{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T13:51:07Z","timestamp":1790171467676,"version":"4.1.0"},"reference-count":308,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2021,4,15]],"date-time":"2021-04-15T00:00:00Z","timestamp":1618444800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Antioxidants"],"abstract":"<jats:p>Mitochondria are popularly called the \u201cpowerhouses\u201d of the cell. They promote energy metabolism through the tricarboxylic acid (TCA) cycle and oxidative phosphorylation, which in contrast to cytosolic glycolysis are oxygen-dependent and significantly more substrate efficient. That is, mitochondrial metabolism provides substantially more cellular energy currency (ATP) per macronutrient metabolised. Enhancement of mitochondrial density and metabolism are associated with endurance training, which allows for the attainment of high relative VO2 max values. However, the sedentary lifestyle and diet currently predominant in the Western world lead to mitochondrial dysfunction. Underdeveloped mitochondrial metabolism leads to nutrient-induced reducing pressure caused by energy surplus, as reduced nicotinamide adenine dinucleotide (NADH)-mediated high electron flow at rest leads to \u201celectron leak\u201d and a chronic generation of superoxide radicals (O2\u2212). Chronic overload of these reactive oxygen species (ROS) damages cell components such as DNA, cell membranes, and proteins. Counterintuitively, transiently generated ROS during exercise contributes to adaptive reduction-oxidation (REDOX) signalling through the process of cellular hormesis or \u201coxidative eustress\u201d defined by Helmut Sies. However, the unaccustomed, chronic oxidative stress is central to the leading causes of mortality in the 21st century\u2014metabolic syndrome and the associated cardiovascular comorbidities. The endurance exercise training that improves mitochondrial capacity and the protective antioxidant cellular system emerges as a universal intervention for mitochondrial dysfunction and resultant comorbidities. Furthermore, exercise might also be a solution to prevent ageing-related degenerative diseases, which are caused by impaired mitochondrial recycling. This review aims to break down the metabolic components of exercise and how they translate to athletic versus metabolically diseased phenotypes. We outline a reciprocal relationship between oxidative metabolism and inflammation, as well as hypoxia. We highlight the importance of oxidative stress for metabolic and antioxidant adaptation. We discuss the relevance of lactate as an indicator of critical exercise intensity, and inferring from its relationship with hypoxia, we suggest the most appropriate mode of exercise for the case of a lost oxidative identity in metabolically inflexible patients. Finally, we propose a reciprocal signalling model that establishes a healthy balance between the glycolytic\/proliferative and oxidative\/prolonged-ageing phenotypes. This model is malleable to adaptation with oxidative stress in exercise but is also susceptible to maladaptation associated with chronic oxidative stress in disease. Furthermore, mutations of components involved in the transcriptional regulatory mechanisms of mitochondrial metabolism may lead to the development of a cancerous phenotype, which progressively presents as one of the main causes of death, alongside the metabolic syndrome.<\/jats:p>","DOI":"10.3390\/antiox10040609","type":"journal-article","created":{"date-parts":[[2021,4,15]],"date-time":"2021-04-15T12:11:00Z","timestamp":1618488660000},"page":"609","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":25,"title":["Re-Evaluating the Oxidative Phenotype: Can Endurance Exercise Save the Western World?"],"prefix":"10.3390","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5575-2037","authenticated-orcid":false,"given":"Filip","family":"Kolodziej","sequence":"first","affiliation":[{"name":"Department of Physiology, School of Medicine, College of Medicine &amp; Health, University College Cork, T12 XF62 Cork, Ireland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ken D.","family":"O\u2019Halloran","sequence":"additional","affiliation":[{"name":"Department of Physiology, School of Medicine, College of Medicine &amp; Health, University College Cork, T12 XF62 Cork, Ireland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,4,15]]},"reference":[{"key":"ref_1","first-page":"438","article-title":"Muscular exercise, lactic acid, and the supply and utilisation of oxygen. Parts I\u2013III","volume":"96","author":"Hill","year":"1924","journal-title":"Proc. R. Soc. Lond. Ser. B Contain. Pap. A Biol. Character"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1152\/jappl.1955.8.1.73","article-title":"Maximal Oxygen Intake as an Objective Measure of Cardio-Respiratory Performance","volume":"8","author":"Taylor","year":"1955","journal-title":"J. Appl. Physiol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1152\/jappl.1961.16.6.977","article-title":"Maximal oxygen uptake and heart rate in various types of muscular activity","volume":"16","author":"Astrand","year":"1961","journal-title":"J. Appl. Physiol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1113\/jphysiol.1930.sp002646","article-title":"Alterations in the lactic acid content of the blood as a result of light exercise, and associated changes in the co2-combining power of the blood and in the alveolar co2pressure","volume":"69","author":"Owles","year":"1930","journal-title":"J. Physiol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1016\/0002-9149(64)90012-8","article-title":"Detecting the threshold of anaerobic metabolism in cardiac patients during exercise","volume":"14","author":"Wasserman","year":"1964","journal-title":"Am. J. Cardiol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1055\/s-2008-1034579","article-title":"Onset of Blood Lactate Accumulation and Marathon Running Performance","volume":"2","author":"Jacobs","year":"1981","journal-title":"Int. J. Sports Med."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"407","DOI":"10.2165\/00007256-200333060-00003","article-title":"The Concept of Maximal Lactate Steady State","volume":"33","author":"Billat","year":"2003","journal-title":"Sports Med."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"E380","DOI":"10.1152\/ajpendo.1993.265.3.E380","article-title":"Regulation of endogenous fat and carbohydrate metabolism in relation to exercise intensity and duration","volume":"265","author":"Romijn","year":"1993","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1055\/s-2003-43265","article-title":"Maximal Fat Oxidation during Exercise in Trained Men","volume":"24","author":"Achten","year":"2003","journal-title":"Int. J. Sports Med."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"784","DOI":"10.1080\/17461391.2018.1554707","article-title":"The biomechanical characteristics of high-performance endurance running","volume":"19","author":"Preece","year":"2018","journal-title":"Eur. J. Sport Sci."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s40798-015-0007-y","article-title":"Running economy: Measurement, norms, and determining factors","volume":"1","author":"Barnes","year":"2015","journal-title":"Sports Med. Open"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1152\/jappl.1970.28.4.452","article-title":"Oxygen deficit-oxygen debt relationships and efficiency of anaerobic work","volume":"28","author":"Whipp","year":"1970","journal-title":"J. Appl. Physiol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1042\/bj2810021","article-title":"Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: The \u2018phosphocreatine circuit\u2019 for cellular energy homeostasis","volume":"281","author":"Wallimann","year":"1992","journal-title":"Biochem. J."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.bpc.2005.03.004","article-title":"Some factors determining the PCr recovery overshoot in skeletal muscle","volume":"116","author":"Korzeniewski","year":"2005","journal-title":"Biophys. Chem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1249\/00005768-198502000-00005","article-title":"Anaerobic threshold","volume":"17","author":"Brooks","year":"1985","journal-title":"Med. Sci. Sports Exerc."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1002\/cphy.c100072","article-title":"Oxygen Uptake Kinetics","volume":"2","author":"Poole","year":"2012","journal-title":"Compr. Physiol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1403","DOI":"10.1111\/j.1432-1033.2004.04044.x","article-title":"Fifty years of muscle and the sliding filament hypothesis","volume":"271","author":"Huxley","year":"2004","journal-title":"Eur. J. Biochem."},{"key":"ref_18","unstructured":"Boron, W., and Boulpaep, E. (2017). Medical Physiology, Elsevier. [3rd ed.]."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1016\/S0006-3495(00)76349-1","article-title":"ATP Consumption and Efficiency of Human Single Muscle Fibers with Different Myosin Isoform Composition","volume":"79","author":"He","year":"2000","journal-title":"Biophys. J."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1002\/mrm.1910030107","article-title":"Energetics of human muscle: Exercise-induced ATP depletion","volume":"3","author":"Taylor","year":"1986","journal-title":"Magn. Reson. Med."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"8780","DOI":"10.1073\/pnas.85.23.8780","article-title":"Energy metabolism of the untrained muscle of elite runners as observed by 31P magnetic resonance spectroscopy: Evidence suggesting a genetic endowment for endurance exercise","volume":"85","author":"Park","year":"1988","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12970-018-0207-1","article-title":"Understanding the factors that effect maximal fat oxidation","volume":"15","author":"Purdom","year":"2018","journal-title":"J. Int. Soc. Sports Nutr."