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Amyotrophic lateral sclerosis associated disturbance of iron metabolism is blunted by swim training-role of AKT signaling pathway

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Targeting Iron Responsive Elements (IREs) of APP mRNA into Novel Therapeutics to Control the Translation of Amyloid-β Precursor Protein in Alzheimer’s Disease

Khan, M. A. (2024) · Pharmaceuticals · doi:10.3390/ph17121669 · Cited by 11 · see citing works

Tip60/Kat5 may be a novel candidate histone acetyltransferase for the regulation of liver iron localization via acetylation

Baltacı, N. G., Toraman, E., Akyüz, M., Kalın, Ş. N., & Budak, H. (2022) · BioMetals · doi:10.1007/s10534-022-00435-z · Cited by 11 · see citing works

Transferrin receptor-mediated transport at the blood-brain barrier is elevated during early development and maintained across aging and in an Alzheimer’s mouse model

Torres, V. O., Pizzo, M. E., Chan, D., Dugas, J. C., Huynh, D., Joy, D. A., Liang, E., Sarrafha, L., Becerra, I. A., Chau, R., et al. (2025) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x251361997 · Cited by 12 · see citing works

Epigenetic Regulation of Ferroportin in Primary Cultures of the Rat Blood-Brain Barrier

Helgudóttir, S. S., Routhe, L. G., Burkhart, A., Jønsson, K., Pedersen, I. S., Lichota, J., & Moos, T. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01953-y · Cited by 9 · see citing works

Ferroptosis and Alzheimer’s disease: a new insight into neurodegeneration

Quan, Y., Liu, H., Zhang, M., Li, M., He, B., Wang, K., Huang, X., Zhou, S., Han, Z., & Fan, H. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1701767 · Cited by 11 · see citing works

Opioid Modulation of Neuronal Iron and Potential Contributions to NeuroHIV

Nash, B., Irollo, E., Brandimarti, R., & Meucci, O. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0884-5_13 · Cited by 8 · see citing works

H2S regulation of iron homeostasis by IRP1 improves vascular smooth muscle cell functions

Zhu, J., Wang, Y., Rivett, A., & Yang, G. (2023) · Cellular Signalling · doi:10.1016/j.cellsig.2023.110826 · Cited by 8 · see citing works

APPealing for a role in cellular iron efflux

Lahiri, D. K., Maloney, B., & Wang, R. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.l119.009216 · Cited by 8 · see citing works

Iron responsive elements mRNA regulate Alzheimer’s amyloid precursor protein translation through iron sensing

Khan, M. A. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1483913 · Cited by 7 · see citing works

A commentary on studies of brain iron accumulation during ageing

Hackett, M. (2024) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-024-02060-2 · Cited by 3 · see citing works

Ferroptosis: a novel pathogenesis and therapeutic strategies for Parkinson disease: A review

Jiao, D., Yang, Y., Wang, K., & Wang, Y. (2025) · Medicine · doi:10.1097/md.0000000000041218 · Cited by 6 · see citing works

Revisit the E2 Domain of Amyloid Precursor Protein: Ferroxidase, Superoxide and Peroxynitrite Scavenging Activities

Poore, A. T., Zuercher, E. C., Bury, G., Whitesell, C., Nguyen, C. C., Pushkar, Y., & Tian, S. (2023) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.3c01336 · Cited by 4 · see citing works

Vitamin C slows primate aging by targeting iron-driven lipid peroxidation

Pei-long, Y., & Xu, C. (2026) · Cell Metabolism · doi:10.1016/j.cmet.2026.02.011 · Cited by 3 · see citing works

Study of molecular patterns associated with ferroptosis in Parkinson’s disease and its immune signature

Chen, L., Xin, G., He, Y., Tian, Q., Kong, X., Fu, Y., Wang, J., Zhang, H., & Wang, L. (2023) · PLoS ONE · doi:10.1371/journal.pone.0295699 · Cited by 3 · see citing works

Ethyl maltol disrupt iron homeostasis in SH‐SY5Y neuroblastoma cell line

Sun, Y., & Bressler, J. P. (2023) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23504 · Cited by 2 · see citing works

Pharmacological mechanisms and therapeutic prospects of plant metabolites from traditional Chinese medicine in regulating programmed cell death in Alzheimer’s disease

Pan, P., Zhao, T., Zhang, J., Zhou, Y., Zhang, X., Li, Q., & Zhou, Y. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1605214 · Cited by 2 · see citing works

Targeting macro- and micro-nutrient regulation of H2S signaling for the aging brain

Godwin, M., & Hine, C. (2025) · Neurotherapeutics · doi:10.1016/j.neurot.2025.e00638 · Cited by 2 · see citing works

Radionuclide selection influences imaging outcomes in immunoPET with a brain-penetrant anti-Aβ antibodyPreprint

van den Broek, S. L., Bratteby, K., Aguilar, X., Tran, T. A., Syvänen, S., & Sehlin, D. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.31.657140 · Cited by 2 · see citing works

Deacylcynaropicrin from Cyclolepis genistoides attenuates iron-induced oxidative stress and inflammatory signaling in neuron and glial cells

Alza, N. P., Juncos, O. N. B., Cavallaro, V., Pferschy‐Wenzig, E., Pirker, T., Bauer, R., Murray, A. P., & Salvador, G. A. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.120348 · Cited by 1 · see citing works

Decreased metallothionein-3 expression in the human spinal cord is a common feature of amyotrophic lateral sclerosis and multiple sclerosis

