Selective accumulation of aluminum and iron in the neurofibrillary tangles of Alzheimer's disease: A laser microprobe (LAMMA) study

Clinical diagnosis of Alzheimer's disease: Report of the NINCDS‐ADRDA Work Group* under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease

McKhann, G., Drachman, D., Folstein, M., Katzman, R., Price, D., & Stadlan, E. M. (1984) · Neurology · doi:10.1212/wnl.34.7.939 · Cited by 27,915 · see citing works

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.

Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676 · see citing works

Diagnosis of Alzheimer's Disease

Khachaturian, Z. S. (1985) · Archives of Neurology · doi:10.1001/archneur.1985.04060100083029 · Cited by 2,499 · see citing works

A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau

Lee, V. M.-Y., Balin, B. J., Otvos, L., & Trojanowski, J. Q. (1991) · Science · doi:10.1126/science.1899488 · Cited by 1,418 · see citing works

Paired Helical Filaments in Electron Microscopy of Alzheimer's Disease

KIDD, M. (1963) · Nature · doi:10.1038/197192b0 · Cited by 1,012 · see citing works

Alzheimer's Disease: X-Ray Spectrometric Evidence of Aluminum Accumulation in Neurofibrillary Tangle-Bearing Neurons

Perl, D. P., & Brody, A. R. (1980) · Science · doi:10.1126/science.7367858 · Cited by 985 · see citing works

Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.

Wischik, C. M., Novak, M., Thøgersen, H. C., Edwards, P. C., Runswick, M. J., Jakes, R., Walker, J. E., Milstein, C., Roth, M., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.12.4506 · Cited by 939 · see citing works

Brain Aluminum Distribution in Alzheimer's Disease and Experimental Neurofibrillary Degeneration

Crapper, D. R., Krishnan, S., & Dalton, A. J. (1973) · Science · doi:10.1126/science.180.4085.511 · Cited by 843 · see citing works

Intramuscular desferrioxamine in patients with Alzheimer's disease

MCLACHLAN, D. (1991) · The Lancet · doi:10.1016/0140-6736(91)92978-b · Cited by 764 · see citing works

EXPERIMENTAL PRODUCTION OF NEUROFIBRILLARY DEGENERATION

KLATZO, I., Wı́sniewski, H. M., & STREICHER, E. (1965) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-196504000-00002 · Cited by 609 · see citing works

The chemistry of aluminum as related to biology and medicine.

Martin, R. B. (1986) · Clinical Chemistry · doi:10.1093/clinchem/32.10.1797 · Cited by 608 · see citing works

Tau Consists of a Set of Proteins with Repeated C-Terminal Microtubule-Binding Domains and Variable N-Terminal Domains

Himmler, A., Drechsel, D. N., Kirschner, M. W., & Martin, D. W. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.4.1381-1388.1989 · Cited by 535 · see citing works

ALUMINIUM, NEUROFIBRILLARY DEGENERATION AND ALZHEIMER'S DISEASE

Crapper, D. R., Krishnan, S., & Quittkat, S. (1976) · Brain · doi:10.1093/brain/99.1.67 · Cited by 451 · see citing works

Neurofibrillary tangles of paired helical filaments

Wı́sniewski, H. M., Narang, H. K., & Terry, R. D. (1976) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(76)90059-9 · Cited by 370 · see citing works

EXPERIMENTAL PRODUCTION OF NEUROFIBRILLARY DEGENERATION

Terry, R. D., & Peña, C. (1965) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-196504000-00003 · Cited by 332 · see citing works

Structure of the Bovine Tau Gene: Alternatively Spliced Transcripts Generate a Protein Family

Himmler, A. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.4.1389 · Cited by 319 · see citing works

Brain aluminum in aging and Alzheimer disease

MCDERMOTT, J. R., Smith, A. I., Iqbal, K., & Wı́sniewski, H. M. (1979) · Neurology · doi:10.1212/wnl.29.6.809 · Cited by 263 · see citing works

Aluminum access to the brain: a role for transferrin and its receptor.

