038/s41586-023-06956-y · Cited by 147
A novel BODIPY-based colorimetric and fluorometric dual-mode chemosensor for Hg2+ and Cu2+
He, X., Zhang, J., Liu, X.-G., Dong, L., Li, D., Qiu, H., & Yin, S. (2013) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2013.10.093 · Cited by 129
Meng, Q., Zhang, X., He, C., He, G., Zhou, P., & Duan, C. (2010) · Advanced Functional Materials · doi:10.1002/adfm.201000080 · Cited by 129
Tabassum, R., & Jeong, N. Y. (2019) · International Journal of Medical Sciences · doi:10.7150/ijms.36516 · Cited by 130
“In HD, mutant Htt binds to p53; subsequently, increased levels of p53 and associated transcriptional factors cause increased depolarization of mitochondrial membrane potential [36].”
BackgroundGrover, K., Koblova, A., Pezacki, A. T., Chang, C. J., & New, E. J. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00819 · Cited by 129
Grossi, C., Francese, S., Casini, A., Rosi, M. C., Luccarini, I., Fiorentini, A., Gabbiani, C., Luigi Messori, A., Moneti, G., & Casamenti, F. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1063 · Cited by 131
“Notably, aggregated or oligomeric Aβ can induce neurotoxicity through pathways involving free radical production and increased oxidative stress [7].”
BackgroundAntioxidant synergism of green tea polyphenols with α-tocopherol and l-ascorbic acid in SDS micelles
Dai, F., Chen, W., & Zhou, B. (2008) · Biochimie · doi:10.1016/j.biochi.2008.05.007 · Cited by 130
The pleiotropic effects of omega-3 docosahexaenoic acid on the hallmarks of Alzheimer's disease
Belkouch, M., Hachem, M., Elgot, A., Van, A. L., Picq, M., Guichardant, M., Lagarde, M., & Bernoud‐Hubac, N. (2016) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2016.03.002 · Cited by 131
“In addition to these neurological deficits, there is growing evidence that inflammatory processes and oxidative stress are important in the progression of AD neuropathology [9-12], according to the amyloid cascade hypothesis of AD [13].”
BackgroundWenk, G. L., Parsons, C. G., & Danysz, W. (2006) · Behavioural Pharmacology · doi:10.1097/00008877-200609000-00007 · Cited by 134
“Memantine was also protective in in-vivo models of brain hypoxia and ischaemia (Block and Schwarz, 1996; Chen et al., 1998; Dogan et al., 1999; Ozsuer et al., 2005), conditions associated with increased oxidative stress and enhanced glutamatergic synaptic function (Barnham et al., 2004).”
BackgroundCalabrese, V., Stella, A. G., Calvani, M., & Butterfield, D. A. (2005) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2005.03.027 · Cited by 130
“Mitochondrial dysfunction is a characteristic of several neurodegenerative disorders, and evidence for mitochondria being a site of damage in neurodegenerative disorders is partially based on decreases in respiratory chain complex activities in Parkinson’s disease, Alzheimer’s disease (AD) and Huntington’s disease [5,…”
BackgroundApoptotic neuronal death in Parkinson's disease: Involvement of nitric oxide
Singh, S., & Dikshit, M. (2007) · Brain Research Reviews · doi:10.1016/j.brainresrev.2007.02.001 · Cited by 131
Production of reactive oxygen species in mitochondria of HeLa cells under oxidative stress
Chernyak, B. V., Izyumov, D. S., Lyamzaev, K. G., Pashkovskaya, A. A., Pletjushkina, O. Y., Antonenko, Y. N., Sakharov, D. V., WIRTZ, K. W. A., & Skulachev, V. P. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.02.019 · Cited by 129
Brain Renin–Angiotensin System at the Intersect of Physical and Cognitive Frailty
Cosarderelioglu, C., Nidadavolu, L. S., George, C. J., Oh, E. S., Bennett, D. A., Walston, J. D., & Abadir, P. M. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.586314 · Cited by 134
Genoud, S., Roberts, B. R., Gunn, A. P., Halliday, G. M., Lewis, S. J. G., Ball, H. J., Hare, D. J., & Double, K. L. (2017) · Metallomics · doi:10.1039/c7mt00244k · Cited by 126
Schmidt, K., Wolfe, D. M., Stiller, B., & Pearce, D. A. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.03.151 · Cited by 127
Antioxidants as a Preventive Treatment for Epileptic Process: A Review of the Current Status
Martinc, B., Grabnar, I., & Vovk, T. (2014) · Current Neuropharmacology · doi:10.2174/1570159x12666140923205715 · Cited by 126
“Antioxidant enzymes block the initiation of reactive species chain reactions, while the non-enzymatic antioxidants react directly with reactive species and thereby prevent the propagation of chain reactions [20].”
