Skulachev, VP. Membrane electricity as a convertible energy currency for the cell. Can J Biochem. 1980; 58, 161–175.
Leverve, XM. Mitochondrial function and substrate availability. Crit Care Med. 2007; 35(Suppl. 9), S454–S460.
Hagberg, H, Mallard, C, Rousset, CI, Thornton, C. Mitochondria: hub of injury responses in the developing brain. Lancet Neurol. 2014; 13, 217–232.
Yin, F, Cadenas, E. Mitochondria: the cellular hub of the dynamic coordinated network. Antioxid Redox Signal. 2015; 22, 961–964.
Ernster, L, Schatz, G. Mitochondria: a historical review. J Cell Biol. 1981; 91(Pt 2), 227s–255s.
Shaughnessy, DT, McAllister, K, Worth, L, et al. Mitochondria, energetics, epigenetics, and cellular responses to stress. Environ Health Perspect. 2014; 122, 1271–1278.
Porter, MH, Berdanier, CD. Oxidative phosphorylation: key to life. Diabetes Technol Ther. 2002; 4, 253–254.
Sztark, F, Payen, JF, Piriou, V, et al. Cellular energy metabolism: physiologic and pathologic aspects. Ann Fr Anes Reanim. 1999; 18, 261–269.
Melov, S. Mitochondrial oxidative stress. Physiologic consequences and potential for a role in aging. Ann N Y Acad Sci. 2000; 908, 219–225.
Turrens, JF, Freeman, BA, Levitt, JG, Crapo, JD. The effect of hyperoxia on superoxide production by lung submitochondrial particles. Arch Biochem Biophys. 1982; 217, 401–410.
Boveris, A, Oshino, N, Chance, B. The cellular production of hydrogen peroxide. Biochem J. 1972; 128, 617–630.
Turrens, JF. Superoxide production by the mitochondrial respiratory chain. Biosci Rep. 1997; 17, 3–8.
Turrens, JF. Mitochondrial formation of reactive oxygen species. J Physiol. 2003; 552(Pt 2), 335–344.
Figueira, TR, Barros, MH, Camargo, AA, et al. Mitochondria as a source of reactive oxygen and nitrogen species: from molecular mechanisms to human health. Antioxid Redox Signal. 2013; 18, 2029–2074.
Andreyev, AY, Kushnareva, YE, Starkov, AA. Mitochondrial metabolism of reactive oxygen species. Biochemistry (Mosc). 2005; 70, 200–214.
Halliwell, B. Oxidative stress and neurodegeneration: where are we now?
J Neurochem. 2006; 97, 1634–1658.
Halliwell, B. Free radicals and antioxidants: a personal view. Nutr Rev. 1994; 52(Pt 1), 253–265.
Halliwell, B. Free radicals and antioxidants: updating a personal view. Nutr Rev. 2012; 70, 257–265.
Flora, SJ. Role of free radicals and antioxidants in health and disease. Cell Mol Biol (Noisy-le-grand). 2007; 53, 1–2.
Jackson, MJ, Papa, S, Bolanos, J, et al. Antioxidants, reactive oxygen and nitrogen species, gene induction and mitochondrial function. Mol Aspects Med. 2002; 23, 209–285.
Conrad, M, Schick, J, Angeli, JP. Glutathione and thioredoxin dependent systems in neurodegenerative disease: what can be learned from reverse genetics in mice. Neurochem Int. 2013; 62, 738–749.
Perkins, A, Nelson, KJ, Parsonage, D, Poole, LB, Karplus, PA. Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling. Trends Biochem Sci. 2015; 40, 435–445.
Hirooka, Y. Role of reactive oxygen species in brainstem in neural mechanisms of hypertension. Auton Neurosci. 2008; 142, 20–24.
Peterson, JR, Sharma, RV, Davisson, RL. Reactive oxygen species in the neuropathogenesis of hypertension. Curr Hypertens Rep. 2006; 8, 232–241.
Shichiri, M. The role of lipid peroxidation in neurological disorders. J Clin Biochem Nutr. 2014; 54, 151–160.
