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Oxidative Pathways for Catecholamines in the Genesis of Neuromelanin and Cytotoxic Quinones
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“When iron is present in the cytosol (as may occur more frequently with ageing)265,266, dopamine can be oxidized into dopamine quinone (DAQ), which is highly reactive and toxic267,268.”
From Rhythms of life: circadian disruption and brain disorders across the lifespan (2019) · cites this paper as [267]
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Gonçalves, L. M. L., Ramkissoon, A., & Wells, P. G. (2009) · Chemical Research in Toxicology · doi:10.1021/tx800423s · Cited by 20
Kim, H. K., & Andreazza, A. C. (2012) · Expert Review of Neurotherapeutics · doi:10.1586/ern.12.64 · Cited by 20
Monocrotaline: Histological Damage and Oxidant Activity in Brain Areas of Mice
Júnior, J. E. R. H., Vasconcelos, G. S., Rodrigues, F. T. S., Filho, J. G. D. S., Barbosa‐Filho, J. M., Aguiar, C. C. T., Leal, L. K. A. M., Soares, P. M. G., Woods, D. J., Fonteles, M. M. D. F., et al. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/697541 · Cited by 20
“Oxidative stress (OS) is classically defined as a redox imbalance caused by an excess of oxidants or a lack of natural antioxidants in the system [14, 15].”
BackgroundBehavioral impairments and serotonin reductions in rats after chronic L-dopa
Stansley, B. J., & Yamamoto, B. K. (2015) · Psychopharmacology · doi:10.1007/s00213-015-3980-4 · Cited by 20
Yadav, S. K., Pandey, S., & Singh, B. (2017) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2017.07.002 · Cited by 20
Some aspects of tyrosine secondary metabolism
Rescigno, A., Rinaldi, A. C., & Sanjust, E. (1998) · Biochemical Pharmacology · doi:10.1016/s0006-2952(98)00170-1 · Cited by 20
“In particular, they can readily cyclize, leading to melanins [9].”
BackgroundModel neuromelanins as antioxidative agents during lipid peroxidation
Wilczok, T., Stȩpień, K. B., Dzierżęga‐Lęcznar, A., Zajdel, A., & Wilczok, A. (1999) · Neurotoxicity Research · doi:10.1007/bf03033277 · Cited by 20
Joseph, J. A., Erat, S., Denisova, N., & Villalobos‐Molina, R. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00379-1 · Cited by 20
Soares, J., Costa, V. M., Gaspar, H., Santos, S., Bastos, M. D. L., Carvalho, F. D., & Capela, J. P. (2020) · Archives of Toxicology · doi:10.1007/s00204-020-02761-y · Cited by 19
“Also, DA may autoxidize leading to hydrogen peroxide and superoxide formation which, in the presence of transition metals, ultimately form the hydroxyl radical (Graham 1978).”
BackgroundVallée, A., Vallée, J.-N., & Lecarpentier, Y. (2021) · Translational Psychiatry · doi:10.1038/s41398-021-01329-3 · Cited by 18
Structural Features and Toxicity of α-Synuclein Oligomers Grown in the Presence of DOPAC
Palazzi, L., Fongaro, B., Leri, M., Acquasaliente, L., Stefani, M., Bucciantini, M., & de Laureto, P. P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22116008 · Cited by 20
“This finding indicates that, apart from the oxidation mediated by H2O2 released by DOPAC, Syn-membrane interaction is also modulated directly by the DOPAC effect on Syn.”
BackgroundInfluentialWang, W., Wu, X., Yang, C. S., & Zhang, J. (2021) · Antioxidants · doi:10.3390/antiox10101564 · Cited by 23
Parkinson's disease: animal models
Betarbet, R. S., & Greenamyre, J. T. (2007) · Handbook of clinical neurology · doi:10.1016/s0072-9752(07)83011-9 · Cited by 18
“Additionally, auto-oxidation of dopamine results in dopamine quinones (Graham, 1978), along with the formation of ROS (Lotharius and O’Malley, 2000).”
