[1] N. Cremades and C. M. Dobson, “The contribution of biophysical and structural studies of protein self-assembly to the design of therapeutic strategies for amyloid diseases,” Neurobiol. Dis., 109, 178–190, 2018.
[2] S. F Lichtenthaler, “Alpha-secretase cleavage of the amyloid precursor protein: proteolysis regulated by signaling pathways and protein trafficking,” Curr. Alzheimer Res., 9, 2, 165–177, 2012.
[3] G. Brinkmalm et al., “Identification of neurotoxic cross-linked amyloid-β dimers in the Alzheimer’s brain,” Brain, 142, 1441–1457, 2019.
[4] T. Guo, D. Zhang, Y. Zeng, T. Y. Huang, H. Xu, and Y. Zhao, “Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease,” Mol. Neurodegener., 15, 1–37, 2020.
[5] P. H. Nguyen et al., “Amyloid oligomers: A joint experimental/computational perspective on Alzheimer’s disease, Parkinson’s disease, Type II diabetes, and amyotrophic lateral sclerosis,” Chem. Rev., 121, 2545–2647, 2021.
[6] A. Ashok et al., “Retinal degeneration and Alzheimer’s disease: an evolving link,” Int. J. Mol. Sci., 21, 7290, 2020.
[7] L. Deng et al., “Amyloid β induces early changes in the ribosomal machinery, cytoskeletal organization and oxidative phosphorylation in retinal photoreceptor cells,” Front. Mol. Neurosci., 12, 24, 2019.
[8] T. Prasad et al., “Amyloid β peptides overexpression in retinal pigment epithelial cells via AAV-mediated gene transfer mimics AMD-like pathology in mice,” Sci. Rep., 7, 1–15, 2017.
[9] K. Araki et al., “Parkinson’s disease is a type of amyloidosis featuring accumulation of amyloid fibrils of α-synuclein,” Proc. Natl. Acad. Sci., 116, 17963–17969, 2019.
[10] D. Yedlapudi, L. Xu, D. Luo, G. B. Marsh, S. V Todi, and A. K. Dutta, “Targeting alpha synuclein and amyloid beta by a multifunctional, brain-penetrant dopamine D2/D3 agonist D-520: Potential therapeutic application in Parkinson’s disease with dementia,” Sci. Rep., 9, 1–12, 2019.
[11] G. Gagno et al., “From Brain to Heart: Possible Role of Amyloid-β in Ischemic Heart Disease and Ischemia-Reperfusion Injury,” Int. J. Mol. Sci., 21, 9655, 2020.
[12] J. Leszek et al., “The Links between Cardiovascular Diseases and Alzheimer’s Disease,” Curr. Neuropharmacol., 19, 152–169, 2021.
[13] D. A. Stakos et al., “The Alzheimer’s disease amyloid-beta hypothesis in cardiovascular aging and disease: JACC focus seminar,” J. Am. Coll. Cardiol., 75, 952–967, 2020.
[14] P. Bharadwaj et al., “The link between type 2 diabetes and neurodegeneration: roles for amyloid-β, amylin, and tau proteins,” J. Alzheimer’s Dis., 59, 421–432, 2017.
[15] M. G. Morgese, S. Schiavone, and L. Trabace, “Emerging role of amyloid beta in stress response: Implication for depression and diabetes,” Eur. J. Pharmacol., 817, 22–29, 2017.
[16] J. B. Bryson et al., “Amyloid precursor protein (APP) contributes to pathology in the SOD1G93A mouse model of amyotrophic lateral sclerosis,” Hum. Mol. Genet., 21, 3871–3882, 2012.
[17] N. Y. Calingasan, J. Chen, M. Kiaei, and M. F. Beal, “β-amyloid 42 accumulation in the lumbar spinal cord motor neurons of amyotrophic lateral sclerosis patients,” Neurobiol. Dis., 19, 340–347, 2005.
[18] J. Ezpeleta et al., “Production of seedable Amyloid-β peptides in model of prion diseases upon PrP Sc-induced PDK1 overactivation,” Nat. Commun., 10, 1–13, 2019.
