References

1. Osbourn, A.E.; Lanzotti, V. Plant-Derived Natural Products: Synthesis, Function, and Application; Springer Science & Business Media: New York, NY, USA, 2009; p. 612.
2. Esposito, E.R.; Bystrek, M.V.; Klein, J.S. An Elective Course in Aromatherapy Science. Am. J. Pharm. Edu. 2014, 78, 79.
3. Robins, J.L.W. The Science and Art of Aromatherapy. J. Holist. Nurs. 1999, 17, 5–17.
4. Smith, C.A.; Collins, C.T.; Crowther, C.A. Aromatherapy for pain management in labour. Cochrane Database Syst. Rev. 2011.
5. Garcia-Salas, P.; Morales-Soto, A.; Segura-Carretero, A.; Fernández-Gutiérrez, A. Phenolic-compound-extraction systems for fruit and vegetable samples. Molecules 2010, 15, 8813–8826.
6. Singer, A.C.; Crowley, D.E.; Thompson, I.P. Secondary plant metabolites in phytoremediation and biotransformation. Trends Biotechnol. 2003, 21, 123–130.
7. Hsieh, M.T.; Peng, W.H.; Wu, C.R.; Wang, W.H. The ameliorating effects of the cognitive-enhancing Chinese herbs on scopolamine-induced amnesia in rats. Phytother. Res. 2000, 14, 375–377.
8. Cioanca, O.; Mircea, C.; Hritcu, L.; Trifan, A.; Marius, M.; Aprotosoaie, A.C.; Robu, S.; Gille, E.; Hancianu, M. In vitro—In vivo correlation of the antioxidant capacity of Salviae aetheroleum essential oil. Farmacia 2015, 63, 34–39.
9. Jové, M.; Portero-Otín, M.; Naudí, A.; Ferrer, I.; Pamplona, R. Metabolomics of Human Brain Aging and Age-Related Neurodegenerative Diseases. J. Neuropath. Exp. Neur. 2014, 73, 640–657.
10. Yan, M.H.; Wang, X.; Zhu, X. Mitochondrial defects and oxidative stress in Alzheimer disease and Parkinson disease. Free Radic. Biol. Med. 2013, 62, 90–101.
11. Sarrafchi, A.; Bahmani, M.; Shirzad, H.; Rafieian-Kopaei, M. Oxidative stress and Parkinson’s disease: New hopes in treatment with herbal antioxidants. Curr. Pharm. Des. 2016, 22, 238–246.
12. González-Burgos, E.; Gómez-Serranillos, M.P. Terpene compounds in nature: A review of their potential antioxidant activity. Curr. Med. Chem. 2012, 19, 5319–5341.
13. Essa, M.; Braidy, N.; Bridge, W.; Subash, S.; Manivasagam, T.; Vijayan, R.; Al-Adawi, S.; Guillemin, G. Review of natural products on Parkinson’s disease pathology. J. Aging Res. Clin. Pract 2014, 3, 1–8.
14. Karakaya, S.; Koca, M.; Yılmaz, S.V.; Yıldırım, K.; Pınar, N.M.; Demirci, B.; Brestic, M.; Sytar, O. Molecular Docking Studies of Coumarins Isolated from Extracts and Essential Oils of Zosima absinthifolia Link as Potential Inhibitors for Alzheimer’s Disease. Molecules 2019, 24, 722.
15. Forrester, L.T.; Maayan, N.; Orrell, M.; Spector, A.E.; Buchan, L.D.; Soares-Weiser, K. Aromatherapy for dementia. Cochrane Database Syst. Rev. 2014, CD003150, 1–56.
16. Xu, P.; Wang, K.; Lu, C.; Dong, L.; Gao, L.; Yan, M.; Aibai, S.; Yang, Y.; Liu, X. Protective effects of linalool against amyloid beta-induced cognitive deficits and damages in mice. Life Sci. 2017, 174, 21–27.
17. Bansal, A.; Kirschner, M.; Zu, L.; Cai, D.; Zhang, L. Coconut oil decreases expression of amyloid precursor protein (APP) and secretion of amyloid peptides through inhibition of ADP-ribosylation factor 1 (ARF1). Brain Res. 2019, 1704, 78–84.
18. Dalai, M.; Bhadra, S.; Chaudhary, S.; Bandyopadhyay, A.; Mukherjee, P. Anti-cholinesterase potential of Cinnamomum tamala (Buch.-Ham.) T.Nees & Eberm. leaves. Indian J. Tradit. Know. 2014, 13, 691–697.
19. Sihoglu Tepe, A.; Ozaslan, M. Anti-Alzheimer, anti-diabetic, skin-whitening, and antioxidant activities of the essential oil of Cinnamomum zeylanicum. Ind. Crop. Prod. 2020, 145, 112069.
20. Bahadori, M.B.; Salehi, P.; Sonboli, A. Comparative study of the essential oil composition of Salvia urmiensis and its enzyme inhibitory activities linked to diabetes mellitus and Alzheimer’s disease. Int. J. Food Prop. 2017, 20, 2974–2981.
21. Cutillas, A.B.; Carrasco, A.; Martinez-Gutierrez, R.; Tomas, V.; Tudela, J. Salvia officinalis L. Essential Oils from Spain: Determination of Composition, Antioxidant Capacity, Antienzymatic, and Antimicrobial Bioactivities. Chem. Biodivers. 2017; 14.
22. Ayaz, M.; Junaid, M.; Ullah, F.; Sadiq, A.; Khan, M.A.; Ahmad, W.; Shah, M.R.; Imran, M.; Ahmad, S. Comparative chemical profiling, cholinesterase inhibitions and anti-radicals properties of essential oils from Polygonum hydropiper L: A Preliminary anti- Alzheimer’s study. Lipids Health Dis. 2015, 14, 141.
23. Ali-Shtayeh, M.S.; Abu-Zaitoun, S.Y.; Dudai, N.; Jamous, R.M. Downy Lavender Oil: A Promising Source of Antimicrobial, Antiobesity, and Anti-Alzheimer’s Disease Agents. Evid-Based Complement. Altern. Med. 2020, 2020, 5679408.
24. Soheili, M.; Khalaji, F.; Mirhashemi, M.; Salami, M. The Effect of Essential Oil of Lavandula Angustifolia on Amyloid Beta Polymerization: An In Vitro Study. Iran. J. Chem. Chem. Eng. 2018, 37, 201–207.
25. Chaiyana, W.; Okonogi, S. Inhibition of cholinesterase by essential oil from food plant. Phytomedicine 2012, 19, 836–839.
26. Shoaib, M.; Shah, I.; Ali, N.; Ali, W. In vitro acetylcholinesterase and butyrylcholinesterase inhibitory potentials of essential oil of Artemisia macrocephala. Bangladesh J. Pharm. 2015, 10, 87–91.
27. Ansari, M.; Eslami, H. Preparation and study of the inhibitory effect of nano-niosomes containing essential oil from artemisia absinthium on amyloid fibril formation. Nanomed. J. 2020, 7, 243–250.