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1007\/s40279-014-0154-1","article-title":"New Insights into the Interaction of Carbohydrate and Fat Metabolism during Exercise","volume":"44","author":"Spriet","year":"2014","journal-title":"Sports Med."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.1016\/j.cmet.2017.04.015","article-title":"Metabolic Flexibility in Health and Disease","volume":"25","author":"Goodpaster","year":"2017","journal-title":"Cell Metab."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"652","DOI":"10.1042\/bj0930652","article-title":"Regulation of glucose uptake by muscle. 8. Effects of fatty acids, ketone bodies and pyruvate, and of alloxan-diabetes and starvation, on the uptake and metabolic fate of glucose in rat heart and diaphragm muscles","volume":"93","author":"Randle","year":"1964","journal-title":"Biochem. J."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"2253","DOI":"10.1152\/jappl.1994.76.6.2253","article-title":"Balance of carbohydrate and lipid utilization during exercise: The \u201ccrossover\u201d concept","volume":"76","author":"Brooks","year":"1994","journal-title":"J. Appl. Physiol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-019-12934-8","article-title":"Complex I is bypassed during high intensity exercise","volume":"10","author":"Nilsson","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1016\/j.cmet.2015.09.004","article-title":"Oxygen Sensing by Arterial Chemoreceptors Depends on Mitochondrial Complex I Signaling","volume":"22","author":"Gao","year":"2015","journal-title":"Cell Metab."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.cmet.2018.05.009","article-title":"Acute O2 Sensing: Role of Coenzyme QH2\/Q Ratio and Mitochondrial ROS Compartmentalization","volume":"28","author":"Gao","year":"2018","journal-title":"Cell Metab."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"2679","DOI":"10.1152\/jappl.2001.91.6.2679","article-title":"Skeletal muscle intracellular Po 2assessed by myoglobin desaturation: Response to graded exercise","volume":"91","author":"Richardson","year":"2001","journal-title":"J. Appl. Physiol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1016\/j.cophys.2019.05.010","article-title":"Exercise physiology: Exercise hyperpnea","volume":"10","author":"Ward","year":"2019","journal-title":"Curr. Opin. Physiol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1373","DOI":"10.1113\/JP275465","article-title":"Identifying the role of group III\/IV muscle afferents in the carotid baroreflex control of mean arterial pressure and heart rate during exercise","volume":"596","author":"Hureau","year":"2018","journal-title":"J. Physiol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1152\/japplphysiol.00490.2019","article-title":"Pharmacological attenuation of group III\/IV muscle afferents improves endurance performance when oxygen delivery to locomotor muscles is preserved","volume":"127","author":"Hureau","year":"2019","journal-title":"J. Appl. Physiol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1548","DOI":"10.1152\/jappl.1988.65.4.1548","article-title":"Responses in muscle sympathetic activity to acute hypoxia in humans","volume":"65","author":"Saito","year":"1988","journal-title":"J. Appl. Physiol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1442","DOI":"10.1111\/j.1476-5381.2011.01647.x","article-title":"\u03b22-Adrenoceptors increase translocation of GLUT4 via GPCR kinase sites in the receptor C-terminal tail","volume":"165","author":"Dehvari","year":"2012","journal-title":"Br. J. Pharmacol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1170","DOI":"10.1152\/japplphysiol.00368.2004","article-title":"Use of intramuscular triacylglycerol as a substrate source during exercise in humans","volume":"97","year":"2004","journal-title":"J. Appl. Physiol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"E1158","DOI":"10.1152\/ajpendo.00272.2012","article-title":"Prolonged exercise training increases intramuscular lipid content and perilipin 2 expression in type I muscle fibers of patients with type 2 diabetes","volume":"303","author":"Shaw","year":"2012","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"5755","DOI":"10.1210\/jcem.86.12.8075","article-title":"Skeletal Muscle Lipid Content and Insulin Resistance: Evidence for a Paradox in Endurance-Trained Athletes","volume":"86","author":"Goodpaster","year":"2001","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.molmet.2018.08.004","article-title":"Distinct lipid droplet characteristics and distribution unmask the apparent contradiction of the athlete\u2019s paradox","volume":"17","author":"Daemen","year":"2018","journal-title":"Mol. Metab."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1194\/jlr.P028910","article-title":"PPAR\u03b3 coactivator-1\u03b1 contributes to exercise-induced regulation of intramuscular lipid droplet programming in mice and humans","volume":"54","author":"Koves","year":"2012","journal-title":"J. Lipid Res."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1172\/JCI10268","article-title":"Peroxisome proliferator\u2013activated receptor \u03b3 coactivator-1 promotes cardiac mitochondrial biogenesis","volume":"106","author":"Lehman","year":"2000","journal-title":"J. Clin. Investig."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/S0092-8674(00)80611-X","article-title":"Mechanisms Controlling Mitochondrial Biogenesis and Respiration through the Thermogenic Coactivator PGC-1","volume":"98","author":"Wu","year":"1999","journal-title":"Cell"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1016\/S0006-291X(02)00881-1","article-title":"Effects of low-intensity prolonged exercise on PGC-1 mRNA expression in rat epitrochlearis muscle","volume":"296","author":"Terada","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1113\/jphysiol.2002.034850","article-title":"Exercise induces transient transcriptional activation of the PGC-1\u03b1 gene in human skeletal muscle","volume":"546","author":"Pilegaard","year":"2003","journal-title":"J. Physiol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"599","DOI":"10.3389\/fphys.2018.00599","article-title":"Contextualising Maximal Fat Oxidation During Exercise: Determinants and Normative Values","volume":"9","author":"Maunder","year":"2018","journal-title":"Front. Physiol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1055\/s-0043-117178","article-title":"Maximal Fat Oxidation is Related to Performance in an Ironman Triathlon","volume":"38","author":"Frandsen","year":"2017","journal-title":"Int. J. Sports Med."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1055\/a-0660-0031","article-title":"Peak Fat Oxidation is not Independently Related to Ironman Performance in Women","volume":"39","author":"Vest","year":"2018","journal-title":"Int. J. Sports Med."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1055\/s-2003-45232","article-title":"Fat Oxidation in Men and Women Endurance Athletes in Running and Cycling","volume":"25","author":"Knechtle","year":"2004","journal-title":"Int. J. Sports Med."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"864","DOI":"10.3945\/ajcn.116.133520","article-title":"Dietary intake is independently associated with the maximal capacity for fat oxidation during exercise","volume":"105","author":"Fletcher","year":"2017","journal-title":"Am. J. Clin. Nutr."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"6472","DOI":"10.1073\/pnas.0308686101","article-title":"The estrogen-related receptor (ERR) functions in PPAR coactivator 1 (PGC-1)-induced mitochondrial biogenesis","volume":"101","author":"Schreiber","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1007\/s11906-006-0080-1","article-title":"Estrogen and hypertension","volume":"8","author":"Ashraf","year":"2006","journal-title":"Curr. Hypertens. Rep."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1161\/01.HYP.0000100443.09293.4F","article-title":"Reactive Oxygen Species in the Vasculature","volume":"42","author":"Taniyama","year":"2003","journal-title":"Hypertension"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12944-018-0730-8","article-title":"Exercise training improves intramuscular triglyceride lipolysis sensitivity in high-fat diet induced obese mice","volume":"17","author":"Ko","year":"2018","journal-title":"Lipids Health Dis."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1055\/s-0030-1249621","article-title":"Effects of One Year Aerobic Endurance Training on Resting Metabolic Rate and Exercise Fat Oxidation in Previously Untrained Men and Women","volume":"31","author":"Meyer","year":"2010","journal-title":"Int. J. Sports Med."},{"key":"ref_55","first-page":"174","article-title":"Relationship between Fat Oxidation and Lactate Threshold in Athletes and Obese Women and Men","volume":"3","author":"Bircher","year":"2004","journal-title":"J. Sports Sci. Med."},{"key":"ref_56","first-page":"31","article-title":"Relationship between training status and maximal fat oxidation","volume":"9","author":"Pires","year":"2010","journal-title":"J. Sports Sci. Med."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"E543","DOI":"10.1152\/ajpendo.00232.2016","article-title":"Liver glycogen metabolism during and after prolonged endurance-type exercise","volume":"311","author":"Gonzalez","year":"2016","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fphys.2011.00112","article-title":"The Role of Skeletal Muscle Glycogen Breakdown for Regulation of Insulin Sensitivity by Exercise","volume":"2","author":"Jensen","year":"2011","journal-title":"Front. Physiol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"4405","DOI":"10.1113\/jphysiol.2013.251629","article-title":"Muscle glycogen stores and fatigue","volume":"591","author":"Westerblad","year":"2013","journal-title":"J. Physiol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1111\/sms.12599","article-title":"Muscle glycogen and cell function-Location, location, location","volume":"25","author":"Nielsen","year":"2015","journal-title":"Scand. J. Med. Sci. Sports"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"E1053","DOI":"10.1152\/ajpendo.00324.2010","article-title":"Subcellular localization-dependent decrements in skeletal muscle glycogen and mitochondria content following short-term disuse in young and old men","volume":"299","author":"Nielsen","year":"2010","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_62","doi-asserted-by":"crossref","unstructured":"Nielsen, J., Farup, J., Rahbek, S., de Paoli, F., and Vissing, K. (2015). Enhanced Glycogen Storage of a Subcellular Hot Spot in Human Skeletal Muscle during Early Recovery from Eccentric Contractions. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0127808"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"2003","DOI":"10.1113\/jphysiol.2014.271528","article-title":"Subcellular distribution of glycogen and decreased tetanic Ca2+ I n fatigued single intact mouse muscle fibres","volume":"592","author":"Nielsen","year":"2014","journal-title":"J. Physiol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1007\/s10974-019-09524-y","article-title":"Effects of reduced muscle glycogen on excitation\u2013contraction coupling in rat fast-twitch muscle: A glycogen removal study","volume":"40","author":"Watanabe","year":"2019","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1113\/JP278543","article-title":"Inhibition of glycogenolysis prolongs action potential repriming period and impairs muscle function in rat skeletal muscle","volume":"598","author":"Jensen","year":"2020","journal-title":"J. Physiol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"890","DOI":"10.3945\/jn.110.137075","article-title":"Carbohydrate Ingestion during Endurance Exercise Improves Performance in Adults","volume":"141","author":"Temesi","year":"2011","journal-title":"J. Nutr."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1136\/bjsm.25.1.41","article-title":"Carbohydrate loading in practice: High muscle glycogen concentration is not certain","volume":"25","author":"Fogelholm","year":"1991","journal-title":"Br. J. Sports Med."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1113\/jphysiol.2007.135301","article-title":"Fatty acid binding protein facilitates sarcolemmal fatty acid transport but not mitochondrial oxidation in rat and human skeletal muscle","volume":"582","author":"Holloway","year":"2007","journal-title":"J. Physiol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"16522","DOI":"10.1074\/jbc.M109.004788","article-title":"Greater Transport Efficiencies of the Membrane Fatty Acid Transporters FAT\/CD36 and FATP4 Compared with FABPpm and FATP1 and Differential Effects on Fatty Acid Esterification and Oxidation in Rat Skeletal Muscle","volume":"284","author":"Nickerson","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1200","DOI":"10.1210\/me.2007-0485","article-title":"Adipose Triglyceride Lipase Regulation of Skeletal Muscle Lipid Metabolism and Insulin Responsiveness","volume":"22","author":"Watt","year":"2008","journal-title":"Mol. Endocrinol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1007\/s40279-015-0394-8","article-title":"The Physiological Regulation of Skeletal Muscle Fatty Acid Supply and Oxidation during Moderate-Intensity Exercise","volume":"45","year":"2015","journal-title":"Sports Med."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"E254","DOI":"10.1152\/ajpendo.00051.2006","article-title":"Coimmunoprecipitation of FAT\/CD36 and CPT I in skeletal muscle increases proportionally with fat oxidation after endurance exercise training","volume":"291","author":"Schenk","year":"2006","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"48","DOI":"10.20463\/jenb.2016.0057","article-title":"Relationship between FAT\/CD36 Protein in Skeletal Muscle and Whole-body Fat Oxidation in Endurance-trained Mice","volume":"20","author":"Kim","year":"2016","journal-title":"J. Exerc. Nutr. Biochem."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.1152\/japplphysiol.01278.2003","article-title":"Lipid-binding proteins and lipoprotein lipase activity in human skeletal muscle: Influence of physical activity and gender","volume":"97","author":"Kiens","year":"2004","journal-title":"J. Appl. Physiol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1139\/H09-019","article-title":"Triglyceride lipases alter fuel metabolism and mitochondrial gene expression","volume":"34","author":"Watt","year":"2009","journal-title":"Appl. Physiol. Nutr. Metab."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"E813","DOI":"10.1152\/ajpendo.00436.2002","article-title":"Regulation of 5\u2032AMP-activated protein kinase activity and substrate utilization in exercising human skeletal muscle","volume":"284","author":"Wojtaszewski","year":"2003","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"E203","DOI":"10.1152\/ajpendo.00624.2007","article-title":"Determinants of intramyocellular triglyceride turnover: Implications for insulin sensitivity","volume":"294","author":"Moro","year":"2008","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1079\/PNS2004360","article-title":"Regulation and role of hormone-sensitive lipase activity in human skeletal muscle","volume":"63","author":"Watt","year":"2004","journal-title":"Proc. Nutr. Soc."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1042\/BJ20082055","article-title":"AMPK and the biochemistry of exercise: Implications for human health and disease","volume":"418","author":"Richter","year":"2009","journal-title":"Biochem. J."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"16092","DOI":"10.1073\/pnas.1105062108","article-title":"AMP-activated protein kinase (AMPK) B1B2 muscle null mice reveal an essential role for AMPK in maintaining mitochondrial content and glucose uptake during exercise","volume":"108","author":"Maarbjerg","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"E47","DOI":"10.1152\/ajpendo.90690.2008","article-title":"\u03b12-AMPK activity is not essential for an increase in fatty acid oxidation during low-intensity exercise","volume":"296","author":"Miura","year":"2009","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1113\/jphysiol.2011.225011","article-title":"Regulation and limitations to fatty acid oxidation during exercise","volume":"590","author":"Jeppesen","year":"2012","journal-title":"J. Physiol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1111\/j.1748-1716.2011.02379.x","article-title":"Endurance but not resistance training increases intra-myocellular lipid content and \u03b2-hydroxyacyl coenzyme A dehydrogenase activity in active elderly men","volume":"205","author":"Ngo","year":"2012","journal-title":"Acta Physiol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"2230","DOI":"10.1152\/jappl.1989.67.6.2230","article-title":"Muscle malonyl-CoA decreases during exercise","volume":"67","author":"Winder","year":"1989","journal-title":"J. Appl. Physiol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"E541","DOI":"10.1152\/ajpendo.1996.270.3.E541","article-title":"Human skeletal muscle malonyl-CoA at rest and during prolonged submaximal exercise","volume":"270","author":"Odland","year":"1996","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"E1080","DOI":"10.1152\/ajpendo.1998.274.6.E1080","article-title":"Skeletal muscle malonyl-CoA content at the onset of exercise at varying power outputs in humans","volume":"274","author":"Odland","year":"1998","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"E133","DOI":"10.1152\/ajpendo.00379.2004","article-title":"Malonyl-CoA and carnitine in regulation of fat oxidation in human skeletal muscle during exercise","volume":"288","author":"Roepstorff","year":"2005","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"E462","DOI":"10.1152\/ajpendo.2000.278.3.E462","article-title":"Sensitivity of CPT I to malonyl-CoA in trained and untrained human skeletal muscle","volume":"278","author":"Starritt","year":"2000","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"E509","DOI":"10.1152\/ajpendo.00312.2005","article-title":"Identification of fatty acid translocase on human skeletal muscle mitochondrial membranes: Essential role in fatty acid oxidation","volume":"290","author":"Bezaire","year":"2006","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1113\/jphysiol.2006.125799","article-title":"New insights concerning the role of carnitine in the regulation of fuel metabolism in skeletal muscle","volume":"581","author":"Stephens","year":"2007","journal-title":"J. Physiol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1002\/mus.880140703","article-title":"Carnitine in muscle, serum, and urine of nonprofessional athletes: Effects of physical exercise, training, and L-carnitine administration","volume":"14","author":"Arenas","year":"1991","journal-title":"Muscle Nerve"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/S0009-8981(01)00804-X","article-title":"Long-term administration of l-carnitine to humans: Effect on skeletal muscle carnitine content and physical performance","volume":"318","author":"Vogt","year":"2002","journal-title":"Clin. Chim. Acta"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1123\/ijsnem.18.6.567","article-title":"Carbohydrate, Protein, and Fat Metabolism during Exercise after Oral Carnitine Supplementation in Humans","volume":"18","author":"Broad","year":"2008","journal-title":"Int. J. Sport Nutr. Exerc. Metab."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1123\/ijsnem.21.5.385","article-title":"Effects of Exercise Intensity and Altered Substrate Availability on Cardiovascular and Metabolic Responses to Exercise after Oral Carnitine Supplementation in Athletes","volume":"21","author":"Broad","year":"2011","journal-title":"Int. J. Sport Nutr. Exerc. Metab."