Fisher-Wellman, K, Bell, HK, Bloomer, RJ. Oxidative stress and antioxidant defense mechanisms linked to exercise during cardiopulmonary and metabolic disorders. Oxid Med Cell Longev. 2009; 2, 43–51.
Powers, SK, Jackson, MJ. Exercise-induced oxidative stress: cellular mechanisms and impact on muscle force production. Physiol Rev. 2008; 88, 1243–1276.
Li, JM, Shah, AM. Endothelial cell superoxide generation: regulation and relevance for cardiovascular pathophysiology. Am J Physiol Regul Integr Comp Physiol. 2004; 287, R1014–R1030.
Pritsos, CA. Cellular distribution, metabolism and regulation of the xanthine oxidoreductase enzyme system. Chem Biol Interact. 2000; 129, 195–208.
Cantu-Medellin, N, Kelley, EE. Xanthine oxidoreductase-catalyzed reactive species generation: a process in critical need of reevaluation. Redox biology. 2013; 1, 353–358.
Bedard, K, Krause, KH. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol Rev. 2007; 87, 245–313.
Murphy, MP. How mitochondria produce reactive oxygen species. Biochem J. 2009; 417, 1–13.
Brand, MD. The sites and topology of mitochondrial superoxide production. Exp Gerontol. 2010; 45, 466–472.
Quinlan, CL, Orr, AL, Perevoshchikova, IV, et al. Mitochondrial complex II can generate reactive oxygen species at high rates in both the forward and reverse reactions. J Biol Chem. 2012; 287, 27255–27264.
Fisher-Wellman, KH, Gilliam, LA, Lin, CT, et al. Mitochondrial glutathione depletion reveals a novel role for the pyruvate dehydrogenase complex as a key H2O2-emitting source under conditions of nutrient overload. Free Radic Biol Med. 2013; 65, 1201–1208.
Brautigam, CA, Wynn, RM, Chuang, JL, Chuang, DT. Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex. J Biol Chem. 2009; 284, 13086–13098.
Ambrus, A, Nemeria, NS, Torocsik, B, et al. Formation of reactive oxygen species by human and bacterial pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components. Free Radic Biol Med. 2015; 89, 642–650.
Tretter, L, Adam-Vizi, V. Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase. J Neurosci. 2004; 24, 7771–7778.
Starkov, AA, Fiskum, G, Chinopoulos, C, et al. Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species. J Neurosci. 2004; 24, 7779–7788.
Orr, AL, Quinlan, CL, Perevoshchikova, IV, Brand, MD. A refined analysis of superoxide production by mitochondrial sn-glycerol 3-phosphate dehydrogenase. J Biol Chem. 2012; 287, 42921–42935.
Tretter, L, Takacs, K, Hegedus, V, Adam-Vizi, V. Characteristics of alpha-glycerophosphate-evoked H2O2 generation in brain mitochondria. J Neurochem. 2007; 100, 650–663.
St-Pierre, J, Buckingham, JA, Roebuck, SJ, Brand, MD. Topology of superoxide production from different sites in the mitochondrial electron transport chain. J Biol Chem. 2002; 277, 44784–44790.
Perevoshchikova, IV, Quinlan, CL, Orr, AL, Gerencser, AA, Brand, MD. Sites of superoxide and hydrogen peroxide production during fatty acid oxidation in rat skeletal muscle mitochondria. Free Radic Biol Med. 2013; 61, 298–309.
Di Lisa, F, Kaludercic, N, Carpi, A, Menabo, R, Giorgio, M. Mitochondria and vascular pathology. Pharmacol Rep. 2009; 61, 123–130.
Youdim, MB, Edmondson, D, Tipton, KF. The therapeutic potential of monoamine oxidase inhibitors. Nat Rev Neurosci. 2006; 7, 295–309.
Tipton, KF, Boyce, S, O’Sullivan, J, Davey, GP, Healy, J. Monoamine oxidases: certainties and uncertainties. Curr Med Chem. 2004; 11, 1965–1982.
Toninello, A, Salvi, M, Pietrangeli, P, Mondovi, B. Biogenic amines and apoptosis: minireview article. Amino Acids. 2004; 26, 339–343.
Herrero, A, Barja, G. Localization of the site of oxygen radical generation inside the complex I of heart and nonsynaptic brain mammalian mitochondria. J Bioenerg Biomembr. 2000; 32, 609–615.