28. Kabuto, H.; Yamanushi, T.T. Effects of zingerone [4-(4-hydroxy-3-methoxyphenyl)-2-butanone] and eugenol [2-methoxy-4-(2-propenyl) phenol] on the pathological progress in the 6-hydroxydopamine-induced parkinson’s disease mouse model. Neurochem. Res. 2011, 36, 2244.
29. Alzheimer’s Association. 2019 Alzheimer’s disease facts and figures. Alzheimer’s Dement. 2019, 15, 321–387.
30. Reitz, C.; Mayeux, R. Alzheimer disease: Epidemiology, diagnostic criteria, risk factors and biomarkers. Biochem. Pharm. 2014, 88, 640–651.
31. Ferretti, C.; Sarti, F.M.; Nitrini, R.; Ferreira, F.F.; Brucki, S.M.D. An assessment of direct and indirect costs of dementia in Brazil. PLoS ONE 2018, 13, e0193209.
32. Weintraub, S.; Wicklund, A.H.; Salmon, D.P. The neuropsychological profile of Alzheimer disease. Cold Spring Harb. Perspect. Med. 2012, 2, a006171.
33. Aliev, G.; Palacios, H.H.; Walrafen, B.; Lipsitt, A.E.; Obrenovich, M.E.; Morales, L. Brain mitochondria as a primary target in the development of treatment strategies for Alzheimer disease. Int. J. Biochem. Cell Biol. 2009, 41, 1989–2004.
34. Serrano-Pozo, A.; Mielke, M.L.; Gómez-Isla, T.; Betensky, R.A.; Growdon, J.H.; Frosch, M.P.; Hyman, B.T. Reactive glia not only associates with plaques but also parallels tangles in Alzheimer’s disease. Am. J. Pathol. 2011, 179, 1373–1384.
35. Villa, V.; Thellung, S.; Bajetto, A.; Gatta, E.; Robello, M.; Novelli, F.; Tasso, B.; Tonelli, M.; Florio, T. Novel celecoxib analogues inhibit glial production of prostaglandin E2, nitric oxide, and oxygen radicals reverting the neuroinflammatory responses induced by misfolded prion protein fragment 90–231 or lipopolysaccharide. Pharm. Res. 2016, 113, 500–514.
36. Masters, C.L.; Selkoe, D.J. Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease. Cold Spring Harb. Perspect. Med. 2012, 2, a006262.
37. Nhan, H.S.; Chiang, K.; Koo, E.H. The multifaceted nature of amyloid precursor protein and its proteolytic fragments: Friends and foes. Acta. Neuropathol. 2015, 129, 1–19.
38. Campora, M.; Francesconi, V.; Schenone, S.; Tasso, B.; Tonelli, M. Journey on Naphthoquinone and Anthraquinone Derivatives: New Insights in Alzheimer’s Disease. Pharmaceuticals 2021, 14, 33.
39. Kocahan, S.; Doğan, Z. Mechanisms of Alzheimer’s Disease Pathogenesis and Prevention: The Brain, Neural Pathology, N-methyl-D-aspartate Receptors, Tau Protein and Other Risk Factors. Clin. Psychopharmacol. Neurosci. 2017, 15, 1–8.
40. Zheng, H.; Fridkin, M.; Youdim, M.B. From antioxidant chelators to site-activated multi-target chelators targeting hypoxia inducing factor, beta-amyloid, acetylcholinesterase and monoamine oxidase A/B. Mini Rev. Med. Chem. 2012, 12, 364–370.
41. Huang, L.; Lu, C.; Sun, Y.; Mao, F.; Luo, Z.; Su, T.; Jiang, H.; Shan, W.; Li, X. Multitarget-directed benzylideneindanone derivatives: Anti-β-amyloid (Aβ) aggregation, antioxidant, metal chelation, and monoamine oxidase B (MAO-B) inhibition properties against Alzheimer’s disease. J. Med. Chem. 2012, 55, 8483–8492.
42. Youdim, M.B.H.; Amit, T.; Bar-Am, O.; Weinreb, O.; Yogev-Falach, M. Implications of co-morbidity for etiology and treatment of neurodegenerative diseases with multifunctional neuroprotective-neurorescue drugs; ladostigil. Neurotox. Res. 2006, 10, 181–192.
43. Bar-Am, O.; Amit, T.; Weinreb, O.; Youdim, M.B.; Mandel, S. Propargylamine containing compounds as modulators of proteolytic cleavage of amyloid-beta protein precursor: Involvement of MAPK and PKC activation. J. Alzheimers Dis. 2010, 21, 361–371.
44. Yogev-Falach, M.; Bar-Am, O.; Amit, T.; Weinreb, O.; Youdim, M.B. A multifunctional, neuroprotective drug, ladostigil (TV3326), regulates holo-APP translation and processing. FASEB J. 2006, 20, 2177–2179.
45. Weinreb, O.; Amit, T.; Bar-Am, O.; Sagi, Y.; Mandel, S.; Youdim, M.B.H. Involvement of multiple survival signal transduction pathways in the neuroprotective, neurorescue and APP processing activity of rasagiline and its propargyl moiety. In Parkinson’s Disease and Related Disorders, 2nd ed.; Springer: Vienna, Austria, 2006; Volume 70, pp. 457–465.
46. Cai, Z. Monoamine oxidase inhibitors: Promising therapeutic agents for Alzheimer’s disease (Review). Mol. Med. Rep. 2014, 9, 1533–1541.
47. Manouchehrabadi, M.; Farhadi, M.; Azizi, Z.; Torkaman-Boutorabi, A. Carvacrol Protects Against 6-Hydroxydopamine-Induced Neurotoxicity in In Vivo and In Vitro Models of Parkinson’s Disease. Neurotox Res. 2020, 37, 156–170.
48. Fahn, S. Description of Parkinson’s disease as a clinical syndrome. Ann. N. Y. Acad. Sci. 2003, 991, 1–14.
49. Goedert, M. Alpha-synuclein and neurodegenerative diseases. Nat. Rev. Neurosci. 2001, 2, 492–501.
50. Jellinger, K.A. The pathology of Parkinson’s disease. Adv. Neurol. 2001, 86, 55–72.
51. Spillantini, M.G.; Crowther, R.A.; Jakes, R.; Hasegawa, M.; Goedert, M. α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodies. Proc. Natl. Acad. Sci. USA 1998, 95, 6469–6473.
52. Schulz, J.B. Update on the pathogenesis of Parkinson’s disease. J. Neurol. 2008, 255, 3–7.
53. Blum, D.; Torch, S.; Lambeng, N.; Nissou, M.; Benabid, A.L.; Sadoul, R.; Verna, J.M. Molecular pathways involved in the neurotoxicity of 6-OHDA, dopamine and MPTP: Contribution to the apoptotic theory in Parkinson’s disease. Prog. Neurobiol. 2001, 65, 135–172.
54. Wexler, N.S. Venezuelan kindreds reveal that genetic and environmental factors modulate Huntington’s disease age of onset. Proc. Natl. Acad. Sci. USA 2004, 101, 3498–3503.
