Oxidative Stress and Neurotoxicity

Increased Neuronal Glucose-6-phosphate Dehydrogenase and Sulfhydryl Levels Indicate Reductive Compensation to Oxidative Stress in Alzheimer Disease

Russell, R. L., Siedlak, S. L., Raina, A. K., Bautista, J. M., Smith, M. A., & Perry, G. L. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1404 · Cited by 126

The role of metals in neurodegenerative diseases.

Lm, S., Perry, G. L., Atwood, C. S., & Ma, S. (2000) · PubMed · Cited by 125

How superoxide radical damages the cell

Benov, L. (2001) · PROTOPLASMA · doi:10.1007/bf01289410 · Cited by 125

Obligatory Role for Complex I Inhibition in the Dopaminergic Neurotoxicity of 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)

Richardson, J. R., Caudle, W. M., Guillot, T. S., Watson, J. L., Nakamaru‐Ogiso, E., Seo, B. B., Sherer, T., Greenamyre, J. T., Yagi, T., Matsuno‐Yagi, A., et al. (2006) · Toxicological Sciences · doi:10.1093/toxsci/kfl133 · Cited by 124

Oxidative stress promotes mutant huntingtin aggregation and mutant huntingtin-dependent cell death by mimicking proteasomal malfunction

Goswami, A., Dikshit, P., Mishra, A., Mulherkar, S. A., Nukina, N., & Jana, N. R. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.01.136 · Cited by 124

α-Lipoic acid is effective in prevention and treatment of experimental autoimmune encephalomyelitis

Morini, M., Roccatagliata, L., Dell’Eva, R., Pedemonte, E., Furlan, R., Minghelli, S., Giunti, D., Pfeffer, U., Marchese, M., Noonan, D. M., et al. (2004) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2003.11.021 · Cited by 124

Does cellular iron dysregulation play a causative role in Parkinson’s disease?

Kaur, D., & Andersen, J. (2004) · Ageing Research Reviews · doi:10.1016/j.arr.2004.01.003 · Cited by 123

On the neurotoxicity mechanism of leukoaminochrome o-semiquinone radical derived from dopamine oxidation: mitochondria damage, necrosis, and hydroxyl radical formation

Arriagada, C., Paris, I. B., Matas, M. J. S. D. L., Martinez-Alvarado, P., Cárdenas, S., Castañeda, P., Graumann, R., Perez-Pastene, C., Olea‐Azar, C., Couve, E., et al. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.03.014 · Cited by 123

Phosphorylated, but not native, tau protein assembles following reaction with the lipid peroxidation product, 4‐hydroxy‐2‐nonenal

Pérez, M., Cuadros, R., Smith, M. A., Perry, G. L., & Ávila, J. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02323-1 · Cited by 121

Alterations in Gene Expression Induced by the Lipid Peroxidation Product, 4-Hydroxy-2-nonenal

West, J. D., & Marnett, L. J. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050211n · Cited by 121

Quinone reductase (NQO1), a sensitive redox indicator, is increased in Alzheimer’s disease

Raina, A. K., Templeton, D. J., deak, J. C., Perry, G., & Smith, M. A. (1999) · Redox Report · doi:10.1179/135100099101534701 · Cited by 120

Reactive Oxygen Species as Causal Agents in the Neurotoxicity of the Alzheimer's Disease‐Associated Amyloid Beta Peptidea

Hensley, K., BUTTERFIELDLD, D. A., Hall, N. C., COLE, P., Subramaniam, R., Mark, R. J., Mattson, M. P., Markesbery, W. R., Harris‐White, M. E., Aksenov, M. Y., et al. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb39057.x · Cited by 117

Biochemical mechanism of action of the dopaminergic neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)

Sayre, L. M. (1989) · Toxicology Letters · doi:10.1016/0378-4274(89)90168-9 · Cited by 117

Methylation of the Imidazole Side Chains of the Alzheimer Disease Amyloid-β Peptide Results in Abolition of Superoxide Dismutase-like Structures and Inhibition of Neurotoxicity

Tickler, 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

Mitochondrial aging and dysfunction in Alzheimer's disease

Sullivan, P. G., & Brown, M. R. (2005) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2004.12.007 · Cited by 114