Roskams, A. J., & Connor, J. R. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.22.9024 · Cited by 230 · see citing works

Common and distinct tubulin binding sites for microtubule-associated proteins.

Littauer, U. Z., Giveon, D., Thierauf, M., Ginzburg, I., & Ponstingl, H. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.19.7162 · Cited by 217 · see citing works

Promotion of Tubulin Assembly by Aluminum Ion in Vitro

Macdonald, T. L., Humphreys, W. G., & Martin, R. B. (1987) · Science · doi:10.1126/science.3105058 · Cited by 177 · see citing works

Instrumental neutron activation analysis of brain aluminum in Alzheimer disease and aging

Markesbery, W. R., Ehmann, W. D., Hossain, T. I. M., Alauddin, M., & Goodin, D. T. (1981) · Annals of Neurology · doi:10.1002/ana.410100604 · Cited by 173 · see citing works

Aluminum levels in brain in Alzheimer's disease.

Trapp, G. A., Miner, G. D., Zimmerman, R. L., Mastri, A. R., & Heston, L. L. (1978) · PubMed · Cited by 120 · see citing works

The Repeat Region of Microtubule-Associated Protein Tau Forms Part of the Core of the Paired Helical Filament of Alzheimer's Disease

Crowther, T., Goedert, M., & Wischik, C. M. (1989) · Annals of Medicine · doi:10.3109/07853898909149199 · Cited by 100 · see citing works

Recent Developments in Mass Spectrometry in Biochemistry and Medicine

(1979) · Springer eBooks · doi:10.1007/978-1-4613-3018-9 · Cited by 88 · see citing works

The competitive equilibrium between aluminium and ferric ions for the binding sites of transferrin

Cochran, M., Coates, J. H., & Neoh, S. H. (1984) · FEBS Letters · doi:10.1016/0014-5793(84)80926-6 · Cited by 69 · see citing works

Laser Microprobe Mass Analyzer (LAMMA) — A New Approach to the Study of the Association of Aluminum and Neurofibrillary Tangle Formation

Perl, D. P., Muñoz, D. G., Good, P., et al. (1986) · Advances in behavioral biology · doi:10.1007/978-1-4613-2179-8_30 · Cited by 21 · see citing works

Reactive Oxygen Species and the Central Nervous System

Halliwell, B. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb10990.x · Cited by 2,947 · see citing works

Oxidative stress hypothesis in Alzheimer’s disease

Markesbery, W. R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00629-6 · Cited by 2,383 · see citing works

Copper, iron and zinc in Alzheimer's disease senile plaques

Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120 · see citing works

Human Health Risk Assessment for Aluminium, Aluminium Oxide, and Aluminium Hydroxide

Krewski, D., Yokel, R. A., Nieboer, E., Borchelt, D., Cohen, J., Harry, J., Kacew, S., Lindsay, J., Mahfouz, A. M., & Rondeau, V. (2007) · Journal of Toxicology and Environmental Health, Part B · doi:10.1080/10937400701597766 · Cited by 998 · see citing works

Oxidative stress in Alzheimer’s disease

Smith, M. A., Rottkamp, C. A., Nunomura, A., Raina, A. K., & Perry, G. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00040-5 · Cited by 895 · see citing works

Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease

Markesbery, W. R., & Lovell, M. A. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00009-8 · Cited by 680 · see citing works

Neuroprotection by the Metabolic Antioxidant α-Lipoic Acid

Packer, L., Tritschler, H. J., & Wessel, K. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00269-9 · Cited by 639 · see citing works

Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases

Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · see citing works

Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer’s disease: possible relation to oxidative stress.