55. Quarrell, O.W.; Nance, M.A.; Nopoulos, P.; Paulsen, J.S.; Smith, J.A.; Squitieri, F. Managing juvenile Huntington’s disease. Neurodegener. Dis. Manag. 2013, 3, 267–276.
56. Lee, J.M.; Ramos, E.M.; Lee, J.H.; Gillis, T.; Mysore, J.S.; Hayden, M.R.; Warby, S.C.; Morrison, P.; Nance, M.; Ross, C.A.; et al. CAG repeat expansion in Huntington disease determines age at onset in a fully dominant fashion. Neurology 2012, 78, 690–695.
57. Koutsis, G.; Karadima, G.; Kladi, A.; Panas, M. Late-onset Huntington’s disease: Diagnostic and prognostic considerations. Parkinsonism Relat. D. 2014, 20, 726–730.
58. Miller, R.G.; Mitchell, J.D.; Lyon, M.; Moore, D.H. Riluzole for amyotrophic lateral sclerosis (ALS)/motor neuron disease (MND). Cochrane Database Syst. Rev. 2007, 7, 1–26.
59. Katyal, N.; Govindarajan, R. Shortcomings in the current amyotrophic lateral sclerosis trials and potential solutions for improvement. Front. Neurol. 2017, 8, 521.
60. Al-Chalabi, A.; Jones, A.; Troakes, C.; King, A.; Al-Sarraj, S.; van den Berg, L.H. The genetics and neuropathology of amyotrophic lateral sclerosis. Acta. Neuropathol. 2012, 124, 339–352.
61. Menke, R.A.; Körner, S.; Filippini, N.; Douaud, G.; Knight, S.; Talbot, K.; Turner, M.R. Widespread grey matter pathology dominates the longitudinal cerebral MRI and clinical landscape of amyotrophic lateral sclerosis. Brain 2014, 137, 2546–2555.
62. Hadzhieva, M.; Kirches, E.; Wilisch-Neumann, A.; Pachow, D.; Wallesch, M.; Schoenfeld, P.; Paege, I.; Vielhaber, S.; Petri, S.; Keilhoff, G. Dysregulation of iron protein expression in the G93A model of amyotrophic lateral sclerosis. Neuroscience 2013, 230, 94–101.
63. De Assis Lima, I.V.; Bastos, L.F.S.; Limborço-Filho, M.; Fiebich, B.L.; de Oliveira, A.C.P. Role of prostaglandins in neuroinflammatory and neurodegenerative diseases. Mediat. Inflamm. 2012, 2012, 1–13.
64. Bassam, A.-S. Antibacterial activities of some plant extracts utilized in popular medicine in Palestine. Turk. J. Biol. 2004, 28, 99–102.
65. Rios, J.-L.; Recio, M. Medicinal plants and antimicrobial activity. J. Ethnopharmacol. 2005, 100, 80–84.
66. Donelian, A.; Carlson, L.H.C.; Lopes, T.J.; Machado, R.A.F. Comparison of extraction of patchouli (Pogostemon cablin) essential oil with supercritical CO2 and by steam distillation. J. Supercrit. Fluids 2009, 48, 15–20.
67. Irshad, M.; Subhani, M.A.; Ali, S.; Hussain, A. Biological Importance of Essential Oils. In Essential Oils-Oils of Nature; El-Shemy, H.A., Ed.; IntechOpen: London, UK, 2020.
68. Natural Living Ideas. The 10 Most Popular Essential Oils & 174 Magical Ways To Use Them. Available online: (accessed on 12 December 2020).
69. Movahhedin, N.; Zengin, G.; Bahadori, M.B.; Sarikurkcu, C.; Bahadori, S.; Dinparast, L. Ajuga chamaecistus subsp. scoparia (Boiss.) Rech.f.: A new source of phytochemicals for antidiabetic, skin-care, and neuroprotective uses. Ind. Crop. Prod. 2016, 94, 89–96.
70. Bahadori, S.; Bahadori, M.B.; Zengin, G.; Maggi, F.; Dinparast, L.; Aktumsek, A. Chemical composition profile of the essential oil from Hymenocrater bituminous and its health functionality. Int. J. Food Prop. 2017, 20, S972–S980.
71. Karakaya, S.; Eksi, G.; Koca, M.; Demirci, B.; Kaymak, H.C.; Kaplan, M.E.; Aksakal, O. Chemical and morphological characterization of Allium tuncelianum (Amaryllidaceae) and its antioxidant and anticholinesterase potentials. Jard. Bot. Madr. 2019, 76, 85.
72. Lamamra, M.; Laouer, H.; Amira, S.; Erdogan Orhan, I.; Senol, F.; Demirci, B.; Akkal, S. Chemical Composition and Cholinesterase Inhibitory Activity of Different Parts of Daucus aristidis Coss. Essential Oils from Two Locations in Algeria. Rec. Nat. Prod. 2017, 11, 147–156.
73. Jyotshna; Srivastava, N.; Singh, B.; Chanda, D.; Shanker, K. Chemical composition and acetylcholinesterase inhibitory activity of Artemisia maderaspatana essential oil. Pharm. Biol. 2015, 53, 1677–1683.
74. Kohoude, M.J.; Gbaguidi, F.; Agbani, P.; Ayedoun, M.A.; Cazaux, S.; Bouajila, J. Chemical composition and biological activities of extracts and essential oil of Boswellia dalzielii leaves. Pharm. Biol. 2017, 55, 33–42.
75. Ali-Shtayeh, M.S.; Jamous, R.M.; Abu-Zaitoun, S.Y.; Akkawi, R.J.; Kalbouneh, S.R.; Bernstein, N.; Dudai, N. Chemical profile and bioactive properties of the essential oil isolated from Clinopodium serpyllifolium (M.Bieb.) Kuntze growing in Palestine. Ind. Crop. Prod. 2018, 124, 617–625.
76. Arruda, M.; Viana, H.; Rainha, N.; Neng, N.R.; Rosa, J.S.; Nogueira, J.M.F.; Barreto, M.d.C. Anti-acetylcholinesterase and antioxidant activity of essential oils from Hedychium gardnerianum Sheppard ex Ker-Gawl. Molecules 2012, 17, 3082–3092.
77. Murata, K.; Tanaka, K.; Akiyama, R.; Noro, I.; Nishio, A.; Nakagawa, S.; Matsumura, S.; Matsuda, H. Anti-cholinesterase Activity of Crude Drugs Selected from the Ingredients of Incense Sticks and Heartwood of Chamaecyparis obtusa. Nat. Prod. Commun. 2018, 13.
78. Ademosun, A.O.; Oboh, G.; Olupona, A.J.; Oyeleye, S.I.; Adewuni, T.M.; Nwanna, E.E. Comparative Study of Chemical Composition, In Vitro Inhibition of Cholinergic and Monoaminergic Enzymes, and Antioxidant Potentials of Essential Oil from Peels and Seeds of Sweet Orange (Citrus Sinensis [L.] Osbeck) Fruits. J. Food Biochem. 2016, 40, 53–60.
