The DOI matches its Crossref record.
ALTERATIONS IN THE LEVELS OF IRON, FERRITIN AND OTHER TRACE METALS IN PARKINSON'S DISEASE AND OTHER NEURODEGENERATIVE DISEASES AFFECTING THE BASAL GANGLIA
Abstract
Levels of iron, copper, zinc and manganese were measured by inductively coupled plasma spectroscopy in frozen postmortem brain tissue from patients with Parkinson's disease (PD), progressive supranuclear palsy (PSP), multiple system atrophy with strionigral degeneration (MSA), and Huntington's disease (HD) compared with control subjects. Total iron levels were found to be elevated in the areas of basal ganglia showing pathological change in these disorders. In particular, total iron content was increased in substantia nigra in PD, PSP and MSA, but not in HD. Total iron levels in the striatum (putamen and/or caudate nucleus) were increased in PSP, MSA and HD but not in PD. Total iron levels were decreased in the globus pallidus in PD. There were no consistent alterations of manganese levels in basal ganglia structures in any of the diseases studied. Copper levels were decreased in the substantia nigra in PD, and in the cerebellum in PSP, and were elevated in the putamen and possibly substantia nigra in HD. Zinc levels were only increased in PD, in substantia nigra and in caudate nucleus and lateral putamen. Levels of the iron binding protein ferritin were measured in the same patient groups using a radio-immunoassay technique. Increased iron levels in basal ganglia were generally associated with normal or elevated levels of ferritin immunoreactivity, for example, the substantia nigra in PSP and possibly MSA, and in putamen in MSA. The exception was PD where there was a generalized reduction in brain ferritin immunoreactivity, even in the substantia nigra. An increase in total iron content appears to be a response to neurodegeneration in affected basal ganglia regions in a number of movement disorders. However, only in PD was there an increased total iron level, decreased ferritin content, decreased copper content, and an increased zinc concentration in substantia nigra. These findings suggest an alteration of iron handling in the substantia nigra in PD. Depending on the form in which the excess iron load exists in nigra in PD, it may contribute to the neurodegenerative process.
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
“Increases of iron and a decrease of ferritin in the substantia nigra101,116–119 are indicative of high iron loading of ferritin.120”
From The role of iron in brain ageing and neurodegenerative disorders (2014) · cites this paper as [117]
In the citing paper
“Moreover, low iron concentrations can reduce the neuronal deposits of ferritin, generating a condition in the substantia nigra neurons of patients with Parkinson’s disease.117,119”
From The role of iron in brain ageing and neurodegenerative disorders (2014) · cites this paper as [117]
In the citing paper
“In the temporal cortex and globus pallidus of patients with Parkinson’s disease, a decrease of total iron concentration was detected by inductively coupled plasma mass spectrometry.101,117,130”
From The role of iron in brain ageing and neurodegenerative disorders (2014) · cites this paper as [117]
Citations
Cited by
Sorted by citations
Items 301–400 of 1,000
Gassen, M., & Youdim, M. B. H. (1997) · Pharmacology & Toxicology · doi:10.1111/j.1600-0773.1997.tb00390.x · Cited by 77
Metallobiology of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine neurotoxicity