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1113\/jphysiol.2010.201343","article-title":"Chronic oral ingestion of l-carnitine and carbohydrate increases muscle carnitine content and alters muscle fuel metabolism during exercise in humans","volume":"589","author":"Wall","year":"2011","journal-title":"J. Physiol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"22840","DOI":"10.1074\/jbc.M109.032888","article-title":"Carnitine Insufficiency Caused by Aging and Overnutrition Compromises Mitochondrial Performance and Metabolic Control","volume":"284","author":"Noland","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1194\/jlr.M043448","article-title":"Obesity and lipid stress inhibit carnitine acetyltransferase activity","volume":"55","author":"Seiler","year":"2014","journal-title":"J. Lipid Res."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"4445","DOI":"10.1016\/S0021-9258(19)41323-9","article-title":"Equilibrium constants of the reactions of choline acetyltransferase, carnitine acetyltransferase, and acetylcholinesterase under physiological conditions","volume":"250","author":"Pieklik","year":"1975","journal-title":"J. Biol. Chem."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"E855","DOI":"10.1152\/ajpendo.00526.2002","article-title":"Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs","volume":"284","author":"Sugden","year":"2003","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1111\/j.1748-1716.1990.tb08845.x","article-title":"Muscle carnitine metabolism during incremental dynamic exercise in humans","volume":"138","author":"Sahlin","year":"1990","journal-title":"Acta Physiol. Scand."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"764","DOI":"10.1016\/j.cmet.2012.04.005","article-title":"Muscle-Specific Deletion of Carnitine Acetyltransferase Compromises Glucose Tolerance and Metabolic Flexibility","volume":"15","author":"Muoio","year":"2012","journal-title":"Cell Metab."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.cmet.2015.06.003","article-title":"Carnitine Acetyltransferase Mitigates Metabolic Inertia and Muscle Fatigue during Exercise","volume":"22","author":"Seiler","year":"2015","journal-title":"Cell Metab."},{"key":"ref_103","first-page":"631","article-title":"The effects of L-carnitine supplementation on glycemic control: A systematic review and meta-analysis of randomized controlled trials","volume":"18","author":"Fathizadeh","year":"2019","journal-title":"Excli J."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"4789","DOI":"10.1113\/JP276460","article-title":"Fatigue-related group III\/IV muscle afferent feedback facilitates intracortical inhibition during locomotor exercise","volume":"596","author":"Sidhu","year":"2018","journal-title":"J. Physiol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.clinph.2016.10.008","article-title":"Group III\/IV locomotor muscle afferents alter motor cortical and corticospinal excitability and promote central fatigue during cycling exercise","volume":"128","author":"Sidhu","year":"2017","journal-title":"Clin. Neurophysiol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1016\/j.cmet.2009.05.001","article-title":"A Branched-Chain Amino Acid-Related Metabolic Signature that Differentiates Obese and Lean Humans and Contributes to Insulin Resistance","volume":"9","author":"Newgard","year":"2009","journal-title":"Cell Metab."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"2757","DOI":"10.2337\/db13-0185","article-title":"Effect of Roux-en-Y Gastric Bypass and Laparoscopic Adjustable Gastric Banding on Branched-Chain Amino Acid Metabolism","volume":"62","author":"Magkos","year":"2013","journal-title":"Diabetes"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"18386","DOI":"10.1016\/S0021-9258(19)81371-6","article-title":"Biosynthesis of branched-chain fatty acids in Bacillus subtilis. A decarboxylase is essential for branched-chain fatty acid synthetase","volume":"263","author":"Oku","year":"1988","journal-title":"J. Biol. Chem."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"E1175","DOI":"10.1152\/ajpendo.00630.2012","article-title":"Regulation of adipose branched-chain amino acid catabolism enzyme expression and cross-adipose amino acid flux in human obesity","volume":"304","author":"Lackey","year":"2013","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1002\/oby.20923","article-title":"Adipose tissue monomethyl branched-chain fatty acids and insulin sensitivity: Effects of obesity and weight loss","volume":"23","author":"Su","year":"2014","journal-title":"Obesity"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1021","DOI":"10.1038\/s41589-018-0132-2","article-title":"Enzyme promiscuity drives branched-chain fatty acid synthesis in adipose tissues","volume":"14","author":"Wallace","year":"2018","journal-title":"Nat. Chem. Biol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/j.celrep.2015.12.030","article-title":"The Acetyl Group Buffering Action of Carnitine Acetyltransferase Offsets Macronutrient-Induced Lysine Acetylation of Mitochondrial Proteins","volume":"14","author":"Davies","year":"2016","journal-title":"Cell Rep."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/j.molcel.2011.07.019","article-title":"SIRT3 Deficiency and Mitochondrial Protein Hyperacetylation Accelerate the Development of the Metabolic Syndrome","volume":"44","author":"Hirschey","year":"2011","journal-title":"Mol. Cell"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"S39","DOI":"10.1016\/j.cardfail.2017.07.107","article-title":"Mitochondrial Hyperacetylation Contributes with Ventricular Dysfunction as Consequence of SIRT3 Deficiency in Obesity and Metabolic Syndrome","volume":"23","author":"Morales","year":"2017","journal-title":"J. Card. Fail."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"8678","DOI":"10.1523\/JNEUROSCI.0798-17.2017","article-title":"AgRP Neurons Can Increase Food Intake during Conditions of Appetite Suppression and Inhibit Anorexigenic Parabrachial Neurons","volume":"37","author":"Essner","year":"2017","journal-title":"J. Neurosci."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"6923","DOI":"10.1096\/fj.201800634R","article-title":"Carnitine acetyltransferase (Crat) in hunger-sensing AgRP neurons permits adaptation to calorie restriction","volume":"32","author":"Reichenbach","year":"2018","journal-title":"FASEB J."},{"key":"ref_117","doi-asserted-by":"crossref","unstructured":"Gilles, R. (1985). Lactate: Glycolytic end product and oxidative substrate during sustained exercise in mammals\u2014the \u201clactate shuttle\u201d. Circulation, Respiration, and Metabolism, Springer.","DOI":"10.1007\/978-3-642-70610-3"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1016\/j.cmet.2018.03.008","article-title":"The Science and Translation of Lactate Shuttle Theory","volume":"27","author":"Brooks","year":"2018","journal-title":"Cell Metab."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"1713","DOI":"10.1152\/jappl.1999.87.5.1713","article-title":"Cardiac and skeletal muscle mitochondria have a monocarboxylate transporter MCT1","volume":"87","author":"Brooks","year":"1999","journal-title":"J. Appl. Physiol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/S0006-291X(03)00550-3","article-title":"Peroxisomal membrane monocarboxylate transporters: Evidence for a redox shuttle system?","volume":"304","author":"McClelland","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1113\/jphysiol.2005.087411","article-title":"Immunohistochemical analysis of MCT1, MCT2 and MCT4 expression in rat plantaris muscle","volume":"567","author":"Hashimoto","year":"2005","journal-title":"J. Physiol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"E1237","DOI":"10.1152\/ajpendo.00594.2005","article-title":"Colocalization of MCT1, CD147, and LDH in mitochondrial inner membrane of L6 muscle cells: Evidence of a mitochondrial lactate oxidation complex","volume":"290","author":"Hashimoto","year":"2006","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"1116","DOI":"10.1152\/jappl.1986.60.4.1116","article-title":"Lactate extraction during net lactate release in legs of humans during exercise","volume":"60","author":"Stanley","year":"1986","journal-title":"J. Appl. Physiol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"1345","DOI":"10.1126\/science.126.3287.1345","article-title":"Relation between Size of Neurons and Their Susceptibility to Discharge","volume":"126","author":"Henneman","year":"1957","journal-title":"Science"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1007\/BF00495780","article-title":"Lactate dehydrogenase isozymes in type I, IIA and IIB fibres of rabbit skeletal muscles","volume":"80","author":"Leberer","year":"1984","journal-title":"Histochemistry"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fnins.2015.00022","article-title":"Lactate is always the end product of glycolysis","volume":"9","author":"Rogatzki","year":"2015","journal-title":"Front. Neurosci."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1152\/physrev.00015.2007","article-title":"Skeletal Muscle Fatigue: Cellular Mechanisms","volume":"88","author":"Allen","year":"2008","journal-title":"Physiol. Rev."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"1479","DOI":"10.1152\/japplphysiol.01189.2009","article-title":"Lactic acidosis in vivo: Testing the link between lactate generation and H+ accumulation in ischemic mouse muscle","volume":"108","author":"Marcinek","year":"2010","journal-title":"J. Appl. Physiol."},{"key":"ref_129","doi-asserted-by":"crossref","unstructured":"Azevedo, J., Tietz, E., Two-Feathers, T., Paull, J., and Chapman, K. (2007). Lactate, Fructose and Glucose Oxidation Profiles in Sports Drinks and the Effect on Exercise Performance. PLoS ONE, 2.","DOI":"10.1371\/journal.pone.0000927"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"R48","DOI":"10.1186\/cc13793","article-title":"Half-molar sodium lactate infusion improves cardiac performance in acute heart failure: A pilot randomised controlled clinical trial","volume":"18","author":"Nalos","year":"2014","journal-title":"Crit. Care"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1113\/jphysiol.2007.129049","article-title":"Additive protective effects of the addition of lactic acid and adrenaline on excitability and force in isolated rat skeletal muscle depressed by elevated extracellular K+","volume":"581","author":"Overgaard","year":"2007","journal-title":"J. Physiol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"101339","DOI":"10.1016\/j.redox.2019.101339","article-title":"Lactate dehydrogenase supports lactate oxidation in mitochondria isolated from different mouse tissues","volume":"28","author":"Young","year":"2020","journal-title":"Redox Biol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fnins.2014.00407","article-title":"The mitochondrial L-lactate dehydrogenase affair","volume":"8","author":"Passarella","year":"2014","journal-title":"Front. Neurosci."