79. Tundis, R.; Loizzo, M.R.; Bonesi, M.; Menichini, F.; Mastellone, V.; Colica, C.; Menichini, F. Comparative Study on the Antioxidant Capacity and Cholinesterase Inhibitory Activity of Citrus aurantifolia Swingle, C. aurantium L., and C. bergamia Risso and Poit. Peel Essential Oils. J. Food Sci. 2012, 77, H40–H46.
80. Loizzo, M.; Ben Jemia, M.; Senatore, F.; Bruno, M.; Menichini, F.; Tundis, R. Chemistry and functional properties in prevention of neurodegenerative disorders of five Cistus species essential oils. Food Chem. Toxicol 2013, 59.
81. Sadlon, A.E.; Lamson, D.W. Immune-modifying and antimicrobial effects of Eucalyptus oil and simple inhalation devices. Altern. Med. Rev. 2010, 15, 33–47.
82. ESCOP. Alchemillae Herba, The Scientific Foundation for Herbal Medicinal Products. Available online: (accessed on 12 December 2020).
83. Juergens, U.R. Anti-inflammatory properties of the monoterpene 1.8-cineole: Current evidence for co-medication in inflammatory airway diseases. Drug Res. 2014, 64, 638–646.
84. El Euch, S.K.; Hassine, D.B.; Cazaux, S.; Bouzouita, N.; Bouajila, J. Salvia officinalis essential oil: Chemical analysis and evaluation of anti-enzymatic and antioxidant bioactivities. S. Afr. J. Bot. 2019, 120, 253–260.
85. Abuhamdah, S.; Abuhamdah, R.; Howes, M.J.; Al-Olimat, S.; Ennaceur, A.; Chazot, P.L. Pharmacological and neuroprotective profile of an essential oil derived from leaves of Aloysia citrodora Palau. J. Pharm. Pharm. 2015, 67, 1306–1315.
86. CSID:2656. 1,8-cineole. Available online: (accessed on 15 January 2021).
87. CSID:6402. α-pinene. Available online: (accessed on 15 January 2021).
88. CSID:14198. β-pinene. Available online: (accessed on 15 January 2021).
89. CSID:28952. Zingerone. Available online: (accessed on 15 January 2021).
90. CSID:388386. Limonene. Available online: (accessed on 15 January 2021).
91. CSID:390582. Ferruginol. Available online: (accessed on 15 January 2021).
92. CSID:454172. Kaur-16-ene. Available online: (accessed on 15 January 2021).
93. CSID:4474888. Rosmarinic acid. Available online: (accessed on 15 January 2021).
94. CSID:13849981. Linalool. Available online: (accessed on 15 January 2021).
95. CSID:21105867. Carvacrol. Available online: (accessed on 15 January 2021).
96. Cutillas, A.B.; Carrasco, A.; Martinez-Gutierrez, R.; Tomas, V.; Tudela, J. Thymus mastichina L. essential oils from Murcia (Spain): Composition and antioxidant, antienzymatic and antimicrobial bioactivities. PLoS ONE 2018, 13, e0190790.
97. Montalván, M.; Peñafiel, M.A.; Ramírez, J.; Cumbicus, N.; Bec, N.; Larroque, C.; Bicchi, C.; Gilardoni, G. Chemical Composition, Enantiomeric Distribution, and Sensory Evaluation of the Essential Oils Distilled from the Ecuadorian Species Myrcianthes myrsinoides (Kunth) Grifo and Myrcia mollis (Kunth) DC. (Myrtaceae). Plants 2019, 8, 511.
98. Dhanasekaran, S.; Perumal, P.; Palayan, M. In-vitro Screening for acetylcholinesterase enzyme inhibition potential and antioxidant activity of extracts of Ipomoea aquatica Forsk: Therapeutic lead for Alzheimer’s disease. J. Appl. Pharm. Sci. 2015, 5, 012–016.
99. Silver, A. The Biology of Cholinesterases, North-Holland Publishing Company: Amsterdam, The Netherlands, 1974; 1–596.
100. Wilson, B.; Philip, W. Cholinesterase inhibition. In Encyclopedia of Toxicology; Elsevier: New York, NY, USA, 2005; pp. 588–599.
101. Wilson, B.W. CHAPTER 48-Cholinesterases. In Handbook of Pesticide Toxicology, 2nd ed.; Krieger, R.I., Krieger, W.C., Eds.; Academic Press: San Diego, CA, USA, 2001; pp. 967–985.
102. Chatonnet, A.; Lockridge, O. Comparison of butyrylcholinesterase and acetylcholinesterase. Biochem. J. 1989, 260, 625–634.
103. Schwarz, M.; Glick, D.; Loewenstein, Y.; Soreq, H. Engineering of human cholinesterases explains and predicts diverse consequences of administration of various drugs and poisons. Pharm. Ther. 1995, 67, 283–322.
104. Tecles, F.; Ceron, J. Determination of whole blood cholinesterase in different animal species using specific substrates. Res. Vet. Sci. 2001, 70, 233–238.
105. Sramek, J.J.; Cutler, N.R. RBC cholinesterase inhibition: A useful surrogate marker for cholinesterase inhibitor activity in Alzheimer disease therapy? Alzheimer Dis. Assoc. Disord 2000, 14, 216–227.
106. Nicolet, Y.; Lockridge, O.; Masson, P.; Fontecilla-Camps, J.C.; Nachon, F. Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. J. Biol. Chem. 2003, 278, 41141–41147.
107. Saxena, A.; Redman, A.M.; Jiang, X.; Lockridge, O.; Doctor, B.P. Differences in active site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase. Biochemistry 1997, 36, 14642–14651.
108. Xu, Y.; Colletier, J.-P.; Weik, M.; Jiang, H.; Moult, J.; Silman, I.; Sussman, J.L. Flexibility of aromatic residues in the active-site gorge of acetylcholinesterase: X-ray versus molecular dynamics. Biophys. J. 2008, 95, 2500–2511.
109. Dighe, S.N.; Deora, G.S.; de la Mora, E.; Nachon, F.; Chan, S.; Parat, M.-O.; Brazzolotto, X.; Ross, B.P. Discovery and Structure–Activity Relationships of a Highly Selective Butyrylcholinesterase Inhibitor by Structure-Based Virtual Screening. J. Med. Chem. 2016, 59, 7683–7689.
110. Zhou, Y.; Lu, X.; Du, C.; Liu, Y.; Wang, Y.; Hong, K.H.; Chen, Y.; Sun, H. Novel BuChE-IDO1 inhibitors from sertaconazole: Virtual screening, chemical optimization and molecular modeling studies. Bioorg. Med. Chem. Lett. 2021, 34, 127756.
111. Miles, J.A.; Kapure, J.S.; Deora, G.S.; Courageux, C.; Igert, A.; Dias, J.; McGeary, R.P.; Brazzolotto, X.; Ross, B.P. Rapid discovery of a selective butyrylcholinesterase inhibitor using structure-based virtual screening. Bioorg. Med. Chem. Lett. 2020, 30, 127609.
