[1] E. Nichols, J.D. Steinmetz, S.E. Vollset, K. Fukutaki, J. Chalek, F. Abd-Allah, A. Abdoli, A. Abualhasan, E. Abu-Gharbieh, T.T. Akram. Estimation of the global prevalence of dementia in 2019 and forecasted prevalence in 2050: an analysis for the Global Burden of Disease Study 2019. The Lancet Public Health 7 (2022) e105-e125. https://doi.org/10.1016/S2468-2667(21)00249-8 DOI: https://doi.org/10.1002/alz.051496

[2] E.R. Dorsey, A. Elbaz, E. Nichols, N. Abbasi, F. Abd-Allah, A. Abdelalim, J.C. Adsuar, M.G. Ansha, C. Brayne, J.-Y.J. Choi. Global, regional, and national burden of Parkinson's disease, 1990–2016: a systematic analysis for the Global Burden of Disease Study 2016. The Lancet Neurology 17 (2018) 939-953. https://doi.org/10.1016/S1474-4422(18)30295-3 DOI: https://doi.org/10.1016/S1474-4422(18)30295-3

[3] World Health Organization. Global status report on the public health response to dementia. World Health Organization, Geneva, Switzerland, 2021. https://www.who.int/publications/i/item/9789240033245 (Accessed February 15, 2026).

[4] W. Yang, J.L. Hamilton, C. Kopil, J.C. Beck, C.M. Tanner, R.L. Albin, E. Ray Dorsey, N. Dahodwala, I. Cintina, P. Hogan. Current and projected future economic burden of Parkinson’s disease in the US. npj Parkinson's Disease 6 (2020) 15. https://doi.org/10.1038/s41531-020-0117-1 DOI: https://doi.org/10.1038/s41531-020-0117-1

[5] M. Edwards, R. Corkill. Disease-modifying treatments in Alzheimer’s disease. Journal of Neurology 270 (2023) 2342-2344. https://doi.org/10.1007/s00415-023-11602-8 DOI: https://doi.org/10.1007/s00415-023-11602-8

[6] A. Lenka, J. Jankovic. How should future clinical trials be designed in the search for disease-modifying therapies for Parkinson’s disease? Expert Review of Neurotherapeutics 23 (2023) 107-122. https://doi.org/10.1080/14737175.2023.2177535 DOI: https://doi.org/10.1080/14737175.2023.2177535

[7] M.A. Wheeler, C.J. Smith, M. Ottolini, B.S. Barker, A.M. Purohit, R.M. Grippo, R.P. Gaykema, A.J. Spano, M.P. Beenhakker, S. Kucenas. Genetically targeted magnetic control of the nervous system. Nature Neuroscience 19 (2016) 756-761. https://doi.org/10.1038/nn.4265 DOI: https://doi.org/10.1038/nn.4265

[8] X. Long, J. Ye, D. Zhao, S.-J. Zhang. Magnetogenetics: remote non-invasive magnetic activation of neuronal activity with a magnetoreceptor. Science Bulletin 60 (2015) 2107-2119. https://doi.org/10.1007/s11434-015-0902-0 DOI: https://doi.org/10.1007/s11434-015-0902-0

[9] S. Safiri, A. Ghaffari Jolfayi, A. Fazlollahi, S. Morsali, A. Sarkesh, A. Daei Sorkhabi, B. Golabi, R. Aletaha, K. Motlagh Asghari, S. Hamidi. Alzheimer's disease: a comprehensive review of epidemiology, risk factors, symptoms diagnosis, management, caregiving, advanced treatments and associated challenges. Frontiers in Medicine 11 (2024) 1474043. https://doi.org/10.3389/fmed.2024.1474043 DOI: https://doi.org/10.3389/fmed.2024.1474043

[10] Q. Zheng, X. Wang. Alzheimer’s disease: insights into pathology, molecular mechanisms, and therapy. Protein & Cell 16 (2025) 83-120. https://doi.org/10.1093/procel/pwae026 DOI: https://doi.org/10.1093/procel/pwae026

[11] J.M. Long, D.M. Holtzman. Alzheimer disease: an update on pathobiology and treatment strategies. Cell 179 (2019) 312-339. https://doi.org/10.1016/j.cell.2019.09.001 DOI: https://doi.org/10.1016/j.cell.2019.09.001

[12] M.A. DeTure, D.W. Dickson. The neuropathological diagnosis of Alzheimer’s disease. Molecular Neurodegeneration 14 (2019) 32. https://doi.org/10.1186/s13024-019-0333-5 DOI: https://doi.org/10.1186/s13024-019-0333-5

[13] U.C. Müller, T. Deller, M. Korte. Not just amyloid: physiological functions of the amyloid precursor protein family. Nature Reviews Neuroscience 18 (2017) 281-298. https://doi.org/10.1038/nrn.2017.29 DOI: https://doi.org/10.1038/nrn.2017.29

[14] R.J. O'brien, P.C. Wong. Amyloid precursor protein processing and Alzheimer's disease. Annual Review of Neuroscience 34 (2011) 185-204. https://doi.org/10.1146/annurev-neuro-061010-113613 DOI: https://doi.org/10.1146/annurev-neuro-061010-113613

[15] D.D.-L. Chau, L.L.-H. Ng, Y. Zhai, K.-F. Lau. Amyloid precursor protein and its interacting proteins in neurodevelopment. Biochemical Society Transactions 51 (2023) 1647-1659. https://doi.org/10.1042/BST20221527 DOI: https://doi.org/10.1042/BST20221527