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"S83","DOI":"10.1016\/j.freeradbiomed.2018.10.188","article-title":"Mitochondria-localized lactate dehydrogenase is not a biologically significant contributor to bioenergetic function in striated muscle","volume":"128","author":"Fulghum","year":"2018","journal-title":"Free Radic. Biol. Med."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1113\/jphysiol.2002.016683","article-title":"No evidence of an intracellular lactate shuttle in rat skeletal muscle","volume":"541","author":"Sahlin","year":"2002","journal-title":"J. Physiol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"6659","DOI":"10.1074\/jbc.RA117.000470","article-title":"Adaptive remodeling of skeletal muscle energy metabolism in high-altitude hypoxia: Lessons from AltitudeOmics","volume":"293","author":"Chicco","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_137","first-page":"467","article-title":"Assessment of Metabolic Flexibility by Means of Measuring Blood Lactate, Fat, and Carbohydrate Oxidation Responses to Exercise in Professional Endurance Athletes and Less-Fit Individuals","volume":"48","author":"Brooks","year":"2017","journal-title":"Sports Med."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"E81","DOI":"10.1152\/ajpendo.1999.277.1.E81","article-title":"Muscle net glucose uptake and glucose kinetics after endurance training in men","volume":"277","author":"Bergman","year":"1999","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"1684","DOI":"10.1152\/jappl.1999.87.5.1684","article-title":"Active muscle and whole body lactate kinetics after endurance training in men","volume":"87","author":"Bergman","year":"1999","journal-title":"J. Appl. Physiol."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"8738","DOI":"10.1073\/pnas.1212976110","article-title":"Skeletal muscle PGC-1a controls whole-body lactate homeostasis through estrogen-related receptor -dependent activation of LDH B and repression of LDH A","volume":"110","author":"Summermatter","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-018-28249-5","article-title":"Utilization of lactic acid in human myotubes and interplay with glucose and fatty acid metabolism","volume":"8","author":"Lund","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1007\/s00421-005-0081-9","article-title":"Linear decrease in VO2max and performance with increasing altitude in endurance athletes","volume":"96","author":"Wehrlin","year":"2005","journal-title":"Eur. J. Appl. Physiol."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1152\/nips.01382.2001","article-title":"The Lactate Paradox in Human High-Altitude Physiological Performance","volume":"17","author":"Hochachka","year":"2002","journal-title":"Physiology"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"1431","DOI":"10.1096\/fj.11-197772","article-title":"Acclimatization of skeletal muscle mitochondria to high-altitude hypoxia during an ascent of Everest","volume":"26","author":"Levett","year":"2011","journal-title":"FASEB J."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1038\/nature00904","article-title":"Transcriptional co-activator PGC-1\u03b1 drives the formation of slow-twitch muscle fibres","volume":"418","author":"Lin","year":"2002","journal-title":"Nature"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"36642","DOI":"10.1074\/jbc.M707006200","article-title":"A Role for the Transcriptional Coactivator PGC-1\u03b1 in Muscle Refueling","volume":"282","author":"Wende","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"1304","DOI":"10.1152\/japplphysiol.01231.2007","article-title":"Muscle-specific expression of PPAR\u03b3 coactivator-1\u03b1 improves exercise performance and increases peak oxygen uptake","volume":"104","author":"Calvo","year":"2008","journal-title":"J. Appl. Physiol."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"1868","DOI":"10.1128\/MCB.20.5.1868-1876.2000","article-title":"The Coactivator PGC-1 Cooperates with Peroxisome Proliferator-Activated Receptor alpha in Transcriptional Control of Nuclear Genes Encoding Mitochondrial Fatty Acid Oxidation Enzymes","volume":"20","author":"Vega","year":"2000","journal-title":"Mol. Cell. Biol."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"3820","DOI":"10.1073\/pnas.061035098","article-title":"Restoration of insulin-sensitive glucose transporter (GLUT4) gene expression in muscle cells by the transcriptional coactivator PGC-1","volume":"98","author":"Michael","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1113\/jphysiol.2008.164210","article-title":"PPAR\u03b4 agonism inhibits skeletal muscle PDC activity, mitochondrial ATP production and force generation during prolonged contraction","volume":"587","author":"Baker","year":"2009","journal-title":"J. Physiol."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1016\/j.bbadis.2011.02.014","article-title":"PPARs are a unique set of fatty acid regulated transcription factors controlling both lipid metabolism and inflammation","volume":"1812","author":"Varga","year":"2011","journal-title":"Biochim. Biophys. Acta (BBA) Mol. Basis Dis."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"2493","DOI":"10.3390\/nu6072493","article-title":"The Effects of a Ketogenic Diet on Exercise Metabolism and Physical Performance in Off-Road Cyclists","volume":"6","author":"Zajac","year":"2014","journal-title":"Nutrients"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1016\/j.cmet.2016.07.010","article-title":"Nutritional Ketosis Alters Fuel Preference and Thereby Endurance Performance in Athletes","volume":"24","author":"Cox","year":"2016","journal-title":"Cell Metab."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1038\/ijo.2016.183","article-title":"High fat induces acute and chronic inflammation in the hypothalamus: Effect of high-fat diet, palmitate and TNF-\u03b1 on appetite-regulating NPY neurons","volume":"41","author":"Dalvi","year":"2016","journal-title":"Int. J. Obes."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1016\/j.celrep.2014.09.025","article-title":"Hypothalamic PGC-1\u03b1 Protects Against High-Fat Diet Exposure by Regulating ER\u03b1","volume":"9","author":"Morselli","year":"2014","journal-title":"Cell Rep."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"15439","DOI":"10.1074\/jbc.M611214200","article-title":"Peroxisome Proliferator Activator Receptor \u03b3 Coactivator-1 Expression Is Reduced in Obesity","volume":"282","author":"Crunkhorn","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"1552","DOI":"10.2337\/db19-0088","article-title":"TFAM Enhances Fat Oxidation and Attenuates High Fat Diet Induced Insulin Resistance in Skeletal Muscle","volume":"68","author":"Koh","year":"2019","journal-title":"Diabetes"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"987","DOI":"10.1016\/j.bbrc.2008.10.088","article-title":"Role of GPR81 in lactate-mediated reduction of adipose lipolysis","volume":"377","author":"Cai","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"2811","DOI":"10.1074\/jbc.M806409200","article-title":"Lactate Inhibits Lipolysis in Fat Cells through Activation of an Orphan G-protein-coupled Receptor, GPR81","volume":"284","author":"Liu","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1038\/nature15721","article-title":"Oxygen regulation of breathing through an olfactory receptor activated by lactate","volume":"527","author":"Chang","year":"2015","journal-title":"Nature"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/ncomms15557","article-title":"Exercise induces cerebral VEGF and angiogenesis via the lactate receptor HCAR1","volume":"8","author":"Morland","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_162","doi-asserted-by":"crossref","unstructured":"Nalbandian, M., Radak, Z., and Takeda, M. (2019). N-acetyl-L-cysteine Prevents Lactate-Mediated PGC1-alpha Expression in C2C12 Myotubes. Biology, 8.","DOI":"10.3390\/biology8020044"},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"1243","DOI":"10.1152\/physrev.00031.2007","article-title":"Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production","volume":"88","author":"Powers","year":"2008","journal-title":"Physiol. Rev."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"356","DOI":"10.3390\/biom5020356","article-title":"Impact of Oxidative Stress on Exercising Skeletal Muscle","volume":"5","author":"Steinbacher","year":"2015","journal-title":"Biomolecules"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"12","DOI":"10.3109\/10715762.2013.830718","article-title":"Redefining the major contributors to superoxide production in contracting skeletal muscle. The role of NAD(P)H oxidases","volume":"48","author":"Sakellariou","year":"2013","journal-title":"Free Radic. Res."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1249\/01.MSS.0000161804.05399.3B","article-title":"Exercise-Induced Muscle Damage, Plasma Cytokines, and Markers of Neutrophil Activation","volume":"37","author":"Peake","year":"2005","journal-title":"Med. Sci. Sports Exerc."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1055\/s-2007-1021207","article-title":"Endothelium-Derived Oxidative Stress May Contribute to Exercise-Induced Muscle Damage","volume":"14","author":"Duarte","year":"1993","journal-title":"Int. J. Sports Med."