Trolox and 17β-Estradiol Protect against Amyloid β-Peptide Neurotoxicity by a Mechanism That Involves Modulation of the Wnt Signaling Pathway

Quintanilla, R. A., Muñoz, F. J., Metcalfe, M., Hitschfeld, M., Olivares, G. H., Godoy, J. A., & Inestrosa, N. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411936200 · Cited by 114

Methamphetamine‐induced dopaminergic neurotoxicity is regulated by quinone formation‐related molecules

Miyazaki, I., Asanuma, M., Diaz-Corrales, F. J. J., Fukuda, M., Kitaichi, K., Miyoshi, K., & Ogawa, N. (2006) · The FASEB Journal · doi:10.1096/fj.05-4996fje · Cited by 111

The oxidative stress mediator 4-hydroxynonenal is an intracellular agonist of the nuclear receptor peroxisome proliferator-activated receptor-β/δ (PPARβ/δ)

Coleman, J. D., Prabhu, K. S., Thompson, J. T., Reddy, P. S., Peters, J. M., Peterson, B. R., Reddy, C. C., & Heuvel, J. P. V. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.01.003 · Cited by 110

Structural Studies of the Alzheimer’s Amyloid Precursor Protein Copper-binding Domain Reveal How it Binds Copper Ions

Kong, G. K.-W., Adams, J. J., Harris, H. H., Boas, J. F., Curtain, C. C., Galatis, D., Masters, C. L., Barnham, K. J., McKinstry, W. J., Cappai, R., et al. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.12.041 · Cited by 109

Oxidative stress and overexpression of manganese superoxide dismutase in patients with Alzheimer's disease

Leo, M. E. D., Borrello, S., Passantino, M., Palazzotti, B., Mordente, A., Daniele, A., Filippini, V., Galeotti, T., & Masullo, C. (1998) · Neuroscience Letters · doi:10.1016/s0304-3940(98)00469-8 · Cited by 108

The Role of Amyloid-Beta Derived Diffusible Ligands (ADDLs) in Alzheimers Disease

Catalano, S. M., Dodson, E., Henze, D. A., Joyce, J. G., Krafft, G. A., & Kinney, G. G. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802606776743066 · Cited by 107

Small Molecule Oxidation Products Trigger Disease-Associated Protein Misfolding

Bieschke, J., Zhang, Q., Bosco, D. A., Lerner, R. A., Powers, E. T., Wentworth, P., & Kelly, J. W. (2006) · Accounts of Chemical Research · doi:10.1021/ar0500766 · Cited by 105

Expanding Insights on the Involvement of Endoplasmic Reticulum Stress in Parkinson's Disease

Wang, H., & Takahashi, R. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.1524 · Cited by 104

Isoprostanes, Novel Markers of Oxidative Injury, Help Understanding the Pathogenesis of Neurodegenerative Diseases

Greco, A., Minghetti, L., & Levi, G. (2000) · Neurochemical Research · doi:10.1023/a:1007608615682 · Cited by 103

Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: Parallels to precursors in amyloid disease

Nordlund, A., & Oliveberg, M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601696103 · Cited by 103

Oxidative stress in Alzheimer’s Disease: Implications for Prevention and Therapy

Behl, C. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_3 · Cited by 100

Role of 4-hydroxynonenal and its metabolites in signaling

Dwivedi, S., Sharma, A., Patrick, B., Sharma, R., & Awasthi, S. (2007) · Redox Report · doi:10.1179/135100007x162211 · Cited by 100

Contribution of redox-active iron and copper to oxidative damage in Alzheimer disease

Castellani, R. J., Honda, K., Zhu, X., Cash, A., Nunomura, A., Perry, G. L., & Smith, M. A. (2004) · Ageing Research Reviews · doi:10.1016/j.arr.2004.01.002 · Cited by 100

Pathogenic superoxide dismutase structure, folding, aggregation and turnover

Hart, P. J. (2006) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2006.02.034 · Cited by 100

Cerebrospinal fluid isoprostane shows oxidative stress in patients with multiple sclerosis

Greco, A., Minghetti, L., Sette, G., Fieschi, C., & Levi, G. (1999) · Neurology · doi:10.1212/wnl.53.8.1876 · Cited by 97

Amyloid Beta: The Alternate Hypothesis

Lee, H., Zhu, X., Nunomura, A., Perry, G. L., & Smith, M. A. (2006) · Current Alzheimer Research · doi:10.2174/156720506775697124 · Cited by 96