BackgroundLuk, B., Mohammed, M., Liu, F., & Lee, F. J. S. (2015) · PLoS ONE · doi:10.1371/journal.pone.0136641 · Cited by 19
“Accumulation of these oxidative metabolites can lead to oxidative stress, which can damage proteins, lipids and DNA [111–113].”
Disease-Toxicant Interactions in Parkinson’s Disease Neuropathology
Kwakye, G. F., McMinimy, R. A., & Aschner, M. (2016) · Neurochemical Research · doi:10.1007/s11064-016-2052-4 · Cited by 21
Kum, W. F., Gao, J., Durairajan, S. S. K., Man, S. C., Xie, L., Lu, J., Fong, W. L., & Li, M. (2009) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2008.10.015 · Cited by 19
Picada, J. N., Roesler, R., & Henriques, J. A. P. (2005) · Brazilian Journal of Medical and Biological Research · doi:10.1590/s0100-879x2005000400001 · Cited by 19
Newcomer, T. A., Palmer, A. M., Rosenberg, P. A., et al. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03602.x · Cited by 19
Baez, S., Linderson, Y., & Segura‐Aguilar, J. (1994) · Chemico-Biological Interactions · doi:10.1016/0009-2797(94)90090-6 · Cited by 19
Yoshioka, Y., Sugino, Y., Tozawa, A., Yamamuro, A., Kasai, A., Ishimaru, Y., & Maeda, S. (2016) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2015.11.002 · Cited by 18
Fischer, A. F., & Matera, K. M. (2015) · Neurochemical Research · doi:10.1007/s11064-015-1597-y · Cited by 18
Milusheva, E., Baranyi, M., Kormos, E., Hracskó, Z., Vizi, E. S., & Sperlágh, B. (2009) · Neuropharmacology · doi:10.1016/j.neuropharm.2009.11.017 · Cited by 18
“Since DAQ is thought to be formed by both enzymatic and non-enzymatic conversion of DA (Graham, 1978), rasagiline, which A C B E M M 0 2 4 6 8 10 12 0 6 12 18 24 30 36 42 48 54 60 min [ 3 H] FR% 0.01 0.1 control 1 H2O2 0.”
InfluentialResveratrol attenuates L-DOPA-induced hydrogen peroxide toxicity in neuronal cells
Peritore, C., Ho, A., Yamamoto, B. K., et al. (2012) · Neuroreport · doi:10.1097/wnr.0b013e32835a4ea4 · Cited by 18
Zhou, Z., Kerk, S. Y., & Lim, T. M. (2008) · Free Radical Research · doi:10.1080/10715760802005177 · Cited by 18
“It is well established that DA oxidation could produce ROS and toxic DA quinones [6].”
BackgroundHagiwara, T., Lee, C. I., & Okabe, E. (2000) · Neuropharmacology · doi:10.1016/s0028-3908(99)00240-3 · Cited by 18
Lifelong Ethanol Consumption and Loss of Locus Coeruleus Neurons in AA and ANA Rats
Rintala, J., Jaatinen, P., Lü, W., et al. (1998) · Alcohol · doi:10.1016/s0741-8329(98)00012-3 · Cited by 18
Pérez, V., Romera, M., Lizcano, J. M., Marco, J. L., & Unzeta, M. (2003) · Journal of Pharmacy and Pharmacology · doi:10.1211/002235703765344649 · Cited by 18
“Dopamine is able to generate free radicals and quinone products that polymerise, generating melanin (Graham 1978).”
BackgroundSurgical Anatomy of the Brain Stem
Lang, J. (1993) · Neurosurgery Clinics of North America · doi:10.1016/s1042-3680(18)30566-7 · Cited by 18
Loven, D. P., James, J. F., Biggs, L., & Little, K. Y. (1996) · Biological Psychiatry · doi:10.1016/0006-3223(95)00669-9 · Cited by 18
“Antipsychotics increase dopamine release, which is a potential free radical donor (Graham 1978).”