Hare, D. J., Adlard, P. A., Doble, P. A., & Finkelstein, D. I. (2013) · Metallomics · doi:10.1039/c2mt20164j · Cited by 78
6-Hydroxydopamine: a far from simple neurotoxin
Varešlija, D., Tipton, K. F., Davey, G. P., & McDonald, A. G. (2020) · Journal of Neural Transmission · doi:10.1007/s00702-019-02133-6 · Cited by 80
Transition metal abnormalities in progressive dementias
Akatsu, H., Hori, A., Yamamoto, T., Yoshida, M., Mimuro, M., Hashizume, Y., Tooyama, I., & Yezdimer, E. M. (2011) · BioMetals · doi:10.1007/s10534-011-9504-8 · Cited by 78
Dopamine and Iron Induce Apoptosis in PC12 Cells
Velez‐Pardo, C., Jiménez-Del-Río, M., Verschueren, H., Ebinger, G., & Vauquelin, G. (1997) · Pharmacology & Toxicology · doi:10.1111/j.1600-0773.1997.tb00287.x · Cited by 77
Rajan, M. T., Rao, K. S. J., Mamatha, B. M., Rao, R. V., Shanmugavelu, P., Menon, R. B., & Pavithran, M. V. (1997) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(96)00300-0 · Cited by 77
Targeting the Progression of Parkinsons Disease
George, J., Mok, S., Moses, D., Wilkins, S., Bush, A., Cherny, R., & Finkelstein, D. (2009) · Current Neuropharmacology · doi:10.2174/157015909787602814 · Cited by 77
Hegde, M. L., Hegde, P. M., Holthauzen, L. M. F., Hazra, T. K., Rao, K. S. J., & MITRA, S. P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.126664 · Cited by 76
Memory deficits in adult rats following postnatal iron administration
Schröder, N. (2001) · Behavioural Brain Research · doi:10.1016/s0166-4328(01)00236-4 · Cited by 76
Quantitative susceptibility mapping in atypical Parkinsonisms
Mazzucchi, S., Frosini, D., Costagli, M., Prete, E. D., Donatelli, G., Cecchi, P. C., Migaleddu, G., Bonuccelli, U., Ceravolo, R., & Cosottini, M. (2019) · NeuroImage Clinical · doi:10.1016/j.nicl.2019.101999 · Cited by 78
Comparison of t2 relaxation in blood, brain, and ferritin
Brooks, R. A., Vymazal, J., Baumgarner, C. D., Tran, V., & Bulte, J. W. M. (1995) · Journal of Magnetic Resonance Imaging · doi:10.1002/jmri.1880050414 · Cited by 76
Disentangling in vivo the effects of iron content and atrophy on the ageing human brain
Lorio, S., Lutti, A., Kherif, F., Ruef, A., Dukart, J., Chowdhury, R., Frackowiak, R. S. J., Ashburner, J., Helms, G., Weiskopf, N., et al. (2014) · NeuroImage · doi:10.1016/j.neuroimage.2014.09.044 · Cited by 74
A multicontrast approach for comprehensive imaging of substantia nigra
Langley, J. A., Huddleston, D. E., Chen, X., Sedlacik, J., Zachariah, N., & Hu, X. P. (2015) · NeuroImage · doi:10.1016/j.neuroimage.2015.02.045 · Cited by 76
Iron induced oxidative stress and mitochondrial dysfunction: relevance to Parkinson's disease
Hartley, A., Cooper, J. M., & Schapira, A. H. V. (1993) · Brain Research · doi:10.1016/0006-8993(93)90341-j · Cited by 75
Kawahata, I., & Fukunaga, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113779 · Cited by 71
Bisaglia, M., Tessari, I., Mammi, S., & Bubacco, L. (2009) · NeuroMolecular Medicine · doi:10.1007/s12017-009-8082-1 · Cited by 74
Synaptic Zinc: An Emerging Player in Parkinson’s Disease
Sikora, J., & Ouagazzal, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094724 · Cited by 71
The future of susceptibility contrast for assessment of anatomy and function
Reichenbach, J. R. (2012) · NeuroImage · doi:10.1016/j.neuroimage.2012.01.004 · Cited by 73
Parkinson’s Disease: The Mitochondria-Iron Link
Muñoz, Y., Carrasco, C. M., Campos, J., Aguirre, P., & Núñez, M. T. (2016) · Parkinson s Disease · doi:10.1155/2016/7049108 · Cited by 76
