(1) Alzheimer’s A. 2015 Alzheimer's disease facts and figures. Alzheimers Dement. (2015) 11: 332.
(2) Amaducci LA, Rocca WA, and Schoenberg BS. Origin of the distinction between Alzheimer's disease and senile dementia How history can clarify nosology. Neurology (1986) 36: 1497-1497.
(3) Prince M, Comas-Herrera A, Knapp M, Guerchet M, and Karagiannidou M. World Alzheimer report 2016: improving healthcare for people living with dementia: coverage, quality and costs now and in the future. London, UK: Alzheimer’s Disease International (2016).
(4) Muñoz-Torrero D. Acetylcholinesterase inhibitors as disease-modifying therapies for Alzheimer's disease. Curr. Med. Chem. (2008) 15: 2433-55.
(5) LaFerla FM, Green KN, and Oddo S. Intracellular amyloid-β in Alzheimer's disease. Nat. Rev. Neurosci. (2007) 8: 499.
(6) Ballatore C, Lee VM-Y, and Trojanowski JQ. Tau-mediated neurodegeneration in Alzheimer's disease and related disorders. Nat. Rev. Neurosci. (2007) 8: 663.
(7) Cheignon C, Tomas M, Bonnefont-Rousselot D, Faller P, Hureau C, and Collin F. Oxidative stress and the amyloid beta peptide in Alzheimer's disease. Redox Biol. (2018) 14: 450-64.
(8) Darvesh S, Hopkins DA, and Geula C. Neurobiology of butyrylcholinesterase. Nat. Rev. Neurosci. (2003) 4: 131.
(9) Mueller C, Perera G, Hayes RD, Shetty H, and Stewart R. Associations of acetylcholinesterase inhibitor treatment with reduced mortality in Alzheimer's disease: a retrospective survival analysis. Age Ageing (2017) 47: 88-94.
(10) Greig NH, Utsuki T, Ingram DK, Wang Y, Pepeu G, Scali C, Yu Q-S, Mamczarz J, Holloway HW, and Giordano T. Selective butyrylcholinesterase inhibition elevates brain acetylcholine, augments learning and lowers Alzheimer β-amyloid peptide in rodent. Proc. Natl. Acad. Sci. U.S.A. (2005) 102: 17213-8.
(11) Small DH, Moir RD, Fuller SJ, Michaelson S, Bush AI, Li QX, Milward E, Hilbich C, and Weidemann A. A protease activity associated with acetylcholinesterase releases the membrane-bound form of the amyloid protein precursor of Alzheimer's disease. Biochem. (1991) 30: 10795-9.
(12) Guillozet A, Mesulam MM, Smiley J, and Mash D. Butyrylcholinesterase in the life cycle of amyloid plaques. Ann. Neurol. (1997) 42: 909-18.
(13) Li Y, Hai S, Zhou Y, and Dong BR. Cholinesterase inhibitors for rarer dementias associated with neurological conditions. Syst. Rev. (2015). p. Cd009444.
(14) Šešok S, Bolle N, Kobal J, Bucik V, and B Vodušek D. Cognitive function in early clinical phase huntington disease after rivastigmine treatment. Psychiatr. Danub. (2014) 26: 239-48.
(15) Wszelaki N, Kuciun A, and Kiss A. Screening of traditional European herbal medicines for acetylcholinesterase and butyrylcholinesterase inhibitory activity. Acta Pharm. (2010) 60: 119-28.
(16) Adams M, Gmünder F, and Hamburger M. Plants traditionally used in age related brain disorders—A survey of ethnobotanical literature. J. Ethnopharmacol. (2007) 113: 363-81.
(17) Akram M and Nawaz A. Effects of medicinal plants on Alzheimer's disease and memory deficits. Neural Regen. Res. (2017) 12: 660.
(18) Su Y, Wang Q, Wang C, Chan K, Sun Y, and Kuang H. The treatment of Alzheimer's disease using Chinese medicinal plants: from disease models to potential clinical applications. J. Ethnopharmacol. (2014) 152: 403-23.
(19) Kurt BZ, Gazioğlu I, Sevgi E and Sönmez F. Anticholinesterase, Antioxidant, Antiaflatoxigenic Activities of Ten Edible Wild Plants from Ordu Area, Turkey. Iran J. Pharm. Res. (2018) 17: 1047.
(20) Raj V, Jain A, and Chaudhary J. Prunus armeniaca (Apricot): an overview. J Pharm. Res. (2012) 5: 3964-6.
(21) Rai I, Bachheti R, Saini C, Joshi A, and Satyan R. A review on phytochemical, biological screening and importance of Wild Apricot (Prunus armeniaca L.). Orient. Pharm. Exp. Med. (2016) 16: 1-15.
(22) Karsavuran N, Charehsaz M, Celik H, Asma BM, Yakıncı C, and Aydın A. Amygdalin in bitter and sweet seeds of apricots. Environ. Toxicol. Chem. (2014) 96: 1564-70.
(23) Katayama S, Ogawa H, and Nakamura S. Apricot carotenoids possess potent anti-amyloidogenic activity in vitro. J. Agric. Food Chem. (2011) 59: 12691-6.
(24) Cheng Y, Yang C, Zhao J, Tse HF, and Rong J. Proteomic identification of calcium-binding chaperone calreticulin as a potential mediator for the neuroprotective and neuritogenic activities of fruit-derived glycoside amygdalin. J. Nutr. Biochem. (2015) 26: 146-54.
(25) Yang C, Zhao J, Cheng Y, Li X, and Rong J. Bioactivity-guided fractionation identifies amygdalin as a potent neurotrophic agent from herbal medicine Semen Persicae extract. Biomed. Res. Int. (2014) 2014: 306857.