[16] M. Chen. The maze of APP processing in Alzheimer’s disease: where did we go wrong in reasoning? Frontiers in Cellular Neuroscience 9 (2015) 186. https://doi.org/10.3389/fncel.2015.00186 DOI: https://doi.org/10.3389/fncel.2015.00186

[17] A. Peric, W. Annaert. Early etiology of Alzheimer’s disease: tipping the balance toward autophagy or endosomal dysfunction? Acta Neuropathologica 129 (2015) 363-381. https://doi.org/10.1007/s00401-014-1379-7 DOI: https://doi.org/10.1007/s00401-014-1379-7

[18] U.C. Müller, H. Zheng. Physiological functions of APP family proteins. Cold Spring Harbor Perspectives in Medicine 2 (2012) a006288. https://doi.org/10.1101/cshperspect.a006288 DOI: https://doi.org/10.1101/cshperspect.a006288

[19] H. Zhang, Q. Ma, Y.w. Zhang, H. Xu. Proteolytic processing of Alzheimer’s β‐amyloid precursor protein. Journal of Neurochemistry 120 (2012) 9-21. https://doi.org/10.1111/j.1471-4159.2011.07519.x DOI: https://doi.org/10.1111/j.1471-4159.2011.07519.x

[20] R. Harrison, P. Sharpe, Y. Singh, D. Fairlie. Amyloid peptides and proteins in review. Reviews of Physiology, Biochemistry and Pharmacology 159 (2007) 1-77. https://doi.org/10.1007/112_2007_0701 DOI: https://doi.org/10.1007/112_2007_0701

[21] Y.J. Chang, Y.R. Chen. The coexistence of an equal amount of Alzheimer's amyloid‐β 40 and 42 forms structurally stable and toxic oligomers through a distinct pathway. The FEBS Journal 281 (2014) 2674-2687. https://doi.org/10.1111/febs.12813 DOI: https://doi.org/10.1111/febs.12813

[22] L.A. Rukmangadachar, P.C. Bollu. Amyloid beta peptide, In StatPearls, StatPearls Publishing, Treasure Island (FL). 2026. https://europepmc.org/article/NBK/nbk459119

[23] Y. Xiao, M. Zhang, N. Lu. Fluorescent Fingerprint Identification of Protein Structural Changes and Disease-Specific Amyloid Beta Aggregates Based on a Single-Nanozyme Sensor Array. Analytical Chemistry 97 (2025) 4978-4986. https://doi.org/10.1021/acs.analchem.4c05508 DOI: https://doi.org/10.1021/acs.analchem.4c05508

[24] S. Bagheri, L. Saso. Biophysical insights into the molecular mechanisms of beta amyloid aggregation and its toxic effects in Alzheimer's disease. Frontiers in Molecular Biosciences 12 (2025) 1704653. https://doi.org/10.3389/fmolb.2025.1704653 DOI: https://doi.org/10.3389/fmolb.2025.1704653

[25] W. Puławski, A. Koliński, M. Koliński. Multiscale modeling of protofilament structures: A case study on insulin amyloid aggregates. International Journal of Biological Macromolecules 285 (2025) 138382. https://doi.org/10.1016/j.ijbiomac.2024.138382 DOI: https://doi.org/10.1016/j.ijbiomac.2024.138382

[26] K. Khodayari, M. Alipour, I. Rad, H. Ramshini, P. Abdolmaleki. Inhibition potential evaluation of two synthetic bis-indole compounds on amyloid fibrillation: A molecular simulation study. Journal of Biomolecular Structure and Dynamics 40 (2022) 4051-4061. https://doi.org/10.1080/07391102.2020.1852962 DOI: https://doi.org/10.1080/07391102.2020.1852962

[27] K.B. Varshavskaya, I.Y. Petrushanko, V.A. Mitkevich, E.P. Barykin, A.A. Makarov. Post-translational modifications of beta-amyloid alter its transport in the blood-brain barrier in vitro model. Frontiers in Molecular Neuroscience 17 (2024) 1362581. https://doi.org/10.20944/preprints202312.1326.v1 DOI: https://doi.org/10.3389/fnmol.2024.1362581

[28] H. Hampel, J. Hardy, K. Blennow, C. Chen, G. Perry, S.H. Kim, V.L. Villemagne, P. Aisen, M. Vendruscolo, T. Iwatsubo. The amyloid-β pathway in Alzheimer’s disease. Molecular Psychiatry 26 (2021) 5481-5503. https://doi.org/10.1038/s41380-021-01249-0 DOI: https://doi.org/10.1038/s41380-021-01249-0

[29] M. Tolar, J. Hey, A. Power, S. Abushakra. Neurotoxic soluble amyloid oligomers drive Alzheimer’s pathogenesis and represent a clinically validated target for slowing disease progression. International Journal of Molecular Sciences 22 (2021) 6355. https://doi.org/10.3390/ijms22126355 DOI: https://doi.org/10.3390/ijms22126355

[30] M.S. Rafii, Z. Schlachetzki, I. Barroeta, E. Head, J. Fortea, B.M. Ances. Down syndrome and Alzheimer's disease: insights into biomarkers, clinical symptoms, and pathology. The Lancet Neurology 24 (2025) 753-762. https://doi.org/10.1016/s1474-4422(25)00237-6 DOI: https://doi.org/10.1016/S1474-4422(25)00237-6