Dopamine efflux by MPTP and hydroxyl radical generation

Obata, T. (2002) · Journal of Neural Transmission · doi:10.1007/s00702-001-0683-2 · Cited by 95

Generation of the Neurotoxin 6-Hydroxydopamine by Peroxidase/H2O2 Oxidation of Dopamine

Napolitano, A., Crescenzi, O., Pezzella, A., & Prota, G. (1995) · Journal of Medicinal Chemistry · doi:10.1021/jm00006a010 · Cited by 95

Ferritin is associated with the aberrant tau filaments present in progressive supranuclear palsy.

Pérez, M., Valpuesta, J., de Garcini, E. M., Quintana, C., Arrasate, M., Carrascosa, J. L., Rábano, A., de Yébenes, J. G., & Ávila, J. (1998) · Europe PMC (PubMed Central) · Cited by 94

Controversies on new animal models of Parkinson’s disease Pro and Con: the rotenone model of Parkinson’s disease (PD)

Schmidt, W., & Alam, M. (2006) · Springer eBooks · doi:10.1007/978-3-211-45295-0_42 · Cited by 94

Neuroprotective properties of statins.

Stępień, K. M., Tomaszewski, M., & Czuczwar, S. J. (2005) · PubMed · Cited by 93

Atherosclerotic Lesions and Mitochondria DNA Deletions in Brain Microvessels as a Central Target for the Development of Human AD and AD‐Like Pathology in Aged Transgenic Mice

Aliev, G., Seyidova, D., Neal, M. L., Shi, J., Lamb, B. T., Siedlak, S. L., Vinters, H. V., Head, E., Perry, G. L., LaManna, J. C., et al. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb04798.x · Cited by 91

Failure of protein quality control in amyotrophic lateral sclerosis

Kabashi, E., & Durham, H. D. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.06.006 · Cited by 90

Lipid peroxidation associated cardiolipin loss and membrane depolarization in rat brain mitochondria

Sen, T., Sen, N., Tripathi, G., Chatterjee, U., & Chakrabarti, S. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2005.12.018 · Cited by 90

Models of Parkinson's disease

Orth, M., & Tabrizi, S. J. (2003) · Movement Disorders · doi:10.1002/mds.10447 · Cited by 89

Methionine regulates copper/hydrogen peroxide oxidation products of Aβ

Ali, F. E. A., Separovic, F., Barrow, C. J., Cherny, R. A., Fraser, F. W., Bush, A. I., Masters, C. L., & Barnham, K. J. (2004) · Journal of Peptide Science · doi:10.1002/psc.626 · Cited by 89

Brain Nitric Oxide and Its Dual Role in Neurodegeneration / Neuroprotection: Understanding Molecular Mechanisms to Devise Drug Approaches

Contestabile, A., Monti, B., Contestabile, A., & Ciani, E. (2003) · Current Medicinal Chemistry · doi:10.2174/0929867033456792 · Cited by 88

Glutamate excitotoxicity — a mechanism for axonal damage and oligodendrocyte death in Multiple Sclerosis?

Werner, P., Pitt, D., & Raine, C. S. (2000) · Springer eBooks · doi:10.1007/978-3-7091-6301-6_27 · Cited by 87

Oxidative stress in serum and peripheral blood leukocytes in patients with different disease courses of multiple sclerosis

Koch, M. W., Ramsaransing, G. S. M., Arutjunyan, A. V., Stepanov, M., Teelken, A. W., Heersema, D. J., & Keyser, J. D. (2005) · Journal of Neurology · doi:10.1007/s00415-005-0037-3 · Cited by 86

Tryptophan 32 Potentiates Aggregation and Cytotoxicity of a Copper/Zinc Superoxide Dismutase Mutant Associated with Familial Amyotrophic Lateral Sclerosis

Taylor, D. M., Gibbs, B. F., Kabashi, E., Minotti, S., Durham, H. D., & Agar, J. N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610119200 · Cited by 85

Neuronal RNA oxidation is a prominent feature of dementia with Lewy bodies

Nunomura, A., Chiba, S., Kosaka, K., Takeda, A., Castellani, R. J., Smith, M. A., & Perry, G. L. (2002) · Neuroreport · doi:10.1097/00001756-200211150-00009 · Cited by 84

Rodent Aβ(1–42) exhibits oxidative stress properties similar to those of human Aβ(1–42): Implications for proposed mechanisms of toxicity

Debra Boyd-kimball, A., Rukhsana Sultana, A., Abdul, H. M., & Butterfield, D. A. (2004) · Journal of Alzheimer s Disease · doi:10.3233/jad-2004-6509 · Cited by 82

Parkin and defective ubiquitination in Parkinson's disease.

