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Chen XQ, Mobley WC. Alzheimer illness pathogenesis: insights from molecular and mobile biology research of oligomeric Abeta and Tau species. Entrance Neurosci. 2019;13:659.
Dawkins E, Small DH. Insights into the physiological perform of the beta-amyloid precursor protein: past Alzheimer’s illness. J Neurochem. 2014;129:756–69.
Lane CA, Hardy J, Schott JM. Alzheimer’s illness. Eur J Neurol. 2018;25:59–70.
Straub JE, Thirumalai D. Towards a molecular principle of early and late occasions in monomer to amyloid fibril formation. Annu Rev Phys Chem. 2011;62:437–63.
Selkoe DJ, Hardy J. The amyloid speculation of Alzheimer’s illness at 25 years. EMBO Mol Med. 2016;8:595–608.
Bisceglia F, Natalello A, Serafini MM, Colombo R, Verga L, Lanni C, De Lorenzi E. An built-in technique to correlate aggregation state, construction and toxicity of Ass 1–42 oligomers. Talanta. 2018;188:17–26.
Maulik M, Westaway D, Jhamandas JH, Kar S. Function of ldl cholesterol in APP metabolism and its significance in Alzheimer’s illness pathogenesis. Mol Neurobiol. 2013;47:37–63.
Ittner A, Chua SW, Bertz J, Volkerling A, van der Hoven J, Gladbach A, Przybyla M, Bi M, van Hummel A, Stevens CH, et al. Web site-specific phosphorylation of tau inhibits amyloid-beta toxicity in Alzheimer’s mice. Science. 2016;354:904–8.
Revett TJ, Baker GB, Jhamandas J, Kar S. Glutamate system, amyloid ss peptides and tau protein: useful interrelationships and relevance to Alzheimer illness pathology. J Psychiatry Neurosci. 2013;38:6–23.
Chen GF, Xu TH, Yan Y, Zhou YR, Jiang Y, Melcher Okay, Xu HE. Amyloid beta: construction, biology and structure-based therapeutic improvement. Acta Pharmacol Sin. 2017;38:1205–35.
Lee SJ, Nam E, Lee HJ, Savelieff MG, Lim MH. In the direction of an understanding of amyloid-beta oligomers: characterization, toxicity mechanisms, and inhibitors. Chem Soc Rev. 2017;46:310–23.
Kusumoto Y, Lomakin A, Teplow DB, Benedek GB. Temperature dependence of amyloid beta-protein fibrillization. Proc Natl Acad Sci USA. 1998;95:12277–82.
Gursky O, Aleshkov S. Temperature-dependent beta-sheet formation in beta-amyloid Abeta(1–40) peptide in water: uncoupling beta-structure folding from aggregation. Biochim Biophys Acta. 2000;1476:93–102.
Yanagisawa Okay, Matsuzaki Okay. Ldl cholesterol-dependent aggregation of amyloid beta-protein. Ann NY Acad Sci. 2002;977:384–6.
Sabate R, Gallardo M, Estelrich J. Temperature dependence of the nucleation fixed charge in beta amyloid fibrillogenesis. Int J Biol Macromol. 2005;35:9–13.
Lin MS, Chen LY, Tsai HT, Wang SS, Chang Y, Higuchi A, Chen WY. Investigation of the mechanism of beta-amyloid fibril formation by kinetic and thermodynamic analyses. Langmuir. 2008;24:5802–8.
Hsu F, Park G, Guo Z. Key residues for the formation of Abeta42 amyloid fibrils. ACS Omega. 2018;3:8401–7.
Ghavami M, Rezaei M, Ejtehadi R, Lotfi M, Shokrgozar MA, Abd Emamy B, Raush J, Mahmoudi M. Physiological temperature has an important function in amyloid beta within the absence and presence of hydrophobic and hydrophilic nanoparticles. ACS Chem Neurosci. 2013;4:375–8.
Naiki H, Gejyo F. Kinetic evaluation of amyloid fibril formation. Strategies Enzymol. 1999;309:305–18.
Korneyev A, Binder L, Bernardis J. Speedy reversible phosphorylation of rat mind tau proteins in response to chilly water stress. Neurosci Lett. 1995;191:19–22.
Planel E, Miyasaka T, Launey T, Chui DH, Tanemura Okay, Sato S, Murayama O, Ishiguro Okay, Tatebayashi Y, Takashima A. Alterations in glucose metabolism induce hypothermia resulting in tau hyperphosphorylation by means of differential inhibition of kinase and phosphatase actions: implications for Alzheimer’s illness. J Neurosci. 2004;24:2401–11.