Lambert, AJ, Brand, MD. Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane. Biochem J. 2004; 382(Pt 2), 511–517.
Babcock, DF, Herrington, J, Goodwin, PC, Park, YB, Hille, B. Mitochondrial participation in the intracellular Ca2+ network. J Cell Biol. 1997; 136, 833–844.
Takeuchi, A, Kim, B, Matsuoka, S. The destiny of Ca(2+) released by mitochondria. J Physiol Sci. 2015; 65, 11–24.
Jakob, R, Beutner, G, Sharma, VK, et al. Molecular and functional identification of a mitochondrial ryanodine receptor in neurons. Neurosci Lett. 2014; 575, 7–12.
Van Petegem, F. Ryanodine receptors: structure and function. J Biol Chem. 2012; 287, 31624–31632.
Csordas, G, Varnai, P, Golenar, T, et al. Imaging interorganelle contacts and local calcium dynamics at the ER-mitochondrial interface. Mol Cell. 2010; 39, 121–132.
Csordas, G, Hajnoczky, G. SR/ER-mitochondrial local communication: calcium and ROS. Biochim Biophys Acta. 2009; 1787, 1352–1362.
Santo-Domingo, J, Demaurex, N. Calcium uptake mechanisms of mitochondria. Biochim Biophys Acta. 2010; 1797, 907–912.
Kim, B, Matsuoka, S. Cytoplasmic Na+-dependent modulation of mitochondrial Ca2+ via electrogenic mitochondrial Na+-Ca2+ exchange. J Physiol. 2008; 586, 1683–1697.
Saris, NE, Carafoli, E. A historical review of cellular calcium handling, with emphasis on mitochondria. Biochemistry (Mosc). 2005; 70, 187–194.
McCormack, JG, Denton, RM. Mitochondrial Ca2+ transport and the role of intramitochondrial Ca2+ in the regulation of energy metabolism. Dev Neurosci. 1993; 15, 165–173.
Grijalba, MT, Vercesi, AE, Schreier, S. Ca2+-induced increased lipid packing and domain formation in submitochondrial particles. A possible early step in the mechanism of Ca2+-stimulated generation of reactive oxygen species by the respiratory chain. Biochemistry. 1999; 38, 13279–13287.
Castilho, RF, Kowaltowski, AJ, Meinicke, AR, Bechara, EJ, Vercesi, AE. Permeabilization of the inner mitochondrial membrane by Ca2+ ions is stimulated by t-butyl hydroperoxide and mediated by reactive oxygen species generated by mitochondria. Free Radic Biol Med. 1995; 18, 479–486.
Rao, VK, Carlson, EA, Yan, SS. Mitochondrial permeability transition pore is a potential drug target for neurodegeneration. Biochim Biophys Acta. 2014; 1842, 1267–1272.
Grancara, S, Battaglia, V, Martinis, P, et al. Mitochondrial oxidative stress induced by Ca2+ and monoamines: different behaviour of liver and brain mitochondria in undergoing permeability transition. Amino Acids. 2012; 42, 751–759.
Quintanilla, RA, Jin, YN, von Bernhardi, R, Johnson, GV. Mitochondrial permeability transition pore induces mitochondria injury in Huntington disease. Mol Neurodegener. 2013; 8, 45.
Frezza, C, Cipolat, S, Martins de Brito, O, et al. OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion. Cell. 2006; 126, 177–189.
Mailly, F, Marin, P, Israel, M, Glowinski, J, Premont, J. Increase in external glutamate and NMDA receptor activation contribute to H2O2-induced neuronal apoptosis. J Neurochem. 1999; 73, 1181–1188.
Spencer, WA, Jeyabalan, J, Kichambre, S, Gupta, RC. Oxidatively generated DNA damage after Cu(II) catalysis of dopamine and related catecholamine neurotransmitters and neurotoxins: Role of reactive oxygen species. Free Radic Biol Med. 2011; 50, 139–147.