BackgroundLinderson, Y., Baez, S., & Segura‐Aguilar, J. (1994) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(94)90136-8 · Cited by 18
Blandini, F., Martignoni, E., Ricotti, R., Jeso, F. D., & Nappi, G. (1999) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(99)00286-8 · Cited by 18
Mondal, R., Banerjee, C., Nandy, S., Roy, M., & Chakraborty, J. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-01068-6 · Cited by 20
“Tyrosinase oxidizes DA (leading to the formation of DAQ) without the production of free radicals [5, 9, 25].”
BackgroundElgawish, M. S., Kishikawa, N., Helal, M. A., Ohyama, K., & Kuroda, N. (2015) · Toxicology Research · doi:10.1039/c5tx00098j · Cited by 18
Chun, S. I., McEvilly, R. J., Foster, J. A., et al. (2007) · Molecular Psychiatry · doi:10.1038/sj.mp.4002078 · Cited by 17
Neurorescue by a ROS Decomposition Catalyst
Soll, M., Am, O. B., Mahammed, A., et al. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00144 · Cited by 17
Choi, H., & Koh, S. (2017) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1080/17425255.2018.1417387 · Cited by 17
“When DA neurons are injured, excess cytosolic DA or L-DOPA is consequently oxidized and generates DA or DOPA quinones [60,61].”
BackgroundCyclization step of noradrenaline and adrenaline autoxidation: a quantum chemical study
Umek, N. (2020) · RSC Advances · doi:10.1039/d0ra02713h · Cited by 17
Crick, E. W., Osorio, I., Frei, M. G., et al. (2014) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2013.11.019 · Cited by 17
“This excess release of DA can be cytotoxic, resulting from both enzymatic and non-enzymatic oxidation processes which generate reactive oxygen species (ROS) (Graham, 1978; Hasting, 1995).”
InfluentialSelective neurotoxins, chemical tools to probe the mind: The first Thirty years and beyond
Kostrzewa, R. M. (1999) · Neurotoxicity Research · doi:10.1007/bf03033336 · Cited by 17
Recent advances in our understanding of Parkinson's disease
Kim, S. W., Ko, H. S., Dawson, V. L., & Dawson, T. M. (2005) · Drug Discovery Today Disease Mechanisms · doi:10.1016/j.ddmec.2005.11.015 · Cited by 17
New hydroxypyridinone iron-chelators as potential anti-neurodegenerative drugs
Arduíno, D. (2008) · Frontiers in bioscience · doi:10.2741/3187 · Cited by 17
“Nigral dopaminergic neurons are particularly exposed to oxidative stress, since dopamine can easily auto-oxidize into toxic dopamine-quinone species, superoxide radicals and hydrogen peroxide (14).”
BackgroundVelez‐Pardo, C. (1995) · Neurochemistry International · doi:10.1016/0197-0186(94)00163-o · Cited by 17
Miyazaki, I., Asanuma, M., Diaz-Corrales, F. J. J., Miyoshi, K., & Ogawa, N. (2005) · Clinical Neuropharmacology · doi:10.1097/01.wnf.0000175523.33334.24 · Cited by 17
“The DA quinones exert cytotoxicity by interacting with the sulfhydryl group of the amino acid cysteine of various bioactive molecules, resulting predominantly in the formation of 5-cysteinyl-DA.(16,17) Because the sulfhydryl group on cysteine is often found at the active site of functional proteins, the covalent modif…”
BackgroundWang, J., Wang, Y., Lv, H., Hui, F., Ma, Y., Lu, S., Sha, Q., & Wang, E. (2006) · Journal of Electroanalytical Chemistry · doi:10.1016/j.jelechem.2006.05.021 · Cited by 17
Apomorphine attenuates 6-hydroxydopamine-induced apoptotic cell death in SH-SY5Y cells
Hara, H., Ohta, M., Ohta, K., et al. (2003) · Redox Report · doi:10.1179/135100003225002682 · Cited by 17
Kingsbury, A. E., Cooper, M., Schapira, A. H. V., & Foster, O. J. F. (2001) · Annals of Neurology · doi:10.1002/ana.1051 · Cited by 17
Erdelyi, E., VandenBerg, S. R., Raese, J. D., et al. (1981) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/bf00430868 · Cited by 17
Monoamine and Iron-Related Toxicity
Velez‐Pardo, C., Jiménez-Del-Río, M., Ebinger, G., & Vauquelin, G. (1998) · General Pharmacology The Vascular System · doi:10.1016/s0306-3623(97)00440-0 · Cited by 17
Koıstınaho, J., Sorvaniemi, M., Alho, H., et al. (1986) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(86)90120-x · Cited by 17
Tatton, W. G., Greenwood, C. E., Seniuk, N. A., & SALO, P. T. (1992) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/s0317167100041494 · Cited by 17
Modulation of Reactive Oxygen Species Homeostasis as a Pleiotropic Effect of Commonly Used Drugs
Thomas, C., Wurzer, L., Malle, E., Ristow, M., & Madreiter‐Sokolowski, C. T. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.905261 · Cited by 18
“Together with dopamine, labile iron is part of a prooxidant synergic interplay in aged SN (Hare and Double, 2016), leading to increased production of highly toxic dopamine-o-quinones (Tse et al., 1976; Graham, 1978; Zhou et al., 2010).”
