[1]
Kim, B.M. The role of saikosaponins in therapeutic strategies for age-related diseases. oxid. Med. Cell Longev., 2018, 17, 1-10.
[2]
Thompson, L.M. An update on pharmacological approaches to neurodegenerative diseases. Nature, 2008, 452(7188), 707-708.
[3]
Scatena, R.; Martorana, G.E.; Bottoni, P.; Botta, G.; Pastore, P.; Giardina, B. An update on pharmacological approaches to neurodegenerative diseases. Expert Opin. Investig. Drugs, 2007, 16(1), 59-72.
[4]
Lucas, S.M.; Rothwell, N.J.; Gibson, R.M. The role of inflammation in CNS injury and disease. Br. J. Pharmacol., 2006, 147, S232-S240.
[5]
Linseman, D.A. Targeting oxidative stress for neuroprotection. Antioxid. Redox Signal., 2009, 11(3), 421-424.
[6]
Gomes, A.; Pimpão, R.C.; Fortalezas, S.; Figueira, I.; Miguel, C.; Aguiar, C.; Salgueiro, L.; Cavaleiro, C.; Gonçalves, M.J.; Clemente, A.; Costa, C.; Martins-Loução, M.A.; Ferreira, R.B.; Santos, C.N. Chemical characterization and bioactivity of phytochemicals from Iberian endemic Santolina semidentata and strategies for ex situ propagation. Ind. Crops Prod., 2015, 74, 505-513.
[7]
Woolley, J.D.; Khan, B.K.; Murthy, N.K.; Miller, B.L.; Rankin, K.P. The diagnostic challenge of psychiatric symptoms in neurodegenerative disease: rates of and risk factors for prior psychiatric diagnosis in patients with early neurodegenerative disease. J. Clin. Psychiatry, 2011, 72(2), 126-133.
[8]
Montero-Odasso, M.; Pieruccini-Faria, F.; Bartha, R.; Black, S.E.; Finger, E.; Freedman, M.; Greenberg, B.; Grimes, D.A.; Hegele, R.A.; Hudson, C.; Kleinstiver, P.W.; Lang, A.E.; Masellis, M.; McLaughlin, P.M.; Munoz, D.P.; Strother, S.; Swartz, R.H.; Symons, S.; Tartaglia, M.C.; Zinman, L.; Strong, M.J. ONDRI, Investigators.; McIlroy, W. Motor phenotype in neurodegenerative disorders: Gait and balance platform study design protocol for the ontario neurodegenerative research initiative (ONDRI). J. Alzheimers Dis., 2017, 59(2), 707-721.
[9]
Hervás, R.; Oroz, J.; Galera-Prat, A.; Goñi, O.; Valbuena, A.; Vera, A.M.; Gómez-Sicilia, A.; Losada-Urzáiz, F.; Uversky, V.N.; Menéndez, M.; Laurents, D.V.; Bruix, M.; Carrión-Vázquez, M. Common features at the start of the neurodegeneration cascade. PLoS Biol., 2012, 10(5), e1001-e1335.
[10]
Vadakkan, K.I. Neurodegenerative disorders share common features of “loss of function” states of a proposed mechanism of nervous system functions. Biomed. Pharmacother., 2016, 83, 412-430.
[11]
Gitler, A.D.; Dhillon, P.; Shorter, J. Neurodegenerative disease: Models, mechanisms, and a new hope. Dis. Model. Mech., 2017, 10(5), 499-502.
[12]
Behl, C. Alzheimer’s disease and oxidative stress: Implications for novel therapeutic approaches. Prog. Neurobiol., 1999, 57(3), 301-323.
[13]
Aruoma, O.I.; Bahorun, T.; Jen, L.S. Neuroprotection by bioactive components in medicinal and food plant extracts. Mutat. Res., 2003, 544(2-3), 203-215.
[14]
Rasool, M.; Malik, A.; Qureshi, M.S.; Manan, A.; Pushparaj, P.N.; Asif, M.; Qazi, M.H.; Qazi, A.M.; Kamal, M.A.; Gan, S.H.; Sheikh, I.A. Recent updates in the treatment of neurodegenerative disorders using natural compounds. Evid. Based Complement. Alternat. Med., 2014, 2014, 979-730.
[15]
Rubinsztein, D.C. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature, 2006, 443(7113), 780-786.
[16]
Hussain, R.; Zubair, H.; Pursell, S.; Shahab, M. Neurodegenerative diseases: Regenerative mechanisms and novel therapeutic approaches. Brain Sci., 2018, 8(9), E177.
[17]
Teles, R.B.A.; Diniz, T.C.; Pinto, T.C.C.; De Oliveira Júnior, R.G.; Silva, M.G.; Lavor, E.M.; Fernandes, A.W.C.; Oliveira, A.P.; Ribeiro, F.P.R.A.; Silva, A.A.M.; Cavalcante, T.C.F.; Quintans Júnior, L.J.; Almeida, J.R.G.S. Flavonoids as therapeutic agents in alzheimer’s and parkinson’s diseases: A systematic review of preclinical evidences. Oxid. Med. Cell. Longev., 2018, 2018, 1-21.
[18]
Borroni, E.; Bohrmann, B.; Grueninger, F.; Prinssen, E.; Nave, S.; Loetscher, H.; Chinta, S.J.; Rajagopalan, S.; Rane, A.; Siddiqui, A.; Ellenbroek, B.; Messer, J.; Pähler, A.; Andersen, J.K.; Wyler, R.; Cesura, A.M. Sembragiline: A novel, selective monoamine oxidase type B inhibitor for the treatment of Alzheimer’s disease. J. Pharmacol. Exp. Ther., 2017, 362, 413-423.
[19]
Reitz, C.; Mayeux, R. Alzheimer disease: Epidemiology, diagnostic criteria, risk factors and biomarkers. Biochem. Pharmacol., 2014, 88, 640-651.
[20]
Tan, R.H.; Kril, J.J.; Yang, Y.; Tom, N.; Hodges, J.R.; Villemagne, V.L.; Rowe, C.C.; Leyton, C.E.; Kwok, J.B.J.; Ittner, L.M.; Halliday, G.M. Assessment of amyloid b in pathologically confirmed frontotemporal dementia syndromes. Alzheimers Dement. (Amst.), 2017, 9, 10-20.
[21]
Tong, T.; Ledig, C.; Guerrero, R.; Schuh, A.; Koikkalainen, J.; Tolonen, A.; Rhodius, H.; Barkhof, F.; Tijms, B.; Lemstra, A.W.; Soininen, H.; Remes, A.M.; Waldemar, G.; Hasselbalch, S.; Mecocci, P.; Baroni, M.; Lötjönen, J.; Flier, W.V.; Rueckert, D. Five-class differential diagnostics of neurodegenerative diseases usingrandom undersampling boosting. Neuroimage Clin., 2017, 15, 613-624.
[22]
Picanço, L.C.S.; Ozela, P.F.; Pinheiro, A.A.; Padilha, E.C.; Braga, F.S.; De Paula Da Silva, C.H.T.; Dos Santos, C.B.R.; Rosa, J.M.C.; Hage-Melim, L.I.S. Alzheimer’s disease: A review from the pathophysiology to diagnosis, new perspectives for pharmacological treatment. Curr. Med. Chem., 2017, 24, 1-19.
[23]
Mishra, C.B.; Manral, A.; Kumari, S.; Saini, V.; Tiwari, M. Design, synthesis and evaluation of novel indandione derivatives as multifunctional agents with cholinesterase inhibition, anti-bamyloid aggregation, antioxidant and neuroprotection properties against Alzheimer’s disease. Bioorg. Med. Chem., 2016, 24, 3829-3841.
[24]
Hussain, G.; Zhang, L.; Rasul, A.; Anwar, H.; Sohail, M.U.; Razzaq, A.; Aziz, N.; Shabbir, A.; Ali, M.; Sun, T. Role of plant-derived flavonoids and their mechanism in attenuation of Alzheimer’s and Parkinson’s diseases: An update of recent data. Molecules, 2018, 23, 814.
[25]
Kolahdouzan, M.; Hamadeh, M.J. The neuroprotective effects of caffeine in neurodegenerative diseases. CNS Neurosci. Ther., 2017, 23(4), 272-290.
[26]
Alzheimer’s Association. 2018 Alzheimer’s disease facts and figures. Alzheimers Dement., 2018, 14, 367-429.
[27]
Zufferey, V.; Donati, A.; Popp, J.; Meuli, R.; Rossier, J.; Frackowiak, R.; Draganski, B.; Von Gunten, A.; Kherif, F. Neuroticism, depression, and anxiety traits exacerbate the state of cognitive impairment and hippocampal vulnerability to Alzheimer’s disease. Alzheimers Dement. (Amst.), 2017, 7, 107-114.
[28]
Bui, T.T.; Nguyen, T.H. Natural product for the treatment of Alzheimer’s disease. J. Basic Clin. Physiol. Pharmacol., 2017, 28(5), 413-423.