[31] H. Zetterberg, K. Blennow. Moving fluid biomarkers for Alzheimer’s disease from research tools to routine clinical diagnostics. Molecular Neurodegeneration 16 (2021) 10. https://doi.org/10.1186/s13024-021-00430-x DOI: https://doi.org/10.1186/s13024-021-00430-x

[32] A. Azargoonjahromi, H. Nasiri, A.s.D.N. Initiative. CSF Amyloid-β42 associates with neuropsychiatric and cognitive outcomes via cerebral glucose metabolism. Molecular Brain 18 (2025) 55. https://doi.org/10.1186/s13041-025-01229-3 DOI: https://doi.org/10.1186/s13041-025-01229-3

[33] S.K. Saxena, S. Ansari, V.K. Maurya, S. Kumar, D. Sharma, H.S. Malhotra, S. Tiwari, C. Srivastava, J.T. Paweska, A.S. Abdel-Moneim. Neprilysin-mediated amyloid beta clearance and its therapeutic implications in neurodegenerative disorders. ACS Pharmacology & Translational Science 7 (2024) 3645-3657. https://doi.org/10.1021/acsptsci.4c00400 DOI: https://doi.org/10.1021/acsptsci.4c00400

[34] J. Chen, P. Xiang, A. Duro-Castano, H. Cai, B. Guo, X. Liu, Y. Yu, S. Lui, K. Luo, B. Ke. Rapid amyloid-β cle¬arance and cognitive recovery through multivalent modulation of blood–brain barrier transport. Signal Transduction and Targeted Therapy 10 (2025) 331. https://doi.org/10.1038/s41392-025-02426-1 DOI: https://doi.org/10.1038/s41392-025-02426-1

[35] L. Huang, M. Liu, Z. Li, B. Li, J. Wang, K. Zhang. Systematic review of amyloid-beta clearance proteins from the brain to the periphery: implications for Alzheimer’s disease diagnosis and therapeutic targets. Neural Regeneration Research 20 (2025) 3574-3590. https://doi.org/10.4103/nrr.nrr-d-24-00865 DOI: https://doi.org/10.4103/NRR.NRR-D-24-00865

[36] M.G. Iadanza, M.P. Jackson, E.W. Hewitt, N.A. Ranson, S.E. Radford. A new era for understanding amyloid structures and disease. Nature Reviews Molecular Cell Biology 19 (2018) 755-773. https://doi.org/10.1038/s41580-018-0060-8 DOI: https://doi.org/10.1038/s41580-018-0060-8

[37] I.A. Pereira, N.S. Rosa, R.R.N.R.d. Nascimento, E.A.M. Freire, F.d.S. Neves, B.E.R.G. Bica, F.A.G. Pinheiro, S.F. Perazzio, R.A. Cordeiro, H.A.M. Giardini. Uncovering the knowledge about systemic amyloidosis relevant to the rheumatologists. Advances in Rheumatology 64 (2024) 71. https://doi.org/10.1186/s42358-024-00399-3 DOI: https://doi.org/10.1186/s42358-024-00399-3

[38] J. Zhang, Y. Zhang, J. Wang, Y. Xia, J. Zhang, L. Chen. Recent advances in Alzheimer’s disease: Mechanisms, clinical trials and new drug development strategies. Signal Transduction and Targeted Therapy 9 (2024) 211. https://doi.org/10.1038/s41392-024-01911-3 DOI: https://doi.org/10.1038/s41392-024-01911-3

[39] H. Jeong, H. Shin, S. Hong, Y. Kim. Physiological roles of monomeric amyloid-β and implications for Alzheimer’s disease therapeutics. Experimental Neurobiology 31 (2022) 65. https://doi.org/10.5607/en22004 DOI: https://doi.org/10.5607/en22004

[40] K. Iqbal, F. Liu, C.-X. Gong, I. Grundke-Iqbal. Tau in Alzheimer disease and related tauopathies. Current Alzheimer Research 7 (2010) 656-664. https://doi.org/10.2174/156720510793611592 DOI: https://doi.org/10.2174/156720510793611592

[41] M. Alipour, M. Motavaf, P. Abdolmaleki, A. Zali, F. Ashrafi, S. Safari, B. Hajipour-Verdom. Structural analysis and conformational dynamics of Short helical hyperphosphorylated segments of tau protein (sequence 254–290) in alzheimer’s disease: a molecular dynamics simulation study. Frontiers in Molecular Biosciences 9 (2022) 884705. https://doi.org/10.3389/fmolb.2022.884705 DOI: https://doi.org/10.3389/fmolb.2022.884705

[42] L. Song, D.E. Oseid, E.A. Wells, A.S. Robinson. The Interplay between GSK3β and Tau Ser262 phosphorylation during the progression of tau pathology. International Journal of Molecular Sciences 23 (2022) 11610. https://doi.org/10.3390/ijms231911610 DOI: https://doi.org/10.3390/ijms231911610

[43] Y. Xia, S. Prokop, B.I. Giasson. “Don’t Phos Over Tau”: recent developments in clinical biomarkers and therapies targeting tau phosphorylation in Alzheimer’s disease and other tauopathies. Molecular Neurodegeneration 16 (2021) 37. https://doi.org/10.1186/s13024-021-00460-5 DOI: https://doi.org/10.1186/s13024-021-00460-5

[44] Z.D. Zhou, L.X. Yi, D.Q. Wang, T.M. Lim, E.K. Tan. Role of dopamine in the pathophysiology of Parkinson’s disease. Translational Neurodegeneration 12 (2023) 44. https://doi.org/10.1186/s40035-023-00378-6 DOI: https://doi.org/10.1186/s40035-023-00378-6