BackgroundComparing the dopaminergic neurotoxic effects of benzylpiperazine and benzoylpiperazine
Katz, D. P., Majrashi, M., Ramesh, S., Govindarajulu, M., Bhattacharya, D., Bhattacharya, S., Shlghom, A., Bradford, C., Suppiramaniam, V. D., DeRuiter, J., et al. (2017) · Toxicology Mechanisms and Methods · doi:10.1080/15376516.2017.1376024 · Cited by 16
Richter, F., Hamann, M., & Richter, A. (2007) · Brain Research · doi:10.1016/j.brainres.2007.09.083 · Cited by 16
Nucleus Accumbens Invulnerability to Methamphetamine Neurotoxicity
Kuhn, D. M., Angoa‐Pérez, M., & Thomas, D. M. (2011) · ILAR Journal · doi:10.1093/ilar.52.3.352 · Cited by 18
“Oxidant attack on DA leads to the formation of DA quinone (Graham 1978; Nappi and Vass 2001), a redox-active species that is implicated in Methinduced toxicity (LaVoie and Hastings 1999) and that alters several of the same critical proteins inhibited by Meth, such as TH (Kuhn et al. 1999) and the…”
Autoxidation of catechol(amine)s
Hees, M. T. I. W. S.-V., Henegouwen, G. M. J. B. V., & Stoutenberg, P. (1985) · Pharmacy World & Science · doi:10.1007/bf01959197 · Cited by 16
Iron contributes to dopamine‐induced toxicity in oligodendrocyte progenitors
Hemdan, S., & Almazán, G. (2006) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2006.00757.x · Cited by 16
Differential alterations of NF‐κB to oxidative stress in primary basal forebrain cultures
Gu, Z., Cain, L., Werrbach‐Perez, K., et al. (2000) · International Journal of Developmental Neuroscience · doi:10.1016/s0736-5748(99)00087-8 · Cited by 16
“Due to the high oxygen consumption and high concentration of oxidizable substances such as catecholamines, ascorbic acid, and lipids in brain, imbalances in oxidative homeostasis trigger oxidative stress cascades that result in neuronal damage [2,9].”
BackgroundThe Oxidation of Catecholamines and 6-Hydroxydopamine by Molecular Oxygen: Effect of Ascorbate
Roginsky, V. A., Barsukova, T. K., Bruchelt, G., et al. (1997) · Zeitschrift für Naturforschung C · doi:10.1515/znc-1997-5-617 · Cited by 16
Ohm, T. G., & Braak, H. (1988) · Acta Neuropathologica · doi:10.1007/bf00688239 · Cited by 16
“a waste product of the catecholamine metabolism [1, 21, 22, 37, 45] and can - in the brain of the human adult - be used as a natural marker for catecholaminergic neurons.”