The Relevance of Iron in the Pathogenesis of Multiple System Atrophy: A Viewpoint
Kaindlstorfer, C., Jellinger, K. A., Eschlböck, S., Stefanova, N., Weiß, G., & Wenning, G. K. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170601 · Cited by 72
Brain proteins that mind metals: a neurodegenerative perspective
Brown, D. R. (2009) · Dalton Transactions · doi:10.1039/b822135a · Cited by 72
Manganese oxidation state mediates toxicity in PC12 cells
Reaney, S. H., & Smith, D. R. (2004) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.10.013 · Cited by 72
Copper Efflux from Murine Microvascular Cells Requires Expression of the Menkes Disease Cu-ATPase
Qian, Y., Tiffany‐Castiglioni, E., Welsh, J., & Harris, E. D. (1998) · Journal of Nutrition · doi:10.1093/jn/128.8.1276 · Cited by 72
Measuring the iron content of dopaminergic neurons in substantia nigra with MRI relaxometry
Brammerloh, M., Morawski, M., Friedrich, I., Reinert, T., Lange, C., Pelicon, P., Vavpetič, P., Jankuhn, S., Jäger, C., Alkemade, A., et al. (2021) · NeuroImage · doi:10.1016/j.neuroimage.2021.118255 · Cited by 76
Tosato, M., & Marco, V. D. (2019) · Biomolecules · doi:10.3390/biom9070269 · Cited by 71
Williams, B. B., Li, D. D., Węgrzynowicz, M., Vadodaria, B. K., Anderson, J. G., Kwakye, G. F., Aschner, M., Erikson, K. M., & Bowman, A. B. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06445.x · Cited by 70
Insights into the pathogenesis of multiple system atrophy: focus on glial cytoplasmic inclusions
Kaji, S., Maki, T., Ishimoto, T., Yamakado, H., & Takahashi, R. (2020) · Translational Neurodegeneration · doi:10.1186/s40035-020-0185-5 · Cited by 71
Iron as the concert master in the pathogenic orchestra playing in sporadic Parkinson’s disease
Riederer, P. F., Monoranu, C., Strobel, S., Iordache, T., & Sian‐Hülsmann, J. (2021) · Journal of Neural Transmission · doi:10.1007/s00702-021-02414-z · Cited by 69
Manganese uptake into rat brain during development and aging
Takeda, A., Ishiwatari, S., & Okada, S. (1999) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19990401)56:1 · Cited by 69
Friedrich, I., Reimann, K., Jankuhn, S., Kirilina, E. P., Stieler, J., Sonntag, M., Meijer, J., Weiskopf, N., Reinert, T., Arendt, T., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01145-2 · Cited by 70
Mapping Brain Metals to Evaluate Therapies for Neurodegenerative Disease
Popescu, B. F. G., & Nichol, H. K. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00149.x · Cited by 68
Iron accumulation in the striatum predicts aging-related decline in motor function in rhesus monkeys
Cass, W. A., Grondin, R., Andersen, A. H., Zhang, Z., Hardy, P. A., Hussey-Andersen, L. K., Rayens, W. S., Gerhardt, G. A., & Gash, D. M. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.12.010 · Cited by 67
Divalent metal ions enhance DOPAL-induced oligomerization of alpha-synuclein
Jinsmaa, Y., Sullivan, P., Gross, D., et al. (2014) · Neuroscience Letters · doi:10.1016/j.neulet.2014.03.016 · Cited by 68
Kumar, A., Singh, B. K., Ahmad, I., Shukla, S., Patel, D. K., Srivastava, G., Kumar, V., Pandey, H. P., & Singh, C. (2011) · Brain Research · doi:10.1016/j.brainres.2011.12.028 · Cited by 70
Fox, J. H., Connor, T., Stiles, M. A., Kama, J. A., Lü, Z., Dorsey, K., Liebermann, G., Sapp, E., Cherny, R. A., Banks, M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.199448 · Cited by 72
Oligomeric alpha‐synuclein and its role in neuronal death
Brown, D. R. (2010) · IUBMB Life · doi:10.1002/iub.316 · Cited by 69