Ahmadian-Attari MM, Dargahi L, Mosaddegh M, Kamalinejad M, Khallaghi B, Noorbala F, Ahmadiani A. Impairment of rat spatial studying and reminiscence in a brand new mannequin of chilly water-induced persistent hypothermia: implication for Alzheimer’s illness. Neurotox Res. 2015;28:95–107.
El Khoury NB, Gratuze M, Petry F, Papon MA, Julien C, Marcouiller F, Morin F, Nicholls SB, Calon F, Hebert SS, et al. Hypothermia mediates age-dependent enhance of tau phosphorylation in db/db mice. Neurobiol Dis. 2016;88:55–65.
Vandal M, White PJ, Tournissac M, Tremblay C, St-Amour I, Drouin-Ouellet J, Bousquet M, Traversy MT, Planel E, Marette A, Calon F. Impaired thermoregulation and helpful results of thermoneutrality within the 3xTg-AD mannequin of Alzheimer’s illness. Neurobiol Ageing. 2016;43:47–57.
Corbett R, Laptook A, Weatherall P. Noninvasive measurements of human mind temperature utilizing volume-localized proton magnetic resonance spectroscopy. J Cereb Blood Stream Metab. 1997;17:363–9.
Collins CM, Smith MB, Turner R. Mannequin of native temperature modifications in mind upon useful activation. J Appl Physiol. 1985;2004(97):2051–5.
Sukstanskii AL, Yablonskiy DA. Theoretical mannequin of temperature regulation within the mind throughout modifications in useful exercise. Proc Natl Acad Sci USA. 2006;103:12144–9.
Sinigaglia-Coimbra R, Cavalheiro EA, Coimbra CG. Postischemic hyperthermia induces Alzheimer-like pathology within the rat mind. Acta Neuropathol. 2002;103:444–52.
Ishigaki D, Ogasawara Okay, Yoshioka Y, Chida Okay, Sasaki M, Fujiwara S, Aso Okay, Kobayashi M, Yoshida Okay, Terasaki Okay, et al. Mind temperature measured utilizing proton MR spectroscopy detects cerebral hemodynamic impairment in sufferers with unilateral persistent main cerebral artery steno-occlusive illness: comparability with positron emission tomography. Stroke. 2009;40:3012–6.
Laukkanen T, Kunutsor S, Kauhanen J, Laukkanen JA. Sauna bathing is inversely related to dementia and Alzheimer’s illness in middle-aged Finnish males. Age Ageing. 2017;46:245–9.
Ashraf GM, Tabrez S, Jabir NR, Firoz CK, Ahmad S, Hassan I, Alexiou A, Kamal MA. An summary on world traits in nanotechnological approaches for Alzheimer remedy. Curr Drug Metab. 2015;16:719–27.
Ansari SA, Satar R, Perveen A, Ashraf GM. Present opinion in Alzheimer’s illness remedy by nanotechnology-based approaches. Curr Opin Psychiatry. 2017;30:128–35.
Hajipour MJ, Santoso MR, Rezaee F, Aghaverdi H, Mahmoudi M, Perry G. Advances in Alzheimer’s prognosis and remedy: the implications of nanotechnology. Tendencies Biotechnol. 2017;35:937–53.
Saraf J, Kalia Okay, Bhattacharya P, Tekade RK. Rising synergy of nanodiamonds in neurodegenerative interventions. Drug Discov In the present day. 2019;24:584–94.
Tosi G, Pederzoli F, Belletti D, Vandelli MA, Forni F, Duskey JT, Ruozi B. Nanomedicine in Alzheimer’s illness: amyloid beta concentrating on technique. Prog Mind Res. 2019;245:57–88.
Danhier F, Ansorena E, Silva JM, Coco R, Le Breton A, Preat V. PLGA-based nanoparticles: an summary of biomedical functions. J Management Launch. 2012;161:505–22.
Baysal I, Ucar G, Gultekinoglu M, Ulubayram Okay, Yabanoglu-Ciftci S. Donepezil loaded PLGA-b-PEG nanoparticles: their capacity to induce destabilization of amyloid fibrils and to cross blood mind barrier in vitro. J Neural Transm. 2017;124:33–45.
