Ahmed, S.S., Santosh, W., Kumar, S., Christlet, H.T.T., 2009. Metabolic profiling of Parkinson’s disease: evidence of biomarker from gene expression analysis and rapid neural network detection. J. Biomed. Sci. 16, 63. https://doi.org/10.1186/1423-0127-16-63
Anandhan, A., Jacome, M.S., Lei, S., Hernandez-Franco, P., Pappa, A., Panayiotidis, M.I., Powers, R., Franco, R., 2017. Metabolic Dysfunction in Parkinson’s Disease: Bioenergetics, Redox Homeostasis and Central Carbon Metabolism. Brain Res. Bull. https://doi.org/10.1016/j.brainresbull.2017.03.009
Berman, S.B., Hastings, T.G., 2001. Dopamine Oxidation Alters Mitochondrial Respiration and Induces Permeability Transition in Brain Mitochondria. J. Neurochem. 73, 1127–1137. https://doi.org/10.1046/j.1471-4159.1999.0731127.x
Braak, H., Del Tredici, K., 2008. Invited Article: Nervous system pathology in sporadic Parkinson disease. Neurology 70, 1916–1925. https://doi.org/10.1212/01.wnl.0000312279.49272.9f
Carter, R.J., Morton, J., Dunnett, S.B., 2001. Motor Coordination and Balance in Rodents. Curr. Protoc. Neurosci. https://doi.org/10.1002/0471142301.ns0812s15
Cenci, M.A., Whishaw, I.Q., Schallert, T., 2002. Animal models of neurological deficits: How relevant is the rat? Nat. Rev. Neurosci. 3, 574–579. https://doi.org/10.1038/nrn877
Church, W.H., 2005. Column chromatography analysis of brain tissue: An advanced laboratory exercise for neuroscience majors. J. Undergrad. Neurosci. Educ. 3, A36-41.
Cirillo, G., Maggio, N., Bianco, M.R., Vollono, C., Sellitti, S., Papa, M., 2010. Discriminative behavioral assessment unveils remarkable reactive astrocytosis and early molecular correlates in basal ganglia of 3-nitropropionic acid subchronic treated rats. Neurochem. Int. 56, 152–160. https://doi.org/10.1016/j.neuint.2009.09.013
Cottet-Rousselle, C., Ronot, X., Leverve, X., Mayol, J.F., 2011. Cytometric assessment of mitochondria using fluorescent probes. Cytom. Part A. https://doi.org/10.1002/cyto.a.21061
Darios, F., Corti, O., Lücking, C.B., Hampe, C., Muriel, M.-P., Abbas, N., Gu, W.-J., Hirsch, E.C., Rooney, T., Ruberg, M., Brice, A., 2003. Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death. Hum. Mol. Genet. 12, 517–526. https://doi.org/10.1093/hmg/ddg044
Davey, G.P., Peuchen, S., Clark, J.B., 1998. Energy thresholds in brain mitochondria: Potential involvement in neurodegeneration. J. Biol. Chem. 273, 12753–12757. https://doi.org/10.1074/jbc.273.21.12753
DeMaagd, G., Philip, A., 2015. Parkinson’s disease and its management part 1: Disease entity, risk factors, pathophysiology, clinical presentation, and diagnosis. P T 40, 504–510.
Eberling, J.L., Richardson, B.C., Reed, B.R., Wolfe, N., Jagust, W.J., 1994. Cortical glucose metabolism in Parkinson’s disease without dementia. Neurobiol. Aging 15, 329–335. https://doi.org/10.1016/0197-4580(94)90028-0
Ellis, G., Goldberg, D.M., 1971. An improved manual and semi-automatic assay for NADP-dependent isocitrate dehydrogenase activity, with a description of some kinetic properties of human liver and serum enzyme. Clin. Biochem. 4, 175–185. https://doi.org/10.1016/S0009-9120(71)91363-4
Fischer, D.A., Ferger, B., Kuschinsky, K., 2002. Discrimination of morphine- and haloperidol-induced muscular rigidity and akinesia/catalepsy in simple tests in rats. Behav. Brain Res. 134, 317–21. https://doi.org/10.1016/S0166-4328(02)00044-X
Fowler, C.J., Wiberg, A., Oreland, L., Marcusson, J., Winblad, B., 1980. The effect of age on the activity and molecular properties of human brain monoamine oxidase. J. Neural Transm. 49, 1–20. https://doi.org/10.1007/bf01249185
Gibrat, C., Saint-Pierre, M., Bousquet, M., Lévesque, D., Rouillard, C., Cicchetti, F., 2009. Differences between subacute and chronic MPTP mice models: investigation of dopaminergic neuronal degeneration and α-synuclein inclusions. J. Neurochem. 109, 1469–1482. https://doi.org/10.1111/j.1471-4159.2009.06072.x
Griffiths, D.E., Houghton, R.L., 1974. Studies on Energy‐Linked Reactions: Modified Mitochondrial ATPase of Oligomycin‐Resistant Mutants of Saccharomyces cerevisiae. Eur. J. Biochem. 46, 157–167. https://doi.org/10.1111/j.1432-1033.1974.tb03608.x
Gupta, D., Kurhe, Y., Radhakrishnan, M., 2014. Antidepressant effects of insulin in streptozotocin induced diabetic mice: Modulation of brain serotonin system. Physiol. Behav. 129, 73–8. https://doi.org/10.1016/j.physbeh.2014.02.036
Hashimoto, M., Rockenstein, E., Masliah, E., 2003. Transgenic models of alpha-synuclein pathology: past, present, and future. Ann. N. Y. Acad. Sci. 991, 171–88. https://doi.org/10.1111/j.1749-6632.2003.tb07475.x
Jogdand, P.S., Singh, S.K., Christiansen, M., Dziegiel, M.H., Singh, S., Theisen, M., 2012. Flow cytometric readout based on Mitotracker Red CMXRos stainingJogdand, P. S., Singh, S. K., Christiansen, M., Dziegiel, M. H., Singh, S., & Theisen, M. (2012). Flow cytometric readout based on Mitotracker Red CMXRos staining of live asexual blood stage . Malar. J. 11, 235. https://doi.org/10.1186/1475-2875-11-235
Kanarek, L., Hill, R.L., 1964. The preparation and characterization of fumarase from swine heart muscle. J. Biol. Chem. 239, 4202–6.