Dawson, T. M. (2006) · Journal of neural transmission. Supplementum · doi:10.1007/978-3-211-45295-0_32 · Cited by 81

Is hemochromatosis a risk factor for Alzheimer's disease?

Connor, J. R., Milward, E. A., Moalem, S., Sampietro, M., Boyer, P. J., Percy, M. E., Vergani, C., Scott, R. J., & Chorney, M. J. (2001) · Journal of Alzheimer s Disease · doi:10.3233/jad-2001-3506 · Cited by 80

FAD mutants unable to increase neurotoxic Aβ 42 suggest that mutation effects on neurodegeneration may be independent of effects on Aβ

Shioi, J., Georgakopoulos, A., Mehta, P. D., Kouchi, Z., Litterst, C. M., Baki, L., & Robakis, N. K. R. K. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04391.x · Cited by 80

Huntington?s disease: pathomechanism and therapeutic perspectives

G�rdi�n, G., & V�csei, L. (2004) · Journal of Neural Transmission · doi:10.1007/s00702-004-0201-4 · Cited by 77

Modification of proteins and lipids by myeloperoxidase

Hazen, S. L., Hsu, F., Gaut, J. P., Crowley, J. R., & Heinecke, J. W. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)00117-2 · Cited by 76

Chemical Nature of Stochastic Generation of Protein-based Carbonyls: Metal-catalyzed Oxidation versus Modification by Products of Lipid Oxidation

Yuan, Q., Zhu, X., & Sayre, L. M. (2006) · Chemical Research in Toxicology · doi:10.1021/tx600270f · Cited by 76

A vicious circle: role of oxidative stress, intraneuronal Abeta and Cu in Alzheimer's disease.

Bayer, T. A., Schäfer, S., Breyhan, H., Wirths, O., Treiber, C., & Multhaup, G. (2006) · PubMed · Cited by 75

Dopamine-Dependent Iron Toxicity in Cells Derived from Rat Hypothalamus

Paris, I., Martinez-Alvarado, P., Cárdenas, S., Perez-Pastene, C., Graumann, R., Fuentes, P., Olea-Azar, C., Caviedes, P., & Segura-Aguilar, J. (2005) · Chemical Research in Toxicology · doi:10.1021/tx0497144 · Cited by 74

Model study on the bioreduction of paraquat, MPP+, and analogs. Evidence against a “redox cycling” mechanism in MPTP neurotoxicity

Frank, D. M., Arora, P. K., Blumer, J. L., & Sayre, L. M. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(87)80183-3 · Cited by 74

Nitric oxide, S-nitrosylation and neurodegeneration.

Chung, K. K. K., Dawson, T. M., & Dawson, V. L. (2005) · PubMed · Cited by 73

Nonenzymatic antioxidants of blood in multiple sclerosis

Karg, E., Klivènyi, P., Németh, I., Bencsik, K., Pintér, S., & Vécsei, L. (1999) · Journal of Neurology · doi:10.1007/s004150050399 · Cited by 72

Site-Specific Synthesis and Reactivity of Oligonucleotides Containing Stereochemically Defined 1,N2-Deoxyguanosine Adducts of the Lipid Peroxidation Product trans-4-Hydroxynonenal

Wang, H., Kozekov, I. D., Harris, T. M., & Rizzo, C. J. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0288800 · Cited by 69

Antioxidants in Multiple Sclerosis: Do They Have a Role in Therapy?

Carlson, N. G., & ROSE, J. W. (2006) · CNS Drugs · doi:10.2165/00023210-200620060-00001 · Cited by 68

An immunochemical study on tau glycation in paired helical filaments

Ko, L., Ko, E. C., Nacharaju, P., Liu, W.-K., Chang, E. C., Kenessey, Á., & Yen, S.-H. C. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01415-8 · Cited by 68

Changes in cerebrospinal fluid levels of malondialdehyde and glutathione reductase activity in multiple sclerosis.