[29]
Piechotta, A.; Parthier, C.; Kleinschmidt, M.; Gnoth, K.; Pillot, T.; Lues, I.; Demuth, H.U.; Schilling, S.; Rahfeld, J.U.; Stubbs, M.T. Structural and functional analyses of Pyroglutamate-Amyloid- β-Specific antibodies as a basis for Alzheimer Immunotherapy. J. Biol. Chem., 2017, 292(30), 12713-12724.
[30]
Kumar, A.; Ekavali, A.S. A review on Alzheimer’s disease pathophysiology and its management: An update. Pharmacol. Rep., 2015, 67, 195-203.
[31]
Picanço, L.C.S.; Castro, L.; Pinheiro, A.; Silva, K.; Souza, L.; Braga, F.; Silva, C.; Santos, B.C.; Hage-Melim, L.I.S. Study of molecular docking, physicochemical and pharmacokinetic properties of GSK-3β inhibitors. Br. J. Pharm. Res., 2015, 7, 152-175.
[32]
Rodrigues, R.P.; Silva, C.H.T.P. da Discovery of potential neurodegenerative inhibitors in Alzheimer’s disease by casein kinase 1 structure-based virtual screening. Med. Chem. Res., 2017, 26, 3274-3285.
[33]
Mishra, C.B.; Kumari, S.; Manral, A.; Prakash, A.; Saini, V.; Lynn, A.M.; Tiwari, M. Design, synthesis, in-silico and biological evaluation of novel donepezil derivatives as multi-target-directed ligands for the treatment of Alzheimer’s disease. Eur. J. Med. Chem., 2017, 125, 736-750.
[34]
Federico, L.B.; Almeida, J.R.; Taft, C.A.; Silva, C.H.T.P. Ligand and structure-based drug design as strategies for the screening of new BACE1 inhibitor candidates. Curr. Phys. Chem., 2016, 5, 253-262.
[35]
Dey, A.; Bhattacharya, R.; Mukherjee, A.; Panday, D.K. Natural products against Alzheimer’s disease: Pharmaco-therapeutics and biotechnological interventions. Biotechnol. Adv., 2017, 35(2), 178-216.
[36]
McKhann, G.M.; Albert, M.S.; Sperling, R.A. Changing diagnostic concepts
of Alzheimer’s Disease. In: Alzheimer’s Disease - Modernizing concept, biological
diagnosis and therapy; Hampel, H., Carrillo, M.C, EDs.; Basal, Switzerland:
Karger; 2012, Vol. 28, 28, 115-21.
[37]
Brito, M.F.B.; Ferreira, J.V.; Souza, L.R.; Gemaque, L.R.; Sousa, K.P.; Santos, C.F.; Braga, F.S.; Pernomian, L.; Silva, C.H.T.P.; Santos, C.B.R. Taft, Carlton A.; Hage-Melim, L.I.S. Computational molecular modeling of compounds from amaryllidaceae family as potential acetylcholinesterase inhibitors. Curr. Bioact. Compd., 2017, 13, 121-129.
[38]
Akram, M.; Nawaz, A. Effects of medicinal plants on alzheimer’s disease and memory deficits. Neural Regen. Res., 2017, 4(12), 660-670.
[39]
Silva, I.X.; Oliveira, M.G. Conceição, E.C.; Taft, C.A.; Da Silva, C.H.T.P.; Da Silva, V.B. Binding model of capsaicin is able to reach the peripheral anionic site of acetylcholinesterase. Curr. Bioact. Compd., 2017, 13(2), 152-156.
[40]
Xu, W.; Liu, J.; Ma, D.; Yuan, G.; Lu, Y.; Yang, Y. Capsaicin reduces Alzheimer-associated tau changes in the hippocampus of type 2 diabetes rats. PLoS One, 2017, 12(2), e0172477.
[41]
Chonpathompikunlert, P.; Wattanathorn, J.; Muchimapura, A. Piperine, the main alkaloid of Thai black pepper, protects against neurodegeneration and cognitive impairment in animal model of cognitive deficit like condition of Alzheimer’s disease. Food Chem. Toxicol., 2010, 48(3), 798-802.
[42]
Figueredo, A.S.; Oliveira, M.G.; Safadi, G.M.V.V.; da Silva, C.H.T.P.; da Silva, V.B.; Taft, C.A.; de Aquino, G.L.B. The natural alkaloid piperine and its acid and ester synthetic derivatives are acetylcholinesterase inhibitors. Curr. Phys. Chem., 2015, 5(4), 294-300.
[43]
Ghareeb, D.A.; Elahwany, A.M.D.; El-Mallawany, S.M.; Saif, A.A. In vitro screening for anti-acetylcholiesterase, anti-oxidant, anti-glucosidase, anti-inflammatory and anti-bacterial effect of three traditional medicinal plants. Biotechnol. Biotechnol. Equip., 2014, 28(6), 1155-1164.
[44]
Jung, H.A.; Min, B-S.; Yokozawa, T.; Lee, J-H.; Kim, Y.S.; Choi, J.S. Anti-Alzheimer and antioxidant activities of Coptidis Rhizoma alkaloids. Biol. Pharm. Bull., 2009, 32, 1433-1438.
[45]
Gunesch, S.; Schramm, S.; Decker, M. Natural antioxidants in hybrids for the treatment of neurodegenerative diseases: a successful strategy? Future Med. Chem., 2017, 9(8), 711-713.
[46]
Savica, R.; Grossardt, B.R.; Bower, J.H.; Eric Ahlskog, J.; Rocca, W.A. Time Trends in the Incidence of Parkinson Disease. JAMA Neurol., 2016, 73, 981-989.
[47]
Delamarre, A.; Meissner, W.G. Épidémiologie, facteurs de risque environnementaux et génétiques de la maladie de parkinson. Presse Med., 2017, 46, 175-181.
[48]
Hassan, A.; Benarroch, E.E. Heterogeneity of the midbrain dopamine system. Neurology, 2015, 85, 1795-1805.
[49]
Siciliano, M.; Trojano, L.; De Micco, R.; De Mase, A.; Garramone, F.; Russo, A.; Tedeschi, G.; Tessitore, A. Motor, behavioural, and cognitive correlates of fatigue in early, de novo parkinson disease patients. Parkinsonism Relat. Disord., 2017, 45, 63-68.
[50]
Niranjan, R. The role of inflammatory and oxidative stress mechanisms in the pathogenesis of parkinson’s disease: focus on astrocytes. Mol. Neurobiol., 2014, 49, 28-38.
[51]
Surmeier, D.J.; Obeso, J.A.; Halliday, G.M. Selective neuronal vulnerability in parkinson disease. Nat. Rev. Neurosci., 2017, 18, 101-113.
[52]
Kiriyama, Y.; Nochi, H. The Function of Autophagy in Neurodegenerative Diseases. Int. J. Mol. Sci., 2015, 16, 26797-26812.
[53]
Guerreiro, R.; Escott-Price, V.; Darwent, L.; Parkkinen, L.; Ansorge, O.; Hernandez, D.G.; Nalls, M.A.; Clark, L.; Honig, L.; Marder, K.; Van der Flier, W.; Holstege, H.; Louwersheimer, E.; Lemstra, A.; Scheltens, P.; Rogaeva, E.; St George-Hyslop, P.; Londos, E.; Zetterberg, H.; Ortega-Cubero, S.; Pastor, P.; Ferman, T.J.; Graff-Radford, N.R.; Ross, O.A.; Barber, I.; Braae, A.; Brown, K.; Morgan, K.; Maetzler, W.; Berg, D.; Troakes, C.; Al-Sarraj, S.; Lashley, T.; Compta, Y.; Revesz, T.; Lees, A.; Cairns, N.J.; Halliday, G.M.; Mann, D.; Pickering-Brown, S.; Powell, J.; Lunnon, K.; Lupton, M.K.; Dickson, D.; Hardy, J.; Singleton, A.; Bras, J. Genome-Wide analysis of genetic correlation in dementia with lewy bodies, parkinson’s and alzheimer’s diseases. Neurobiol. Aging, 2016, 38, 214.e7-214.e10.
[54]
Zhang, S.; Xiao, Q.; Le, W. Olfactory dysfunction and neurotransmitter disturbance in olfactory bulb of transgenic mice expressing human A53T mutant α-synuclein. PLoS One, 2015, 10.
[55]
Small, S.A.; Petsko, G.A. Retromer in alzheimer disease, parkinson disease and other neurological disorders. Nat. Rev. Neurosci., 2015, 16, 126-132.
[56]
McMillan, K.J.; Korswagen, H.C.; Cullen, P.J. The emerging role of retromer in neuroprotection. Curr. Opin. Cell Biol., 2017, 47, 72-82.