[45] A. Martirosyan, R. Ansari, F. Pestana, K. Hebestreit, H. Gasparyan, R. Aleksanyan, S. Hnatova, S. Poovathingal, C. Marneffe, D.R. Thal. Unravelling cell type-specific responses to Parkinson’s Disease at single cell resolution. Molecular Neurodegeneration 19 (2024) 1-24. https://doi.org/10.1186/s13024-023-00699-0 DOI: https://doi.org/10.1186/s13024-024-00717-9

[46] J. Pitton Rissardo, A. McGarry, Y. Shi, A.L. Fornari Caprara, G.T. Kannarkat. Alpha-Synuclein Neurobiology in Parkinson’s Disease: A Comprehensive Review of Its Role, Mechanisms, and Therapeutic Perspectives. Brain Sciences 15 (2025) 1260. https://doi.org/10.3390/brainsci15121260 DOI: https://doi.org/10.3390/brainsci15121260

[47] C.A. Morato Torres, Z. Wassouf, F. Zafar, D. Sastre, T.F. Outeiro, B. Schüle. The role of alpha-synuclein and other Parkinson’s genes in neurodevelopmental and neurodegenerative disorders. International Journal of Molecular Sciences 21 (2020) 5724. https://doi.org/10.3390/ijms21165724 DOI: https://doi.org/10.3390/ijms21165724

[48] M. Alipour, B. Hajipour-Verdom, A. Zali, F. Ashrafi, P. Abdolmaleki, S. Oraee-Yazdani, M. Akhlaghdoust, N. Karimi. Interaction of α-synuclein with DJ-1 in homodimer and L166P mutant monomer forms in Parkinson’s disease: a molecular dynamics study. Journal of Biomolecular Structure and Dynamics 44 (2024) 1558-1565. https://doi.org/10.1080/07391102.2024.2446660 DOI: https://doi.org/10.1080/07391102.2024.2446660

[49] N. Ramalingam, U. Dettmer. α-Synuclein serine129 phosphorylation–the physiology of pathology. Molecular neurodegeneration 18 (2023) 84. https://doi.org/10.1186/s13024-023-00680-x DOI: https://doi.org/10.1186/s13024-023-00680-x

[50] K. Beyer, A. Ariza. alpha-Synuclein posttranslational modification and alternative splicing as a trigger for neurodegeneration. Molecular Neurobiology 47 (2013) 509-524. https://doi.org/10.1007/s12035-012-8330-5 DOI: https://doi.org/10.1007/s12035-012-8330-5

[51] R. Andrews, B. Fu, C.E. Toomey, J.C. Breiter, J. Lachica, J.S. Beckwith, R. Tian, E.E. Brock, L.-M. Needham, G.J. Chant. Large-scale visualization of α-synuclein oligomers in Parkinson’s disease brain tissue. Nature Biomedical Engineering (2025). https://doi.org/10.1038/s41551-025-01496-4 DOI: https://doi.org/10.1038/s41551-025-01496-4

[52] A. Bigi, R. Cascella, C. Cecchi. α-Synuclein oligomers and fibrils: partners in crime in synucleinopathies. Neural Regeneration Research 18 (2023) 2332-2342. https://doi.org/10.4103/1673-5374.371345 DOI: https://doi.org/10.4103/1673-5374.371345

[53] F.N. Emamzadeh. Alpha-synuclein structure, functions, and interactions. Journal of Research in Medical Sciences 21 (2016) 29. https://doi.org/10.4103/1735-1995.181989 DOI: https://doi.org/10.4103/1735-1995.181989

[54] T. Tripathi. A master regulator of α-synuclein aggregation. ACS Chemical Neuroscience 11 (2020) 1376-1378. https://doi.org/10.1021/acschemneuro.0c00216 DOI: https://doi.org/10.1021/acschemneuro.0c00216

[55] N. Exner, A.K. Lutz, C. Haass, K.F. Winklhofer. Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences. The EMBO Journal 31 (2012) 3038-3062. https://doi.org/10.1038/emboj.2012.170 DOI: https://doi.org/10.1038/emboj.2012.170

[56] S. Miller, M.M. Muqit. Therapeutic approaches to enhance PINK1/Parkin mediated mitophagy for the treatment of Parkinson’s disease. Neuroscience Letters 705 (2019) 7-13. https://doi.org/10.1016/j.neulet.2019.04.029 DOI: https://doi.org/10.1016/j.neulet.2019.04.029

[57] J. Zhang, X. Li, J.-D. Li. The roles of post-translational modifications on α-synuclein in the pathogenesis of Parkinson’s diseases. Frontiers in Neuroscience 13 (2019) 381. https://doi.org/10.3389/fnins.2019.00381 DOI: https://doi.org/10.3389/fnins.2019.00381

[58] S. Sahoo, A.A. Padhy, V. Kumari, P. Mishra. Role of ubiquitin–proteasome and autophagy-lysosome pathways in α-synuclein aggregate clearance. Molecular Neurobiology 59 (2022) 5379-5407. https://doi.org/10.1007/s12035-022-02897-1 DOI: https://doi.org/10.1007/s12035-022-02897-1

[59] I. Stojkovska, D. Krainc, J.R. Mazzulli. Molecular mechanisms of α-synuclein and GBA1 in Parkinson’s disease. Cell and Tissue Research 373 (2018) 51-60. https://doi.org/10.1007/s00441-017-2704-y DOI: https://doi.org/10.1007/s00441-017-2704-y