Singh, Y. P., Pandey, A., Vishwakarma, S., & Modi, G. P. (2018) · Molecular Diversity · doi:10.1007/s11030-018-9878-4 · Cited by 69
Chege, P. M., & McColl, G. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00089 · Cited by 68
Dexras1, a Small GTPase, Is Required for Glutamate-NMDA Neurotoxicity
Chen, Y., Khan, R. S., Cwanger, A., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.1497-12.2013 · Cited by 67
Martín‐Bastida, A., Lao–Kaim, N. P., Loane, C., Politis, M., Roussakis, A., Valle‐Guzman, N., Kefalopoulou, Z. M., Paul, G., Widner, H., Xing, Y., et al. (2016) · European Journal of Neurology · doi:10.1111/ene.13208 · Cited by 67
Brain iron in the ferrocene-loaded rat: Its chelation and influence on dopamine metabolism
Ward, R. J., Dexter, D. T., Florence, A., Aouad, F., Hider, R. C., Jenner, P. G., & Crichton, R. R. (1995) · Biochemical Pharmacology · doi:10.1016/0006-2952(94)00521-m · Cited by 67
Self-citationNeuroprotection by nitric oxide against hydroxyl radical-induced nigral neurotoxicity
Mohanakumar, K. P., Hanbauer, I., & Chiueh, C. C. (1998) · Journal of Chemical Neuroanatomy · doi:10.1016/s0891-0618(98)00032-5 · Cited by 69
The Role of Conformational Dynamics and Allostery in the Disease Development of Human Ferritin
Kumar, A., Glembo, T. J., & Ozkan, S. B. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.06.060 · Cited by 61
Poujois, A., Mikol, J., & Woimant, F. (2017) · Handbook of clinical neurology · doi:10.1016/b978-0-444-63625-6.00008-2 · Cited by 66
Evidence of Functional Zinc Deficiency in Parkinson's Disease
Forsleff, L., Schauss, A. G., Bier, I. D., & Stuart, S. M. (1999) · The Journal of Alternative and Complementary Medicine · doi:10.1089/acm.1999.5.57 · Cited by 66
Kumar, A., Ahmad, I., Shukla, S., Singh, B. K., Patel, D. K., Pandey, H. P., & Singh, C. (2010) · Free Radical Research · doi:10.3109/10715762.2010.492832 · Cited by 65
Ikeda, K., Nakamura, Y., Kiyozuka, T., Aoyagi, J., Hirayama, T., Nagata, R., Ito, H., Iwamoto, K., Murata, K., Yoshii, Y., et al. (2011) · Neurodegenerative Diseases · doi:10.1159/000323265 · Cited by 66
Parkinson's disease–related increase of ‐weighted hypointensity in substantia nigra pars compacta
Langley, J. A., Huddleston, D. E., Sedlacik, J., Boelmans, K., & Hu, X. P. (2016) · Movement Disorders · doi:10.1002/mds.26883 · Cited by 64
T2*-weighted MRI in diagnosis of multiple system atrophy
von Lewinski, F., Werner, C., Jörn, T., Mohr, A., Sixel‐Döring, F., & Trenkwalder, C. (2007) · Journal of Neurology · doi:10.1007/s00415-006-0496-1 · Cited by 62
Neonatal iron exposure induces oxidative stress in adult Wistar rat
Dal‐Pizzol, F., Klamt, F., da Frota, M. L. C., Andrades, M. É., Caregnato, F. F., Vianna, M. R. M. R., Schröder, N., Quevedo, J., Izquierdo, I., Archer, T., et al. (2001) · Developmental Brain Research · doi:10.1016/s0165-3806(01)00218-8 · Cited by 64
Baksi, S., Tripathi, A. K., & Singh, N. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.06.025 · Cited by 64
Dolichol is the major lipid component of human substantia nigra neuromelanin
Fedorow, H., Pickford, R., Hook, J. M., Double, K. L., Halliday, G. M., Gerlach, M., Riederer, P. F., & Garner, B. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02975.x · Cited by 64
Sources and triggers of oxidative damage in neurodegeneration
Angelova, P. R. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.07.003 · Cited by 67
Iron Deposition in Parkinson’s Disease: A Mini-Review
Zeng, W., Cai, J., Zhang, L., & Peng, Q. (2024) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-024-01459-4 · Cited by 64