112. Ellman, G.L.; Courtney, K.D.; Andres, V., Jr.; Featherstone, R.M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharm. 1961, 7, 88–95.
113. Pohanka, M.; Jun, D.; Kuca, K. Improvement of acetylcholinesterase-based assay for organophosphates in way of identification by reactivators. Talanta 2008, 77, 451–454.
114. Morizono, M.; Akinaga, Y. Studies on Tissue Cholinesterase in Domestic Animals II. Detection of Tissue Cholinesterase Isoenzymes. Mem. Fac. Agr. Kagoshima. Univ. 1981, 17, 219–234.
115. Frasco, M.; Fournier, D.; Carvalho, F.; Guilhermino, L. Do metals inhibit acetylcholinesterase (AChE)? Implementation of assay conditions for the use of AChE activity as a biomarker of metal toxicity. Biomarkers 2005, 10, 360–375.
116. Šinko, G.; Čalić, M.; Bosak, A.; Kovarik, Z. Limitation of the Ellman method: Cholinesterase activity measurement in the presence of oximes. Anal. Biochem. 2007, 370, 223–227.
117. Marrs, T.C. Organophosphates: History, chemistry, pharmacology. In Organophosphates and Health; Imperial College Press: London, UK, 2001; pp. 1–36.
118. Michel, H.O. An electrometric method for the determination of red blood cell and plasma cholinesterase activity. J. Lab. Clin. Med. 1949, 34, 1564–1568.
119. Selkoe, D.J. Alzheimer’s disease: Genes, proteins, and therapy. Physiol. Rev. 2001, 81, 742–760.
120. Rochette, M.; Murphy, M. Gamma-secretase: Substrates and inhibitors. Mol. Neurobiol. 2002, 26, 81–95.
121. Lee, V.M.; Goedert, M.; Trojanowski, J.Q. Neurodegenerative tauopathies. Annu Rev. Neurosci. 2001, 24, 1121–1159.
122. Satou, T.; Cummings, B.J.; Head, E.; Nielson, K.A.; Hahn, F.F.; Milgram, N.W.; Velazquez, P.; Cribbs, D.H.; Tenner, A.J.; Cotman, C.W. The progression of β-amyloid deposition in the frontal cortex of the aged canine. Brain Res. 1997, 774, 35–43.
123. Cummings, B.J.; Head, E.; Afagh, A.J.; Milgram, N.W.; Cotman, C.W. β-amyloid accumulation correlates with cognitive dysfunction in the aged canine. Neurobiol. Learn. Mem. 1996, 66, 11–23.
124. De Felice, F.G.; Munoz, D.P. Opportunities and challenges in developing relevant animal models for Alzheimer’s disease. Ageing Res. Rev. 2016, 26, 112–114.
125. Casadesus, G. Handbook of Animal Models in Alzheimer’s Disease, 1st ed.; IOS Press: Amsterdam, The Netherlands, 2011; Volume 1, p. 340.
126. Lecanu, L.; Papadopoulos, V. Modeling Alzheimer’s disease with non-transgenic rat models. Alzheimer’s Res. 2013, 5, 17.
127. Temel, H.E.; Demirci, B.; Demirci, F.; Celep, F.; Kahraman, A.; Doğan, M.; Hüsnü Can Başer, K. Chemical characterization and anticholinesterase effects of essential oils derived from Salvia species. J. Essent Oil Res. 2016, 28, 322–331.
128. Demirezer, L.; Gürbüz, P.; Kelicen Uğur, E.P.; Bodur, M.; Özenver, N.; Uz, A.; Güvenalp, Z. Molecular docking and ex vivo and in vitro anticholinesterase activity studies of Salvia sp. and highlighted rosmarinic acid. Turk. J. Med. Sci. 2015, 45, 1141–1148.
129. Videira, R.; Castanheira, P.; Grãos, M.; Salgueiro, L.; Faro, C.; Cavaleiro, C. A necrodane monoterpenoid from Lavandula luisieri essential oil as a cell-permeable inhibitor of BACE-1, the β-secretase in Alzheimer’s disease. Flavour Frag J. 2013, 28, 380–388.
130. Baser, K.H. Biological and pharmacological activities of carvacrol and carvacrol bearing essential oils. Curr Pharm. Des. 2008, 14, 3106–3119.
131. Kaufmann, D.; Dogra, A.; Wink, M. Myrtenal inhibits acetylcholinesterase, a known Alzheimer target. J. Pharm. Pharm. 2011, 63, 1368–1371.
132. Jukic, M.; Politeo, O.; Maksimovic, M.; Milos, M.; Milos, M. In vitro acetylcholinesterase inhibitory properties of thymol, carvacrol and their derivatives thymoquinone and thymohydroquinone. Phytother. Res. 2007, 21, 259–261.
133. Melo, F.H.; Venâncio, E.T.; de Sousa, D.P.; de França Fonteles, M.M.; de Vasconcelos, S.M.; Viana, G.S.; de Sousa, F.C. Anxiolytic-like effect of Carvacrol (5-isopropyl-2-methylphenol) in mice: Involvement with GABAergic transmission. Fundam. Clin. Pharm. 2010, 24, 437–443.
134. Melo, F.H.; Moura, B.A.; de Sousa, D.P.; de Vasconcelos, S.M.; Macedo, D.S.; Fonteles, M.M.; Viana, G.S.; de Sousa, F.C. Antidepressant-like effect of carvacrol (5-Isopropyl-2-methylphenol) in mice: Involvement of dopaminergic system. Fundam. Clin. Pharm. 2011, 25, 362–367.
135. Krishtal, J.; Bragina, O.; Metsla, K.; Palumaa, P.; Tõugu, V. In situ fibrillizing amyloid-beta 1-42 induces neurite degeneration and apoptosis of differentiated SH-SY5Y cells. PLoS ONE 2017, 12, e0186636.
136. Xu, W.; Yang, L.; Li, J. Protection against β-amyloid-induced neurotoxicity by naturally occurring Z-ligustilide through the concurrent regulation of p38 and PI3-K/Akt pathways. Neurochem. Int. 2016, 100, 44–51.
137. Pike, C.J.; Walencewicz-Wasserman, A.J.; Kosmoski, J.; Cribbs, D.H.; Glabe, C.G.; Cotman, C.W. Structure-activity analyses of β-amyloid peptides: Contributions of the β25–35 region to aggregation and neurotoxicity. J. Neurochem. 1995, 64, 253–265.
138. Kaminsky, Y.G.; Marlatt, M.W.; Smith, M.A.; Kosenko, E.A. Subcellular and metabolic examination of amyloid-β peptides in Alzheimer disease pathogenesis: Evidence for Aβ25–35. Exp. Neurol. 2010, 221, 26–37.