Cardaci, S, Filomeni, G, Rotilio, G, Ciriolo, MR. p38(MAPK)/p53 signalling axis mediates neuronal apoptosis in response to tetrahydrobiopterin-induced oxidative stress and glucose uptake inhibition: implication for neurodegeneration. Biochem J. 2010; 430, 439–451.
Zheng, H, Gal, S, Weiner, LM, et al. Novel multifunctional neuroprotective iron chelator-monoamine oxidase inhibitor drugs for neurodegenerative diseases: in vitro studies on antioxidant activity, prevention of lipid peroxide formation and monoamine oxidase inhibition. J Neurochem. 2005; 95, 68–78.
Kwan, SW, Bergeron, JM, Abell, CW. Molecular properties of monoamine oxidases A and B. Psychopharmacology (Berl). 1992; 106(Suppl), S1–S5.
Cobb, CA, Cole, MP. Oxidative and nitrative stress in neurodegeneration. Neurobiol Dis. 2015; 84, 4–21.
Pratico, D, Uryu, K, Leight, S, Trojanoswki, JQ, Lee, VM. Increased lipid peroxidation precedes amyloid plaque formation in an animal model of Alzheimer amyloidosis. J Neurosci. 2001; 21, 4183–4187.
Reed, TT, Pierce, WM, Markesbery, WR, Butterfield, DA. Proteomic identification of HNE-bound proteins in early Alzheimer disease: insights into the role of lipid peroxidation in the progression of AD. Brain Res. 2009; 1274, 66–76.
Bubber, P, Haroutunian, V, Fisch, G, Blass, JP, Gibson, GE. Mitochondrial abnormalities in Alzheimer brain: mechanistic implications. Ann Neurol. 2005; 57, 695–703.
Chen, X, Stern, D, Yan, SD. Mitochondrial dysfunction and Alzheimer’s disease. Curr Alzheimer Res. 2006; 3, 515–520.
Damiano, M, Galvan, L, Deglon, N, Brouillet, E. Mitochondria in Huntington’s disease. Biochim Biophys Acta. 2010; 1802, 52–61.
Nasr, P, Gursahani, HI, Pang, Z, et al. Influence of cytosolic and mitochondrial Ca2+, ATP, mitochondrial membrane potential, and calpain activity on the mechanism of neuron death induced by 3-nitropropionic acid. Neurochem Int. 2003; 43, 89–99.
Luo, Y, Hoffer, A, Hoffer, B, Qi, X. Mitochondria: a therapeutic target for Parkinson’s disease?
Int J Mol Sci. 2015; 16, 20704–20730.
Abdin, AA, Sarhan, NI. Intervention of mitochondrial dysfunction-oxidative stress-dependent apoptosis as a possible neuroprotective mechanism of alpha-lipoic acid against rotenone-induced parkinsonism and L-dopa toxicity. Neurosci Res. 2011; 71, 387–395.
Seet, RC, Lee, CY, Lim, EC, et al. Oxidative damage in Parkinson disease: measurement using accurate biomarkers. Free Radic Biol Med. 2010; 48, 560–566.
Dutta, R, McDonough, J, Yin, X, et al. Mitochondrial dysfunction as a cause of axonal degeneration in multiple sclerosis patients. Ann Neurol. 2006; 59, 478–489.
Schapira, AH. Complex I: inhibitors, inhibition and neurodegeneration. Exp Neurol. 2010; 224, 331–335.
Broadwater, L, Pandit, A, Clements, R, et al. Analysis of the mitochondrial proteome in multiple sclerosis cortex. Biochim Biophys Acta. 2011; 1812, 630–641.
Sarti, P, Giuffre, A, Barone, MC, et al. Nitric oxide and cytochrome oxidase: reaction mechanisms from the enzyme to the cell. Free Radic Biol Med. 2003; 34, 509–520.
Pollari, E, Goldsteins, G, Bart, G, Koistinaho, J, Giniatullin, R. The role of oxidative stress in degeneration of the neuromuscular junction in amyotrophic lateral sclerosis. Front Cell Neurosci. 2014; 8, 131.
Robberecht, W, Philips, T. The changing scene of amyotrophic lateral sclerosis. Nat Rev Neurosci. 2013; 14, 248–264.
Beal, MF, Ferrante, RJ, Browne, SE, et al. Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis. Ann Neurol. 1997; 42, 644–654.