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.exger.2003.09.012","article-title":"The contribution of reactive oxygen species to sarcopenia and muscle ageing","volume":"39","author":"Fulle","year":"2004","journal-title":"Exp. Gerontol."},{"key":"ref_169","doi-asserted-by":"crossref","unstructured":"Burns, D., Ali, I., Rieux, C., Healy, J., Jasionek, G., and O\u2019Halloran, K. (2017). Tempol Supplementation Restores Diaphragm Force and Metabolic Enzyme Activities in mdx Mice. Antioxidants, 6.","DOI":"10.3390\/antiox6040101"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fphys.2016.00623","article-title":"Diaphragm Muscle Adaptation to Sustained Hypoxia: Lessons from Animal Models with Relevance to High Altitude and Chronic Respiratory Diseases","volume":"7","author":"Lewis","year":"2016","journal-title":"Front. Physiol."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1152\/jappl.1993.75.3.1081","article-title":"Reactive oxygen in skeletal muscle. III. Contractility of unfatigued muscle","volume":"75","author":"Reid","year":"1993","journal-title":"J. Appl. Physiol."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fphys.2015.00239","article-title":"Potential molecular mechanisms underlying muscle fatigue mediated by reactive oxygen and nitrogen species","volume":"6","author":"Debold","year":"2015","journal-title":"Front. Physiol."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"8665","DOI":"10.1073\/pnas.0903485106","article-title":"Antioxidants prevent health-promoting effects of physical exercise in humans","volume":"106","author":"Ristow","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1080\/02640410903473844","article-title":"Altered oxidative stress in overtrained athletes","volume":"28","author":"Tanskanen","year":"2010","journal-title":"J. Sports Sci."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1139\/h03-045","article-title":"Overloaded Training Increases Exercise-Induced Oxidative Stress and Damage","volume":"28","author":"Palazzetti","year":"2003","journal-title":"Can. J. Appl. Physiol."},{"key":"ref_176","doi-asserted-by":"crossref","unstructured":"176 Gumucio, J., and Mendias, C. (2012). Atrogin-1, MuRF-1, and sarcopenia. Endocrine, 43, 12\u201321.","DOI":"10.1007\/s12020-012-9751-7"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1083\/jcb.200901052","article-title":"During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation","volume":"185","author":"Cohen","year":"2009","journal-title":"J. Cell Biol."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"26597","DOI":"10.1074\/jbc.M301850200","article-title":"Bioenergetic Analysis of Peroxisome Proliferator-activated Receptor \u03b3 Coactivators 1\u03b1 and 1\u03b2 (PGC-1\u03b1 and PGC-1\u03b2) in Muscle Cells","volume":"278","author":"Lin","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/j.cell.2006.09.024","article-title":"Suppression of Reactive Oxygen Species and Neurodegeneration by the PGC-1 Transcriptional Coactivators","volume":"127","author":"Drori","year":"2006","journal-title":"Cell"},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1016\/j.cardiores.2005.01.026","article-title":"PGC-1\u03b1 regulates the mitochondrial antioxidant defense system in vascular endothelial cells","volume":"66","author":"Valle","year":"2005","journal-title":"Cardiovasc. Res."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"2111","DOI":"10.1007\/s00421-018-3930-z","article-title":"The acute effects of walking exercise intensity on systemic cytokines and oxidative stress","volume":"118","author":"Brown","year":"2018","journal-title":"Eur. J. Appl. Physiol."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"2080","DOI":"10.1080\/02640414.2020.1770918","article-title":"Differential time responses in inflammatory and oxidative stress markers after a marathon: An observational study","volume":"38","author":"Larsen","year":"2020","journal-title":"J. Sports Sci."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12970-017-0181-z","article-title":"Effects of Methylsulfonylmethane (MSM) on exercise-induced oxidative stress, muscle damage, and pain following a half-marathon: A double-blind, randomized, placebo-controlled trial","volume":"14","author":"Withee","year":"2017","journal-title":"J. Int. Soc. Sports Nutr."},{"key":"ref_184","first-page":"501","article-title":"The Effects of Acute Low-Volume HIIT and Aerobic Exercise on Leukocyte Count and Redox Status","volume":"17","author":"Jamurtas","year":"2018","journal-title":"J. Sports Sci. Med."},{"key":"ref_185","doi-asserted-by":"crossref","unstructured":"Holloway, T., Bloemberg, D., da Silva, M., Simpson, J., Quadrilatero, J., and Spriet, L. (2015). High Intensity Interval and Endurance Training Have Opposing Effects on Markers of Heart Failure and Cardiac Remodeling in Hypertensive Rats. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0121138"},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"R927","DOI":"10.1152\/ajpregu.00048.2015","article-title":"High-intensity interval and endurance training are associated with divergent skeletal muscle adaptations in a rodent model of hypertension","volume":"308","author":"Holloway","year":"2015","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"1901","DOI":"10.1002\/jcp.24664","article-title":"Negative Regulators of Brown Adipose Tissue (BAT)-Mediated Thermogenesis","volume":"229","author":"Sharma","year":"2014","journal-title":"J. Cell. Physiol."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"1300","DOI":"10.1042\/bst0311300","article-title":"Mitochondrial matrix reactive oxygen species production is very sensitive to mild uncoupling","volume":"31","author":"Miwa","year":"2003","journal-title":"Biochem. Soc. Trans."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1016\/j.cmet.2010.11.015","article-title":"Calorie Restriction Reduces Oxidative Stress by SIRT3-Mediated SOD2 Activation","volume":"12","author":"Qiu","year":"2010","journal-title":"Cell Metab."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"14447","DOI":"10.1073\/pnas.0803790105","article-title":"A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis","volume":"105","author":"Ahn","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_191","doi-asserted-by":"crossref","unstructured":"Finley, L., Haas, W., Desquiret-Dumas, V., Wallace, D., Procaccio, V., Gygi, S., and Haigis, M. (2011). Succinate Dehydrogenase Is a Direct Target of Sirtuin 3 Deacetylase Activity. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0023295"},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"7808","DOI":"10.4049\/jimmunol.179.11.7808","article-title":"Activation of p38 MAPK by Reactive Oxygen Species Is Essential in a Rat Model of Stress-Induced Gastric Mucosal Injury","volume":"179","author":"Jia","year":"2007","journal-title":"J. Immunol."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1080\/10715760701445045","article-title":"The endogenous reactive oxygen species promote NF-\u03baB activation by targeting on activation of NF-\u03baB-inducing kinase in oral squamous carcinoma cells","volume":"41","author":"Wang","year":"2007","journal-title":"Free Radic. Res."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1161\/CIRCRESAHA.110.221911","article-title":"Reactive Oxygen Species\u2013Activated Ca\/Calmodulin Kinase II\u03b4 Is Required for Late I(Na) Augmentation Leading to Cellular Na and Ca Overload","volume":"108","author":"Wagner","year":"2011","journal-title":"Circ. Res."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1128\/MCB.19.1.21","article-title":"Regulation of the MEF2 Family of Transcription Factors by p38","volume":"19","author":"Zhao","year":"1999","journal-title":"Mol. Cell. Biol."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"7111","DOI":"10.1073\/pnas.1232352100","article-title":"An autoregulatory loop controls peroxisome proliferator-activated receptor coactivator 1 expression in muscle","volume":"100","author":"Handschin","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1006\/bbrc.1999.1145","article-title":"Role of the \u03b23-Adrenergic Receptor and\/or a Putative \u03b24-Adrenergic Receptor on the Expression of Uncoupling Proteins and Peroxisome Proliferator-Activated Receptor-\u03b3 Coactivator-1","volume":"261","author":"Boss","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"19587","DOI":"10.1074\/jbc.M408862200","article-title":"Exercise Stimulates Pgc-1\u03b1 Transcription in Skeletal Muscle through Activation of the p38 MAPK Pathway","volume":"280","author":"Akimoto","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1016\/S1097-2765(01)00390-2","article-title":"Cytokine Stimulation of Energy Expenditure through p38 MAP Kinase Activation of PPAR\u03b3 Coactivator-1","volume":"8","author":"Puigserver","year":"2001","journal-title":"Mol. Cell"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/srep32642","article-title":"Sustained elevation of NF-\u03baB activity sensitizes offspring of maternal inflammation to hypertension via impairing PGC-1\u03b1 recovery","volume":"6","author":"Deng","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1093\/cvr\/cvq080","article-title":"The p65 subunit of NF-\u03baB binds to PGC-1\u03b1, linking inflammation and metabolic disturbances in cardiac cells","volume":"87","author":"Palomer","year":"2010","journal-title":"Cardiovasc. Res."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"2246","DOI":"10.1074\/jbc.M112.375253","article-title":"The Peroxisome Proliferator-activated Receptor \u03b3 Coactivator 1\u03b1\/\u03b2 (PGC-1) Coactivators Repress the Transcriptional Activity of NF-\u03baB in Skeletal Muscle Cells","volume":"288","author":"Eisele","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"H936","DOI":"10.1152\/ajpheart.00870.2007","article-title":"Overexpression of pyruvate dehydrogenase kinase 4 in heart perturbs metabolism and exacerbates calcineurin-induced cardiomyopathy","volume":"294","author":"Zhao","year":"2008","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1113\/jphysiol.2002.017129","article-title":"Calcineurin and cardiac hypertrophy: Where have we been? Where are we going?","volume":"541","author":"Wilkins","year":"2002","journal-title":"J. Physiol."