[57]
Manoharan, S.; Guillemin, G.J.; Abiramasundari, R.S.; Essa, M.M.; Akbar, M.; Akbar, M.D. The role of reactive oxygen species in the pathogenesis of alzheimer’s disease, parkinson’s disease, and huntington’s disease: A mini review. Oxi. Med. Cell. Longev., 2016, 2016
[58]
Buddhala, C.; Loftin, S.K.; Kuley, B.M.; Cairns, N.J.; Campbell, M.C.; Perlmutter, J.S.; Kotzbauer, P.T. Dopaminergic, serotonergic, and noradrenergic deficits in parkinson disease. Ann. Clin. Transl. Neurol., 2015, 2, 949-959.
[59]
Sauerbier, A.; Jenner, P.; Todorova, A.; Chaudhuri, K.R. Non motor subtypes and parkinson’s disease. Parkinsonism Relat. Disord., 2016, 22, S41-S46.
[60]
Schapira, A.H.V.; Chaudhuri, K.R.; Jenner, P. Non-Motor features of parkinson disease. Nat. Rev. Neurosci., 2017, 18, 435-450.
[61]
Quik, M.; Zhang, D.; McGregor, M.; Bordia, T. Alpha7 nicotinic receptors as therapeutic targets for parkinson’s disease. Biochem. Pharmacol., 2015, 97, 399-407.
[62]
Mogg, A.J.; Whiteaker, P.; McIntosh, J.M.; Marks, M.; Collins, A.C.; Wonnacott, S. Methyllycaconitine is a potent antagonist of alpha-conotoxin-mii-sensitive presynaptic nicotinic acetylcholine receptors in rat striatum. J. Pharmacol. Exp. Ther., 2002, 302, 197-204.
[63]
Chekani, F.; Bali, V.; Aparasu, R.; Mullen, P. A systematic review of the impact of adjuvant antiparkinson medications on disability and quality of life of patients with parkinson’s disease. Value Health, 2016, 19, A67.
[64]
Crispo, J.A.G.; Fortin, Y.; Thibault, D.P.; Emons, M.; Bjerre, L.M.; Kohen, D.E.; Perez-Lloret, S.; Mattison, D.; Willis, A.W.; Krewski, D. Trends in Inpatient antiparkinson drug use in the USA, 2001-2012. Eur. J. Clin. Pharmacol., 2015, 71, 1011-1019.
[65]
Mallajosyula, J.K.; Kaur, D.; Chinta, S.J.; Rajagopalan, S.; Rane, A.; Nicholls, D.G.; Di Monte, D.A.; Macarthur, H.; Andersen, J.K. MAO-B elevation in mouse brain astrocytes results in parkinson’s pathology. PLoS One, 2008, 3, e1616.
[66]
Lee, E.K.; Lee, Y.J. Prescription patterns of anticholinergic agents and their associated factors in korean elderly patients with dementia. Int. J. Clin. Pharm., 2013, 35, 711-718.
[67]
Bonifácio, M.J.; Torrão, L.; Loureiro, A.I.; Palma, P.N.; Wright, L.C.; Soares-Da-Silva, P. Pharmacological profile of opicapone, a third-generation nitrocatechol catechol-o-methyl transferase inhibitor, in the rat. Br. J. Pharmacol., 2015, 172, 1739-1752.
[68]
Poewe, W.; Antonini, A. Novel formulations and modes of delivery of levodopa. Mov. Disord., 2015, 30, 114-120.
[69]
Souza, L.R.; De Picanço, R.D.M.; Pinheiro, A.A.; Silva, K.R.; Taft, C.A.; Da Silva, C.H.T.P.; Santos, C.B.R.; Hage-Melim, L.I.S. Development of monoamine oxidase b inhibitors with antipark- inson activity. Curr. Phys. Chem., 2016, 6, 40-52.
[70]
Zhang, Z.; Li, G.; Szeto, S.S.W.; Chong, C.M.; Quan, Q.; Huang, C.; Cui, W.; Guo, B.; Wang, Y.; Han, Y.; Michael Siu, K.W.; Lee, Yuen. S.M.; Chu, I.K. Examining the neuroprotective effects of protocatechuic acid and chrysin on in vitro and in vivo models of parkinson disease. Free Radic. Biol. Med., 2015, 84, 331-343.
[71]
Ojha, S.; Javed, H.; Azimullah, S.; Haque, M.E. β-Caryophyllene, a phytocannabinoid attenuates oxidative stress, neuroinflammation, glial activation, and salvages dopaminergic neurons in a rat model of parkinson disease. Mol. Cell. Biochem., 2016, 418, 59-70.
[72]
Schober, A. Classic toxin-induced animal models of parkinson’s disease: 6-OHDA and MPTP. Cell Tissue Res., 2004, 318, 215-224.
[73]
Zhao, Z.; Wang, J.; Wang, L.; Yao, X.; Liu, Y.; Li, Y.; Chen, S.; Yue, T.; Wang, X.; Yu, W.; Liu, Y. Capsaicin protects against oxidative insults and alleviates behavioral deficits in rats with 6-OHDA-induced parkinson’s disease via activation of TRPV1. Neurochem. Res., 2017, 42(12), 3431-3438.
[74]
Baluchnejadmojarad, T.; Mansouri, M.; Ghalami, J.; Mokhtari, Z.; Roghani, M. Sesamin imparts neuroprotection against intrastriatal 6-hydroxydopamine toxicity by inhibition of astroglial activation, apoptosis, and oxidative stress. Biomed. Pharmacother., 2017, 88, 754-761.
[75]
Park, H.J.; Zhao, T.T.; Lee, K.S.; Lee, S.H.; Shin, K.S.; Park, K.H.; Choi, H.S.; Lee, M.K. Effects of (-)-sesamin on 6-hydroxydopamine-induced neurotoxicity in PC12 cells and dopaminergic neuronal cells of parkinson’s disease rat models. Neurochem. Int., 2015, 83-84, 19-27.
[76]
Jung, U.J.; Jeon, M-T.; Choi, M-S.; Kim, S.R. Silibinin attenuates mpp + -induced neurotoxicity in the substantia nigra in vivo. J. Med. Food, 2014, 17, 599-605.
[77]
Lee, Y.; Park, H.R.; Chun, H.J.; Lee, J. Silibinin prevents dopaminergic neuronal loss in a mouse model of parkinson’s disease via mitochondrial stabilization. J. Neurosci. Res., 2015, 93, 755-765.
[78]
Zhang, Z.; Li, G.; Szeto, S.S.W.; Chong, C.M.; Quan, Q.; Huang, C.; Cui, W.; Guo, B.; Wang, Y.; Han, Y.; Michael Siu, K.W.; Lee, Yuen. S.M.; Chu, I.K. Examining the neuroprotective effects of protocatechuic acid and chrysin on in vitro and in vivo models of parkinson disease. Free Radic. Biol. Med., 2015, 84, 331-343.
[79]
Abushouk, A.I.; Negida, A.; Ahmed, H.; Abdel-Daim, M.M. Neuroprotective mechanisms of plant extracts against mptp induced neurotoxicity: Future applications in parkinson’s disease. Biomed. Pharmacother., 2017, 85, 635-645.
[80]
Bitu Pinto, N.; Da Silva Alexandre, B.; Neves, K.R.T.; Silva, A.H.; Leal, L.K.A.M.; Viana, G.S.B. Neuroprotective properties of the standardized extract from camellia sinensis (green tea) and its main bioactive components, epicatechin and epigallocatechin gallate, in the 6-OHDA model of parkinson’s disease. Evid. Based Complement. Alternat. Med., 2015, 2015, 161092.
[81]
Chowdhury, A.; Sarkar, J.; Chakraborti, T.; Pramanik, P.K.; Chakraborti, S. Protective role of epigallocatechin-3-gallate in health and disease: A perspective. Biomed. Pharmacother., 2016, 78, 50-59.
[82]
Choi, D.Y.; Choi, H. Natural products from marine organisms with neuroprotective activity in the experimental models of alzheimer’s disease, parkinson’s disease and ischemic brain stroke: their molecular targets and action mechanisms. Arch. Pharm. Res., 2015, 38, 139-170.
[83]
Ravi, S.K.; Narasingappa, R.B.; Joshi, C.G.; Girish, T.K.; Vincent, B. Neuroprotective effects of cassia tora against paraquatinduced neurodegeneration: relevance for parkinson’s disease. Nat. Prod. Res., 2018, 32, 1476-1480.
[84]
Zhao, Q.; Yang, X.; Cai, D.; Ye, L.; Hou, Y.; Zhang, L.; Cheng, J.; Shen, Y.; Wang, K.; Bai, Y. Echinacoside protects against MPP+-induced neuronal apoptosis via ros/atf3/chop pathway regulation. Neurosci. Bull., 2016, 32, 349-362.
[85]
Li, M.; Zhou, F.; Xu, T.; Song, H.; Lu, B. Acteoside protects against 6-OHDA-induced dopaminergic neuron damage via Nrf2-ARE signaling pathway. Food Chem. Toxicol., 2018, 119, 6-13.