Ding D, Zhu Q. Current advances of PLGA micro/nanoparticles for the supply of biomacromolecular therapeutics. Mater Sci Eng C Mater Biol Appl. 2018;92:1041–60.
Fan S, Zheng Y, Liu X, Fang W, Chen X, Liao W, Jing X, Lei M, Tao E, Ma Q, et al. Curcumin-loaded PLGA-PEG nanoparticles conjugated with B6 peptide for potential use in Alzheimer’s illness. Drug Deliv. 2018;25:1091–102.
Sanchez-Lopez E, Ettcheto M, Egea MA, Espina M, Cano A, Calpena AC, Camins A, Carmona N, Silva AM, Souto EB, Garcia ML. Memantine loaded PLGA PEGylated nanoparticles for Alzheimer’s illness: in vitro and in vivo characterization. J Nanobiotechnol. 2018;16:32.
Wang Y, Qin B, Xia G, Choi SH. FDA’s poly (lactic-co-glycolic acid) analysis program and regulatory outcomes. AAPS J. 2021;23:92. https://doi.org/10.1208/s12248-021-00611-y.
Wang Y, Wu Q, Anand BG, Karthivashan G, Phukan G, Yang J, Thinakaran G, Westaway D, Kar S. Significance of cytosolic cathepsin D in Alzheimer’s illness pathology: protecting mobile results of PLGA nanoparticles towards beta-amyloid-toxicity. Neuropathol Appl Neurobiol. 2020;46:686–706.
Anand BG WQ, Nejad MN, Karthivashan G, Dorosh L, Amidian S, Dahal A, Stepanova M, Wille H, Giuliani F, Kar S. Significance of unconjugated PLGA nanoparticles within the remedy of Alzheimer’s illness pathology. Bioact Mater (Unpublished knowledge).
Foroutanpay BV, Kumar J, Kang SG, Danaei N, Westaway D, Sim VL, Kar S. The consequences of N-terminal mutations on beta-amyloid peptide aggregation and toxicity. Neuroscience. 2018;379:177–88.
Anand BG, Wu Q, Karthivashan G, Shejale KP, Amidian S, Wille H, Kar S. Mimosine functionalized gold nanoparticles (Mimo-AuNPs) suppress beta-amyloid aggregation and neuronal toxicity. Bioact Mater. 2021;6:4491–505.
Wang Q, Shah N, Zhao J, Wang C, Zhao C, Liu L, Li L, Zhou F, Zheng J. Structural, morphological, and kinetic research of beta-amyloid peptide aggregation on self-assembled monolayers. Phys Chem Chem Phys. 2011;13:15200–10.
Li X, Zhang X, Ladiwala AR, Du D, Yadav JK, Tessier PM, Wright PE, Kelly JW, Buxbaum JN. Mechanisms of transthyretin inhibition of beta-amyloid aggregation in vitro. J Neurosci. 2013;33:19423–33.
Dahlgren KN, Manelli AM, Stine WB Jr, Baker LK, Krafft GA, LaDu MJ. Oligomeric and fibrillar species of amyloid-beta peptides differentially have an effect on neuronal viability. J Biol Chem. 2002;277:32046–53.
Track MS, Rauw G, Baker GB, Kar S. Memantine protects rat cortical cultured neurons towards beta-amyloid-induced toxicity by attenuating tau phosphorylation. Eur J Neurosci. 2008;28:1989–2002.
Maity S, Lyubchenko YL. AFM probing of amyloid-beta 42 dimers and trimers. Entrance Mol Biosci. 2020;7:69.
Wei Z, Track MS, MacTavish D, Jhamandas JH, Kar S. Function of calpain and caspase in beta-amyloid-induced cell dying in rat major septal cultured neurons. Neuropharmacology. 2008;54:721–33.
Amritraj A, Wang Y, Revett TJ, Vergote D, Westaway D, Kar S. Function of cathepsin D in U18666A-induced neuronal cell dying: potential implication in Niemann-Choose sort C illness pathogenesis. J Biol Chem. 2013;288:3136–52.
Hawkes C, Kabogo D, Amritraj A, Kar S. Up-regulation of cation-independent mannose 6-phosphate receptor and endosomal-lysosomal markers in surviving neurons after 192-IgG-saporin administrations into the grownup rat mind. Am J Pathol. 2006;169:1140–54.
Maulik M, Ghoshal B, Kim J, Wang Y, Yang J, Westaway D, Kar S. Mutant human APP exacerbates pathology in a mouse mannequin of NPC and its reversal by a beta-cyclodextrin. Hum Mol Genet. 2012;21:4857–75.