139. Gabbouj, S.; Ryhänen, S.; Marttinen, M.; Wittrahm, R.; Takalo, M.; Kemppainen, S.; Martiskainen, H.; Tanila, H.; Haapasalo, A.; Hiltunen, M.; et al. Altered Insulin Signaling in Alzheimer’s Disease Brain—Special Emphasis on PI3K-Akt Pathway. Front. Neurosci. 2019, 13.
140. Wu, Y.; Han, X.; Yuan, W.; Wang, X.; Meng, D.; Hu, J.; Lv, Z. Salt intervention for the diversities of essential oil composition, aroma and antioxidant activities of Kushui rose (R. setate× R. rugosa). Ind. Crop. Prod. 2020, 150, 112417.
141. Hsu, H.; Hsu, C. Commonly used Chinese herb formulas with illustrations, 2nd ed.; Oriental Healing Arts Institute: Long Beach, CA, USA, 1980; Volume 1, p. 671.
142. Wang, M.C.; Bohmann, D.; Jasper, H. JNK signaling confers tolerance to oxidative stress and extends lifespan in Drosophila. Dev. Cell 2003, 5, 811–816.
143. Wang, M.C.; Bohmann, D.; Jasper, H. JNK extends life span and limits growth by antagonizing cellular and organism-wide responses to insulin signaling. Cell 2005, 121, 115–125.
144. Gulactı, T.; Ufuk, K.; Mehmet, O.; Mehmet, B.; Seda Damla, H.; Fatemeh, B.; Burcu, C.; Tuncay, D. Investigation of Anticholinesterase Activity of a Series of Salvia Extracts and the Constituents of Salvia staminea. Nat. Prod. J. 2013, 3, 3–9.
145. Liu, B.; Kou, J.; Li, F.; Huo, D.; Xu, J.; Zhou, X.; Meng, D.; Ghulam, M.; Artyom, B.; Gao, X.; et al. Lemon essential oil ameliorates age-associated cognitive dysfunction via modulating hippocampal synaptic density and inhibiting acetylcholinesterase. Aging 2020, 12, 8622–8639.
146. Chen, J.; Montanari, A.M.; Widmer, W.W. Two New Polymethoxylated Flavones, a Class of Compounds with Potential Anticancer Activity, Isolated from Cold Pressed Dancy Tangerine Peel Oil Solids. J. Agric. Food Chem. 1997, 45, 364–368.
147. Nogata, Y.; Sakamoto, K.; Shiratsuchi, H.; Ishii, T.; Yano, M.; Ohta, H. Flavonoid Composition of Fruit Tissues of Citrus Species. Biosci. Biotechnol. Biochem. 2006, 70, 178–192.
148. Ayuob, N.N.; El Wahab, M.G.A.; Ali, S.S.; Abdel-Tawab, H.S. Ocimum basilicum improve chronic stress-induced neurodegenerative changes in mice hippocampus. Metab. Brain Dis. 2018, 33, 795–804.
149. Avetisyan, A.; Markosian, A.; Petrosyan, M.; Sahakyan, N.; Babayan, A.; Aloyan, S.; Trchounian, A. Chemical composition and some biological activities of the essential oils from basil Ocimum different cultivars. BMC Complement. Altern. Med. 2017, 17, 60.
150. Batista, P.A.; Werner, M.F.; Oliveira, E.C.; Burgos, L.; Pereira, P.; Brum, L.F.; Story, G.M.; Santos, A.R. The antinociceptive effect of (-)-linalool in models of chronic inflammatory and neuropathic hypersensitivity in mice. J. Pain 2010, 11, 1222–1229.
151. Elisabetsky, E.; Marschner, J.; Souza, D.O. Effects of Linalool on glutamatergic system in the rat cerebral cortex. Neurochem. Res. 1995, 20, 461–465.
152. Letizia, C.S.; Cocchiara, J.; Lalko, J.; Api, A.M. Fragrance material review on linalool. Food Chem. Toxicol. 2003, 41, 943–964.
153. Mitić-Culafić, D.; Zegura, B.; Nikolić, B.; Vuković-Gacić, B.; Knezević-Vukcević, J.; Filipic, M. Protective effect of linalool, myrcene and eucalyptol against t-butyl hydroperoxide induced genotoxicity in bacteria and cultured human cells. Food Chem. Toxicol. 2009, 47, 260–266.
154. Sabogal-Guáqueta, A.M.; Osorio, E.; Cardona-Gómez, G.P. Linalool reverses neuropathological and behavioral impairments in old triple transgenic Alzheimer’s mice. Neuropharmacology 2016, 102, 111–120.
155. Gradinariu, V.; Cioanca, O.; Hritcu, L.; Trifan, A.; Gille, E.; Hancianu, M. Comparative efficacy of Ocimum sanctum L. and Ocimum basilicum L. essential oils against amyloid beta (1–42)-induced anxiety and depression in laboratory rats. PhytoChem. Rev. 2014, 14, 1–9.
156. Jankovic, J.; Aguilar, L.G. Current approaches to the treatment of Parkinson’s disease. Neuropsych. Dis. Treat. 2008, 4, 743–757.
157. Beserra-Filho, J.I.; de Macêdo, A.M.; Leão, A.H.; Bispo, J.M.M.; Santos, J.R.; de Oliveira-Melo, A.J.; Menezes, P.D.P.; Duarte, M.C.; de Souza Araújo, A.A.; Silva, R.H. Eplingiella fruticosa leaf essential oil complexed with β-cyclodextrin produces a superior neuroprotective and behavioral profile in a mice model of Parkinson’s disease. Food Chem. Toxicol. 2019, 124, 17–29.
158. Ramazani, E.; YazdFazeli, M.; Emami, S.A.; Mohtashami, L.; Javadi, B.; Asili, J.; Tayarani-Najaran, Z. Protective effects of Cinnamomum verum, Cinnamomum cassia and cinnamaldehyde against 6-OHDA-induced apoptosis in PC12 cells. Mol. Biol. Rep. 2020, 7, 2437–2445.
159. Rao, P.V.; Gan, S.H. Cinnamon: A multifaceted medicinal plant. Evid-Based Complement. Altern. Med. 2014, 2014, 1–2.
160. Brahmachari, S.; Jana, A.; Pahan, K. Sodium benzoate, a metabolite of cinnamon and a food additive, reduces microglial and astroglial inflammatory responses. J. Immunol. 2009, 183, 5917–5927.
161. Mollazadeh, H.; Hosseinzadeh, H. Cinnamon effects on metabolic syndrome: A review based on its mechanisms. Iran. J. Basic Med. Sci. 2016, 19, 1258.
162. Liu, X.C.; Cheng, J.; Zhao, N.N.; Liu, Z.L. Insecticidal activity of essential oil of Cinnamomum cassia and its main constituent, trans-cinnamaldehyde, against the booklice, Liposcelis bostrychophila. Trop. J. Pharm. Res. 2014, 13, 1697–1702.
163. Nabavi, S.F.; di Lorenzo, A.; Izadi, M.; Sobarzo-Sánchez, E.; Daglia, M.; Nabavi, S.M. Antibacterial effects of cinnamon: From farm to food, cosmetic and pharmaceutical industries. Nutrients 2015, 7, 7729–7748.