BackgroundTiffany, S. M., Dg, G., Fs, V., et al. (1978) · PubMed · Cited by 16
Aizenman, E., Loring, R. H., Reynolds, I. J., & Rosenberg, P. A. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00778 · Cited by 15
“Importantly, TOPA solutions allowed to oxidize for up to 4 h produced only one major product, with spectrophotometrically distinct profile from all other catecholamine oxidation products, such as dopachrome and dopa quinone (Graham, 1978; Rosenberg et al., 1991).”
BackgroundTherapeutic Effects of Hydrogen in Animal Models of Parkinson's Disease
Fujita, K., Nakabeppu, Y., & Noda, M. (2011) · Parkinson s Disease · doi:10.4061/2011/307875 · Cited by 15
“From dopaminergic neurons, superoxide is produced not only in mitochondria but also by autooxidation of DA [35].”
BackgroundSchmitt, G. C., Arbo, M. D., Lorensi, A. L., Jacques, A. L. B., Nascimento, S., Mariotti, K. D. C., García, S. C., Dallegrave, E., Leal, M. B., & Limberger, R. P. (2016) · Brazilian Journal of Pharmaceutical Sciences · doi:10.1590/s1984-82502016000100007 · Cited by 15
“Since amphetamines cause the release of dopamine, another potential source of these ROS is from the autoxidation of dopamine via the Fenton reaction which uses iron as a cofactor (Graham, 1978).”
BackgroundTryptophan hydroxylase and serotonin synthesis regulation
Kuhn, D. M., & Hasegawa, H. (2020) · Handbook of behavioral neuroscience · doi:10.1016/b978-0-444-64125-0.00012-8 · Cited by 16
L-DOPA oxidation products prevent H2O2-induced oxidative damage to cellular DNA
Shi, Y., Benzie, I. F. F., & Buswell, J. A. (2002) · Life Sciences · doi:10.1016/s0024-3205(02)02172-0 · Cited by 15
Teixeira, A. I., Müller, L. G., Reckziegel, P., Boufleur, N., Pase, C. S., Villarinho, J. G., Fachinetto, R., Ferreira, J., da Rocha, J. B. T., & Bürger, M. E. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.10.017 · Cited by 15
“Furthermore, DA reacts with molecular oxygen to form dopaminequinones which can deplete glutathione, generating ROS during this process (Graham, 1978).”
BackgroundNeuroprotection of Brain Cells by Lipoic Acid Treatment after Cellular Stress
Paradells, S., Benlloch-Navarro, M. S., Frias, M. I. A., García-Esparza, M. A., Broccoli, V., Miranda, M., & Soria, J. M. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00306 · Cited by 15
Jaisin, Y., Ratanachamnong, P., Prachayasittikul, S., et al. (2016) · ScienceAsia · doi:10.2306/scienceasia1513-1874.2016.42.259 · Cited by 15
L-DOPA-induced neurotoxic and apoptotic changes on cultured chromaffin cells
Corona-Morales, A. A., Castell, A., & Zhang, L. (2000) · Neuroreport · doi:10.1097/00001756-200002280-00015 · Cited by 15
Interruption of the MnO2 oxidative process on dopamine and l-dopa by the action of S2O32−
Barreto, W. J., Barreto, S. R. G., Santos, M. A., et al. (2001) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(00)00207-5 · Cited by 15
Lei, B., Adachi, N., Nagaro, T., et al. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00680-x · Cited by 15
de Souza-Pinto, N. C., Vercesi, A. E., & Hoffmann, M. E. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)02179-5 · Cited by 15
Oxidative Stress in Parkinson's Disease
Vaya, J., Aluf, Y., & Finberg, J. P. M. (2010) · Humana Press eBooks · doi:10.1007/978-1-60327-514-9_12 · Cited by 16
Leng, A., Feldon, J., & Ferger, B. (2003) · Synapse · doi:10.1002/syn.10260 · Cited by 15
Cell Culture Models of Neuronal Degeneration and Neuroprotection
Leonardi, E. T. K., & Mytilineou, C. (1998) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-4869-0_12 · Cited by 14
Fast Atom Bombardment Mass Spectrometry in the Study of Dopamine Melanogenesis Intermediates
Allegri, G., Arban, R., Costa, C., et al. (1990) · Pigment Cell Research · doi:10.1111/j.1600-0749.1990.tb00287.x · Cited by 15
Hao, C., March, R. E., Croley, T. R., et al. (2002) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.589 · Cited by 14
Tran, H., Shin, E., Saito, K., Tran, T.-V., Phan, D., Sharma, N., Kim, D. W., Choi, S. Y., Jeong, J. H., Jang, C., et al. (2019) · Food and Chemical Toxicology · doi:10.1016/j.fct.2019.110986 · Cited by 15
Pathology of Neurodegenerative Diseases
Kim, Y. S., Kim, Y.-K., Hwang, O., & Dong, J. (2012) · InTech eBooks · doi:10.5772/38028 · Cited by 16
“The DA quinone species are capable of covalently modifying cellular nucleophiles, including low molecular weight sulfhydryls such as GSH and protein cysteinyl residues (Graham, 1978), whose normal functions are important for cell survival.”