Ke, C.J., He, Y.H., He, H.W., Yang, X., Li, R., Yuan, J., 2014. A new spectrophotometric assay for measuring pyruvate dehydrogenase complex activity: A comparative evaluation. Anal. Methods 6, 6381–6388. https://doi.org/10.1039/c4ay00804a
King, T.E., Howard, R.L., 1967. [52] Preparations and properties of soluble NADH dehydrogenases from cardiac muscle. Methods Enzymol. 10, 275–294. https://doi.org/10.1016/0076-6879(67)10055-4
King, T.E., Ohnishi, T., Winter, D.B., Wu, J.T., 1976. Biochemical and EPR probes for structure-function studies of iron sulfur centers of succinate dehydrogenase. Adv. Exp. Med. Biol. https://doi.org/10.1007/978-1-4684-3270-1_15
Kristián, T., Gertsch, J., Bates, T.E., Siesjö, B.K., 2000. Characteristics of the calcium-triggered mitochondrial permeability transition in nonsynaptic brain mitochondria: Effect of cyclosporin A and ubiquinone O. J. Neurochem. 74, 1999–2009. https://doi.org/10.1046/j.1471-4159.2000.0741999.x
Lee, K.S., Lee, J.K., Kim, H.G., Kim, H.R., 2013. 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. Pharmacol. 17, 89–97. https://doi.org/10.4196/kjpp.2013.17.1.89
Liang, L.P., Patel, M., 2004. Iron-sulfur enzyme mediated mitochondrial superoxide toxicity in experimental Parkinson’s disease. J. Neurochem. 90, 1076–1084. https://doi.org/10.1111/j.1471-4159.2004.02567.x
Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J., 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265–275. https://doi.org/10.1016/0922-338X(96)89160-4
Masliah, E., Rockenstein, E., Veinbergs, I., Mallory, M., Hashimoto, M., Takeda, A., Sagara, Y., Sisk, A., Mucke, L., 2000. Dopaminergic loss and inclusion body formation in α-synuclein mice: Implications for neurodegenerative disorders. Science (80-. ). 287, 1265–1269. https://doi.org/10.1126/science.287.5456.1265
Mattson, M.P., Pedersen, W.A., Duan, W., Culmsee, C., Camandola, S., 1999. Cellular and molecular mechanisms underlying perturbed energy metabolism and neuronal degeneration in Alzheimer’s and Parkinson’s diseases. Ann. N. Y. Acad. Sci. 893, 154–75. https://doi.org/10.1111/j.1749-6632.1999.tb07824.x
McCormack, A.L., Thiruchelvam, M., Manning-Bog, A.B., Thiffault, C., Langston, J.W., Cory-Slechta, D.A., Di Monte, D.A., 2002. Environmental risk factors and Parkinson’s disease: Selective degeneration of nigral dopaminergic neurons caused by the herbicide paraquat. Neurobiol. Dis. 10, 119–127. https://doi.org/10.1006/nbdi.2002.0507
Meredith, G.E., Rademacher, D.J., 2011. MPTP mouse models of Parkinson’s disease: An update. J. Parkinsons. Dis. https://doi.org/10.3233/JPD-2011-11023
Mizuno, Y., Ohta, S., Tanaka, M., Takamiya, S., Suzuki, K., Sato, T., Oya, H., Ozawa, T., Kagawa, Y., 1989. Deficiencies in Complex I subunits of the respiratory chain in Parkinson’s disease. Biochem. Biophys. Res. Commun. 163, 1450–1455. https://doi.org/10.1016/0006-291X(89)91141-8
Morton, R.L., Iklé, D., White, C.W., 1998. Loss of lung mitochondrial aconitase activity due to hyperoxia in bronchopulmonary dysplasia in primates. Am. J. Physiol. Cell. Mol. Physiol. 274, L127–L133. https://doi.org/10.1152/ajplung.1998.274.1.L127
Parker, W.D., Parks, J.K., Swerdlow, R.H., 2008. Complex I deficiency in Parkinson’s disease frontal cortex. Brain Res. 1189, 215–218. https://doi.org/10.1016/j.brainres.2007.10.061