164. Klein-Júnior, L.C.; dos Santos Passos, C.; Tasso de Souza, T.J.; Gobbi de Bitencourt, F.; Salton, J.; de Loreto Bordignon, S.A.; Henriques, A.T. The monoamine oxidase inhibitory activity of essential oils obtained from Eryngium species and their chemical composition. Pharm. Biol. 2016, 54, 1071–1076.
165. Youdim, M.B.; Bakhle, Y. Monoamine oxidase: Isoforms and inhibitors in Parkinson’s disease and depressive illness. Br. J. Pharm. 2006, 147, S287–S296.
166. Youdim, M.B.; Edmondson, D.; Tipton, K.F. The therapeutic potential of monoamine oxidase inhibitors. Nat. Rev. Neurosci. 2006, 7, 295–309.
167. Morshedi, D.; Nasouti, M. Essential Oils May Lead α-Synuclein towards Toxic Fibrils Formation. Parkinsons Dis. 2016, 2016, 6219249.
168. McCormack, A.L.; Mak, S.K.; Shenasa, M.; Langston, W.J.; Forno, L.S.; di Monte, D.A. Pathologic modifications of α-synuclein in 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine (MPTP)-treated squirrel monkeys. J. Neuropath Exp. Neur. 2008, 67, 793–802.
169. Ahmad, A.; Burns, C.S.; Fink, A.L.; Uversky, V.N. Peculiarities of copper binding to α-synuclein. J. Biomol. Struct. Dyn. 2012, 29, 825–842.
170. Mohammad-Beigi, H.; Shojaosadati, S.A.; Marvian, A.T.; Pedersen, J.N.; Klausen, L.H.; Christiansen, G.; Pedersen, J.S.; Dong, M.; Morshedi, D.; Otzen, D.E. Strong interactions with polyethylenimine-coated human serum albumin nanoparticles (PEI-HSA NPs) alter α-synuclein conformation and aggregation kinetics. Nanoscale 2015, 7, 19627–19640.
171. Silva, B.A.; Breydo, L.; Fink, A.L.; Uversky, V.N. Agrochemicals, α-synuclein, and Parkinson’s disease. Mol. Neurobiol. 2013, 47, 598–612.
172. Morshedi, D.; Aliakbari, F.; Tayaranian-Marvian, A.; Fassihi, A.; Pan-Montojo, F.; Pérez-Sánchez, H. Cuminaldehyde as the major component of Cuminum cyminum, a natural aldehyde with inhibitory effect on alpha-synuclein fibrillation and cytotoxicity. J. Food Sci. 2015, 80, H2336–H2345.
173. Ning, B.; Deng, M.; Zhang, Q.; Wang, N.; Fang, Y. β-Asarone inhibits IRE1/XBP1 endoplasmic reticulum stress pathway in 6-OHDA-induced parkinsonian rats. Neurochem. Res. 2016, 41, 2097–2101.
174. Ning, B.; Zhang, Q.; Wang, N.; Deng, M.; Fang, Y. β-Asarone regulates ER stress and autophagy via inhibition of the PERK/CHOP/Bcl-2/Beclin-1 Pathway in 6-OHDA-induced parkinsonian rats. Neurochem. Res. 2019, 44, 1159–1166.
175. Schröder, M.; Kaufman, R.J. ER stress and the unfolded protein response. Mutat Res./Fund Mol. M. 2005, 569, 29–63.
176. Ryu, E.J.; Harding, H.P.; Angelastro, J.M.; Vitolo, O.V.; Ron, D.; Greene, L.A. Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson’s disease. J. Neurosci. 2002, 22, 10690–10698.
177. Hoozemans, J.; van Haastert, E.; Eikelenboom, P.; de Vos, R.; Rozemuller, J.; Scheper, W. Activation of the unfolded protein response in Parkinson’s disease. Biochem. Biophys. Res. Commun. 2007, 354, 707–711.
178. Jiang, P.; Gan, M.; Ebrahim, A.S.; Lin, W.-L.; Melrose, H.L.; Yen, S.-H.C. ER stress response plays an important role in aggregation of α-synuclein. Mol. Neurodegener. 2010, 5, 1–15.
179. Gardner, B.M.; Pincus, D.; Gotthardt, K.; Gallagher, C.M.; Walter, P. Endoplasmic reticulum stress sensing in the unfolded protein response. Cold Spring Harb Perspect. Biol. 2013, 5, a013169.
180. Hotamisligil, G.S. Endoplasmic reticulum stress and atherosclerosis. Nat. Med. 2010, 16, 396–399.
181. Hotamisligil, G.S. Endoplasmic reticulum stress and the inflammatory basis of metabolic disease. Cell 2010, 140, 900–917.
182. Todd, D.J.; Lee, A.-H.; Glimcher, L.H. The endoplasmic reticulum stress response in immunity and autoimmunity. Nat. Rev. Immunol. 2008, 8, 663–674.
183. Senft, D.; Ze’ev, A.R. UPR, autophagy, and mitochondria crosstalk underlies the ER stress response. Trends Biochem. Sci. 2015, 40, 141–148.
184. Yorimitsu, T.; Nair, U.; Yang, Z.; Klionsky, D.J. Endoplasmic reticulum stress triggers autophagy. J. Biol. Chem. 2006, 281, 30299–30304.
185. Wei, Y.; Pattingre, S.; Sinha, S.; Bassik, M.; Levine, B. JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy. Mol. Cell 2008, 30, 678–688.
186. Kabuto, H.; Nishizawa, M.; Tada, M.; Higashio, C.; Shishibori, T.; Kohno, M. Zingerone [4-(4-hydroxy-3-methoxyphenyl)-2-butanone] prevents 6-hydroxydopamine-induced dopamine depression in mouse striatum and increases superoxide scavenging activity in serum. Neurochem. Res. 2005, 30, 325–332.
187. Kabuto, H.; Tada, M.; Kohno, M. Eugenol [2-methoxy-4-(2-propenyl) phenol] prevents 6-hydroxydopamine-induced dopamine depression and lipid peroxidation inductivity in mouse striatum. Biol. Pharm. Bull. 2007, 30, 423–427.
188. Siqueira-Lima, P.S.; Brito, R.G.; Araújo-Filho, H.G.; Santos, P.L.; Lucchesi, A.; Araújo, A.A.; Menezes, P.P.; Scotti, L.; Scotti, M.T.; Menezes, I.R. Anti-hyperalgesic effect of Lippia grata leaf essential oil complexed with β-cyclodextrin in a chronic musculoskeletal pain animal model: Complemented with a molecular docking and antioxidant screening. Biomed. Pharm. 2017, 91, 739–747.
189. Oliveira, M.A.; Guimarães, A.G.; Araújo, A.A.; Quintans-Júnior, L.J.; Quintans, J.S. New drugs or alternative therapy to blurring the symptoms of fibromyalgia—a patent review. Expert Opin. Pat. 2017, 27, 1147–1157.