[19] A. Cornejo, J. M. Jiménez, L. Caballero, F. Melo, and R. B. Maccioni, “Fulvic acid inhibits aggregation and promotes disassembly of tau fibrils associated with Alzheimer’s disease,” J. Alzheimer’s Dis., 27, 143–153, 2011.
[20] K. Gade Malmos et al., “ThT 101: a primer on the use of thioflavin T to investigate amyloid formation,” Amyloid, 24, 1–16, 2017.
[21] S. A. Hudson, H. Ecroyd, T. W. Kee, and J. A. Carver, “The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds,” FEBS J., 276, 5960–5972, 2009.
[22] L. P. Jameson, N. W. Smith, and S. V Dzyuba, “Dye-binding assays for evaluation of the effects of small molecule inhibitors on amyloid (Aβ) self-assembly,” ACS Chem. Neurosci., 3, 807–819, 2012.
[23] D. J. Lindberg, A. Wenger, E. Sundin, E. Wesén, F. Westerlund, and E. K. Esbjörner, “Binding of thioflavin-T to amyloid fibrils leads to fluorescence self-quenching and fibril compaction,” Biochemistry, 56, 2170–2174, 2017.
[24] N. R. Rovnyagina et al., “Fluorescence Lifetime and Intensity of Thioflavin T as Reporters of Different Fibrillation Stages: Insights Obtained from Fluorescence Up-Conversion and Particle Size Distribution Measurements,” Int. J. Mol. Sci., 21, 6169, 2020.
[25] M. Sebastiao, N. Quittot, and S. Bourgault, “Thioflavin T fluorescence to analyse amyloid formation kinetics: Measurement frequency as a factor explaining irreproducibility,” Anal. Biochem., 532, 83–86, 2017.
[26] A. I. Sulatskaya, M. I. Sulatsky, I. A. Antifeeva, I. M. Kuznetsova, and K. K. Turoverov, “Structural analogue of thioflavin T, DMASEBT, as a tool for amyloid fibrils study,” Anal. Chem., 91, 3131–3140, 2019.
[27] M. M. Wördehoff and W. Hoyer, “α-Synuclein aggregation monitored by thioflavin T fluorescence assay,” Bio-protocol, 8,12-18, 2018.
[28] M. Yousaf, H. Huang, P. Li, C. Wang, and Y. Yang, “Fluorine functionalized graphene quantum dots as inhibitor against hIAPP amyloid aggregation,” ACS Chem. Neurosci., 8, 1368–1377, 2017.
[29] E. W. Van Stryland and M. Sheik-Bahae, “Z-scan technique for nonlinear materials characterization,” in Materials Characterization and Optical Probe Techniques: A Critical Review, 10291, 102910Q, 1997.
[30] H. M. El-Rafie and M. A.-A. Hamed, “Antioxidant and anti-inflammatory activities of silver nanoparticles biosynthesized from aqueous leaves extracts of four Terminalia species,” Adv. Nat. Sci. Nanosci. Nanotechnol., 5, 35008, 2014.
[31] R. Rajeswari, H. G. Prabu, and D. M. Amutha, “One Pot Hydrothermal synthesis characterizations of silver nanoparticles on reduced graphene oxide for its enhanced antibacterial and antioxidant properties,” IOSR J. Appl. Chem, 10, 64–69, 2017.
[32] J. H. Hardesty and B. Attili, “Spectrophotometry and the Beer-Lambert Law: An Important Analytical Technique in Chemistry,” Collin Coll. Dep. Chem., 2010.
[33] E. A. Mamonov et al., “Anisotropy versus circular dichroism in second harmonic generation from fourfold symmetric arrays of G-shaped nanostructures,” Phys. Rev. B, 89, 121113, 2014.
[34] K. Itoh, W. Watanabe, and Y. Ozeki, “Nonlinear ultrafast focal-point optics for microscopic imaging, manipulation, and machining,” Proc. IEEE, 97, 1011–1030, 2009.