BackgroundMaity, D., & Govindaraju, T. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201002570 · Cited by 126
Rangsinth, P., Sharika, R., Pattarachotanant, N., Duangjan, C., Wongwan, C., Sillapachaiyaporn, C., Nilkhet, S., Wongsirojkul, N., Prasansuklab, A., Tencomnao, T., et al. (2023) · Foods · doi:10.3390/foods12132529 · Cited by 126
A novel optical sensor for copper ions based on phthalocyanine tetrasulfonic acid
Kumawat, L. K., Mergu, N., Singh, A. K., & Gupta, V. K. (2015) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2015.02.027 · Cited by 125
Pathophysiological importance of aggregated damaged proteins
Höhn, A., Jung, T., & Grune, T. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.02.028 · Cited by 130
Medicinal chemistry of acridine and its analogues
Prasher, P., & Sharma, M. (2018) · MedChemComm · doi:10.1039/c8md00384j · Cited by 125
Afrin, A., Jayaraj, A., Gayathri, M. S. L., & Chinna Ayya Swamy, P. (2023) · Sensors & Diagnostics · doi:10.1039/d3sd00110e · Cited by 127
Redox Silencing of Copper in Metal-linked Neurodegenerative Disorders
Meloni, G., Faller, P., & Vaša´k, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701357200 · Cited by 130
Kim, Y., Kim, H. J., Kim, J. S., & Kim, H. (2008) · Advanced Materials · doi:10.1002/adma.200801001 · Cited by 125
Angeletti, B., Waldron, K. J., Freeman, K. B., Bawagan, H., Hussain, I., Miller, C. C. J., Lau, K., Tennant, M. E., Dennison, C., Robinson, N. J., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412034200 · Cited by 126
Mitochondrial Thiols in the Regulation of Cell Death Pathways
Yin, F., Sancheti, H., & Cadenas, E. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4639 · Cited by 128
“Cells with high metabolic rate are exposed to large quantities of oxidants, which renders them more vulnerable to oxidative stress-induced cell death (2); thus, high levels of oxidants disrupt redox signaling and mediate detrimental effects inherent in mitochondrial dysfunction in a variety of pathologies including ne…”
BackgroundA Boronate-Caged [18F]FLT Probe for Hydrogen Peroxide Detection Using Positron Emission Tomography
Carroll, V., Michel, B. W., Blecha, J. E., VanBrocklin, H. F., Keshari, K. R., Wilson, D. M., & Chang, C. J. (2014) · Journal of the American Chemical Society · doi:10.1021/ja509198w · Cited by 125
Gray, N. E., Harris, C. J., Quinn, J. F., & Soumyanath, A. (2016) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2016.01.013 · Cited by 123
Giacoppo, S., Galuppo, M., Montaut, S., Iori, R., Rollin, P., Bramanti, P., & Mazzon, E. (2015) · Fitoterapia · doi:10.1016/j.fitote.2015.08.001 · Cited by 126
“Briefly, oxidative stress is the result of an unbalance in prooxidant/antioxidant homeostasis that leads to the generation of free radicals [16].”
BackgroundTherapeutic inhibition of ferroptosis in neurodegenerative disease
Ryan, S. K., Ugalde, C. L., Rolland, A., Skidmore, J., Devos, D., & Hammond, T. R. (2023) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2023.07.007 · Cited by 127
The role of TRPM channels in cell death
McNulty, S., & Fonfría, E. (2005) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-005-1440-4 · Cited by 122
“Neurodegenerative diseases such as Alzheimer’s and Parkinson’s diseases are associated with oxidant stress that occurs as a consequence of an imbalance between the production of ROS and cellular defences [2].”