[86]
Zhang, H.; Bai, L.; He, J.; Zhong, L.; Duan, X.; Ouyang, L.; Zhu, Y.; Wang, T.; Zhang, Y.; Shi, J. Recent advances in discovery and development of natural products as source for anti-parkinson’s disease lead compounds. Eur. J. Med. Chem., 2017, 141, 257-272.
[87]
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.
[88]
Chen, W.C.; Lai, Y.S.; Lu, K.H.; Lin, S.H.; Liao, L.Y.; Ho, C.T.; Sheen, L.Y. Method development and validation for the high-performance liquid chromatography assay of gastrodin in water extracts from different sources of gastrodia elata blume. Food Drug Anal., 2015, 23, 803-810.
[89]
Jang, J.H.; Son, Y.; Kang, S.S.; Bae, C.S.; Kim, J.C.; Kim, S.H.; Shin, T.; Moon, C. Neuropharmacological potential of gastrodia elata blume and its components. Evid. Based Complement. Alternat. Med., 2015, 2015, 1-14.
[90]
Jiang, F.; Gao, R.; Liu, H.; Zhao, D.; Xu, P.; Zhang, L.; Qian, X. Neuroprotective effect of hyperoside on human pc12 cells against the oxidative damage. Int. J. Clin. Exp. Pathol., 2016, 9, 5176-5183.
[91]
Kiasalari, Z.; Baluchnejadmojarad, T.; Roghani, M. Hypericum perforatum hydroalcoholic extract mitigates motor dysfunction and is neuroprotective in intrastriatal 6-hydroxydopamine rat model of parkinson’s disease. Cell. Mol. Neurobiol., 2016, 36, 521-530.
[92]
Lu, C.; Zhang, J.; Shi, X.; Miao, S.; Bi, L.; Zhang, S.; Yang, Q.; Zhou, X.; Zhang, M.; Xie, Y.; Miao, Q.; Wang, S.W. Neuroprotective effects of tetramethylpyrazine against dopaminergic neuron injury in a rat model of parkinson’s disease induced by MPTP. Int. J. Biol. Sci., 2014, 10, 350-357.
[93]
Michel, H.E.; Tadros, M.G.; Esmat, A.; Khalifa, A.E.; Abdel-Tawab, A.M. Tetramethylpyrazine ameliorates rotenone-induced parkinson’s disease in rats: involvement of its anti-inflammatory and anti-apoptotic actions. Mol. Neurobiol., 2017, 54, 4866-4878.
[94]
Zheng, M.; Liu, C.; Fan, Y.; Yan, P.; Shi, D.; Zhang, Y. Neuroprotection by paeoniflorin in the mptp mouse model of parkinson’s disease. Neuropharmacology, 2017, 116, 412-420.
[95]
Manayi, A.; Omidpanah, S.; Barreca, D.; Ficarra, S.; Daglia, M.; Nabavi, S.F.; Nabavi, S.M. Neuroprotective effects of paeoniflorin in neurodegenerative diseases of the central nervous system. Phytochem. Rev., 2017, 16, 1173-1181.
[96]
Fan, Z.; Liang, Z.; Yang, H.; Pan, Y.; Zheng, Y.; Wang, X. Tenuigenin protects dopaminergic neurons from inflammation via suppressing nlrp3 inflammasome activation in microglia. J. Neuroinflammation, 2017, 14, 256.
[97]
Lu, L.; Li, X.; Xu, P.; Zheng, Y.; Wang, X. Tenuigenin down-regulates the release of nitric oxide, matrix metalloproteinase-9 and cytokines from lipopolysaccharide-stimulated microglia. Neurosci. Lett., 2017, 650, 82-88.
[98]
Lofrumento, D.D.; Nicolardi, G.; Cianciulli, A.; Nuccio, F.; De Pesa, V.; La Carofiglio, V.; Dragone, T.; Calvello, R.; Panaro, M.A. Neuroprotective effects of resveratrol in an mptp mouse model of parkinson’s-like disease: Possible role of socs-1 in reducing pro-inflammatory responses. Innate Immun., 2014, 20, 249-260.
[99]
Allen, E.N.; Potdar, S.; Tapias, V.; Parmar, M.; Mizuno, C.S.; Rimando, A.; Cavanaugh, J.E. Resveratrol and pinostilbene confer neuroprotection against aging-related deficits through an ERK1/2-dependent mechanism. J. Nutr. Biochem., 2018, 54, 77-86.
[100]
Hu, Q.; Uversky, V.N.; Huang, M.; Kang, H.; Xu, F.; Liu, X.; Lian, L.; Liang, Q.; Jiang, H.; Liu, A.; Zhang, C.; Pan-Montojo, F.; Zhu, S. Baicalein inhibits α-synuclein oligomer formation and prevents progression of α-synuclein accumulation in a rotenone mouse model of parkinson’s disease. Biochim. Biophys. Acta, 2016, 1862, 1883-1890.
[101]
Zhu, Q.; Zhuang, X.; Lu, J. Neuroprotective effects of baicalein in animal
models of parkinson’s disease: A systematic review of experimental studies. phytomedicine, 2018, phytomedicine.
[102]
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(2), 238-246.
[103]
Huang, Y.Y.; Zhang, Q.; Zhang, J.N.; Zhang, Y.N.; Gu, L.; Yang, H.M.; Xia, N.; Wang, X.M.; Zhang, H. Triptolide up-regulates metabotropic glutamate receptor 5 to inhibit microglia activation in the lipopolysaccharide-induced model of parkinson’s disease. Brain Behav. Immun., 2018, 71, 93-107.
[104]
Jiang, M.; Yun, Q.; Niu, G.; Gao, Y.; Shi, F.; Yu, S. puerarin prevents inflammation and apoptosis in the neurocytes of a murine parkinson’s disease model. Genet. Mol. Res., 2016, •••, 15.
[105]
Shiying, L.; Xinhui, Q.; Guanghua, J.; Feng, N.; Feng, L.; Shumei, C.; Fan, H. puerarin promoted proliferation and differentiation of dopamine-producing cells in parkinson’s animal models. Biomed. Pharmacother., 2018, 106, 1236-1242.
[106]
Fernández-Moriano, C.; González-Burgos, E.; Gómez-Serranillos, M.P. Mitochondria-Targeted protective compounds in parkinson’s and alzheimer’s diseases. Oxid. Med. Cell. Longev., 2015, 2015, 408927.
[107]
Liu, H.; Ma, S.; Xia, H.; Lou, H.; Zhu, F.; Sun, L. Anti-inflammatory activities and potential mechanisms of phenolic acids isolated from salvia miltiorrhiza f. alba roots in thp-1 macrophages. J. Ethnopharmacol., 2018, 222, 201-207.
[108]
Mccolgan, P.; Tabrizi, S.J. Huntington’s disease: A clinical review. Eur. J. Neurol., 2017, 25(1), 24-34.
[109]
Pandey, M.; Rajamma, U. Huntington’s disease: The coming of age. J. Genet., 2018, 97(3), 649-664.
[110]
Wexler, A.; Wild, E.J.; Tabrizi, S.J. George Huntington: A legacy of inquiry, empathy and hope. Brain, 2016, 139, 2326-2333.
[111]
Veenhuizen, R.; Nijsten, H.; Van Roosmalen, P.; Lammertsen, K.; Stor, T.; De Jager, L.; De Man, J.; Van Der Doelen, R.; Landa, K.; Grond, V.; Heffels, J.; Groenewoud, R.; Rovers, L.; Bakker, C.; Leiwakabessy, S.; Van Der Wedden, D.; Van Blitterswijk, J.; Van Den Bosch, D. Huntington’s disease outpatient clinic for functional diagnosis and treatment: Coming to consensus: How long term care facility procedures complement specialist diagnosis and treatment. J. Huntingtons Dis., 2018, 7(2), 189-191.
[112]
Krench, M.; Littleton, J.T. Modeling huntington disease in drosophila: insights into axonal transport defects and modifiers of toxicity. Fly (Austin), 2013, 7, 229-236.
[113]
Bates, E.A.; Victor, M.; Jones, A.K.; Shi, Y.; Hart, A.C. Differential contributions of caenorhabditis elegans histone deacetylases to huntingtin polyglutamine toxicity. J. Neurosci., 2006, 26, 2830-2838.
[114]
Yang, S.H.; Cheng, P.H.; Banta, H.; Piotrowska-Nitsche, K.; Yang, J.J.; Cheng, E.C.; Snyder, B.; Larkin, K.; Liu, J.; Orkin, J.; Fang, Z.H.; Smith, Y.; Bachevalier, J.; Zola, S.M.; Li, S.H.; Li, X.J.; Chan, A.W. Towards a transgenic model of Huntington’s disease in a non-human primate. Nature, 2008, 453(7197), 921-925.