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fphys.2018.00242","article-title":"Moderate Modulation of Cardiac PGC-1\u03b1 Expression Partially Affects Age-Associated Transcriptional Remodeling of the Heart","volume":"9","author":"Whitehead","year":"2018","journal-title":"Front. Physiol."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1038\/nrm1155","article-title":"Calcium signalling: Dynamics, homeostasis and remodelling","volume":"4","author":"Berridge","year":"2003","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1007\/s10522-012-9399-y","article-title":"\u201cSR stress\u201d in mixed hindlimb muscles of aging male rats","volume":"13","author":"Russ","year":"2012","journal-title":"Biogerontology"},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"e12993","DOI":"10.1111\/acel.12993","article-title":"Peroxisome proliferator-activated receptor \u03b3 coactivator 1\u03b1 regulates mitochondrial calcium homeostasis, sarcoplasmic reticulum stress, and cell death to mitigate skeletal muscle aging","volume":"18","author":"Gill","year":"2019","journal-title":"Aging Cell"},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1074\/jbc.M606116200","article-title":"Exercise-induced Mitochondrial Biogenesis Begins before the Increase in Muscle PGC-1\u03b1 Expression","volume":"282","author":"Wright","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"R912","DOI":"10.1152\/ajpregu.00409.2009","article-title":"Acute endurance exercise increases the nuclear abundance of PGC-1\u03b1 in trained human skeletal muscle","volume":"298","author":"Little","year":"2010","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1042\/BJ20120546","article-title":"AMP-activated protein kinase: New regulation, new roles?","volume":"445","author":"Carling","year":"2012","journal-title":"Biochem. J."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"1056","DOI":"10.1038\/nature07813","article-title":"AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity","volume":"458","author":"Feige","year":"2009","journal-title":"Nature"},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"R67","DOI":"10.1152\/ajpregu.00417.2010","article-title":"Nuclear SIRT1 activity, but not protein content, regulates mitochondrial biogenesis in rat and human skeletal muscle","volume":"301","author":"Gurd","year":"2011","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"12017","DOI":"10.1073\/pnas.0705070104","article-title":"AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1","volume":"104","author":"Jager","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1111\/j.1469-7793.2000.t01-1-00221.x","article-title":"Isoform-specific and exercise intensity-dependent activation of 5\u2032-AMP-activated protein kinase in human skeletal muscle","volume":"528","author":"Wojtaszewski","year":"2000","journal-title":"J. Physiol."},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/S0006-291X(02)02465-8","article-title":"Dissociation of AMPK activity and ACC\u03b2 phosphorylation in human muscle during prolonged exercise","volume":"298","author":"Wojtaszewski","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"2205","DOI":"10.2337\/diabetes.52.9.2205","article-title":"Effect of Exercise Intensity on Skeletal Muscle AMPK Signaling in Humans","volume":"52","author":"Chen","year":"2003","journal-title":"Diabetes"},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1016\/0092-8674(95)90471-9","article-title":"Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy","volume":"82","author":"Brenman","year":"1995","journal-title":"Cell"},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1007\/s12551-011-0060-9","article-title":"nNOS regulation of skeletal muscle fatigue and exercise performance","volume":"3","author":"Percival","year":"2011","journal-title":"Biophys. Rev."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"15944","DOI":"10.1073\/pnas.0404136101","article-title":"Neuronal nitric oxide synthase negatively regulates xanthine oxidoreductase inhibition of cardiac excitation-contraction coupling","volume":"101","author":"Khan","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1152\/jappl.1997.82.1.359","article-title":"Evidence that nitric oxide increases glucose transport in skeletal muscle","volume":"82","author":"Balon","year":"1997","journal-title":"J. Appl. Physiol."},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/j.freeradbiomed.2017.06.018","article-title":"Neuronal nitric oxide synthase mediates insulin- and oxidative stress-induced glucose uptake in skeletal muscle myotubes","volume":"110","author":"Kellogg","year":"2017","journal-title":"Free Radic. Biol. Med."},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"26473","DOI":"10.1074\/jbc.M600451200","article-title":"A Transverse Tubule NADPH Oxidase Activity Stimulates Calcium Release from Isolated Triads via Ryanodine Receptor Type 1S-Glutathionylation","volume":"281","author":"Hidalgo","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"C994","DOI":"10.1152\/ajpcell.00031.2005","article-title":"Differential susceptibility of subsarcolemmal and intermyofibrillar mitochondria to apoptotic stimuli","volume":"289","author":"Adhihetty","year":"2005","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fncel.2016.00301","article-title":"NOX Activation by Subunit Interaction and Underlying Mechanisms in Disease","volume":"10","author":"Rastogi","year":"2017","journal-title":"Front. Cell. Neurosci."},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1155\/2016\/6738701","article-title":"Differential Expression of NADPH Oxidases Depends on Skeletal Muscle Fiber Type in Rats","volume":"2016","author":"Loureiro","year":"2016","journal-title":"Oxidative Med. Cell. Longev."},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"1185","DOI":"10.1089\/ars.2007.1959","article-title":"Nitric Oxide in the Vasculature: Where Does It Come from and Where Does It Go? A Quantitative Perspective","volume":"10","author":"Chen","year":"2008","journal-title":"Antioxid. Redox Signal."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"940","DOI":"10.1016\/j.freeradbiomed.2017.05.008","article-title":"Aging-associated metabolic disorder induces Nox2 activation and oxidative damage of endothelial function","volume":"108","author":"Fan","year":"2017","journal-title":"Free Radic. Biol. Med."},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"798","DOI":"10.1016\/j.bbrc.2016.08.028","article-title":"Chronic reactive oxygen species exposure inhibits glucose uptake and causes insulin resistance in C2C12 myotubes","volume":"478","author":"Ding","year":"2016","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"1474","DOI":"10.1152\/jappl.2000.88.4.1474","article-title":"HIF-1: Mediator of physiological and pathophysiological responses to hypoxia","volume":"88","author":"Semenza","year":"2000","journal-title":"J. Appl. Physiol."},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1152\/jappl.1990.69.2.785","article-title":"Muscle oxidative capacity and work performance after training under local leg ischemia","volume":"69","author":"Kaijser","year":"1990","journal-title":"J. Appl. Physiol."},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1007\/BF00374176","article-title":"Effects of training in normoxia and normobaric hypoxia on human muscle ultrastructure","volume":"425","author":"Desplanches","year":"1993","journal-title":"Pflug. Arch. Eur. J. Physiol."},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1016\/j.fob.2013.09.004","article-title":"Different evolutionary patterns of hypoxia-inducible factor \u03b1 (HIF-\u03b1) isoforms in the basal branches of Actinopterygii and Sarcopterygii","volume":"3","author":"Chi","year":"2013","journal-title":"Febs Open Bio"},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"2445","DOI":"10.1096\/fj.01-0125com","article-title":"HIF-1 is expressed in normoxic tissue and displays an organ-specific regulation under systemic hypoxia","volume":"15","author":"Stroka","year":"2001","journal-title":"FASEB J."},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1126\/science.1059817","article-title":"HIFalpha Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O2 Sensing","volume":"292","author":"Ivan","year":"2001","journal-title":"Science"},{"key":"ref_236","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1007\/s00421-005-0085-5","article-title":"Regular endurance training reduces the exercise induced HIF-1\u03b1 and HIF-2\u03b1 mRNA expression in human skeletal muscle in normoxic conditions","volume":"96","author":"Lundby","year":"2005","journal-title":"Eur. J. Appl. Physiol."},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"9723","DOI":"10.1038\/s41598-017-10097-4","article-title":"TCA cycle rewiring fosters metabolic adaptation to oxygen restriction in skeletal muscle from rodents and humans","volume":"7","author":"Capitanio","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fped.2015.00033","article-title":"Hypoxia-Inducible Factor as an Angiogenic Master Switch","volume":"3","author":"Hashimoto","year":"2015","journal-title":"Front. Pediatrics"},{"key":"ref_239","doi-asserted-by":"crossref","unstructured":"Mason, S., Howlett, R., Kim, M., Olfert, I., Hogan, M., McNulty, W., Hickey, R., Wagner, P., Kahn, C., and Giordano, F. (2004). Loss of Skeletal Muscle HIF-1\u03b1 Results in Altered Exercise Endurance. PLoS Biol., 2.","DOI":"10.1371\/journal.pbio.0020288"},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"R2059","DOI":"10.1152\/ajpregu.00335.2007","article-title":"HIF-1\u03b1 in endurance training: Suppression of oxidative metabolism","volume":"293","author":"Mason","year":"2007","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"R248","DOI":"10.1152\/ajpregu.00036.2013","article-title":"Negative regulation of HIF in skeletal muscle of elite endurance athletes: A tentative mechanism promoting oxidative metabolism","volume":"307","author":"Lindholm","year":"2014","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.celrep.2015.06.006","article-title":"Suppression of PGC-1\u03b1 Is Critical for Reprogramming Oxidative Metabolism in Renal Cell Carcinoma","volume":"12","author":"LaGory","year":"2015","journal-title":"Cell Rep."