Parnetti, L., Gaiti, A., Polidori, M.C., Brunetti, M., Palumbo, B., Chionne, F., Cadini, D., Cecchetti, R., Senin, U., 1995. Increased cerebrospinal fluid pyruvate levels in Alzheimer’s disease. Neurosci. Lett. 199, 231–3. https://doi.org/10.1016/0304-3940(95)12058-c
Perier, C., Bové, J., Vila, M., Przedborski, S., 2003. The rotenone model of Parkinson’s disease [1]. Trends Neurosci. https://doi.org/10.1016/S0166-2236(03)00144-9
Przedborski, S., Jackson-Lewis, V., Naini, A.B., Jakowec, M., Petzinger, G., Miller, R., Akram, M., 2001. The parkinsonian toxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP): A technical review of its utility and safety. J. Neurochem. https://doi.org/10.1046/j.1471-4159.2001.00183.x
Puka-Sundvall, M., Wallin, C., Gilland, E., Hallin, U., Wang, X., Sandberg, M., Karlsson, J.O., Blomgren, K., Hagberg, H., 2000. Impairment of mitochondrial respiration after cerebral hypoxia-ischemia in immature rats: Relationship to activation of caspase-3 and neuronal injury. Dev. Brain Res. 125, 43–50. https://doi.org/10.1016/S0165-3806(00)00111-5
Saura, D.J., Richards, J.G., Mahy, N., 1994. Age-related changes on MAO in Bl/C57 mouse tissues: A quantitative radioautographic study, in: Journal of Neural Transmission, Supplement. pp. 89–94. https://doi.org/10.1007/978-3-7091-9324-2_11
Schapira, A.H. V., Cooper, J.M., Dexter, D., Clark, J.B., Jenner, P., Marsden, C.D., 1990. Mitochondrial Complex I Deficiency in Parkinson’s Disease. J. Neurochem. 54, 823–827. https://doi.org/10.1111/j.1471-4159.1990.tb02325.x
Schapira, A.H. V, 2007. Mitochondrial dysfunction in Parkinson’s disease. Cell Death Differ. 14, 1261–1266. https://doi.org/10.1038/sj.cdd.4402160
Sedelis, M., Hofele, K., Auburger, G.W., Morgan, S., Huston, J.P., Schwarting, R.K.W., 2000. MPTP susceptibility in the mouse: Behavioral, neurochemical, and histological analysis of gender and strain differences. Behav. Genet. 30, 171–182. https://doi.org/10.1023/A:1001958023096
Seibenhener, M.L., Wooten, M.C., 2015. Use of the open field maze to measure locomotor and anxiety-like behavior in mice. J. Vis. Exp. 6, 52434. https://doi.org/10.3791/52434
Sottocasa, G.L., Kuylenstierna, B., Ernster, L., Bergstrand, A., 1967. An electron-transport system associated with the outer membrane of liver mitochondria. A biochemical and morphological study. J. Cell Biol. 32, 415–38. https://doi.org/10.1083/jcb.32.2.415
Southwell, A.L., Ko, J., Patterson, P.H., 2009. Intrabody gene therapy ameliorates motor, cognitive, and neuropathological symptoms in multiple mouse models of Huntington’s disease. J. Neurosci. 29, 13589–602. https://doi.org/10.1523/JNEUROSCI.4286-09.2009
Spinazzi, M., Casarin, A., Pertegato, V., Salviati, L., Angelini, C., 2012. Assessment of mitochondrial respiratory chain enzymatic activities on tissues and cultured cells. Nat. Protoc. 7, 1235–1246. https://doi.org/10.1038/nprot.2012.058
Tegge, G., 1987. Bergmeyer, H. U. (Editor-in-Chief): Methods of Enzymatic Analysis (Methoden der enzymatischen Analyse). Third Edition. Editors: J. Bergmeyer and Marianne Graßl, Ed. consultant: R. F. Masseyeff. Volume XI: Antigens and Antibodies 2. VCH Verlagsgesellschaft mbH, Weinheim; Deerfield Beach, Florida; Basel, 1986. 508 pages with numerous figures and tables. ISBN 3-527-26052-8. Cloth binding DM 315,00. Starch - Stärke 39, 218–218. https://doi.org/10.1002/star.19870390614