[60] K. Wakabayashi, K. Tanji, S. Odagiri, Y. Miki, F. Mori, H. Takahashi. The Lewy body in Parkinson’s disease and related neurodegenerative disorders. Molecular Neurobiology 47 (2013) 495-508. https://doi.org/10.1007/s12035-012-8280-y DOI: https://doi.org/10.1007/s12035-012-8280-y

[61] D. Sulzer, R.H. Edwards. The physiological role of α‐synuclein and its relationship to Parkinson’s disease. Journal of Neurochemistry 150 (2019) 475-486. https://doi.org/10.1111/jnc.14810 DOI: https://doi.org/10.1111/jnc.14810

[62] S. Del Sol-Fernández, P. Martínez-Vicente, P. Gomollón-Zueco, C. Castro-Hinojosa, L. Gutiérrez, R.M. Fratila, M. Moros. Magnetogenetics: remote activation of cellular functions triggered by magnetic switches. Nanoscale 14 (2022) 2091-2118. https://doi.org/10.1039/d1nr06303k DOI: https://doi.org/10.1039/D1NR06303K

[63] S. Qin, H. Yin, C. Yang, Y. Dou, Z. Liu, P. Zhang, H. Yu, Y. Huang, J. Feng, J. Hao. A magnetic protein biocompass. Nature Materials 15 (2016) 217-226. https://doi.org/10.1038/nmat4484 DOI: https://doi.org/10.1038/nmat4484

[64] S.A. Stanley, J. Sauer, R.S. Kane, J.S. Dordick, J.M. Friedman. Remote regulation of glucose homeostasis in mice using genetically encoded nanoparticles. Nature Medicine 21 (2015) 92-98. https://doi.org/10.1038/nm.3730 DOI: https://doi.org/10.1038/nm.3730

[65] S.A. Ralph, G.G. Van Dooren, R.F. Waller, M.J. Crawford, M.J. Fraunholz, B.J. Foth, C.J. Tonkin, D.S. Roos, G.I. McFadden. Metabolic maps and functions of the Plasmodium falciparum apicoplast. Nature Reviews Microbiology 2 (2004) 203-216. https://doi.org/10.1038/nrmicro843 DOI: https://doi.org/10.1038/nrmicro843

[66] D. Schüler. Magnetoreception and magnetosomes in bacteria. Springer-Verlag, Berlin, Germany (2006). https://doi.org/10.1007/11741862 DOI: https://doi.org/10.1007/11741862

[67] P.J. Hore, H. Mouritsen. The radical-pair mechanism of magnetoreception. Annual Review of Biophysics 45 (2016) 299-344. https://doi.org/10.1146/annurev-biophys-032116-094545 DOI: https://doi.org/10.1146/annurev-biophys-032116-094545

[68] H. Huang, S. Delikanli, H. Zeng, D.M. Ferkey, A. Pralle. Remote control of ion channels and neurons through magnetic-field heating of nanoparticles. Nature Nanotechnology 5 (2010) 602-606. https://doi.org/10.1038/nnano.2010.125 DOI: https://doi.org/10.1038/nnano.2010.125

[69] R.J. Gegear, A. Casselman, S. Waddell, S.M. Reppert. Cryptochrome mediates light-dependent magnetosensitivity in Drosophila. Nature 454 (2008) 1014-1018. https://doi.org/10.1038/nature07183 DOI: https://doi.org/10.1038/nature07183

[70] I. Chaves, R. Pokorny, M. Byrdin, N. Hoang, T. Ritz, K. Brettel, L.-O. Essen, G.T. Van Der Horst, A. Batschauer, M. Ahmad. The cryptochromes: blue light photoreceptors in plants and animals. Annual Review of Plant Biology 62 (2011) 335-364. https://doi.org/10.1146/annurev-arplant-042110-103759 DOI: https://doi.org/10.1146/annurev-arplant-042110-103759

[71] K.J. Lohmann. A candidate magnetoreceptor. Nature Materials 15 (2016) 136-138. https://doi.org/10.1038/nmat4550 DOI: https://doi.org/10.1038/nmat4550

[72] K. Maeda, A.J. Robinson, K.B. Henbest, H.J. Hogben, T. Biskup, M. Ahmad, E. Schleicher, S. Weber, C.R. Timmel, P.J. Hore. Magnetically sensitive light-induced reactions in cryptochrome are consistent with its proposed role as a magnetoreceptor. Proceedings of the National Academy of Sciences 109 (2012) 4774-4779. https://doi.org/10.1073/pnas.1118959109 DOI: https://doi.org/10.1073/pnas.1118959109

[73] C.A. Dodson, P.J. Hore, M.I. Wallace. A radical sense of direction: signalling and mechanism in cryptochrome magnetoreception. Trends in Biochemical Sciences 38 (2013) 435-446. https://doi.org/10.1016/j.tibs.2013.07.002 DOI: https://doi.org/10.1016/j.tibs.2013.07.002

[74] M.A. Gauger, A. Sancar. Cryptochrome, circadian cycle, cell cycle checkpoints, and cancer. Cancer Research 65 (2005) 6828-6834. https://doi.org/10.1158/0008-5472.can-05-1119 DOI: https://doi.org/10.1158/0008-5472.CAN-05-1119

[75] H. Yu, X. Meng, J. Wu, C. Pan, X. Ying, Y. Zhou, R. Liu, W. Huang. Cryptochrome 1 overexpression correlates with tumor progression and poor prognosis in patients with colorectal cancer. PloS One 8 (2013) e61679. https://doi.org/10.1371/journal.pone.0061679 DOI: https://doi.org/10.1371/journal.pone.0061679