Deibel, M. A., Ehmann, W. D., & Markesbery, W. R. (1996) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(96)00203-1 · Cited by 540 · see citing works

An Assessment of Oxidative Damage to Proteins, Lipids, and DNA in Brain from Patients with Alzheimer's Disease

Lyras, L., Cairns, N. J., Jenner, A., Jenner, P., & Halliwell, B. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68052061.x · Cited by 531 · see citing works

Neuromelanin-containing neurons of the substantia nigra accumulate iron and aluminum in Parkinson's disease: a LAMMA study

Good, P. F., Olanow, C. W., & Perl, D. P. (1992) · Brain Research · doi:10.1016/0006-8993(92)91334-b · Cited by 427 · see citing works

Iron Toxicity in Diseases of Aging: Alzheimer's Disease, Parkinson's Disease and Atherosclerosis

Altamura, S., & Muckenthaler, M. U. (2009) · Journal of Alzheimer's Disease · doi:10.3233/jad-2009-1010 · Cited by 369 · see citing works

The role of oxidative stress in the toxicity induced by amyloid β-peptide in Alzheimer’s disease

Miranda, S., Opazo, C., Larrondo, L. F., Muñoz, F. J., Ruiz, F., Leighton, F., & Inestrosa, N. C. (2000) · Progress in Neurobiology · doi:10.1016/s0301-0082(00)00015-0 · Cited by 369 · see citing works

Towards a unifying, systems biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson’s, Huntington’s, Alzheimer’s, prions, bactericides, chemical toxicology and others as examples

Kell, D. B. (2010) · Archives of Toxicology · doi:10.1007/s00204-010-0577-x · Cited by 361 · see citing works

Overview of quantitative susceptibility mapping

Deistung, A., Schweser, F., & Reichenbach, J. R. (2017) · NMR in Biomedicine · doi:10.1002/nbm.3569 · Cited by 338 · see citing works

Medicinal Inorganic Chemistry Approaches to Passivation and Removal of Aberrant Metal Ions in Disease

Scott, L. E., & Orvig, C. (2009) · Chemical Reviews · doi:10.1021/cr9000176 · Cited by 332 · see citing works

A Novel Glycosylphosphatidylinositol-anchored Form of Ceruloplasmin Is Expressed by Mammalian Astrocytes

Patel, B. N., & David, S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.32.20185 · Cited by 327 · see citing works

Iron-melanin complex in substantia nigra of parkinsonian brains: an x-ray microanalysis

Jellinger, K., Kienzl, E., Rumpelmair, G., Riederer, P., Stachelberger, H., Ben‐Shachar, D., & Youdim, M. B. H. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb08362.x · Cited by 313 · see citing works

Iron (III) induces aggregation of hyperphosphorylated τ and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease

Yamamoto, A., Shin, R., Hasegawa, K., Naiki, H., Sato, H., Yoshimasu, F., & Kitamoto, T. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.t01-1-01061.x · Cited by 313 · see citing works

Increased Iron Levels and Decreased Tissue Integrity in Hippocampus of Alzheimer’s Disease Detected in vivo with Magnetic Resonance Imaging

Raven, E. P., Lu, P. H., Tishler, T. A., Heydari, P., & Bartzokis, G. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130209 · Cited by 270 · see citing works

Iron and neurodegenerative disorders

Thompson, K. J., Shoham, S., & Connor, J. R. (2001) · Brain Research Bulletin · doi:10.1016/s0361-9230(01)00510-x · Cited by 235 · see citing works

Metal ions, Alzheimer's disease and chelation therapy

Budimir, A. (2011) · Acta Pharmaceutica · doi:10.2478/v10007-011-0006-6 · Cited by 202 · see citing works

Cerebrospinal fluid levels of transition metals in patients with Alzheimer's disease

Molina, J. A., Jiménez-Jiménez, F. J., Aguilar, M. V., Meseguer, I., Mateos-Vega, C. J., González-Muñoz, M. J., de Bustos, F., Porta, J., Ortí-Pareja, M., Zurdo, M., et al. (1998) · Journal of Neural Transmission · doi:10.1007/s007020050071 · Cited by 167 · see citing works