BackgroundProtective effects of baicalein against excess L-DOPA-induced dopamine quinone neurotoxicity
Takeshima, M., Murata, M., Urasoe, N., Murakami, S., Miyazaki, I., Asanuma, M., & Kita, T. (2011) · Neurological Research · doi:10.1179/1743132811y.0000000032 · Cited by 14
Ud‐Daula, A., Pfister, G., & Schramm, K. (2008) · Journal of Environmental Science and Health Part A · doi:10.1080/10934520802329885 · Cited by 14
“There are many investigation reported that due to the unstable nature of catechol ring, it could be spontaneously oxidised and converted into quinone and the reaction is accelerated in presence of manganese or iron ions.[17,22,23] Its degradation occurred in the 96-well plate with PPY medium and Tetrahymena culture se…”
BackgroundZhang, Y., Deng, P., Ruan, Y., et al. (2008) · Stroke · doi:10.1161/strokeaha.107.506824 · Cited by 14
Age Pigments in Different Populations of Peripheral Neurons in Vivo and in Vitro
Koıstınaho, J., Hartikainen, K. M., Hatanpaa, K. J., et al. (1990) · Advances in experimental medicine and biology · doi:10.1007/978-1-4899-5339-1_4 · Cited by 14
Oxidative ring-coupling of tyrosine and its derivatives by purified rat intestinal peroxidase
Valoti, M., Tipton, K. F., & Sgaragli, G. P. (1992) · Biochemical Pharmacology · doi:10.1016/0006-2952(92)90597-c · Cited by 14
Catechol-O-Methyltransferase Decreases Levodopa Toxicity In Vitro
Offen, D., Panet, H., Galili-Mosberg, R., et al. (2001) · Clinical Neuropharmacology · doi:10.1097/00002826-200101000-00006 · Cited by 14
Metodiewa, D., & Dunford, H. B. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19358.x · Cited by 14
MPTP-Induced Parkinsonian Syndromes in Humans and Animals
Kopin, I. J., Burns, S., Chiueh, C. C., et al. (1986) · Advances in behavioral biology · doi:10.1007/978-1-4613-2179-8_59 · Cited by 14
Neurotoxic Phenylalkylamines and Indolealkylamines
Baumgarten, H. G., & Zimmermann, B. A. (1994) · Springer eBooks · doi:10.1007/978-3-642-85117-9_8 · Cited by 14
Yoshioka, Y., Sugino, Y., Yamamuro, A., Ishimaru, Y., & Maeda, S. (2021) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2021.10.004 · Cited by 13
Direct intranigral injection of dopaminochrome causes degeneration of dopamine neurons
Touchette, J. C., Breckenridge, J. M., Wilken, G. H., & Macarthur, H. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.12.028 · Cited by 13
Light modulates Drosophila lifespan via perceptual systems independent of circadian rhythms
Johnson, J. C., Munneke, A. S., Richardson, H. M., Gendron, C. M., & Pletcher, S. D. (2023) · Aging · doi:10.18632/aging.204472 · Cited by 13
“Bright light exposure has been shown to induce neurodegeneration and reduce dopamine levels in the mouse and rat substantia nigra [20, 21] potentially by oxidation and generation of cytotoxic byproducts [22].”