[76] F.C. Kelleher, A. Rao, A. Maguire. Circadian molecular clocks and cancer. Cancer Letters 342 (2014) 9-18. https://doi.org/10.1016/j.canlet.2013.09.040 DOI: https://doi.org/10.1016/j.canlet.2013.09.040

[77] G. Fedele, M.D. Edwards, S. Bhutani, J.M. Hares, M. Murbach, E.W. Green, S. Dissel, M.H. Hastings, E. Rosato, C.P. Kyriacou. Genetic analysis of circadian responses to low frequency electromagnetic fields in Drosophila melanogaster. PLoS Genetics 10 (2014) e1004804. https://doi.org/10.1371/journal.pgen.1004804 DOI: https://doi.org/10.1371/journal.pgen.1004804

[78] R. Marley, C.N. Giachello, N.S. Scrutton, R.A. Baines, A.R. Jones. Cryptochrome-dependent magnetic field effect on seizure response in Drosophila larvae. Scientific Reports 4 (2014) 5799. https://doi.org/10.1038/srep05799 DOI: https://doi.org/10.1038/srep05799

[79] T. Ritz, S. Adem, K. Schulten. A model for photoreceptor-based magnetoreception in birds. Biophysical Journal 78 (2000) 707-718. https://doi.org/10.1016/s0006-3495(00)76629-x DOI: https://doi.org/10.1016/S0006-3495(00)76629-X

[80] R. Wiltschko, P. Thalau, D. Gehring, C. Nießner, T. Ritz, W. Wiltschko. Magnetoreception in birds: the effect of radio-frequency fields. Journal of the Royal Society Interface 12 (2015) 20141103. https://doi.org/10.1098/rsif.2014.1103 DOI: https://doi.org/10.1098/rsif.2014.1103

[81] H. Mouritsen. Long-distance navigation and magnetoreception in migratory animals. Nature 558 (2018) 50-59. https://doi.org/10.1038/s41586-018-0176-1 DOI: https://doi.org/10.1038/s41586-018-0176-1

[82] D.R. Kattnig, E.W. Evans, V. Déjean, C.A. Dodson, M.I. Wallace, S.R. Mackenzie, C.R. Timmel, P. Hore. Chemical amplification of magnetic field effects relevant to avian magnetoreception. Nature Chemistry 8 (2016) 384-391. https://doi.org/10.1038/nchem.2447 DOI: https://doi.org/10.1038/nchem.2447

[83] C.T. Rodgers, P.J. Hore. Chemical magnetoreception in birds: the radical pair mechanism. Proceedings of the National Academy of Sciences 106 (2009) 353-360. https://doi.org/10.1073/pnas.0711968106 DOI: https://doi.org/10.1073/pnas.0711968106

[84] C. Feillet, G.T. van Der Horst, F. Levi, D.A. Rand, F. Delaunay. Coupling between the circadian clock and cell cycle oscillators: implication for healthy cells and malignant growth. Frontiers in Neurology 6 (2015) 96. https://doi.org/10.3389/fneur.2015.00096 DOI: https://doi.org/10.3389/fneur.2015.00096

[85] N. Ozturk, D. Ozturk, I. Halil Kavakli, A. Okyar. Molecular aspects of circadian pharmacology and relevance for cancer chronotherapy. International Journal of Molecular Sciences 18 (2017) 2168. https://doi.org/10.3390/ijms18102168 DOI: https://doi.org/10.3390/ijms18102168

[86] A. Sancar, R.N. Van Gelder. Clocks, cancer, and chronochemotherapy. Science 371 (2021) eabb0738. https://doi.org/10.1126/science.abb0738 DOI: https://doi.org/10.1126/science.abb0738

[87] R.M. Sherrard, N. Morellini, N. Jourdan, M. El-Esawi, L.-D. Arthaut, C. Niessner, F. Rouyer, A. Klarsfeld, M. Doulazmi, J. Witczak. Low-intensity electromagnetic fields induce human cryptochrome to modulate intracellular reactive oxygen species. PLoS Biology 16 (2018) e2006229. https://doi.org/10.1371/journal.pbio.2006229 DOI: https://doi.org/10.1371/journal.pbio.2006229

[88] P. Boesch, F. Weber-Lotfi, N. Ibrahim, V. Tarasenko, A. Cosset, F. Paulus, R.N. Lightowlers, A. Dietrich. DNA repair in organelles: pathways, organization, regulation, relevance in disease and aging. Biochimica et Biophysica Acta-Molecular Cell Research 1813 (2011) 186-200. https://doi.org/10.1016/j.bbamcr.2010.10.002 DOI: https://doi.org/10.1016/j.bbamcr.2010.10.002

[89] T. Helleday, E. Petermann, C. Lundin, B. Hodgson, R.A. Sharma. DNA repair pathways as targets for cancer therapy. Nature Reviews Cancer 8 (2008) 193-204. https://doi.org/10.1038/nrc2342 DOI: https://doi.org/10.1038/nrc2342

[90] C.N. Giachello, N.S. Scrutton, A.R. Jones, R.A. Baines. Magnetic fields modulate blue-light-dependent regulation of neuronal firing by cryptochrome. Journal of Neuroscience 36 (2016) 10742-10749. https://doi.org/10.1523/jneurosci.2140-16.2016 DOI: https://doi.org/10.1523/JNEUROSCI.2140-16.2016