Estevez, AG, Crow, JP, Sampson, JB, et al. Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase. Science. 1999; 286, 2498–2500.
Harraz, MM, Marden, JJ, Zhou, W, et al. SOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS model. J Clin Invest. 2008; 118, 659–670.
Paravicini, TM, Touyz, RM. Redox signaling in hypertension. Cardiovasc Res. 2006; 71, 247–258.
Chan, SH, Chan, JY. Brain stem NOS and ROS in neural mechanisms of hypertension. Antioxid Redox Signal. 2013; 20, 146–163.
Hirooka, Y, Kishi, T, Sakai, K, Takeshita, A, Sunagawa, K. Imbalance of central nitric oxide and reactive oxygen species in the regulation of sympathetic activity and neural mechanisms of hypertension. Am J Physiol Regul Integr Comp Physiol. 2011; 300, R818–R826.
Chan, SH, Tai, MH, Li, CY, Chan, JY. Reduction in molecular synthesis or enzyme activity of superoxide dismutases and catalase contributes to oxidative stress and neurogenic hypertension in spontaneously hypertensive rats. Free Radic Biol Med. 2006; 40, 2028–2039.
Chan, SH, Wu, KL, Chang, AY, Tai, MH, Chan, JY. Oxidative impairment of mitochondrial electron transport chain complexes in rostral ventrolateral medulla contributes to neurogenic hypertension. Hypertension. 2009; 53, 217–227.
Chan, SH, Wu, CA, Wu, KL, et al. Transcriptional upregulation of mitochondrial uncoupling protein 2 protects against oxidative stress-associated neurogenic hypertension. Circ Res. 2009; 105, 886–896.
Chan, SH, Chan, JY. Angiotensin-generated reactive oxygen species in brain and pathogenesis of cardiovascular diseases. Antioxid Redox Signal. 2013; 19, 1074–1084.
Nozoe, M, Hirooka, Y, Koga, Y, et al. Inhibition of Rac1-derived reactive oxygen species in nucleus tractus solitarius decreases blood pressure and heart rate in stroke-prone spontaneously hypertensive rats. Hypertension. 2007; 50, 62–68.
Godfrey, KM, Gluckman, PD, Hanson, MA. Developmental origins of metabolic disease: life course and intergenerational perspectives. Trends Endocrinol Metab. 2010; 21, 199–205.
Lucas, A, Fewtrell, MS, Cole, TJ. Fetal origins of adult disease-the hypothesis revisited. BMJ. 1999; 319, 245–249.
Colombo, J. The critical period concept: research, methodology, and theoretical issues. Psychol Bull. 1982; 91, 260–275.
Hales, CN, Barker, DJ, Clark, PM, et al. Fetal and infant growth and impaired glucose tolerance at age 64. BMJ. 1991; 303, 1019–1022.
Pigliucci, M. Developmental phenotypic plasticity: where internal programming meets the external environment. Curr Opin Plant Biol. 1998; 1, 87–91.
Khan, I, Dekou, V, Hanson, M, Poston, L, Taylor, P. Predictive adaptive responses to maternal high-fat diet prevent endothelial dysfunction but not hypertension in adult rat offspring. Circulation. 2004; 110, 1097–1102.
Hanson, M, Gluckman, P. Endothelial dysfunction and cardiovascular disease: the role of predictive adaptive responses. Heart. 2005; 91, 864–866.
Nettle, D, Frankenhuis, WE, Rickard, IJ. The evolution of predictive adaptive responses in human life history. Proc Biol Sci. 2013; 280, 20131343.
Wells, JC. The thrifty phenotype hypothesis: thrifty offspring or thrifty mother?
J Theor Biol. 2003; 221, 143–161.
Wells, JC. Flaws in the theory of predictive adaptive responses. Trends Endocrinol Metab. 2007; 18, 331–337.
Wells, JC. The thrifty phenotype: an adaptation in growth or metabolism?
Am J Hum Biol. 2011; 23, 65–75.
Bale, TL. Epigenetic and transgenerational reprogramming of brain development. Nat Rev Neurosci. 2015; 16, 332–344.