BackgroundDesrumaux, C., Risold, P.-Y., Schroeder, H., Deckert, V., Masson, D., Athias, A., Laplanche, H., Le Guern, N., Blache, D., Jiang, X.-C., et al. (2005) · The FASEB Journal · doi:10.1096/fj.04-2400fje · Cited by 122
Highly Selective Excited State Intramolecular Proton Transfer (ESIPT)-Based Superoxide Probing
Murale, D. P., Kim, H., Choi, W. S., & Churchill, D. G. (2013) · Organic Letters · doi:10.1021/ol4017222 · Cited by 124
Rakotoarisoa, M., Angelov, B., Garamus, V. M., & Angelova, A. (2019) · ACS Omega · doi:10.1021/acsomega.8b03101 · Cited by 125
Evaluation of HOCl-generating anticancer agents by an ultrasensitive dual-mode fluorescent probe
Shi, D., Chen, S., Dong, B., Zhang, Y., Sheng, C., James, T. D., & Guo, Y. (2019) · Chemical Science · doi:10.1039/c9sc00180h · Cited by 122
Role of the K eap1/ N rf2 pathway in neurodegenerative diseases
Yamazaki, H., Tanji, K., Wakabayashi, K., Matsuura, S., & Itoh, K. (2015) · Pathology International · doi:10.1111/pin.12261 · Cited by 123
Jayasena, T., Poljak, A., Smythe, G. A., Braidy, N., Münch, G. W., & Sachdev, P. S. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2013.06.003 · Cited by 122
“Oxidative stress results when pro-oxidant and anti-oxidant activities in the body are not occurring at a balanced rate, leading to the production of excess reactive oxygen species, such as peroxides and free radicals (Barnham et al., 2004).”
BackgroundSridhar, V., Gaud, R. S., Bajaj, A., & Wairkar, S. (2018) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2018.08.004 · Cited by 121
Shah, R., Farmer, L. A., Zilka, O., Kessel, A. T. M. V., & Pratt, D. A. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.09.007 · Cited by 127
Discovery of Soluble Epoxide Hydrolase Inhibitors from Chemical Synthesis and Natural Products
Sun, C., Zhang, X., Morisseau, C. H. P., Hwang, S. H., Zhang, Z., Hammock, B. D., & Ma, X. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01507 · Cited by 123
Bai, J., & Lipski, J. (2010) · NeuroToxicology · doi:10.1016/j.neuro.2010.01.001 · Cited by 120
The structure of the amyloid-beta peptide high-affinity copper II binding site in Alzheimer disease.
Streltsov, V., Titmuss, S. J., Epa, V., Barnham, K., Masters, C. L., & Varghese, J. (2008) · Biophysical Journal · doi:10.1529/biophysj.108.134429 · Cited by 103
Self-citationLeng, T., Shi, Y., Xiong, Z., & Sun, D. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.12.008 · Cited by 123
Fang, H., Chen, M., Ding, Y., Shang, W. H., Xu, J., Zhang, X., Zhang, W., Li, K., Xiao, Y., Gao, F., et al. (2011) · Cell Research · doi:10.1038/cr.2011.81 · Cited by 120
Nanoencapsulation of gallic acid and evaluation of its cytotoxicity and antioxidant activity
Alves, A. D. C. S., Mainardes, R. M., & Khalil, N. M. (2015) · Materials Science and Engineering C · doi:10.1016/j.msec.2015.11.014 · Cited by 120
Free Superoxide is an Intermediate in the Production of H 2 O 2 by Copper(I)‐Aβ Peptide and O 2
Reybier, K., Ayala, S., Aliès, B., Rodrigues, J. V., Rodriguez, S. B., Penna, G. L., Collin, F., Gomes, C. M., Hureau, C., & Faller, P. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201508597 · Cited by 122
Kim, B.-W., Koppula, S., Kumar, H., Park, J., Kim, I.-W., More, S. V., Kim, I., Han, S.-D., Kim, S., Yoon, S., et al. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.04.037 · Cited by 119
“…the last three decades strongly suggest that excessive microglial activation produce abnormal levels of proinflammatory cytokines, chemokines, prostaglandins, complement cascade proteins, and reactive oxygen and nitrogen species in post-mortem PD brains (Barnham et al., 2004; Koppula et al., 2012).”
DNA end joining activity is reduced in Alzheimer's disease
Shackelford, D. A. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.03.009 · Cited by 124
“Increased oxidative damage detected in AD brains includes lipid peroxidation, DNA base hydroxylation, protein carbonylation and nitration, and glycation and glycoxidation of lysine residues [3,36,37,46].”