Gunn, A. P., Hilton, J. B. W., Mukherjee, S., Liddell, J. R., Mercer, S. W., McLean, C. A., Masters, C. L., Crouch, P. J., & Roberts, B. R. (2026) · Scientific Reports · doi:10.1038/s41598-025-31283-9 · Cited by 1 · see citing works

The Outcome of Therapeutic Trials Using Iron and Iron Chelator in Acute Murine Toxoplasmosis: Histopathological and Immunohistochemical study

Mostafa, E., Abdel-Hameed, B. H., & Yousef, A. (2024) · Afro-Egyptian Journal of Infectious and Endemic Diseases · doi:10.21608/aeji.2024.272563.1360

Transferrin receptor-mediated transport at the blood-brain barrier is elevated during early development but maintained across adult agingPreprint

Torres, V. O., Pizzo, M. E., Chan, D., Dugas, J. C., Huynh, D., Joy, D. A., Liang, E., Sarrafha, L., Becerra, I. A., Chau, R., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.12.623253

Radionuclide Selection Influences Imaging Outcomes in Immuno-PET with a Brain-Penetrating Anti–Amyloid-β Antibody

van den Broek, S. L., Bratteby, K., Aguilar, X., Tran, T. A., Syvänen, S., & Sehlin, D. (2025) · Journal of Nuclear Medicine · doi:10.2967/jnumed.125.271194

Additional file 1 of Age, dose, and binding to TfR on blood cells influence brain delivery of a TfR-transported antibody

Faresjö, R., Sehlin, D., & Syvänen, S. (2024) · Figshare · doi:10.6084/m9.figshare.26588739

Additional file 2 of Age, dose, and binding to TfR on blood cells influence brain delivery of a TfR-transported antibody

Faresjö, R., Sehlin, D., & Syvänen, S. (2024) · Figshare · doi:10.6084/m9.figshare.26588742

Characterising the role of alpha synuclein in Ferroptosis, in the context of Parkinson's Disease

Mahoney‐Sanchez, L. (2022) · doi:10.70675/a7f080d0z9ffaz4e1ez9550z0e29c4958e66

Rôle du métabolisme des acides gras polyinsaturés et du fer dans la vulnérabilité des neurones dopaminergiques à la ferroptose : nouvelles approches pharmacologiques pour la maladie de Parkinson.

Bouchaoui, H. (2024) · doi:10.70675/e68098e9z03c2z494bza798zfc26b3eb872c

Ferroptosis: an emerging key mechanism linking aging, surgical and anesthetic exposure to postoperative cognitive dysfunction

Jiang, D., Zhang, Q., Tong, Y., Lou, K., & Liu, H. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1836516

Plasma α-synuclein and QSM-derived susceptibility in Parkinson’s disease: associations with clinical features

Li, X., Luo, T., & Bai, J. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1740309

Metal Ions and Protein Aggregation: Unraveling Molecular Interactions and Theranostic Prospects in Proteinopathies

Milardi, D., Han, J., Lee, H. J., Ding, F., Miller, Y., Faller, P., Bush, A. I., Crouch, P. J., Finkelstein, D. I., Double, K. L., et al. (2026) · Chemical Reviews · doi:10.1021/acs.chemrev.5c00420

Catechol- O -methyltransferase connects dopamine homeostasis to redox signaling, metal homeostasis, and protein folding in schizophrenia

Tripathi, S. J., Chakraborty, S., Wood, N. B., Hoopes, D., Barker, S., Vázquez‐Rosa, E., An, J., Ma, C., Hou, Y., Sharma, S. M., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2606205123

A putative iron-related evolving framework in Alzheimer's disease: From iron dyshomeostasis and ferro-aging to ferroptosis

Tian, D., Shi, T., Xu, S., Lan, J., Zhao, M., 吴红艳, Yang, J., Wang, Z., & Wang, J. (2026) · Journal of Alzheimer s Disease · doi:10.1177/13872877261501439

P3‐325: Alzheimer's disease β‐amyloid protein precursor is ferroxidase II, a ceruloplasmin‐like iron detoxification enzyme

Duce, J. A., Rogers, J. T., Tsatsanis, A., Moir, R. D., Robb, E. L., Leong, S. L., Harding, S. M., Venti, A., Masters, C. L., Cappai, R., et al. (2008) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2008.05.1894

Amyloidogenic processing of Alzheimer’s disease β-amyloid precursor protein induces cellular iron retention

Tsatsanis, A., Wong, B. X. W., Gunn, A. P., Ayton, S., Bush, A. I., Devos, D., & Duce, J. A. (2020) · Molecular Psychiatry · doi:10.1038/s41380-020-0762-0 · Cited by 87 · see citing works

Age-related changes of brain iron load changes in the frontal cortex in APPswe/PS1ΔE9 transgenic mouse model of Alzheimer's disease

Dong, X., Gao, W., Shao, T.-M., Hong-lin, X., Jiang-tao, B., Jing-yi, Z., & Xi-qing, C. (2014) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2014.11.009 · Cited by 59 · see citing works

P4‐253: EVIDENCE FOR APOE PROTECTING AGAINST BRAIN IRON OVERLOAD

Bush, A. I., Ayton, S., Faux, N. G., Xu, H. J., Finkelstein, D., & Adlard, P. A. (2014) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2014.07.024 · Cited by 1 · see citing works

Overexpression of Alzheimer's Disease Amyloid-β Opposes the Age-dependent Elevations of Brain Copper and Iron

Maynard, C. J., Cappai, R., Volitakis, I., Cherny, R. A., White, A. R., Beyreuther, K. T., Masters, C. L., Bush, A. I., & Li, Q. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204379200 · Cited by 352 · see citing works