Calabrese, V., Raffaele, R., Cosentino, E. R., & Rizza, V. (1994) · PubMed · Cited by 68

Biliverdin reductase, a major physiologic cytoprotectant, suppresses experimental autoimmune encephalomyelitis

Liu, Y., Liu, J., Tetzlaff, W., Paty, D. W., & Cynader, M. S. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.07.021 · Cited by 67

Redox Properties of Met35in Neurotoxic β-Amyloid Peptide. A Molecular Modeling Study

Pogocki, D., & Schöneich, C. (2002) · Chemical Research in Toxicology · doi:10.1021/tx0101550 · Cited by 67

Submicromolar concentrations of 4-hydroxynonenal induce glutamate cysteine ligase expression in HBE1 cells

Zhang, H., Court, N., & Forman, H. J. (2007) · Redox Report · doi:10.1179/135100007x162266 · Cited by 67

Plasma lipid peroxidation and progression of disability in multiple sclerosis

Koch, M. W., Mostert, J. P., Arutjunyan, A. V., Stepanov, M., Teelken, A. W., Heersema, D. J., & Keyser, J. D. (2007) · European Journal of Neurology · doi:10.1111/j.1468-1331.2007.01739.x · Cited by 67

Oxidative Stress in Skin Fibroblasts Cultures of Patients with Huntington’s Disease

del Hoyo, P., García‐Redondo, A., Bustos, F., Molina, J. A., Sayed, Y., Alonso‐Navarro, H., Caballero, L., Arenas, J., & Jiménez‐Jiménez, F. J. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9110-2 · Cited by 66

Is levodopa toxic?

M�ller, T., Hefter, H., Hueber, R., Jost, W., Leenders, K., Odin, P., & Schwarz, J. (2004) · Journal of Neurology · doi:10.1007/s00415-004-1610-x · Cited by 66

The Amyloid Paradox: Amyloid‐β‐Metal Complexes can be Neurotoxic and Neuroprotective

Bishop, G. M., & Robinson, S. R. (2004) · Brain Pathology · doi:10.1111/j.1750-3639.2004.tb00089.x · Cited by 66

Frequent coexistence of Lewy bodies and neurofibrillary tangles in the same neurons of patients with diffuse Lewy body disease

Iseki, E., Marui, W., Kosaka, K., & Uéda, K. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00178-0 · Cited by 65

Causes of neuronal death in Parkinson's disease.

Schapira, A. H. V. (2001) · PubMed · Cited by 65

4-Hydroxy-2-nonenal Adduction of Extracellular Signal-Regulated Kinase (Erk) and the Inhibition of Hepatocyte Erk-Est–Like Protein-1-Activating Protein-1 Signal Transduction

Sampey, B. P., Carbone, D. L., Doorn, J. A., Drechsel, D. A., & Petersen, D. R. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.029686 · Cited by 64

Hydrogen peroxide induces apoptosis in cerebral vascular smooth muscle cells: possible relation to neurodegenerative diseases and strokes

Li, J., Li, W., Su, J., Liu, W., Altura, B. T., & Altura, B. M. (2003) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2003.08.011 · Cited by 61

Detection and Quantification of Endogenous Cyclic DNA Adducts Derived from trans-4-Hydroxy-2-nonenal in Human Brain Tissue by Isotope Dilution Capillary Liquid Chromatography Nanoelectrospray Tandem Mass Spectrometry

Liu, X., Lovell, M. A., & Lynn, B. C. (2006) · Chemical Research in Toxicology · doi:10.1021/tx0502903 · Cited by 60

Apoptosis signalling by 4-hydroxynonenal: a role for JNK–c-Jun/AP-1 pathway

Kütük, Ö., & Başağa, H. (2007) · Redox Report · doi:10.1179/135100007x162329 · Cited by 60

The Therapeutic Potential of Statins in Neurological Disorders

Rajanikant, G. K., Zemke, D., Kassab, M., & Majid, A. (2006) · Current Medicinal Chemistry · doi:10.2174/092986707779313462 · Cited by 60

Involvement of Superoxide in Excitotoxicity and DNA Fragmentation in Striatal Vulnerability in Mice after Treatment with the Mitochondrial Toxin, 3-Nitropropionic Acid