Martin-Gronert, MS, Ozanne, SE. Mechanisms underlying the developmental origins of disease. Rev Endocr Metab Disord. 2012; 13, 85–92.
Martinez, SR, Gay, MS, Zhang, L. Epigenetic mechanisms in heart development and disease. Drug Discov Today. 2015; 20, 799–811.
Ozanne, SE, Constancia, M. Mechanisms of disease: the developmental origins of disease and the role of the epigenotype. Nat Clin Pract Endocrinol Metab. 2007; 3, 539–546.
Luo, ZC, Fraser, WD, Julien, P, et al. Tracing the origins of ‘fetal origins’ of adult diseases: programming by oxidative stress?
Med Hypotheses. 2006; 66, 38–44.
Mitchell, M, Schulz, SL, Armstrong, DT, Lane, M. Metabolic and mitochondrial dysfunction in early mouse embryos following maternal dietary protein intervention. Biol Reprod. 2009; 80, 622–630.
Theys, N, Clippe, A, Bouckenooghe, T, Reusens, B, Remacle, C. Early low protein diet aggravates unbalance between antioxidant enzymes leading to islet dysfunction. PLoS One. 2009; 4, e6110.
Tarry-Adkins, JL, Chen, JH, Jones, RH, Smith, NH, Ozanne, SE. Poor maternal nutrition leads to alterations in oxidative stress, antioxidant defense capacity, and markers of fibrosis in rat islets: potential underlying mechanisms for development of the diabetic phenotype in later life. FASEB J. 2010; 24, 2762–2771.
Tarry-Adkins, JL, Martin-Gronert, MS, Fernandez-Twinn, DS, et al. Poor maternal nutrition followed by accelerated postnatal growth leads to alterations in DNA damage and repair, oxidative and nitrosative stress, and oxidative defense capacity in rat heart. FASEB J. 2013; 27, 379–390.
McGaughy, JA, Amaral, AC, Rushmore, RJ, et al. Prenatal malnutrition leads to deficits in attentional set shifting and decreases metabolic activity in prefrontal subregions that control executive function. Dev Neurosci. 2014; 36, 532–541.
Duran, P, Galler, JR, Cintra, L, Tonkiss, J. Prenatal malnutrition and sleep states in adult rats: effects of restraint stress. Physiol Behav. 2006; 89, 156–163.
Faa, G, Marcialis, MA, Ravarino, A, et al. Fetal programming of the human brain: is there a link with insurgence of neurodegenerative disorders in adulthood?
Curr Med Chem. 2014; 21, 3854–3876.
Airey, CJ, Smith, PJ, Restall, K, et al. Maternal undernutrition affects neurogenesis in the foetal mouse brain. Int J Dev Neurosci. 2015; 47(Pt A), 72.
Field, ME, Anthony, RV, Engle, TE, et al. Duration of maternal undernutrition differentially alters fetal growth and hormone concentrations. Domest Anim Endocrinol. 2015; 51, 1–7.
Partadiredja, G, Worrall, S, Bedi, KS. Early life undernutrition alters the level of reduced glutathione but not the activity levels of reactive oxygen species enzymes or lipid peroxidation in the mouse forebrain. Brain Res. 2009; 1285, 22–29.
Partadiredja, G, Worrall, S, Simpson, R, Bedi, KS. Pre-weaning undernutrition alters the expression levels of reactive oxygen species enzymes but not their activity levels or lipid peroxidation in the rat brain. Brain Res. 2008; 1222, 69–78.
Franco, MC, Akamine, EH, Reboucas, N, et al. Long-term effects of intrauterine malnutrition on vascular function in female offspring: implications of oxidative stress. Life Sci. 2007; 80, 709–715.
Franco Mdo, C, Dantas, AP, Akamine, EH, et al. Enhanced oxidative stress as a potential mechanism underlying the programming of hypertension in utero. J Cardiovasc Pharmacol. 2002; 40, 501–509.
Gupta, P, Narang, M, Banerjee, BD, Basu, S. Oxidative stress in term small for gestational age neonates born to undernourished mothers: a case control study. BMC Pediatr. 2004; 4, 14.