[115]
Hodgson, J.G.; Agopyan, N.; Gutekunst, C.A.; Leavitt, B.R.; Lepiane, F.; Singaraja, R.; Smith, D.J.; Bissada, N.; Mccutcheon, K.; Nasir, J.; Jamot, L.; Li, X.J.; Stevens, M.E.; Rosemond, E.; Roder, J.C.; Phillips, A.G.; Rubin, E.M.; Hersch, S.M.; Hayden, M.R. A YAC mouse model for Huntington’s disease with full-length mutant huntingtin, cytoplasmic toxicity, and selective striatal neurodegeneration. Neuron, 1999, 23(1), 181-192.
[116]
Bates, G.P.; Dorsey, R.; Gusella, J.F.; Hayden, M.R.; Kay, C.; Leavitt, B.R.; Nance, M.; Ross, C.A.; Scahill, R.I.; Wetzel, R.; Wild, E.J.; Tabrizi, S.J. Huntington disease. Nat. Rev. Dis. Primers, 2015, 1, 1-21.
[117]
Castilhos, R.M.; Souza, A.F.; Furtado, G.V.; Gheno, T.C.; Silva, A.L.; Vargas, F.R.; Lima, M.A.; Barsottini, O.; Pedroso, J.L.; Godeiro, C.J.; Salarini, D.; Pereira, E.T.; Lin, K.; Toralles, M.B.; Saute, J.A.; Rieder, C.R.; Quintas, M.; Sequeiros, J.; Alonso, I.; Saraiva-Pereira, M.L.; Jardim, L.B. Huntington disease and huntington disease-like in a case series from brazil. Clin. Genet., 2014, 86, 373-377.
[118]
Ross, C.A.; Aylward, E.H.; Wild, E.J.; Langbehn, D.R.; Long, J.D.; Warner, J.H.; Scahill, R.I.; Leavitt, B.R.; Stout, J.C.; Paulsen, J.S.; Reilmann, R.; Unschuld, P.G.; Wexler, A.; Margolis, R.L.; Tabrizi, S.J. Huntington disease: Natural history, biomarkers and prospects for therapeutics. Nat. Rev. Neurol., 2014, 10(4), 204-216.
[119]
Xi, W.; Wang, X.; Laue, T.M.; Denis, C.L. Multiple discrete soluble aggregates influence polyglutamine toxicity in a Huntington’s disease model system. Sci. Rep., 2016, 6, 1-14.
[120]
Grima, J.C.; Daigle, J.G.; Arbez, N.; Cunningham, K.C.; Zhang, K.; Ochaba, J.; Geater, C.; Morozko, E.; Stocksdale, J.; Glatzer, J.C.; Pham, J.T.; Ahmed, I.; Peng, Q.; Wadhwa, H.; Pletnikova, O.; Troncoso, J.C.; Duan, W.; Snyder, S.H.; Ranum, L.P.W.; Thompson, L.M.; Lloyd, T.E.; Ross, C.A.; Rothstein, J.D. Mutant huntingtin disrupts the nuclear pore complex. Neuron, 2017, 94(1), 93-107.
[121]
Croce, K.R.; Yamamoto, A. A role for autophagy in Huntington’s disease. Neurobiol. Dis., 2018, 18, 30481-30489.
[122]
Andrich, J.; Saft, C.; Ostholt, N.; Müller, T. Complex movement behavior and progression of Huntington’s disease. Neurosci. Lett., 2007, 416, 272-274.
[123]
Bonilla, E. Huntington disease. A review. Invest. Clin., 2000, 41(2), 117-141.
[124]
Bouwens, J.A.; Van Duijn, E.; Van Der Mast, R.C.; Roos, R.A.; Giltay, E.J. Irritability in a prospective cohort of Huntington’s disease mutation carriers. J. Neuropsychiatry Clin. Neurosci., 2015, 27, 206-212.
[125]
Bora, E.; Velakoulis, D.; Walterfang, M. Social cognition in Huntington’s disease: A meta-analysis. Behav. Brain Res., 2016, 297, 131-140.
[126]
Southwell, A.L.; Franciosi, S.; Villanueva, E.B.; Xie, Y.; Winter, L.A.; Veeraraghavan, J.; Jonason, A.; Felczak, B.; Zhang, W.; Kovalik, V.; Waltl, S.; Hall, G.; Pouladi, M.A.; Smith, E.S.; Bowers, W.J.; Zauderer, M.; Hayden, M.R. Anti-semaphorin 4D immunotherapy ameliorates neuropathology and some cognitive impairment in the YAC128 mouse model of Huntington disease. Neurobiol. Dis., 2015, 76, 46-56.
[127]
Padovan-Neto, F.E.; Sammut, S.; Chakroborty, S.; Dec, A.M.; Threlfell, S.; Campbell, P.W.; Mudrakola, V.; Harms, J.F.; Schmidt, C.J.; West, A.R. Facilitation of corticostriatal transmission following pharmacological inhibition of striatal phosphodiesterase 10A: Role of nitric oxide-soluble guanylyl cyclase-cGMP signaling pathways. J. Neurosci., 2015, 35(14), 5781-5791.
[128]
Smith, M.R.; Syed, A.; Lukacsovich, T.; Purcell, J.; Barbaro, B.A.; Worthge, S.A.; Wei, S.R.; Pollio, G.; Magnoni, L.; Scali, C.; Massai, L. F ranceschini, D.; Camarri, M.; Gianfriddo, M.; Diodato, E.; Thomas, R.; Gokce, O.; Tabrizi, S.J.; Caricasole, A.; Landwehrmeyer, B.; Menalled, L.; Murphy, C.; Ramboz, S.; Luthi-Carter, R.; Westerberg, G.; Marsh, J.L. A potent and selective Sirtuin 1 inhibitor alleviates pathology in multiple animal and cell models of Huntington’s disease. Hum. Mol. Genet., 2014, 23(11), 2995-3007.
[129]
Simmons, D.A. Modulating neurotrophin receptor signaling as a therapeutic strategy for Huntington’s disease. J. Huntingtons Dis., 2017, 6(4), 303-325.
[130]
Kieburtz, K.; Reilmann, R.; Olanow, C.W. Huntington’s disease: Current and future therapeutic prospects. Mov. Disord., 2018, 33, 1033-1041.
[131]
Huntington study group. Tetrabenazine as antichorea therapy in Huntington disease: A randomized controlled trial. Neurology, 2006, 66(3), 366-372.
[132]
Mestre, T.A.; Ferreira, J.J. An evidence-based approach in the treatment of Huntington’s disease. Parkinsonism Relat. Disord., 2012, 18(4), 316-320.
[133]
Krishnan, H.S.; Bernard-Gauthier, V.; Placzek, M.S.; Dahl, K.; Narayanaswami, V.; Livni, E.; Chen, Z.; Yang, J.; Collier, T.L.; Ran, C.; Hooker, J.M.; Liang, S.H.; Vasdev, N. Metal protein-attenuating compound for PET neuroimaging: Synthesis and preclinical evaluation of [11C] PBT2. Mol. Pharm., 2018, 15(2), 695-702.
[134]
Huang, Z.; Adachi, H. Natural compounds preventing neurodegenerative diseases through autophagic activation. J. UOEH, 2016, 38(2), 139-148.
[135]
Zeng, Y.; Guo, W.; Xu, G.; Wang, Q.; Feng, L.; Long, S.; Liang, F.; Huang, Y.; Lu, X.; Li, S.; Zhou, J.; Burgunder, J.M.; Pang, J.; Pei, Z. Xyloketal-derived small molecules show protective effect by decreasing mutant Huntingtin protein aggregates in Caenorhabditis elegans model of Huntington’s disease. Drug Des. Devel. Ther., 2016, 10, 1443-1451.
[136]
Long, S.M.; Liang, F.Y.; Wu, Q.; Lu, X.L.; Yao, X.L.; Li, S.C.; Li, J.; Su, H.; Pang, J.Y.; Pei, Z. Identification of marine neuroactive molecules in behaviour-based screens in the larval zebrafish. Mar. Drugs, 2014, 12(6), 3307-3322.
[137]
Ehrnhoefer, D.E.; Duennwald, M.; Markovic, P.; Wacker, J.L.; Engemann, S.; Roark, M.; Legleiter, J.; Marsh, J.L.; Thompson, L.M.; Lindquist, S.; Muchowski, P.J.; Wanker, E.E. Green tea (-)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington’s disease models. Hum. Mol. Genet., 2006, 15(18), 2743-2751.
[138]
Sarkar, S.; Davies, J.E.; Huang, Z.; Tunnacliffe, A.; Rubinsztein, D.C. Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein. J. Biol. Chem., 2007, 282(8), 5641-5652.
[139]
Wu, A.G.; Wong, V.K.; Xu, S.W.; Chan, W.K.; Ng, C.I.; Liu, L.; Law, B.Y. Onjisaponin B derived from Radix Polygalae enhances autophagy and accelerates the degradation of mutant α-synuclein and huntingtin in PC-12 cells. Int. J. Mol. Sci., 2013, 14(11), 22618-22641.
[140]
Jiang, W.; Wei, W.; Gaertig, M.A.; Li, S.; Li, X.J. Therapeutic effect of berberine on Huntington’s disease transgenic mouse model. PLoS One, 2015, 10(7), 1-16.