Elevated brain iron is independent from atrophy in Huntington's Disease
Dumas, E. M., Versluis, M. J., van den Bogaard, S. J. A., van Osch, M. J. P., Hart, E. P., van Roon‐Mom, W., van Buchem, M. A., WEBB, A. G., van der Grond, J., & Roos, R. A. C. (2012) · NeuroImage · doi:10.1016/j.neuroimage.2012.03.056 · Cited by 62
The R6 lines of transgenic mice: A model for screening new therapies for Huntington's disease
Gil‐Mohapel, J., & Rego, A. C. (2008) · Brain Research Reviews · doi:10.1016/j.brainresrev.2008.12.001 · Cited by 67
Lower serum ceruloplasmin levels correlate with younger age of onset in Parkinson’s disease
Bharucha, K. J., Friedman, J. H., Vincent, A. S., & Ross, E. D. (2008) · Journal of Neurology · doi:10.1007/s00415-009-0063-7 · Cited by 62
Pantothenate Kinase-Associated Neurodegeneration
Hartig, M., Prokisch, H., Meitinger, T., & Klopstock, T. (2012) · Current Drug Targets · doi:10.2174/138945012802002384 · Cited by 63
Nexus between mitochondrial function, iron, copper and glutathione in Parkinson's disease
Liddell, J. R., & White, A. R. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.05.016 · Cited by 64
Zhang, J., Stanton, D. M., Nguyen, X. V., Liu, M., Zhang, Z., Gash, D. M., & Bing, G. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2005.06.049 · Cited by 64
Supported Treadmill Training for Gait and Balance in a Patient With Progressive Supranuclear Palsy
Suteerawattananon, M., MacNeill, B., & Protas, E. J. (2002) · Physical Therapy · doi:10.1093/ptj/82.5.485 · Cited by 63
A brief history of brain iron accumulation in Parkinson disease and related disorders
Foley, P. B., Hare, D. J., & Double, K. L. (2022) · Journal of Neural Transmission · doi:10.1007/s00702-022-02505-5 · Cited by 61
Ban, X.-X., Wan, H., Wan, X.-X., Tan, Y.-T., Hu, X., Ban, H.-X., Chen, X., Huang, K. L., Zhāng, Q., & Xiong, K. (2024) · Current Medical Science · doi:10.1007/s11596-024-2832-z · Cited by 68
Ferroptosis in Parkinson's disease —— The iron-related degenerative disease
Yao, Z., Jiao, Q., Du, X., Jia, F., Chen, X., Yan, C., & Jiang, H. F. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102477 · Cited by 65
Ageing neuroinflammation and neurodegeneration
Ward, R. J. (2015) · Frontiers in Bioscience-Scholar · doi:10.2741/s433 · Cited by 64
Bjørklund, G., Hofer, T., Nurchi, V. M., & Aaseth, J. (2019) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2019.110717 · Cited by 62
Iron elevations in the aging Parkinsonian brain: a consequence of impaired iron homeostasis?
Lee, D. W., & Andersen, J. K. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06470.x · Cited by 63
Metal binding to alpha-synuclein peptides and its contribution to toxicity
Brown, D. R. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.01.103 · Cited by 61
da Silva, V. K., de Freitas, B. S., Dornelles, V. C., Kist, L. W., Bogo, M. R., Silva, M. C., STRECK, E. L., Hallak, J. E. C., Zuardi, A. W., Crippa, J. A. S., et al. (2018) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2018.01.014 · Cited by 65
Phosphorylation-dependent metal binding by α-synuclein peptide fragments
Liu, L. L., & Franz, K. J. (2006) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-006-0181-y · Cited by 61
Recent advances in understanding haemochromatosis: a transition state
Robson, K., Merryweather-Clarke, A. T., Cadet, E., Viprakasit, V., Zaahl, M. G., Pointon, J. J., Weatherall, D. J., & Rochette, J. (2004) · Journal of Medical Genetics · doi:10.1136/jmg.2004.020644 · Cited by 62