Wu Q, Cortez L, Kamali-Jamil R, Sim V, Wille H, Kar S. Implication of exosomes derived from cholesterol-accumulated astrocytes in Alzheimer’s illness pathology. Dis Mannequin Mech. 2021. https://doi.org/10.1242/dmm.048929.
Lin H, Yue Y, Maidana DE, Bouzika P, Atik A, Matsumoto H, Miller JW, Vavvas DG. Drug supply nanoparticles: toxicity comparability in retinal pigment epithelium and retinal vascular endothelial cells. Semin Ophthalmol. 2016;31:1–9.
Lukasiewicz S, Mikolajczyk A, Blasiak E, Fic E, Dziedzicka-Wasylewska M. Polycaprolactone nanoparticles as promising candidates for nanocarriers in novel nanomedicines. Pharmaceutics. 2021. https://doi.org/10.3390/pharmaceutics13020191.
Reiss AB, Arain HA, Stecker MM, Siegart NM, Kasselman LJ. Amyloid toxicity in Alzheimer’s illness. Rev Neurosci. 2018;29:613–27.
Zheng WH, Bastianetto S, Mennicken F, Ma W, Kar S. Amyloid beta peptide induces tau phosphorylation and lack of cholinergic neurons in rat major septal cultures. Neuroscience. 2002;115:201–11.
Teplow DB. Structural and kinetic options of amyloid beta-protein fibrillogenesis. Amyloid. 1998;5:121–42.
Galzitskaya OV, Galushko EI, Selivanova OM. Research of the method of amyloid formation by Abeta peptide. Biochemistry. 2018;83:S62–80.
Buell AK. The expansion of amyloid fibrils: charges and mechanisms. Biochem J. 2019;476:2677–703.
Kim HY, Choi I. Ultrafast colorimetric dedication of predominant protein construction evolution with gold nanoplasmonic particles. Nanoscale. 2016;8:1952–9.
Krol S, Macrez R, Docagne F, Defer G, Laurent S, Rahman M, Hajipour MJ, Kehoe PG, Mahmoudi M. Therapeutic advantages from nanoparticles: the potential significance of nanoscience in ailments with compromise to the blood mind barrier. Chem Rev. 2013;113:1877–903.
Huo X, Zhang Y, Jin X, Li Y, Zhang L. A novel synthesis of selenium nanoparticles encapsulated PLGA nanospheres with curcumin molecules for the inhibition of amyloid beta aggregation in Alzheimer’s illness. J Photochem Photobiol B. 2019;190:98–102.
Baysal I, Yabanoglu-Ciftci S, Tunc-Sarisozen Y, Ulubayram Okay, Ucar G. Interplay of selegiline-loaded PLGA-b-PEG nanoparticles with beta-amyloid fibrils. J Neural Transm. 2013;120:903–10.
Solar D, Li N, Zhang W, Zhao Z, Mou Z, Huang D, Liu J, Wang W. Design of PLGA-functionalized quercetin nanoparticles for potential use in Alzheimer’s illness. Colloids Surf B Biointerfaces. 2016;148:116–29.
Sharma S, Nehru B, Saini A. Inhibition of Alzheimer’s amyloid-beta aggregation in-vitro by carbenoxolone: perception into mechanism of motion. Neurochem Int. 2017;108:481–93.
Aalinkeel R, Kutscher HL, Singh A, Cwiklinski Okay, Khechen N, Schwartz SA, Prasad PN, Mahajan SD. Neuroprotective results of a biodegradable poly(lactic-co-glycolic acid)-ginsenoside Rg3 nanoformulation: a possible nanotherapy for Alzheimer’s illness? J Drug Goal. 2018;26:182–93.
Silva-Abreu M, Calpena AC, Andres-Benito P, Aso E, Romero IA, Roig-Carles D, Gromnicova R, Espina M, Ferrer I, Garcia ML, Male D. PPARgamma agonist-loaded PLGA-PEG nanocarriers as a possible remedy for Alzheimer’s illness: in vitro and in vivo research. Int J Nanomed. 2018;13:5577–90.
Lee J, Culyba EK, Powers ET, Kelly JW. Amyloid-beta types fibrils by nucleated conformational conversion of oligomers. Nat Chem Biol. 2011;7:602–9.