[141]
Paez-Colasante, X.; Figueroa-Romero, C.; Sakowski, S.A.; Goutman, S.A.; Feldman, E.L.X. Amyotrophic lateral sclerosis: Mechanisms and therapeutics in the epigenomic era. Nat. Rev. Neurol., 2015, 11(5), 266-279.
[142]
Schultz, J. Disease-Modifying treatment of amyotrophic lateral sclerosis. Am. J. Manag. Care, 2018, 24(15), 327-335.
[143]
Volk, A.E.; Weishaupt, J.H.; Andersen, P.M.; Ludolph, A.C.; Kubisch, C. Current knowledge and recent insights into the genetic basis of amyotrophic lateral sclerosis. Med. Genetik, 2018, 30(2), 252-258.
[144]
Kumar, V.; Islam, A.; Hassan, Md. I.; Ahmad, F. Therapeutic progress in amyotrophic lateral sclerosis-beginning to learning. Eur. J. Med. Chem., 2016, 121, 903-917.
[145]
Dervishi, I.; Gozutok, O.; Murnan, K.; Gautam, M.; Heller, D.; Bigio, E.; Ozdinler, P.H. Protein-protein interactions reveal key canonical pathways, upstream regulators, interactome domains, and novel targets in ALS. Sci. Rep., 2018, 8(1), 1-19.
[146]
Brown, R.H.; Al-Chalabi, A. Amyotrophic lateral sclerosis. N. Engl. J. Med., 2017, 377(2), 162-172.
[147]
Ip, P.; Sharda, P.R.; Cunningham, A.; Chakrabartty, S.; Pande, V.; Chakrabartty, A. quercitrin and quercetin 3-β-d-glucoside as chemical chaperones for the a4v sod1 als-causing mutant. Protein Eng. Des. Sel., 2017, 30(6), 431-440.
[148]
Khan, S.; Ahmad, K.; Alshammari, E.M.A.; Adnan, M.; Baig, M.H.; Lohani, M.; Somvanshi, P.; Haque, S. Implication of caspase-3 as a common therapeutic target for multineurodegenerative disorders and its inhibition using nonpeptidyl natural compounds. BioMed Res. Int., 2015, 2015, 1-9.
[149]
Zhu, J.; Shen, L.; Lin, X.; Hong, Y.; Feng, Y. Clinical research on traditional chinese medicine compounds and their preparations for amyotrophic lateral sclerosis. Biomed. Pharmacother., 2017, 96, 854-864.
[150]
Barbeito, L. Astrocyte-based cell therapy: new hope for amyotrophic lateral sclerosis patients? Stem Cell Res. Ther., 2018, 9(1), 241.
[151]
Li, J. Chen, Jing-Yi; Deng, Ya-Lin; Zhou, Q.; Wu, Y.; Wu, D.; Luo, Hai-Bin. Structure-based design, synthesis, biological evaluation, and molecular docking of Novel PDE10 inhibitors with antioxidant activities. Front Chem., 2018, 6, 1-12.
[152]
Wu, B.; De, S.K.; Kulinich, A.; Salem, A.F.; Koeppen, J.; Wang, R.; Barile, E.; Wang, S.; Zhang, D.; Ethell, I.; Pellecchia, M. Potent and selective EphA4 agonists for the treatment of als. Cell Chem. Biol., 2017, 24(3), 293-305.
[153]
Stanga, S.; Brambilla, L.; Tasiaux, B.; Dang, A.H.; Ivanoiu, A.; Octave, J.N.; Rossi, D.; Pesch, V.V.; Kienlen-Campard, P. A role for GDNF and soluble APP as biomarkers of amyotrophic lateral sclerosis pathophysiology. Front. Neurol., 2018, 9, 1-9.
[154]
Durães, F.; Pinto, M.; Sousa, E. Old drugs as new treatments for neurodegenerative diseases. Pharmaceuticals, 2018, 11(2), 1-21.
[155]
Nabavi, S.; Daglia, M.; D’Antona, Gi.; Sobarzo-Sanchez, E.; Talas, Z.; Nabavi, S. Natural compounds used as therapies targeting to amyotrophic lateral sclerosis. Curr. Pharm. Biotechnol., 2015, 16(3), 211-218.
[156]
Nakano, K.K.; Dawson, D.M.; Spence, A. Machado disease: a hereditary ataxia in Portuguese emigrants to Massachusetts. Neurology, 1972, 22, 49-55.
[157]
Rosenberg, R.N.; Nyhan, W.L.; Bau, C.; Shore, R. Autosomal dominant striatonigral degeneration. Neurology, 1976, 26, 703-714.
[158]
Dawson, D.M. Ataxia in families from the Azores. A. Eng. J. Med., 1977, 296, 1529-1530.
[159]
Romanul, E.C.A.; Fowler, H.L.; Radvany, J. Azorean disease of the nervous system. N. Engl. J. Med., 1977, 296, 1505-1508.
[160]
Schols, L. Machado-Joseph disease mutation as the genetic basis of most spinocerebellar ataxias in Germany. J. Neurol. Neurosurg. Psychiatry, 1995, 59, 49-50.
[161]
Durr, A.; Stevanin, G.; Cancel, G.; Duyckaerts, C.; Abbas, N.; Didierjean, O.; Chneiweiss, H.; Benomar, A.; Lyon-Caen, O.; Julien, J.; Serdaru, M.; Penet, C.; Agid, Y.; Brice, A. Spinocerebellar ataxia 3 and Machado-Joseph disease: clinical, molecular and neuropathological features. Ann. Neurol., 1996, 39, 490-499.
[162]
Inoue, K.; Hanihara, T.; Yamada, Y.; Kosaka, K.; Katsuragi, K.; Iwabuchi, K. Clinical and genetic evaluation of Japanese autosomal dominant cerebellar ataxias: is Machado-Joseph disease common in the Japanese? J. Neurol. Neurosurg. Psychiatry, 1996, 60(6), 697-698.
[163]
Watanabe, H.; Tanaka, P.; Matsumoto, M.; Doyu, M.; Ando, T.; Mitsuma, T.; Sobue, G. Frequency analysis of autosomal dominant cerebellar ataxias in Japanese patietns and clinical characterization of spinocerebellar ataxia 6. Clin. Genet., 1998, 53, 13-19.
[164]
Moseley, M.L.; Benzow, K.A.; Schut, L.J.; Bird, T.D.; Gomez, C.M.; Barkhaus, R.E.; Blindauer, K.A.; Labuda, M.; Pandolfo, M.; Koob, M.D.; Ranum, L.P. Incidence of dominant spinocerebellar and Friedreich triplet repeats among 361 ataxia families. Neurology, 1998, 51, 1666-1671.
[165]
Soong, B.; Lu, Y.; Choo, K. Frequency analysis of autosomal dominant cerebellar ataxias in Taiwanese patients and clinical and molecular characterization of spinocerebellar ataxia type 6. Arch. Neurol., 2001, 5, 1105-1109.
[166]
Paulson, H.L. The Spinocerebellar Ataxias. J. Neuroophthalmol., 2009, 29(3), 227-237.
[167]
Bevivino, A.E.; Loll, R.J. An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta-fibrils. Proc. Natl Acad. Set U.S.A., 2001, 98, 11955-11960.
[168]
Suenaga, T.; Matsushima, H. Ubiquitin-immunoreactive inclusions in anterior horn cells and hypoglossal neurons in a case with Joseph’s disease. Acta Neuropathol., 1993, 85, 341-344.
[169]
Rub, U.; Brunt, E.R.; Deller, T. New insights into the pathoanatomy of spinocerebellar ataxia type 3 (Machado-Joseph disease). Curr. Opin. Neurol., 2008, 21, 111-116.
[170]
Takiyama, Y.; Nishizawa, S.; Tanaka, H. The gene for Machado-Joseph disease maps to human chromosome 14q. Nat. Genet., 1993, 4, 300-305.
[171]
Kawaguchi, Y.; Okamoto, T.; Taniwaki, M. CAG expansions in a novel gene for machado-joseph disease at chromosome 14q32.1. Nat. Genet., 1994, 8, 221-228.
[172]
Klockgether, T.; Schols, L.; Abele, M.; Burk, K.; Topka, H.; Andres, E.; Amoiridis, G.; Ludtke, R.; Riess, L.; Laccone, R.; Dichgans, J. Age related axonal neuropathy in spinocerebellar ataxia type 3/Machado-Joseph disease (SCA3/MJD). J. Neurol. Neurosurg. Psychiatry, 1996, 66, 222-224.
[173]
Warrick, J.M.; Chan, E.; Gray-Board, G.L. Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone Hsp70. Nat. Genet., 1999, 23, 425-442.
[174]
Sakai, T.; Antoku, Y.; Matsuishi, T.; Iwashita, H. Tetrahydrobiopterin double-blind, crossover trial in machado-joseph disease. J. Neurol. Sci., 1996, 136, 71-72.