Williams, B. B., Kwakye, G. F., Węgrzynowicz, M., Li, D. D., Aschner, M., Erikson, K. M., & Bowman, A. B. (2010) · Toxicological Sciences · doi:10.1093/toxsci/kfq174 · Cited by 60
PPARα controls the intracellular coenzyme A concentration via regulation of PANK1α gene expression
Ramaswamy, G., Karim, M. A., Murti, K. G., & Jackowski, S. (2004) · Journal of Lipid Research · doi:10.1194/jlr.m300279-jlr200 · Cited by 60
Atasoy, H. T., Nuyan, O., Tunç, T., et al. (2004) · PubMed · Cited by 60
He, Y., Thong, P. S. P., Lee, T., Leong, S. K., Shi, C., Wong, P. T. ‐., Yuan, S. Y., & Watt, F. (1996) · Brain Research · doi:10.1016/0006-8993(96)00313-7 · Cited by 61
Bourdenx, M., Nioche, A., Doveró, S., Arotçarena, M.-L., Camus, S. M. J., Porras, G., Thiolat, M.-L., Rougier, N. P., Prigent, A., Aubert, P., et al. (2020) · Science Advances · doi:10.1126/sciadv.aaz9165 · Cited by 64
Evaluation of new iron chelators and their therapeutic potential
Aouad, F., Florence, A., Zhang, Y., Collins, F., Henry, C., Ward, R. J., & Crichton, R. R. (2002) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(02)01040-x · Cited by 58
McNaught, K. S. P., Thull, U., Carrupt, P., et al. (1995) · Biochemical Pharmacology · doi:10.1016/0006-2952(95)02086-1 · Cited by 58
Self-citationImaging Brain Iron and Diffusion Patterns
Rossi, M. E., Ruottinen, H., Saunamäki, T., et al. (2013) · Academic Radiology · doi:10.1016/j.acra.2013.09.018 · Cited by 57
Valiente‐Gabioud, A. A., Monserrat, V. T., Molina-Rubino, L., Binolfi, A., Griesinger, C., & Fernández, C. O. (2012) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2012.06.011 · Cited by 57
Toni, M., Massimino, M. L., Mario, A. D., Angiulli, E., & Spisni, E. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00003 · Cited by 56
Restless Legs Syndrome and Parkinson Disease: A Causal Relationship Between the Two Disorders?
Ferini‐Strambi, L., Carli, G., Casoni, F. M., & Galbiati, A. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2018.00551 · Cited by 57
Long Term Exposure to Manganese in Rural Well Water Has No Neurological Effects
Vieregge, P., Heinzow, B., Korf, G., et al. (1995) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/s0317167100039482 · Cited by 57
Lactoferrin is synthesized by mouse brain tissue and its expression is enhanced after MPTP treatment
Fillebeen, C., Mitchell, V. A., Dexter, D. T., Benaı̈ssa, M., Beauvillain, J., Spik, G., & Pierce, A. (1999) · Molecular Brain Research · doi:10.1016/s0169-328x(99)00221-1 · Cited by 56
Self-citationIntermediates of α-synuclein aggregation: Implications in Parkinson's disease pathogenesis
Gadhe, L. G., Sakunthala, A., Mukherjee, S., Gahlot, N., Bera, R., Sawner, A. S., Kadu, P., & Maji, S. K. (2021) · Biophysical Chemistry · doi:10.1016/j.bpc.2021.106736 · Cited by 56
α-Synuclein as a ferrireductase
Brown, D. R. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130130 · Cited by 57
Metallothioneins and copper metabolism are candidate therapeutic targets in Huntington's disease
Hands, S. L., Mason, R. P., Sajjad, M. U., Giorgini, F., & Wyttenbach, A. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380552 · Cited by 55
Wang, C. Y., Coppo, S., Mehta, B. B., Seiberlich, N., Yu, X., & Griswold, M. A. (2018) · Magnetic Resonance in Medicine · doi:10.1002/mrm.27543 · Cited by 56
Chakraborty, H., Ray, S. N., & Chakrabarti, S. (2001) · Neurochemistry International · doi:10.1016/s0197-0186(00)00117-0 · Cited by 56