Hayden EY, Hoi KK, Lopez J, Inayathullah M, Condron MM, Teplow DB. Identification of key areas and residues controlling Abeta folding and meeting. Sci Rep. 2017;7:12434.
Gremer L, Scholzel D, Schenk C, Reinartz E, Labahn J, Ravelli RBG, Tusche M, Lopez-Iglesias C, Hoyer W, Heise H, et al. Fibril construction of amyloid-beta(1–42) by cryo-electron microscopy. Science. 2017;358:116–9.
Thapa A, Jett SD, Chi EY. Curcumin attenuates amyloid-beta combination toxicity and modulates amyloid-beta aggregation pathway. ACS Chem Neurosci. 2016;7:56–68.
Andarzi Gargari S, Barzegar A, Tarinejad A. The function of phenolic OH teams of flavonoid compounds with H-bond formation capacity to suppress amyloid mature fibrils by destabilizing beta-sheet conformation of monomeric Abeta17–42. PLoS ONE. 2018;13:e0199541.
Andrade S, Ramalho MJ, Loureiro JA, Pereira MDC. Pure compounds for Alzheimer’s illness remedy: a scientific overview of preclinical and medical research. Int J Mol Sci. 2019;20:2313.
Kanchi PK, Dasmahapatra AK. Polyproline chains destabilize the Alzheimer’s amyloid-beta protofibrils: a molecular dynamics simulation research. J Mol Graph Mannequin. 2019;93:107456.
Stefanescu R, Stanciu GD, Luca A, Paduraru L, Tamba BI. Secondary metabolites from crops possessing inhibitory properties towards beta-amyloid aggregation as revealed by Thioflavin-T assay and correlations with investigations on transgenic mouse fashions of Alzheimer’s illness. Biomolecules. 2020;10:870.
Ahmed M, Davis J, Aucoin D, Sato T, Ahuja S, Aimoto S, Elliott JI, Van Nostrand WE, Smith SO. Structural conversion of neurotoxic amyloid-beta(1–42) oligomers to fibrils. Nat Struct Mol Biol. 2010;17:561–7.
Sonzini S, Stanyon HF, Scherman OA. Reducing amyloid toxicity by means of an elevated charge of aggregation. Phys Chem Chem Phys. 2017;19:1458–65.
Gast Okay, Modler AJ, Damaschun H, Krober R, Lutsch G, Zirwer D, Golbik R, Damaschun G. Impact of environmental circumstances on aggregation and fibril formation of barstar. Eur Biophys J. 2003;32:710–23.
Anand R, Gill KD, Mahdi AA. Therapeutics of Alzheimer’s illness: previous, current and future. Neuropharmacology. 2014;76:27–50.
Herrmann N, Chau SA, Kircanski I, Lanctot KL. Present and rising drug remedy choices for Alzheimer’s illness: a scientific overview. Medicine. 2011;71:2031–65.
Avgerinos KI, Ferrucci L, Kapogiannis D. Results of monoclonal antibodies towards amyloid-beta on medical and biomarker outcomes and hostile occasion dangers: a scientific overview and meta-analysis of part III RCTs in Alzheimer’s illness. Ageing Res Rev. 2021;68:101339.
Mukhopadhyay S, Banerjee D. A primer on the evolution of Aducanumab: the primary antibody accredited for remedy of Alzheimer’s illness. J Alzheimers Dis. 2021. https://doi.org/10.3233/JAD-215065.
Fornaguera C, Feiner-Gracia N, Caldero G, Garcia-Celma MJ, Solans C. Galantamine-loaded PLGA nanoparticles, from nano-emulsion templating, as novel superior drug supply methods to deal with neurodegenerative ailments. Nanoscale. 2015;7:12076–84.
Jeon SG, Cha MY, Kim JI, Hwang TW, Kim KA, Kim TH, Track KC, Kim JJ, Moon M. Vitamin D-binding protein-loaded PLGA nanoparticles suppress Alzheimer’s disease-related pathology in 5XFAD mice. Nanomedicine. 2019;17:297–307.
Eckenhoff RG, Johansson JS, Wei H, Carnini A, Kang B, Wei W, Pidikiti R, Keller JM, Eckenhoff MF. Inhaled anesthetic enhancement of amyloid-beta oligomerization and cytotoxicity. Anesthesiology. 2004;101:703–9.
Du Z, Li M, Ren J, Qu X. Present methods for modulating Abeta aggregation with multifunctional brokers. Acc Chem Res. 2021;54:2172–84.
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