BackgroundInfluentialAntioxidant and anti-glycation properties of Thai herbal teas in comparison with conventional teas
Deetae, P., Parichanon, P., Trakunleewatthana, P., Chanseetis, C., & Lertsiri, S. (2012) · Food Chemistry · doi:10.1016/j.foodchem.2012.02.012 · Cited by 120
Preparation and use of Coppersensor-1, a synthetic fluorophore for live-cell copper imaging
Miller, E. W., Zeng, L., Domaille, D. W., & Chang, C. J. (2006) · Nature Protocols · doi:10.1038/nprot.2006.140 · Cited by 119
Vuković, N. L., Sukdolak, S., Solujić, S., & Nićiforović, N. (2009) · Food Chemistry · doi:10.1016/j.foodchem.2009.11.040 · Cited by 120
Wang, S., Sheng, Z., Yang, Z., Hu, D., Long, X., Feng, G., Liu, Y., Yuan, Z., Zhang, J., Zheng, H., et al. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201904047 · Cited by 119
A Thermoresponsive Biodegradable Polymer with Intrinsic Antioxidant Properties
Yang, J. H., van Lith, R., Baler, K., Hoshi, R. A., & Ameer, G. A. (2014) · Biomacromolecules · doi:10.1021/bm5010004 · Cited by 118
Yoo, D., Magsam, A. W., Kelly, A. M., Stayton, P. S., Kievit, F. M., & Convertine, A. J. (2017) · ACS Nano · doi:10.1021/acsnano.7b03426 · Cited by 121
Autophagy in Human Health and Disease: Novel Therapeutic Opportunities
Giampieri, F., Afrin, S., Forbes-Hernández, T. Y., Gasparrini, M., Cianciosi, D., Reboredo‐Rodríguez, P., Varela‐López, A., Quiles, J. L., & Battino, M. A. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7234 · Cited by 117
Novel Chemosensor for the Visual Detection of Copper(II) in Aqueous Solution at the ppm Level
Chandrasekhar, V., Das, S., Yadav, R., Hossain, S., Parihar, R., Subramaniam, G., & Sen, P. (2012) · Inorganic Chemistry · doi:10.1021/ic301399a · Cited by 117
Shen, L., & Ji, H. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150140 · Cited by 118
Modifications of the iron–neuromelanin system in Parkinson's disease
Fasano, M., Bergamasco, B., & Lopiano, L. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03638.x · Cited by 117
Protein aggregation, metals and oxidative stress in neurodegenerative diseases
Tabner, B. J., El-Agnaf, O. M. A., German, M. J., Fullwood, N. J., & Allsop, D. (2005) · Biochemical Society Transactions · doi:10.1042/bst20051082 · Cited by 118
Cu2+-selective naked-eye and fluorescent probe: its crystal structure and application in bioimaging
Yu, F., Zhang, W., Li, P., Xing, Y., Tong, L., Ma, J., & Tang, B. (2009) · The Analyst · doi:10.1039/b823360h · Cited by 116
Potapov, A., Yau, W., Ghirlando, R., Thurber, K. R., & Tycko, R. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b04843 · Cited by 116
Chen, B., Zhao, J., Zhang, R., Zhang, L., Zhang, Q., Yang, H., & An, J. (2020) · Nutritional Neuroscience · doi:10.1080/1028415x.2020.1840035 · Cited by 116
Reactive oxygen species-sensitive polymeric nanocarriers for synergistic cancer therapy
Cao, Z., Li, D., Wang, J., & Yang, X. (2021) · Acta Biomaterialia · doi:10.1016/j.actbio.2021.05.023 · Cited by 119
The multifaceted role of mitochondria in autism spectrum disorder
Khaliulin, I., Hamoudi, W., & Amal, H. (2024) · Molecular Psychiatry · doi:10.1038/s41380-024-02725-z · Cited by 128
Wang, Z., Wang, Y., Li, W., Mao, F., Sun, Y., Huang, L., & Li, X. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500119g · Cited by 117
Park, J., Baik, S. H., Han, S., Cho, H. J., Choi, H., Kim, H. J., Choi, H., Lee, W., Kim, D. K., & Mook‐Jung, I. (2016) · Aging Cell · doi:10.1111/acel.12530 · Cited by 115
“stress associated pathway, up-regulation of receptor for advanced glycation end products (RAGEs), and enhanced expression of matrix metalloproteinase 9 (Barnham et al., 2004; Kook et al., 2012).”