(26) Jorjani SI. Yadegar on Medicine and Pharmacology (Mohaghegh, M, ed.). Tehran: Iran: Institute of Islamic Studies in Tehran. (2003) 44: 31.[In Persian].
(27) Saeedi M, Babaie K, Karimpour-Razkenari E, Vazirian M, Akbarzadeh T, Khanavi M, Hajimahmoodi M, and Shams Ardekani MR. In vitro cholinesterase inhibitory activity of some plants used in Iranian traditional medicine. Nat. Prod. Res. (2017) 31: 2690-4.
(28) Saeedi M, Safavi M, Karimpour-Razkenari E, Mahdavi M, Edraki N, Moghadam FH, Khanavi M, and Akbarzadeh T. Synthesis of novel chromenones linked to 1, 2, 3-triazole ring system: Investigation of biological activities against Alzheimer’s disease. Bioorg. Chem. (2017) 70: 86-93.
(29) Gerlier D and Thomasset N. Use of MTT colorimetric assay to measure cell activation. J. Immunol. Methods. (1986) 94: 57-63.
(30) Singleton VL, Orthofer R, and Lamuela-Raventós RM.  Analysis of total phenols and other oxidation substrates and antioxidants by means of folin-ciocalteu reagent. Meth. Enzymol. (1999) 299: 152-78.
(31) Marinova D, Ribarova F, and Atanassova M. Total phenolics and total flavonoids in Bulgarian fruits and vegetables. J. Univ. Chem. Technol. Metallurgy (2005) 40: 255-60.
(32) Savic IM, Nikolic VD, Savic-Gajic IM, Nikolic LB, Ibric SR, and Gajic DG. Optimization of technological procedure for amygdalin isolation from plum seeds (Pruni domesticae semen). Front. Plant Sci. (2015) 6: 276.
(33) Lv W-F, Ding M-Y, and Zheng R. Isolation and quantitation of amygdalin in Apricot-kernel and Prunus Tomentosa Thunb. by HPLC with solid-phase extraction. J. Chromatogr. Sci. (2005) 43: 383-7.
(34) Suchaichit N, Kanokmedhakul S, Kanokmedhakul K, Moosophon P, Boonyarat C, Plekratoke K, Tearavarich R, and Suchaichit NP. Phytochemical investigation and acetylcholinesterase inhibitory activity of bark of Hymenodictyon orixense. Nat. Prod. Res. (2017): 1-4.
(35) Nugroho A, Choi JS, Hong J-P, and Park H-J. Anti-acetylcholinesterase activity of the aglycones of phenolic glycosides isolated from Leonurus japonicus. Asian Pac. J. Trop. Biomed. (2017) 7: 849-54.
(36) Mukherjee PK, Kumar V, Mal M, and Houghton PJ. Acetylcholinesterase inhibitors from plants. Phytomedicine (2007) 14: 289-300.
(37) Murray AP, Faraoni MB, Castro MJ, Alza NP, and Cavallaro V. Natural AChE inhibitors from plants and their contribution to Alzheimer’s disease therapy. Curr. Neuropharmacol. (2013) 11: 388-413.
(38) Yıldırım FA, Yıldırım AN, Şan B, Aşkın MA, and Polat M. Variability of phenolics and mineral composition in kernels of several bitter and sweet apricot (Prunus armeniaca Batsch.) cultivars. J. Food Agri. Environ. (2010) 8: 179-84.
(39) Stoewsand G, Anderson J, and Lamb R. Cyanide content of apricot kernels. J. Food Sci. (1975) 40: 1107-1107.
(40) Esmaeili S, Ara L, Hajimehdipoor H, Kolivand H, and Mohammadi Motamed S. Acetylcholinesterase inhibitory effects of some plants from Rosaceae. Res. J. Pharmacogn. (2015) 2: 33-7.
(41) Tan HP, Wong DZH, Ling SK, Chuah CH, and Kadir HA. Neuroprotective activity of galloylated cyanogenic glucosides and hydrolysable tannins isolated from leaves of Phyllagathis rotundifolia. Fitoterapia (2012) 83: 223-9.
(42) Vauzour D, Vafeiadou K, Rodriguez-Mateos A, Rendeiro C, and Spencer JP. The neuroprotective potential of flavonoids: a multiplicity of effects. Genes Nutr. (2008) 3:115-26.
(43) Dajas F, Rivera F, Blasina F, Arredondo F, Echeverry C, Lafon L, Morquio A, and Heizen H. Cell culture protection andin vivo neuroprotective capacity of flavonoids. Neurotox. Res. (2003) 5: 425-32.
(44) Checkoway H, Powers K, Smith-Weller T, Franklin GM, Longstreth Jr WT, and Swanson PD. Parkinson's disease risks associated with cigarette smoking, alcohol consumption, and caffeine intake. Am. J. Epidemiol. (2002) 155: 732-8.
(45) Tohda C, Tamura T, and Komatsu K. Repair of amyloid β (25–35)-induced memory impairment and synaptic loss by a Kampo formula, Zokumei-to. Brain Res. (2003) 990: 141-7.
(46) Xiang Z, Ho L, Valdellon J, Borchelt D, Kelley K, Spielman L, Aisen PS, and Pasinetti GM. Cyclooxygenase (COX)-2 and cell cycle activity in a transgenic mouse model of Alzheimer’s disease neuropathology. Neurobiol. Aging (2002) 23: 327-34.
(47) Yang H-Y, Chang H-K, Lee J-W, Kim Y-S, Kim H, Lee M-H, Shin M-S, Ham D-H, Park H-K, and Lee H. Amygdalin suppresses lipopolysaccharide-induced expressions of cyclooxygenase-2 and inducible nitric oxide synthase in mouse BV2 microglial cells. Neurol. Res. (2007) 29: 59-64.