Sabogal-Guáqueta, A. M., Arango, C. A., Cardona‐Gómez, G. P., et al. (2014) · Biomédica · doi:10.7705/biomedica.v34i2.1851 · Cited by 13
Rafiee, M., & Khalafi, L. (2009) · Electrochimica Acta · doi:10.1016/j.electacta.2009.10.071 · Cited by 13
Giovanni, G. D., Chagraoui, A., Puginier, E., Galati, S., & Deurwaerdère, P. D. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.08.014 · Cited by 13
Moy, L. Y., Wang, S.-P., & Sonsalla, P. K. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.110791 · Cited by 13
“Moreover, exogenously applied DA can be toxic in vitro and in vivo (Graham, 1978; Michel and Hefti, 1990; Filloux and Townsend, 1993; McLaughlin et al., 1998a), and results in free and protein-bound cysteinyl DA formation (Hastings et al.”
BackgroundOxidative damage in brains of mice treated with apomorphine and its oxidized derivative
Moreira, J. C. F., Dal‐Pizzol, F., Bonatto, F., et al. (2003) · Brain Research · doi:10.1016/j.brainres.2003.08.051 · Cited by 13
“Increasing evidence suggests that some of the neurotoxic effects of dopamine, apomorphine and other dopamine agonists might be mediated by their quinone and semiquinone oxidation derivatives [3,11,16,28].”
BackgroundFornai, F., Gesi, M., Saviozzi, M., Lenzi, P., Piaggi, S., Ferrucci, M., & Casini, A. (2001) · Journal of Neurocytology · doi:10.1023/a:1011973522055 · Cited by 13
Antioxidant effect of simvastatin throught oxidative imbalance caused by lisdexamfetamine dimesylate
Eger, G. A., Ferreira, V. V., Batista, C. R., Bonde, H., Lima, D. D. D., Wyse, A. T. S., Cruz, J. N. D., Rodrigues, A. F., Magro, D. D. D., & Cruz, J. G. P. D. (2016) · Anais da Academia Brasileira de Ciências · doi:10.1590/0001-3765201620140490 · Cited by 13
“Oxidation of dopamine can produce both superoxide and hydrogen peroxide, which may then form hydroxyl radicals in the presence of certain metals (Graham 1978).”
Marsden, C. D. (1992) · Postgraduate Medical Journal · doi:10.1136/pgmj.68.801.538 · Cited by 13
Lundqvist, G., & Morgenstern, R. (1992) · Biochemical Pharmacology · doi:10.1016/0006-2952(92)90702-k · Cited by 13
Metadata
- Authors
- GRAHAM, D. G.
- Affiliations
- Duke Medical Center (US)
- Corresponding author
- GRAHAM, DOYLE G.
- Venue
- Molecular Pharmacology
- Publisher
- Elsevier BV
- Published
- 1978-07
- Volume
- 14
- Issue
- 4
- Pages
- 633-643
- ISSN
- 0026-895X (ISSN-L)
- OpenAlex
- W2211987820
- Cited by
- 1,126
- References
- 0
- Citations by year
- 2026: 11 · 2025: 12 · 2024: 6 · 2023: 11 · 2022: 13 · 2021: 20 · 2020: 23 · 2019: 26 · 2018: 29 · 2017: 30 · 2016: 26 · 2015: 29 · 2014: 26 · 2013: 26 · 2012: 49
- FWCI
- 1.86
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Molecular Pharmacology (publishedVersion)
- PubMed (publishedVersion)
- PubMed
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › melanin and skin pigmentation
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
- Keywords
- catecholamines, autoxidation, periodate oxidation, 6-hydroxydopamine, dopamine, norepinephrine, epinephrine, aminochrome, adrenochrome, o-quinones, p-quinones, cyclization, tautomerism, neuromelanin
- MeSH terms
- Catecholamines, Dopamine, Epinephrine, Hydroxydopamines, Melanins, Norepinephrine, Oxidation-Reduction, Quinones, Monophenol Monooxygenase
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