[175]
Menzies, F.M.; Huebener, J.; Renna, M.; Bonin, M.; Riess, O.; Rubinsztein, D.C. Autophagy induction reduces mutant ataxin-3 levels and toxicity in a mouse model of spinocerebellar ataxia type 3. Brain, 2010, 133, 93-104.
[176]
Chang, K.H.; Chen, W.L.; Lee, L.C.; Lin, C.H.; Kung, P.J.; Lin, T.H.; Wu, Y.C.; Wu, Y.R.; Chen, Y.C.; Lee-Chen, G.J.; Chen, C.M. Aqueous extract of paeonia lactiflora and paeoniflorin as aggregation reducers targeting chaperones in cell models of spinocerebellar ataxia 3. Evid. Based Complement. Alternat. Med., 2013, 1-11.
[177]
Zhou, L.; Wang, H.; Wang, P.; Ren, H.; Chen, D.; Ying, Z.; Wang, G. Ataxin-3 protects cells against H2O2-induced oxidative stress by enhancing the interaction between Bcl-XL and Bax. Neuroscience, 2013, 243C, 14-21.
[178]
Goodwin, V.A.; Richards, S.H.; Taylor, R.S.; Taylor, A.H.; Campbell, J.L. The effectiveness of exercise interventions for people with Parkinson’s disease: a systematic review and meta-analysis. Mov. Disord., 2008, 23(5), 631-640.
[179]
Tuite, P.J.; Rogaeva, E.A.; St. George-Hyslop, P.H.; Lang, A.E. Dopa-responsive parkinsonism phenotype of Machado-Joseph disease: confirmation of 14q CAG expansion. Ann. Neurol., 1995, 38, 684-687.
[180]
França Jr, M.C.; D’Abreu, A.; Friedman, J.H.; Nucci, A.; Lopes-Cendes, I. Chronic pain in Machado-Joseph disease: a frequent and disabling symptom. Arch. Neurol., 2007, 64, 1767-1770.
[181]
França Jr, M.C.; D’Abreu, A.; Nucci, A.; Lopes-Cendes, I. Muscle excitability abnormalities in Machado-Joseph disease. Arch. Neurol., 2008, 65, 525-529.
[182]
Levine, J.; Greenwald, B.D. Fatigue in Parkinson disease, stroke, and traumatic brain injury. Phys. Med. Rehabil. Clin. N. Am., 2009, 20(2), 347-361.
[183]
Adam, O.R.; Jankovic, J. Treatment of dystonia. Parkinsonism Relat. Disord., 2007, 13(3), 362-368.
[184]
Chang, K.H.; Chen, W.L.; Wu, Y.R.; Lin, T.H.; Wu, Y.C.; Chao, C.Y.; Lin, J.Y.; Lee, L.C.; Chen, Y.C.; Lee-Chen, G.J. Aqueous extract of gardenia jasminoides targeting oxidative stress to reduce polyQ aggregation in cell models of spinocerebellar ataxia 3. Neuropharmacology, 2014, 81, 166-175.
[185]
Chou, A.H.; Chen, Y.L.; Chiu, C.C.; Yuan, S.J.; Weng, Y.H.; Yeh, T.H.; Lin, Y.L.; Fang, J.M.; Wang, H.L. T1-11 and JMF1907 ameliorate polyglutamine-expanded ataxin-3-induced neurodegeneration, transcriptional dysregulation and ataxic symptom in the SCA3 transgenic mouse. Neuropharmacology, 2015, 99, 308-317.
[186]
Rajamani, K.; Liu, J.W.; Wu, C.H.; Chiang, I.T.; You, D.H.; Lin, S.Y.; Hsieh, D.K.; Lin, S.Z.; Harn, H.J.; Chiou, T.W. n-Butylidenephthalide exhibits protection against neurotoxicity through regulation of tryptophan 2, 3 dioxygenase in spinocerebellar ataxia type 3. Neuropharmacology, 2017, 117, 434-446.
[187]
La Spada, A.R.; Wilson, E.M.; Lubahn, D.B.; Harding, A.E.; Fischbeck, K.H. Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy. Nature, 1991, 352, 77-79.
[188]
Schmidt, B.J.; Greenberg, C.R.; Allingham-Hawkins, D.J.; Spriggs, E.L. Expression of X-linked bulbospinal muscular atrophy (Kennedy disease) in two homozygous women. Neurology, 2002, 59, 770-772.
[189]
Rhodes, L.E.; Freeman, B.K.; Auh, S.; Kokkinis, A.D.; La Pean, A.; Chen, C.; Lehky, T.J.; Shrader, J.A.; Levy, E.W.; Harris-Love, M.; Di Prospero, N.A.; Fischbeck, K.H. Clinical features of spinal and bulbar muscular atrophy. Brain, 2009, 132, 3242-3251.
[190]
Roselli, F.; Caroni, P. From intrinsic firing properties to selective neuronal vulnerability in neurodegenerative diseases. Neuron, 2015, 85, 901-910.
[191]
Tut, T.G.; Ghadessy, F.J.; Trifiro, M.A.; Pinsky, L.; Yong, E.L. Long polyglutamine tracts in the androgen receptor are associated with reduced trans-activation, impaired sperm production, and male infertility. J. Clin. Endocrinol. Metab., 1997, 82, 3777-3782.
[192]
Wang, Q.; Udayakumar, T.S.; Vasaitis, T.S.; Brodie, A.M.; Fondell, J.D. Mechanistic relationship between androgen receptor polyglutamine tract truncation and androgen-dependent transcriptional hyperactivity in prostate cancer cells. J. Biol. Chem., 2004, 279, 17319-17328.
[193]
Parodi, S.; Pennuto, M. Neurotoxic effects of androgens in spinal and bulbar muscular atrophy. Front. Neuroendocrinol., 2011, 32, 416-425.
[194]
Klement, I.A.; Skinner, P.J.; Kaytor, M.D.; Yi, H.; Hersch, S.M.; Clark, H.B.; Zoghbi, H.Y.; Orr, H.T. Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice. Cell, 1998, 95, 41-53.
[195]
Bichelmeier, U.; Schmidt, T.; Hubener, J.; Boy, J.; Ruttiger, L.; Habig, K.; Poths, S.; Bonin, M.; Knipper, M.; Schmidt, W.J.; Wilbertz, J.; Wolburg, H.; Laccone, F.; Riess, O. Nuclear localization of ataxin-3 is required for the manifestation of symptoms in SCA3: in vivo evidence. J. Neurosci., 2007, 27, 7418-7428.
[196]
Montie, H.L.; Cho, M.S.; Holder, L.; Liu, Y.; Tsvetkov, A.S.; Finkbeiner, S.; Merry, D.E. Cytoplasmic retention of polyglutamine-expanded androgen receptor ameliorates disease via autophagy in a mouse model of spinal and bulbar muscular atrophy. Hum. Mol. Genet., 2009, 18, 1937-1950.
[197]
Nedelsky, N.B.; Pennuto, M.; Smith, R.B.; Palazzolo, I.; Moore, J.; Nie, Z.; Neale, G.; Taylor, J.P. Native functions of the androgen receptor are essential to pathogenesis in a Drosophila model of spinobulbar muscular atrophy. Neuron, 2010, 67, 936-952.
[198]
Young, J.E.; Garden, G.A.; Martinez, R.A.; Tanaka, F.; Sandoval, C.M.; Smith, A.C.; Sopher, B.L.; Lin, A.; Fischbeck, K.H.; Ellerby, L.M.; Morrison, R.S.; Taylor, J.P.; La Spada, A.R. Polyglutamine-expanded androgen receptor truncation fragments activate a Bax-dependent apoptotic cascade mediated by DP5/Hrk. J. Neurosci., 2009, 29, 1987-1997.
[199]
Borgia, D.; Malena, A.; Spinazzi, M.; Desbats, M.A.; Salviati, L.; Russell, A.P.; Miotto, G.; Tosatto, L.; Pegoraro, E.; Soraru, G.; Pennuto, M.; Vergani, L. Increased mitophagy in the skeletal muscle of spinal and bulbar muscular atrophy patients. Hum. Mol. Genet., 2017, 26, 1087-1103.
[200]
Palazzolo, I.; Burnett, B.G.; Young, J.E. Akt blocks ligand binding and protects against expanded polyglutamine androgen receptortoxicity. Hum. Mol. Genet., 2007, 16, 1593-1603.
[201]
Palazzolo, I.; Stack, C.; Kong, L. Overexpression of IGF-1 in muscle attenuates disease in a mouse model of spinal and bulbarmuscular atrophy. Neuron, 2009, 63, 316-328.
[202]
Guler, H.P.; Zapf, J.; Schmid, C.; Froesch, E.R. Insulin-like growth factors I and II in healthy man. Estimations of half-lives and production rates. Acta Endocrinol., 1989, 121, 753-758.
[203]
Yakar, S.; Rosen, C.J.; Beamer, W.G. Circulating levels of IGF-1 directly regulate bone growth and density. J. Clin. Invest., 2002, 110, 771-781.