Kim, G. W., & Chan, P. H. (2002) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200207000-00005 · Cited by 59

α-Synuclein Is Required for the Fibrillar Nature of Ubiquitinated Inclusions Induced by Proteasomal Inhibition in Primary Neurons

Rideout, H. J., Dietrich, P., Wang, Q., Dauer, W. T., & Stefanis, L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405146200 · Cited by 59

Cyclooxygenase-2 Is an Obligatory Factor in Methamphetamine-Induced Neurotoxicity

Thomas, D. M., & Kuhn, D. M. (2005) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.104.080242 · Cited by 58

The activation of protein kinase C induces higher production of reactive oxygen species by mononuclear cells in patients with multiple sclerosis than in controls

Vladimirova, O. V., Lu, F. M., Shawver, L., & Kálmán, B. (1999) · Inflammation Research · doi:10.1007/s000110050480 · Cited by 58

Cellular cofactors potentiating induction of stress and cytotoxicity by amyloid β-peptide

Yan, S. D., Roher, A. E., Chaney, M., Zloković, B. V., Schmidt, A. M., & Stern, D. M. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00041-7 · Cited by 58

Free radical-mediated neurotoxicity may be caused by inhibition of mitochondrial dehydrogenases in vitro and in vivo

Sheline, C. T., & Wei, L. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.02.019 · Cited by 57

Differential regulation of cyclooxygenase‐2 and inducible nitric oxide synthase by 4‐hydroxynonenal in human osteoarthritic chondrocytes through ATF‐2/CREB‐1 transactivation and concomitant inhibition of NF‐κB signaling cascade

Vaillancourt, F., Morquette, B., Shi, Q., Fahmi, H., Lavigne, P., Battista, J. A. D., Fernandes, J., & Benderdour, M. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21110 · Cited by 55

Integrative hypothesis for Huntington’s disease: a brief review on experimental evidence.

de la Cruz, V. P., & Santamaría, A. (2007) · Physiological Research · doi:10.33549/physiolres.931049 · Cited by 54

Attenuated amyloid-β aggregation and neurotoxicity owing to methionine oxidation

Johansson, A., Bergquist, J., Volbracht, C., Päiviö, A., Leist, M., Lannfelt, L., & Westlind‐Danielsson, A. (2007) · Neuroreport · doi:10.1097/wnr.0b013e3280b07c21 · Cited by 53

Behavioral effects of manganese injected in the rat substantia nigra are potentiated by dicumarol, a DT-diaphorase inhibitor

Díaz‐Véliz, G. (2003) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2003.10.016 · Cited by 52

Increased affinity for copper mediated by cysteine 111 in forms of mutant superoxide dismutase 1 linked to amyotrophic lateral sclerosis

Watanabe, S., Nagano, S., Duce, J. A., Kiaei, M., Li, Q.-X., Tucker, S. M., Tiwari, A., Brown, R. H., Beal, M. F., Hayward, L. J., et al. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.02.004 · Cited by 52

Application of proteasomal inhibitors to mouse sympathetic neurons activates the intrinsic apoptotic pathway

Lang‐Rollin, I., Vekrellis, K., Wang, Q., Rideout, H. J., & Stefanis, L. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02684.x · Cited by 52

Oxidative stress in patients with multiple sclerosis.

Syburra, C., & Passi, S. (1999) · PubMed · Cited by 51

[10] In situ methods for detection and localization of markers of oxidative stress: Application in neurodegenerative disorders

Sayre, L. M., Perry, G. L., & Smith, M. A. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)09012-6 · Cited by 50

Translesion DNA Synthesis across the Heptanone−Etheno-2‘-Deoxycytidine Adduct in Cells

Pollack, M., Yang, I.-Y., Kim, H., Blair, I. A., & Moriya, M. (2006) · Chemical Research in Toxicology · doi:10.1021/tx0600503 · Cited by 50

Reduction of inclusion body pathology in ApoE-deficient mice fed a combination of antioxidants

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Synthesis and 32P-Postlabeling/High-Performance Liquid Chromatography Separation of Diastereomeric 1,N2-(1,3-Propano)-2‘-deoxyguanosine 3‘-Phosphate Adducts Formed from 4-Hydroxy-2-nonenal

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