Gveric-Ahmetasevic, S, Sunjic, SB, Skala, H, et al. Oxidative stress in small-for-gestational age (SGA) term newborns and their mothers. Free Radic Res. 2009; 43, 376–384.
Tonkiss, J, Galler, J, Morgane, PJ, Bronzino, JD, Austin-LaFrance, RJ. Prenatal protein malnutrition and postnatal brain function. Ann N Y Acad Sci. 1993; 678, 215–227.
Morgane, PJ, Austin-LaFrance, R, Bronzino, J, et al. Prenatal malnutrition and development of the brain. Neurosci Biobehav Rev. 1993; 17, 91–128.
Morgane, PJ, Mokler, DJ, Galler, JR. Effects of prenatal protein malnutrition on the hippocampal formation. Neurosci Biobehav Rev. 2002; 26, 471–483.
Al-Gubory, KH, Fowler, PA, Garrel, C. The roles of cellular reactive oxygen species, oxidative stress and antioxidants in pregnancy outcomes. Int J Biochem Cell Biol. 2010; 42, 1634–1650.
Bonatto, F, Polydoro, M, Andrades, ME, et al. Effect of protein malnutrition on redox state of the hippocampus of rat. Brain Res. 2005; 1042, 17–22.
Halliwell, B. Free radicals, reactive oxygen species and human disease: a critical evaluation with special reference to atherosclerosis. Br J Exp Pathol. 1989; 70, 737–757.
Jackson, JH, Schraufstatter, IU, Hyslop, PA, et al. Role of hydroxyl radical in DNA damage. Transactions of the Association of American Physicians. 1987; 100, 147–157.
Gutteridge, JM, Wilkins, S. Copper salt-dependent hydroxyl radical formation. Damage to proteins acting as antioxidants. Biochim Biophys Acta. 1983; 759, 38–41.
Bonatto, F, Polydoro, M, Andrades, ME, et al. Effects of maternal protein malnutrition on oxidative markers in the young rat cortex and cerebellum. Neurosci Lett. 2006; 406, 281–284.
Alvarez, B, Radi, R. Peroxynitrite reactivity with amino acids and proteins. Amino Acids. 2003; 25, 295–311.
Feoli, AM, Siqueira, IR, Almeida, L, et al. Effects of protein malnutrition on oxidative status in rat brain. Nutrition. 2006; 22, 160–165.
Voog, L, Eriksson, T. Toluene-induced decrease in rat plasma concentrations of tyrosine and tryptophan. Acta Pharmacol Toxicol. 1984; 54, 151–153.
Tatli, M, Guzel, A, Kizil, G, et al. Comparison of the effects of maternal protein malnutrition and intrauterine growth restriction on redox state of central nervous system in offspring rats. Brain Res. 2007; 1156, 21–30.
Ferreira, DJ, Liu, Y, Fernandes, MP, Lagranha, CJ. Perinatal low-protein diet alters brainstem antioxidant metabolism in adult offspring. Nutr Neurosci. 2015; doi:10.1179/1476830515Y.0000000030, in press.
Cardoso, LM, Colombari, DS, Menani, JV, et al. Cardiovascular responses to hydrogen peroxide into the nucleus tractus solitarius. Am J Physiol Regul Integr Comp Physiol. 2009; 297, R462–R469.
Chan, SH, Chan, JY. Brain stem oxidative stress and its associated signaling in the regulation of sympathetic vasomotor tone. J Appl Physiol (1985). 2012; 113, 1921–1928.
Muzzo, S, Gregory, T, Gardner, LI. Oxygen consumption by brain mitochondria of rats malnourished in utero. J Nutr. 1973; 103, 314–317.
Alamy, M, Bengelloun, WA. Malnutrition and brain development: an analysis of the effects of inadequate diet during different stages of life in rat. Neurosci Biobehav Rev. 2012; 36, 1463–1480.
Mokler, DJ, Galler, JR, Morgane, PJ. Modulation of 5-HT release in the hippocampus of 30-day-old rats exposed in utero to protein malnutrition. Brain Res Dev Brain Res. 2003; 142, 203–208.
Olorunsogo, OO. Changes in brain mitochondrial bioenergetics in protein-deficient rats. Br J Exp Pathol. 1989; 70, 607–619.