BackgroundNiu, Q., Sun, T., Li, T., Guo, Z., & Pang, H. (2018) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2018.03.089 · Cited by 115
A computational study of the Fenton reaction in different pH ranges
Lu, H., Chen, H., Kao, C., Chao, I., & Chen, H. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c8cp04381g · Cited by 115
Electrochemical Monitoring of Paclitaxel‐Induced ROS Release from Mitochondria inside Single Cells
Jiang, H., Zhang, X., Liao, Q., Wu, W., Liu, Y., & Huang, W. (2019) · Small · doi:10.1002/smll.201901787 · Cited by 115
Antioxidant Nanotherapies for the Treatment of Inflammatory Diseases
Li, C., Li, L., Chen, S., Zhang, J., & Lü, W.-L. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.00200 · Cited by 120
Association between chronic stress and Alzheimer’s disease: Therapeutic effects of Saffron
Saeedi, M., & Rashidy‐Pour, A. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110995 · Cited by 123
Reactive oxygen species-responsive polymer drug delivery systems
Liu, J., Jia, B., Li, Z., & Li, W. (2023) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2023.1115603 · Cited by 123
“, 1998) and many diseases, such as cancer, neurodegenerative diseases, diabetes, and inflammation (Barnham et al., 2004; Fraisl et al., 2009; Trachootham et al., 2009; Schieber and Chandel, 2014; Shi et al., 2022).”
BackgroundIron: A New Target for Pharmacological Intervention in Neurodegenerative Diseases
Whitnall, M., & Richardson, D. R. (2006) · Seminars in Pediatric Neurology · doi:10.1016/j.spen.2006.08.008 · Cited by 113
Three-Dimensional Atlas of Iron, Copper, and Zinc in the Mouse Cerebrum and Brainstem
Hare, D. J., Lee, J. K., Beavis, A. D., Gramberg, A. V., George, J. L., Adlard, P. A., Finkelstein, D. I., & Doble, P. (2012) · Analytical Chemistry · doi:10.1021/ac300374x · Cited by 114
Lan, M., Di, Y., Zhu, X. A., Ng, T., Xia, J., Liu, W., Meng, X., Wang, P., Lee, C., & Zhang, W. (2015) · Chemical Communications · doi:10.1039/c5cc05835j · Cited by 114
A two-photon NIR-to-NIR fluorescent probe for imaging hydrogen peroxide in living cells
Li, H., Yao, Q., Fan, J., Du, J., Wang, J., & Peng, X. (2017) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2017.03.039 · Cited by 116
“…(Kanvah et al. 2009; Shibutani et al. 1991) but is also relevant to serious diseases such as cardiovascular disorders (Abe and Berk 1998), neurodegenerative diseases (Barnham et al. 2004), Alzheimer’s disease (Behl et al. 1994) and cancer (Finkel et al. 2007; Murphy et al. 2011; Park et al. 2008).”
BackgroundMetal transporters in intestine and brain: their involvement in metal-associated neurotoxicities
Bressler, J. P., Olivi, L., Cheong, J. H., Kim, Y., Maerten, A., & Bannon, D. I. (2007) · Human & Experimental Toxicology · doi:10.1177/0960327107070573 · Cited by 114
Arnal, N., Cristalli, D. O., de Alaniz, M. J. T., & Marra, C. A. (2009) · Brain Research · doi:10.1016/j.brainres.2009.11.085 · Cited by 113
Recent advances in hydrogen peroxide imaging for biological applications
Guo, H., Aleyasin, H., Dickinson, B. C., Haskew-Layton, R. E., & Ratan, R. R. (2014) · Cell & Bioscience · doi:10.1186/2045-3701-4-64 · Cited by 114
Wang, H., Wang, N., Xu, D., Ma, Q., Chen, Y., Xu, S., Qin, X., Zhang, Y., Prehn, J. H. M., Wang, G., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1704104 · Cited by 114
“Relevant to this, mutations of proteins in autophagylysosome system can lead to neurodegenerative disorders including amyotrophic lateral sclerosis (ALS) and Parkinson disease (PD) [4,5], the key feature of which is aggregation of misfolded proteins [6].”