190. Araújo-Filho, H.G.; Pereira, E.W.; Rezende, M.M.; Menezes, P.P.; Araújo, A.A.; Barreto, R.S.; Martins, A.O.; Albuquerque, T.R.; Silva, B.A.; Alcantara, I.S. D-limonene exhibits superior antihyperalgesic effects in a β-cyclodextrin-complexed form in chronic musculoskeletal pain reducing Fos protein expression on spinal cord in mice. Neuroscience 2017, 358, 158–169.
191. Santos, P.L.; Brito, R.G.; Quintans, J.S.S.; Araujo, A.A.S.; Menezes, I.R.A.; Brogden, N.K.; Quintans-Junior, L.J. Cyclodextrins as complexation agents to improve the anti-inflammatory drugs profile: A systematic review and meta-analysis. In Curr. Pharm. Des.; 2017; Volume 23, pp. 2096–2107.
192. Brito, R.G.; Araujo, A.A.; Quintans, J.S.; Sluka, K.A.; Quintans-Junior, L.J. Enhanced analgesic activity by cyclodextrins–a systematic review and meta-analysis. Expert Opin Drug Del. 2015, 12, 1677–1688.
193. Andrade, A.M.; Oliveira, J.P.; Santos, A.L.; Franco, C.R.; Antoniolli, Â.R.; Estevam, C.S.; Thomazzi, S.M. Preliminary study on the anti-inflammatory and antioxidant activities of the leave extract of Hyptis fruticosa Salzm. ex Benth., Lamiaceae. Rev. Bras. Farm. 2010, 20, 962–968.
194. De Lima, A.C.B.; Paixão, M.S.; Melo, M.; de Santana, M.T.; Damascena, N.P.; Dias, A.S.; Porto, Y.C.B.S.; Fernandes, X.A.; Santos, C.C.S.; Lima, C.A.; et al. Orofacial antinociceptive effect and antioxidant properties of the hydroethanol extract of Hyptis fruticosa salmz ex Benth. J. Ethnopharmacol. 2013, 146, 192–197.
195. Nemati, M.; Hemmati, A.A.; Najafzadeh, H.; Mansouri, M.T.; Khodayar, M.J. Evaluation of the Effects of Foeniculum vulgare Essence on Behavioral-Motor Disorders of Parkinson’s Disease induced by Reserpine in Ovariectomized and Non Ovariectomized Rats. Jundishapur J. Nat. Pharm. Prod. 2018, 13, e67391.
196. Tadaiesky, M.T.; Andreatini, R.; Vital, M.A. Different effects of 7-nitroindazole in reserpine-induced hypolocomotion in two strains of mice. Eur. J. Pharm. 2006, 535, 199–207.
197. Ben, J.; Soares, F.M.; Scherer, E.B.; Cechetti, F.; Netto, C.A.; Wyse, A.T. Running exercise effects on spatial and avoidance tasks in ovariectomized rats. Neurobiol. Learn. Mem. 2010, 94, 312–317.
198. Scott, E.L.; Zhang, Q.G.; Han, D.; Desai, B.N.; Brann, D.W. Long-term estrogen deprivation leads to elevation of Dickkopf-1 and dysregulation of Wnt/β-Catenin signaling in hippocampal CA1 neurons. Steroids 2013, 78, 624–632.
199. Sarkaki, A.; Badavi, M.; Hoseiny, N.; Gharibnaseri, M.K.; Rahim, F. Postmenopausal effects of intrastriatal estrogen on catalepsy and pallidal electroencephalogram in an animal model of Parkinson’s disease. Neuroscience 2008, 154, 940–945.
200. Namavar Jahromi, B.; Tartifizadeh, A.; Khabnadideh, S. Comparison of fennel and mefenamic acid for the treatment of primary dysmenorrhea. Int. J. Gynaecol. Obs. 2003, 80, 153–157.
201. Modaress Nejad, V.; Asadipour, M. Comparison of the effectiveness of fennel and mefenamic acid on pain intensity in dysmenorrhoea. East. Mediterr. Health J. 2006, 12, 423–427.
202. Betarbet, R.; Sherer, T.B.; MacKenzie, G.; Garcia-Osuna, M.; Panov, A.V.; Greenamyre, J.T. Chronic systemic pesticide exposure reproduces features of Parkinson’s disease. Nat. Neurosci. 2000, 3, 1301–1306.
203. Talpade, D.J.; Greene, J.G.; Higgins, D.S., Jr.; Greenamyre, J.T. In vivo labeling of mitochondrial complex I (NADH:ubiquinone oxidoreductase) in rat brain using [(3)H]dihydrorotenone. J. Neurochem. 2000, 75, 2611–2621.
204. Sherer, T.B.; Richardson, J.R.; Testa, C.M.; Seo, B.B.; Panov, A.V.; Yagi, T.; Matsuno-Yagi, A.; Miller, G.W.; Greenamyre, J.T. Mechanism of toxicity of pesticides acting at complex I: Relevance to environmental etiologies of Parkinson’s disease. J. Neurochem. 2007, 100, 1469–1479.
205. Issa, M.Y.; Ezzat, M.I.; Sayed, R.H.; Elbaz, E.M.; Omar, F.A.; Mohsen, E. Neuroprotective effects of Pulicaria undulata essential oil in rotenone model of parkinson’s disease in rats: Insights into its anti-inflammatory and anti-oxidant effects. S. Afr. J. Bot. 2020, 132, 289–298.
206. Liu, L.-L.; Yang, J.-L.; Shi, Y.-P. Phytochemicals and biological activities of Pulicaria species. Chem. Biodivers. 2010, 7, 327–349.
207. Liu, Q.; Sang Heon, K.; Yung-Wei, S.; Sok Cheon, P.; Wonwoong, L.; Jongki, H.; Jaehwan, J.; Kyoung Sang, C.; Songhee, J.; Byung-Soo, K. Neuroprotective effects of Suhexiang Wan on the in vitro and in vivo models of Parkinson’s disease. J. Tradit. Chin. Med. 2019, 39, 800–808.
208. Lee, K.S.; Lee, J.K.; Kim, H.G.; Kim, H.R. Differential Effects of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine on Motor Behavior and Dopamine Levels at Brain Regions in Three Different Mouse Strains. Korean J. Physiol. Pharm. 2013, 17, 89–97.
209. Nikolova, G.; Karamalakova, Y.; Kovacheva, N.; Stanev, S.; Zheleva, A.; Gadjeva, V. Protective effect of two essential oils isolated from Rosa damascena Mill. and Lavandula angustifolia Mill, and two classic antioxidants against L-dopa oxidative toxicity induced in healthy mice. Regul. Toxicol. Pharm. 2016, 81, 1–7.
210. Nikolova, G.; Karamalakova, Y.; Gadjeva, V. Reducing oxidative toxicity of L-dopa in combination with two different antioxidants: An essential oil isolated from Rosa Damascena Mill., and vitamin C. Toxicol. Rep. 2019, 6, 267–271.