Iron dysregulation in Alzheimer's disease: Multimodal brain permeable iron chelating drugs, possessing neuroprotective-neurorescue and amyloid precursor protein-processing regulatory activities as therapeutic agents

Mandel, S., Amit, T., Bar-Am, O., & Youdim, M. B. H. (2007) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2007.06.001 · Cited by 164 · see citing works

Abnormal localization of iron regulatory protein in Alzheimer’s disease

Smith, M. A., Wehr, K., Harris, P. L. R., Siedlak, S. L., Connor, J. R., & Perry, G. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00002-x · Cited by 162 · see citing works

Targeting multiple Alzheimer's disease etiologies with multimodal neuroprotective and neurorestorative iron chelators

Amit, T., Avramovich‐Tirosh, Y., Youdim, M. B. H., & Mandel, S. (2008) · The FASEB Journal · doi:10.1096/fj.07-8627rev · Cited by 126 · see citing works

Role of brain iron accumulation in cognitive dysfunction: evidence from animal models and human studies

Schröder, N., Figueiredo, L. S., & de Lima, M. N. M. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-121996 · Cited by 113 · see citing works

PICALM and Alzheimer’s Disease: An Update and Perspectives

Ando, K., Nagaraj, S., Küçükali, F., de Fisenne, M.-A., Kosa, A.-C., Doeraene, E., Lopez Gutierrez, L., Brion, J.-P., & Leroy, K. (2022) · Cells · doi:10.3390/cells11243994 · Cited by 104 · see citing works

Cannabidiol normalizes caspase 3, synaptophysin, and mitochondrial fission protein DNM1L expression levels in rats with brain iron overload: implications for neuroprotection

da Silva, V. K., de Freitas, B. S., da Silva Dornelles, A., Nery, L. R., Falavigna, L., Ferreira, R. D. P., Bogo, M. R., Hallak, J. E. C., Zuardi, A. W., Crippa, J. A. S., et al. (2014) · Molecular Neurobiology · doi:10.1007/s12035-013-8514-7 · Cited by 91 · see citing works

Iron Pathophysiology in Alzheimer’s Diseases

Wang, T., Xu, S.-F., Fan, Y.-G., Li, L.-B., & Guo, C. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-9589-5_5 · Cited by 64 · see citing works

Phosphorylated tau fluid biomarker sites recognize earlier neurofibrillary tangle maturity levels in the postmortem Alzheimer’s disease brain

(2021) · doi:10.1101/2021.08.25.457363 · Cited by 3 · see citing works

Tangle-bearing neurons show more extensive dendritic trees than tangle-free neurons in area CA1 of the hippocampus in Alzheimer's disease

Gertz, H., Krüger, H., Patt, S., & Cervós‐Navarro, J. (1991) · Brain Research · doi:10.1016/0006-8993(91)91130-s · Cited by 20 · see citing works

Distribution of neurofibrillary tangle formation and [3H]-D-aspartate receptor binding in the thalamus in the normal elderly brain, in Alzheimer's disease and in Parkinson's disease

Xuereb, J. H., Candy, J., Perry, E. K., Perry, R. H., MARSHALL, E., & Bonham, J. R. (1990) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.1990.tb01287.x · Cited by 9 · see citing works

Neurons bearing neurofibrillary tangles are responsible for selected synaptic deficits in Alzheimer's disease

Callahan, L. M., & Coleman, P. D. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00035-d · Cited by 77 · see citing works

Relationship between microtubule-binding repeats and morphology of neurofibrillary tangle in Alzheimer's disease

Kitamura, T., Sugimori, K., Sudo, S., & Kobayashi, K. (2005) · Acta Neurologica Scandinavica · doi:10.1111/j.1600-0404.2005.00488.x · Cited by 14 · see citing works