[91] A. Shostak. Circadian clock, cell division, and cancer: from molecules to organism. International Journal of Molecular Sciences 18 (2017) 873. https://doi.org/10.3390/ijms18040873 DOI: https://doi.org/10.3390/ijms18040873

[92] A. Sancar, L.A. Lindsey-Boltz, T.-H. Kang, J.T. Reardon, J.H. Lee, N. Ozturk. Circadian clock control of the cellular response to DNA damage. FEBS Letters 584 (2010) 2618-2625. https://doi.org/10.1016/j.febslet.2010.03.017 DOI: https://doi.org/10.1016/j.febslet.2010.03.017

[93] B.A. Carneiro, W.S. El-Deiry. Targeting apoptosis in cancer therapy. Nature Reviews Clinical Oncology 17 (2020) 395-417. https://doi.org/10.1038/s41571-020-0341-y DOI: https://doi.org/10.1038/s41571-020-0341-y

[94] J. Qiu, T. Dai, H. Tao, X. Li, C. Luo, Y. Sima, S. Xu. Inhibition of expression of the circadian clock gene cryptochrome 1 causes abnormal glucometabolic and cell growth in Bombyx mori Cells. International Journal of Molecular Sciences 24 (2023) 5435. https://doi.org/10.3390/ijms24065435 DOI: https://doi.org/10.3390/ijms24065435

[95] K.H.C. Baser, I.C. Haskologlu, E. Erdag. Molecular links between circadian rhythm disruption, melatonin, and neurodegenerative diseases: an updated review. Molecules 30 (2025) 1888. https://doi.org/10.3390/molecules30091888 DOI: https://doi.org/10.3390/molecules30091888

[96] V.S. Sukhorukov, N.M. Mudzhiri, A.S. Voronkova, T.I. Baranich, V.V. Glinkina, S.N. Illarioshkin. Mitochondrial disorders in Alzheimer’s disease. Biochemistry (Moscow) 86 (2021) 667-679. https://doi.org/10.1134/s0006297921060055 DOI: https://doi.org/10.1134/S0006297921060055

[97] C. Suárez-Barrio, S. del Olmo-Aguado, E. García-Pérez, M. de la Fuente, F. Muruzabal, E. Anitua, B. Baamonde-Arbaiza, L. Fernández-Vega-Cueto, L. Fernández-Vega, J. Merayo-Lloves. Antioxidant role of PRGF on RPE cells after blue light insult as a therapy for neurodegenerative diseases. International Journal of Molecular Sciences 21 (2020) 1021. https://doi.org/10.3390/ijms21031021 DOI: https://doi.org/10.3390/ijms21031021

[98] E. Mitroshina, E. Kalinina, M. Vedunova. Optogenetics in Alzheimer’s disease: focus on astrocytes. Antioxidants 12 (2023) 1856. https://doi.org/10.3390/antiox12101856 DOI: https://doi.org/10.3390/antiox12101856

[99] B.H. Correa, C.R. Moreira, M.E. Hildebrand, L.B. Vieira. The role of voltage-gated calcium channels in basal ganglia neurodegenerative disorders. Current Neuropharmacology 21 (2023) 183-201. https://doi.org/10.2174/1570159x20666220327211156 DOI: https://doi.org/10.2174/1570159X20666220327211156

[100] C. Cheignon, F. Collin, L. Sabater, C. Hureau. Oxidative damages on the Alzheimer’s related-Aβ peptide alters its ability to assemble. Antioxidants 12 (2023) 472. https://doi.org/10.3390/antiox12020472 DOI: https://doi.org/10.3390/antiox12020472

[101] M. Gu, D.C. Bode, J.H. Viles. Copper redox cycling inhibits Aβ fibre formation and promotes fibre fragmentation, while generating a dityrosine Aβ dimer. Scientific Reports 8 (2018) 16190. https://doi.org/10.1038/s41598-018-33935-5 DOI: https://doi.org/10.1038/s41598-018-33935-5

[102] S.R. D’Mello. When good kinases go rogue: GSK3, p38 MAPK and CDKs as therapeutic targets for Alzheimer’s and Huntington’s disease. International Journal of Molecular Sciences 22 (2021) 5911. https://doi.org/10.3390/ijms22115911 DOI: https://doi.org/10.3390/ijms22115911

[103] S. Somin, D. Kulasiri, S. Samarasinghe. Alleviating the unwanted effects of oxidative stress on Aβ clearance: a review of related concepts and strategies for the development of computational model-ling. Translational Neurodegeneration 12 (2023) 11. https://doi.org/10.1186/s40035-023-00344-2 DOI: https://doi.org/10.1186/s40035-023-00344-2

[104] V. Pillai, L. Buck, E. Lari. Scavenging of reactive oxygen species mimics the anoxic response in goldfish pyramidal neurons. Journal of Experimental Biology 224 (2021) jeb238147. https://doi.org/10.1242/jeb.238147 DOI: https://doi.org/10.1242/jeb.238147

[105] M. Alipour, M. Abdolmaleki, Y. Shabanpour, A. Zali, F. Ashrafi, S. Nohesara, B. Hajipour-Verdom. Advances in magnetic field approaches for non-invasive targeting neuromodulation. Frontiers in Human Neuroscience 19 (2025) 1489940. https://doi.org/10.3389/fnhum.2025.1489940 DOI: https://doi.org/10.3389/fnhum.2025.1489940