BackgroundTickler, A. K., Smith, D. G., Ciccotosto, G. D., Tew, D. J., Curtain, C. C., Carrington, D., Masters, C. L., Bush, A. I., Cherny, R. A., Cappai, R., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414178200 · Cited by 115
Self-citationModeling mitochondrial function in aging neurons
Melov, S. (2004) · Trends in Neurosciences · doi:10.1016/j.tins.2004.08.004 · Cited by 117
Dual protection of hydroxytyrosol, an olive oil polyphenol, against oxidative damage in PC12 cells
Peng, S., Zhang, B., Yao, J., Duan, D., & Fang, J. (2015) · Food & Function · doi:10.1039/c5fo00097a · Cited by 112
Zhang, W., Liu, W., Li, P., Huang, F., Wang, H., & Tang, B. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b02194 · Cited by 112
Senthilkumar, S., Goswami, R., Smith, V. J., Bajaj, H. C., & Neogi, S. (2018) · ACS Sustainable Chemistry & Engineering · doi:10.1021/acssuschemeng.8b01646 · Cited by 112
Rana, M., & Sharma, A. K. (2018) · Metallomics · doi:10.1039/c8mt00203g · Cited by 116
Messias, C. M. B. D. O., Valentim, I. B., Guedes, G. D. S., Rabelo, L. A., Mano, C. M., Bechara, E. J. H., Sawaya, A. C. H. F., Trevisan, M. T. S., da Costa, J. G., Ferreira, R. C. S., et al. (2012) · Food Research International · doi:10.1016/j.foodres.2012.07.010 · Cited by 111
A Self-Organizing Chemical Assembly Line
Junior, A. G. S., Zarra, S., Turner, R. M., & Nitschke, J. R. (2013) · Journal of the American Chemical Society · doi:10.1021/ja412235e · Cited by 112
Protein misfolding and amyloid nucleation through liquid–liquid phase separation
Mukherjee, S., Poudyal, M., Dave, K., Kadu, P., & Maji, S. K. (2024) · Chemical Society Reviews · doi:10.1039/d3cs01065a · Cited by 117
Yang, W., & Tiffany‐Castiglioni, E. (2005) · Journal of Toxicology and Environmental Health · doi:10.1080/15287390500226987 · Cited by 112
“There is extensive evidence that oxidative stress is associated with neurodegenerative diseases such as Parkinson’s disease (PD), Alzheimer’s disease (AD), Huntington’s disease (HD), and amyotropic lateral sclerosis (ALS) (Barnham et al., 2004).”
BackgroundA colorimetric chemosensor for the sequential detection of copper(II) and cysteine
Lee, S. A., Lee, J. J., Shin, J. W., Min, K. S., & Kim, C. (2015) · Dyes and Pigments · doi:10.1016/j.dyepig.2015.01.020 · Cited by 110
“4 mM) for Cu2þ is much below the World Health Organization (WHO) guideline (30 mM) in the drinking water [10,11], suggesting that 1 could be a powerful chemosensor for the detection of copper in the drinking water.”
BackgroundMayes, J., Tinker, C. L., Kolosov, O., Zhang, H., Tabner, B. J., & Allsop, D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.525212 · Cited by 110
“The redox activity of the copper-bound peptide converts any physiological H2O2 to OH (60), thus acting as a source of ROS.”
Background
Metadata
- Authors
- Barnham, K. J., Masters, C. L., & Bush, A. I.
- Affiliations
- Mental Health Research Institute (AU)
- Harvard University (US)
- Corresponding author
- Bush, Ashley I.
- Venue
- Nature Reviews Drug Discovery
- Published
- 2004-03
- Volume
- 3
- Issue
- 3
- Pages
- 205-214
- ISSN
- 1474-1776 (ISSN-L)
- 1474-1784
- OpenAlex
- W2044627978
- Cited by
- 3,683
- References
- 140
- Citations by year
- 2026: 121 · 2025: 164 · 2024: 173 · 2023: 217 · 2022: 194 · 2021: 218 · 2020: 208 · 2019: 228 · 2018: 213 · 2017: 229 · 2016: 196 · 2015: 208 · 2014: 209 · 2013: 168 · 2012: 160
- FWCI
- 7.81
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Drug Discovery (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Keywords
- oxidative stress, neurodegenerative diseases, Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, reactive oxygen species, antioxidant homeostasis, oxygen regulation, therapeutic target
- MeSH terms
- Animals, Antioxidants, Homeostasis, Humans, Clioquinol, Metals, Reactive Oxygen Species, Oxidative Stress, Neurodegenerative Diseases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review