Visanji, N. P., Collingwood, J. F., Finnegan, M. E., Tandon, A., House, E. R., & Hazrati, L. (2013) · Journal of Parkinson s Disease · doi:10.3233/jpd-130197 · Cited by 57
Carmona, F., Palacios, Ò., Gálvez, N., Cuesta, R., Atrian, S., Capdevila, M., & Dominguez-Vera, J. M. (2013) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2013.03.034 · Cited by 56
Bocca, B., Forte, G., Petrucci, F., Senofonte, O., Violante, N., & Alimonti, A. (2005) · PubMed · Cited by 54
Cukierman, D. S., Pinheiro, A. B., Filho, S. L. P. C., da Silva, A. S. P., Miotto, M., Falco, A. D., Ribeiro, T. D. P., Maisonnette, S. S., da Cunha, A. L. M. C., Hauser‐Davis, R. A., et al. (2017) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2017.02.020 · Cited by 57
Guan, X., Zhang, Y., Wei, H., Guo, T., Zeng, Q., Zhou, C., Wang, J., Gao, T., Xuan, M., Gu, Q., et al. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.11.013 · Cited by 56
Reversion of age-related recognition memory impairment by iron chelation in rats
de Lima, M. N. M., Dias, C. P., Torres, J. P., Dornelles, A. D. S., Garcia, V. A., Scalco, F. S., Guimarães, M. R., Petry, R. C., Bromberg, E., Constantino, L. D. S., et al. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.02.006 · Cited by 55
Singh, C., Ahmad, I., & Kumar, A. (2007) · PubMed · Cited by 54
Torres-Vega, A., Pliego‐Rivero, B., Otero, G., Gómez‐Oliván, L. M., & Vieyra-Reyes, P. (2012) · Nutrition Reviews · doi:10.1111/j.1753-4887.2012.00521.x · Cited by 55
Serum levels of zinc and copper in patients with Parkinson's disease
Jiménez‐Jiménez, F. J., Fernández–Calle, P., Martı́nez, M., Herrero, E., Molina, J. A., Vázquez, A., & Codoceo, R. (1992) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(92)90127-7 · Cited by 54
Pharmacology of Lazaroids and Brain Energy Metabolism: A Review
Villa, R. F., & Gorini, A. (1997) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01314-0 · Cited by 54
Paraquat induced activation of transcription factor AP-1 and apoptosis in PC12 cells
Li, X., & Sun, A. Y. (1999) · Journal of Neural Transmission · doi:10.1007/s007020050137 · Cited by 54
Metadata
- Authors
- DEXTER, D. T., CARAYON, A., JAVOY-AGID, F., AGID, Y., WELLS, F. R., DANIEL, S. E., LEES, A. J., JENNER, P., & MARSDEN, C. D.
- Affiliations
- King's College London (GB)
- Inserm (FR)
- Parkinson's UK (GB)
- Corresponding author
- JENNER, P.
- Venue
- Brain
- Publisher
- Oxford University Press (OUP)
- Published
- 1991
- Volume
- 114
- Issue
- 4
- Pages
- 1953-1975
- ISSN
- 0006-8950 (ISSN-L)
- 1460-2156
- OpenAlex
- W2123913108
- Cited by
- 1,043
- References
- 0
- Citations by year
- 2026: 18 · 2025: 29 · 2024: 47 · 2023: 28 · 2022: 37 · 2021: 43 · 2020: 36 · 2019: 38 · 2018: 30 · 2017: 45 · 2016: 56 · 2015: 45 · 2014: 41 · 2013: 44 · 2012: 32
- FWCI
- 12.57
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Brain (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Royal Society
- Topics
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Keywords
- Parkinson's disease, progressive supranuclear palsy, multiple system atrophy, Huntington's disease, basal ganglia, iron, ferritin, copper, zinc, manganese, substantia nigra, striatum, globus pallidus, neurodegeneration, trace metals, iron overload
- MeSH terms
- Aging, Atrophy, Basal Ganglia Diseases, Brain, Brain Diseases, Ferritins, Humans, Huntington Disease, Iron, Metals, Parkinson Disease, Radioimmunoassay, Reference Values, Supranuclear Palsy, Progressive, Trace Elements
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