[106] K.R. Hoyt, K. Obrietan. Circadian clocks, cognition, and Alzheimer’s disease: synaptic mechanisms, signaling effectors, and chronotherapeutics. Molecular Neurodegeneration 17 (2022) 35. https://doi.org/10.1186/s13024-022-00537-9 DOI: https://doi.org/10.1186/s13024-022-00537-9

[107] C. Xu, Y. Lv, C. Chen, Y. Zhang, S. Wei. Blue light-dependent phosphorylations of cryptochromes are affected by magnetic fields in Arabidopsis. Advances in Space Research 53 (2014) 1118-1124. https://doi.org/10.1016/j.asr.2014.01.033 DOI: https://doi.org/10.1016/j.asr.2014.01.033

[108] H. Zadeh-Haghighi, C. Simon. Radical pairs can explain magnetic field and lithium effects on the circadian clock. Scientific Reports 12 (2022) 269. https://doi.org/10.1038/s41598-021-04334-0 DOI: https://doi.org/10.1038/s41598-021-04334-0

[109] L. Zhang, E.P. Malkemper. Cryptochromes in mammals: a magnetoreception misconception? Frontiers in Physiology 14 (2023) 1250798. https://doi.org/10.3389/fphys.2023.1250798 DOI: https://doi.org/10.3389/fphys.2023.1250798

[110] G. Minakaki, D. Krainc, L.F. Burbulla. The convergence of alpha-synuclein, mitochondrial, and lysosomal pathways in vulnerability of midbrain dopaminergic neurons in Parkinson’s disease. Frontiers in Cell and Developmental Biology 8 (2020) 580634. https://doi.org/10.3389/fcell.2020.580634 DOI: https://doi.org/10.3389/fcell.2020.580634

[111] M. Yalçin, V. Grande, T.F. Outeiro, A. Relógio. Circadian clock dysfunction in Parkinson’s disease: mechanisms, consequences, and therapeutic strategy. npj Parkinson's Disease 11 (2025) 213. https://doi.org/10.1038/s41531-025-01009-9 DOI: https://doi.org/10.1038/s41531-025-01009-9

[112] R. Rishabh, H. Zadeh-Haghighi, D. Salahub, C. Simon. Radical pairs may explain reactive oxygen species-mediated effects of hypomagnetic field on neurogenesis. PLOS Computational Biology 18 (2022) e1010198. https://doi.org/10.1371/journal.pcbi.1010198 DOI: https://doi.org/10.1371/journal.pcbi.1010198

[113] K.M. Ricke, T. Paß, S. Kimoloi, K. Fährmann, C. Jüngst, A. Schauss, O.R. Baris, M. Aradjanski, A. Trifunovic, T.M.E. Faelker. Mitochondrial dysfunction combined with high calcium load leads to impaired antioxidant defense underlying the selective loss of nigral dopaminergic neurons. Journal of Neuroscience 40 (2020) 1975-1986. https://doi.org/10.1523/jneurosci.1345-19.2019 DOI: https://doi.org/10.1523/JNEUROSCI.1345-19.2019

[114] A. Bose, M.F. Beal. Mitochondrial dysfunction in Parkinson's disease. Journal of Neurochemistry 139 (2016) 216-231. https://doi.org/10.1111/jnc.13731 DOI: https://doi.org/10.1111/jnc.13731

[115] S.J. Chinta, J.K. Mallajosyula, A. Rane, J.K. Andersen. Mitochondrial alpha-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo. Neuroscience Letters 486 (2010) 235-239. https://doi.org/10.1016/j.neulet.2010.09.061 DOI: https://doi.org/10.1016/j.neulet.2010.09.061

[116] I. Kawahata, D.I. Finkelstein, K. Fukunaga. Pathogenic impact of α-synuclein phosphorylation and its kinases in α-synucleinopathies. International Journal of Molecular Sciences 23 (2022) 6216. https://doi.org/10.3390/ijms23116216 DOI: https://doi.org/10.3390/ijms23116216

[117] J. Wu, H. Lou, T.N. Alerte, E.K. Stachowski, J. Chen, A.B. Singleton, R.L. Hamilton, R.G. Perez. Lewy-like aggregation of α-synuclein reduces protein phosphatase 2A activity in vitro and in vivo. Neuroscience 207 (2012) 288-297. https://doi.org/10.1016/j.neuroscience.2012.01.028 DOI: https://doi.org/10.1016/j.neuroscience.2012.01.028

[118] D. Ebrahimi-Fakhari, L. Wahlster, P.J. McLean. Protein degradation pathways in Parkinson’s disease: curse or blessing. Acta Neuropathologica 124 (2012) 153-172. https://doi.org/10.1007/s00401-012-1004-6 DOI: https://doi.org/10.1007/s00401-012-1004-6

[119] K. Xu, Y. Zhang, Y. Shi, Y. Zhang, C. Zhang, T. Wang, P. Lv, Y. Bai, S. Wang. Circadian rhythm disruption: a potential trigger in Parkinson’s disease pathogenesis. Frontiers in Cellular Neuroscience 18 (2024) 1464595. https://doi.org/10.3389/fncel.2024.1464595 DOI: https://doi.org/10.3389/fncel.2024.1464595

[120] T. Yoshii, M. Ahmad, C. Helfrich-Förster. Cryptochrome mediates light-dependent magnetosensitivity of Drosophila's circadian clock. PLoS Biology 7 (2009) e1000086. https://doi.org/10.1371/journal.pbio.1000086 DOI: https://doi.org/10.1371/journal.pbio.1000086