[204]
Sumner, C.J.; Fischbeck, K.H. Jaw drop in Kennedy’s disease. Neurology, 2002, 59, 1471-1472.
[205]
Sinclair, R.; Greenland, K.J.; Egmond, S.; Hoedemaker, C.; Chapman, A.; Zajac, J.D. Men with Kennedy disease have a reduced risk of androgenetic alopecia. Br. J. Dermatol., 2007, 157, 290-294.
[206]
Bailey, C.K.; Andriola, I.F.; Kampinga, H.H.; Merry, D.E. Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy. Hum. Mol. Genet., 2002, 11, 515-523.
[207]
Ishihara, K.; Yamagishi, N.; Saito, Y.; Adachi, H.; Kobayashi, Y.; Sobue, G.; Ohtsuka, K.; Hatayama, T. Hsp105alpha suppresses the aggregation of truncated androgen receptor with expanded CAG repeats and cell toxicity. J. Biol. Chem., 2003, 278, 25143-25150.
[208]
Howarth, J.L.; Kelly, S.; Keasey, M.P.; Glover, C.P.; Lee, Y.B.; Mitrophanous, K.; Chapple, J.P.; Gallo, J.M.; Cheetham, M.E.; Uney, J.B. Hsp40 molecules that target to the ubiquitin-proteasome system decrease inclusion formation in models of polyglutamine disease. Mol. Ther., 2007, 15, 1100-1105.
[209]
Katsuno, M.; Adachi, H.; Doyu, M.; Minamiyama, M.; Sang, C.; Kobayashi, Y.; Inukai, A.; Sobue, G. Leuprorelin rescues polyglutamine-dependent phenotypes in a transgenic mouse model of spinal and bulbar muscular atrophy. Nat. Med., 2003, 9, 768-773.
[210]
Chevalier-Larsen, E.S.; O’Brien, C.J.; Wang, H.; Jenkins, S.C.; Holder, L.; Lieberman, A.P.; Merry, D.E. Castration restores function and neurofilament alterations of aged symptomatic males in a transgenic mouse model of spinal and bulbar muscular atrophy. J. Neurosci., 2004, 24, 4778-4786.
[211]
Katsuno, M.; Sang, C.; Adachi, H.; Minamiyama, M.; Waza, M.; Tanaka, F.; Doyu, M.; Sobue, G. Pharmacological induction of heat-shock proteins alleviates polyglutamine-mediated motor neuron disease. Proc. Natl. Acad. Sci. USA, 2005, 102, 16801-16806.
[212]
Tokui, K.; Adachi, H.; Waza, M.; Katsuno, M.; Minamiyama, M.; Doi, H.; Tanaka, K.; Hamazaki, J.; Murata, S.; Tanaka, F.; Sobue, G. 17-DMAG ameliorates polyglutamine-mediated motor neuron degeneration through well-preserved proteasome function in an SBMA model mouse. Hum. Mol. Genet., 2009, 18, 898-910.
[213]
Rinaldi, C.; Malik, B.; Greensmith, L. 2016. Targeted molecular therapies for SBMA. J. Mol. Neurosci., 2016, 58, 335-342.
[214]
Pennuto, M.; Palazzolo, I.; Poletti, A. Post-translational modifications of expanded polyglutamine proteins: Impact on neurotoxicity. Hum. Mol. Genet., 2009, 18, 40-47.
[215]
Montie, H.L.; Pestell, R.G.; Merry, D.E. SIRT1 modulates aggregation and toxicity through deacetylation of the androgen receptor in cell models of SBMA. J. Neurosci., 2011, 31, 17425-17436.
[216]
Scaramuzzino, C.; Casci, I.; Parodi, S.; Lievens, P.M.; Polanco, M.J.; Milioto, C.; Chivet, M.; Monaghan, J.; Mishra, A.; Badders, N.; Aggarwal, T.; Grunseich, C.; Sambataro, F.; Basso, M.; Fackelmayer, F.O.; Taylor, J.P.; Pandey, U.B.; Pennuto, M. Protein arginine methyltransferase 6 enhances polyglutamine-expanded androgen receptor function and toxicity in spinal and bulbar muscular atrophy. Neuron, 2015, 85, 88-100.
[217]
Grunseich, C.; Kats, I.R.; Bott, L.C.; Rinaldi, C.; Kokkinis, A.; Fox, D.; Chen, K.L.; Schindler, A.B.; Mankodi, A.K.; Shrader, J.A.; Schwartz, D.P.; Lehky, T.J.; Liu, C.Y.; Fischbeck, K.H. Early onset and novel features in a spinal and bulbar muscular atrophy patient with a 68 CAG repeat. Neuromuscul. Disord., 2014, 24, 978-981.
[218]
Milioto, C.; Malena, A.; Maiano, E.; Polanco, M.J.; Marchioretti, C.; Borgia, D.; Pereira, M.G.; Blaauw, B.; Lieberman, A.P.; Venturini, R.; Plebani, M.; Sambataro, F.; Vergani, L.; Pegoraro, E.; Soraru, G.; Pennuto, M. Beta-agonist stimulationameliorates the phenotype ofspinal and bulbar muscular atrophymice and patient-derived myotubes. Scientific Reports, 2016, 7(41046), 1-14.
[219]
Hijikata, Y.; Katsuno, M.; Suzuki, K.; Hashizume, A.; Araki, A.; Yamada, S. Impaired muscle uptake of creatine in spinal and bulbar muscular atrophy. Ann. Clin. Transl. Neurol., 2016, 7, 537-546.
[220]
Rinaldi, C.; Bott, L.C.; Chen, K.L.; Harmison, G.G.; Katsuno, M.; Sobue, G.; Pennuto, M.; Fischbeck, K.H. IGF-1 administration ameliorates disease manifestations in a mouse model of spinal and bulbar muscular atrophy. Mol. Med., 2012, 18, 1261-1268.
[221]
Qiang, Q.; Adachi, H.; Huang, Z.; Jiang, Y.M.; Katsuno, M.; Minamiyama, M.; Doi, H.; Matsumoto, S.; Kondo, N.; Miyazaki, Y.; Iida, M.; Tohnai, G.; Sobue, G. Genistein, a natural product derived from soybeans, ameliorates polyglutamine-mediated motor neuron disease. J. Neurochem., 2013, 126, 122-130.
[222]
Tee, B.L.; Longoria Ibarrola, E.M.; Geschwind, M.D. Prion Diseases. Neurol. Clin., 2018, 36(4), 865-897.
[223]
Joyner, P.M.; Cichewicz, R.H. Bringing natural products into the fold - exploring the therapeutic lead potential of secondary metabolites for the treatment of protein-misfolding-related neurodegenerative diseases. Nat. Prod. Rep., 2011, 28(1), 26-47.
[224]
Sitammagari, K.K.; Masood, W. Creutzfeldt Jakob Disease; StatPearls Publishing
[Internet]: Treasure Island, 2018.
[225]
Mackenzie, G.; Will, R. Creutzfeldt-Jakob disease: Recent developments. F1000 Res., 2017, 6, 2053.
[226]
Manix, M.; Kalakoti, P.; Henry, M.; Thakur, J.; Menger, R.; Guthikonda, B.; Nanda, A. Creutzfeldt-Jakob disease: Updated diagnostic criteria, treatment algorithm, and the utility of brain biopsy. Neurosurg. Focus, 2015, 39(5), E2.
[227]
Guest, W.C.; Silverman, J.M.; Pokrishevsky, E.; O’Neill, M.A.; Grad, L.I.; Cashman, N.R. Generalization of the prion hypothesis to other. neurodegenerative diseases: an imperfect fit. J. Toxicol. Environ. Health A, 2011, 74(22-24), 1433-1459.
[228]
Dirikoc, S.; Priola, S.A.; Marella, M.; Zsurger, N.; Chabry, J. Nonpsychoactive cannabidiol prevents prion accumulation and protects neurons against prion toxicity. J. Neurosci., 2007, 27(36), 9537-9544.
[229]
Iuvone, T.; Esposito, G.; De Filippis, D.; Scuderi, C.; Steardo, L. Cannabidiol: A promising drug for neurodegenerative disorders? CNS Neurosci. Ther., 2009, 15(1), 65-75.
[230]
Anand, P.; Thomas, S.G.; Kunnumakkara, A.B.; Sundaram, C.; Harikumar, K.B.; Sung, B.; Tharakan, S.T.; Misra, K.; Priyadarsini, I.K.; Rajasekharan, K.N.; Aggarwal, B.B. Biological activities of curcumin and its analogues (Congeners) made by man and mother nature. Biochem. Pharmacol., 2008, 76(11), 1590-1611.
[231]
Caughey, B.; Raymond, L.D.; Raymond, G.J.; Maxson, L.; Silveira, J.; Baron, G.S. Inhibition of protease-resistant prion protein accumulation in vitro by curcumin. J. Virol., 2003, 77(9), 5499-5502.