},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1016\/j.ccr.2007.04.001","article-title":"HIF-1 Inhibits Mitochondrial Biogenesis and Cellular Respiration in VHL-Deficient Renal Cell Carcinoma by Repression of C-MYC Activity","volume":"11","author":"Zhang","year":"2007","journal-title":"Cancer Cell"},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"1624","DOI":"10.1016\/j.cell.2013.11.037","article-title":"Declining NAD+ Induces a Pseudohypoxic State Disrupting Nuclear-Mitochondrial Communication during Aging","volume":"155","author":"Gomes","year":"2013","journal-title":"Cell"},{"key":"ref_245","first-page":"6669","article-title":"HIF-1-dependent regulation of hypoxic induction of the cell death factors BNIP3 and NIX in human tumors","volume":"61","author":"Sowter","year":"2001","journal-title":"Cancer Res."},{"key":"ref_246","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1097\/SHK.0b013e3182205e07","article-title":"Hypoxia-Induced Overexpression of BNIP3 is Not Dependent on Hypoxia-Inducible Factor 1\u03b1 in Mouse Hepatocytes","volume":"36","author":"Namas","year":"2011","journal-title":"Shock"},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-017-03980-7","article-title":"HIF-1-mediated suppression of mitochondria electron transport chain function confers resistance to lidocaine-induced cell death","volume":"7","author":"Okamoto","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_248","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.redox.2019.101109","article-title":"HIF-1\u03b1 protects against oxidative stress by directly targeting mitochondria","volume":"25","author":"Li","year":"2019","journal-title":"Redox Biol."},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"2925","DOI":"10.1002\/jcp.22640","article-title":"Hypoxia-inducible factor 1 mediates increased expression of NADPH oxidase-2 in response to intermittent hypoxia","volume":"226","author":"Yuan","year":"2011","journal-title":"J. Cell. Physiol."},{"key":"ref_250","first-page":"1","article-title":"Cytosolic ROS production by NADPH oxidase 2 regulates muscle glucose uptake during exercise","volume":"10","author":"Knudsen","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_251","doi-asserted-by":"crossref","unstructured":"Nanduri, J., Vaddi, D., Khan, S., Wang, N., Makarenko, V., Semenza, G., and Prabhakar, N. (2015). HIF-1\u03b1 Activation by Intermittent Hypoxia Requires NADPH Oxidase Stimulation by Xanthine Oxidase. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0119762"},{"key":"ref_252","doi-asserted-by":"crossref","unstructured":"Nanduri, J., Vaddi, D., Khan, S., Wang, N., Makerenko, V., and Prabhakar, N. (2013). Xanthine Oxidase Mediates Hypoxia-Inducible Factor-2\u03b1 Degradation by Intermittent Hypoxia. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0075838"},{"key":"ref_253","doi-asserted-by":"crossref","first-page":"21866","DOI":"10.1073\/pnas.1016089107","article-title":"PGC-1 regulates a HIF2-dependent switch in skeletal muscle fiber types","volume":"107","author":"Rasbach","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"8019","DOI":"10.1074\/jbc.M611569200","article-title":"NAD(P)H Oxidases Regulate HIF-2\u03b1 Protein Expression","volume":"282","author":"Block","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_255","doi-asserted-by":"crossref","first-page":"1297","DOI":"10.1152\/japplphysiol.00499.2015","article-title":"High-intensity interval training-induced metabolic adaptation coupled with an increase in Hif-1\u03b1 and glycolytic protein expression","volume":"119","author":"Abe","year":"2015","journal-title":"J. Appl. Physiol."},{"key":"ref_256","doi-asserted-by":"crossref","first-page":"111","DOI":"10.5604\/945117","article-title":"The HIF1A Gene Pro582Ser in Polish Power-Orientated Athletes","volume":"28","author":"Eider","year":"2011","journal-title":"Biol. Sport"},{"key":"ref_257","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1016\/j.cell.2016.07.002","article-title":"Mitochondria and Cancer","volume":"166","author":"Vyas","year":"2016","journal-title":"Cell"},{"key":"ref_258","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1111\/cns.12655","article-title":"Mitochondrial Dysfunction and Biogenesis in Neurodegenerative diseases: Pathogenesis and Treatment","volume":"23","author":"Golpich","year":"2016","journal-title":"CNS Neurosci. Ther."},{"key":"ref_259","doi-asserted-by":"crossref","first-page":"3662","DOI":"10.1172\/JCI120842","article-title":"The role of mitochondria in aging","volume":"128","author":"Jang","year":"2018","journal-title":"J. Clin. Investig."},{"key":"ref_260","doi-asserted-by":"crossref","first-page":"4137","DOI":"10.1016\/j.bbagen.2013.04.006","article-title":"Punctum on two different transcription factors regulated by PGC-1\u03b1: Nuclear factor erythroid-derived 2-like 2 and nuclear respiratory factor 2","volume":"1830","author":"Baldelli","year":"2013","journal-title":"Biochim. Biophys. Acta (BBA) Gen. Subj."},{"key":"ref_261","doi-asserted-by":"crossref","unstructured":"Rowe, G., El-Khoury, R., Patten, I., Rustin, P., and Arany, Z. (2012). PGC-1\u03b1 is Dispensable for Exercise-Induced Mitochondrial Biogenesis in Skeletal Muscle. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0041817"},{"key":"ref_262","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1073\/pnas.91.4.1309","article-title":"Activation of the human mitochondrial transcription factor A gene by nuclear respiratory factors: A potential regulatory link between nuclear and mitochondrial gene expression in organelle biogenesis","volume":"91","author":"Virbasius","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_263","doi-asserted-by":"crossref","first-page":"33554","DOI":"10.1074\/jbc.M804597200","article-title":"Nrf1 and Nrf2 Play Distinct Roles in Activation of Antioxidant Response Element-dependent Genes","volume":"283","author":"Ohtsuji","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_264","doi-asserted-by":"crossref","first-page":"6044","DOI":"10.3390\/ijms14036044","article-title":"The Role of Metallothionein in Oxidative Stress","volume":"14","author":"Nejdl","year":"2013","journal-title":"Int. J. Mol. Sci."},{"key":"ref_265","doi-asserted-by":"crossref","first-page":"GRSB.S13204","DOI":"10.4137\/GRSB.S13204","article-title":"Pathway Analysis of ChIP-Seq-Based NRF1 Target Genes Suggests a Logical Hypothesis of their Involvement in the Pathogenesis of Neurodegenerative Diseases","volume":"7","author":"Satoh","year":"2013","journal-title":"Gene Regul. Syst. Biol."},{"key":"ref_266","doi-asserted-by":"crossref","first-page":"1232","DOI":"10.1161\/01.RES.0000338597.71702.ad","article-title":"Heme Oxygenase-1 Regulates Cardiac Mitochondrial Biogenesis via Nrf2-Mediated Transcriptional Control of Nuclear Respiratory Factor-1","volume":"103","author":"Piantadosi","year":"2008","journal-title":"Circ. Res."},{"key":"ref_267","doi-asserted-by":"crossref","first-page":"2673","DOI":"10.1016\/j.yexcr.2013.07.015","article-title":"Nrf2 modulates contractile and metabolic properties of skeletal muscle in streptozotocin-induced diabetic atrophy","volume":"319","author":"Whitman","year":"2013","journal-title":"Exp. Cell Res."},{"key":"ref_268","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1089\/ars.2012.4615","article-title":"p53 Orchestrates the PGC-1\u03b1-Mediated Antioxidant Response Upon Mild Redox and Metabolic Imbalance","volume":"18","author":"Aquilano","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"ref_269","doi-asserted-by":"crossref","first-page":"8137","DOI":"10.1128\/MCB.23.22.8137-8151.2003","article-title":"Distinct Cysteine Residues in Keap1 Are Required for Keap1-Dependent Ubiquitination of Nrf2 and for Stabilization of Nrf2 by Chemopreventive Agents and Oxidative Stress","volume":"23","author":"Zhang","year":"2003","journal-title":"Mol. Cell. Biol."},{"key":"ref_270","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.redox.2012.10.001","article-title":"The Keap1-Nrf2 pathway: Mechanisms of activation and dysregulation in cancer","volume":"1","author":"Kansanen","year":"2013","journal-title":"Redox Biol."},{"key":"ref_271","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.freeradbiomed.2015.04.036","article-title":"The emerging role of Nrf2 in mitochondrial function","volume":"88","author":"Abramov","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"ref_272","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1111\/j.1474-9726.2007.00357.x","article-title":"Dynamic regulation of PGC-1\u03b1 localization and turnover implicates mitochondrial adaptation in calorie restriction and the stress response","volume":"7","author":"Anderson","year":"2008","journal-title":"Aging Cell"},{"key":"ref_273","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1042\/BST20150011","article-title":"Dual regulation of transcription factor Nrf2 by Keap1 and by the combined actions of \u03b2-TrCP and GSK-3","volume":"43","author":"Hayes","year":"2015","journal-title":"Biochem. Soc. Trans."},{"key":"ref_274","doi-asserted-by":"crossref","first-page":"511","DOI":"10.3892\/ijmm.2013.1235","article-title":"Redox regulation of tumor suppressor PTEN in cancer and aging","volume":"31","author":"Kitagishi","year":"2013","journal-title":"Int. J. Mol. Med."},{"key":"ref_275","first-page":"1","article-title":"PGC-1\u03b1 attenuates hydrogen peroxide-induced apoptotic cell death by upregulating Nrf-2 via GSK3\u03b2 inactivation mediated by activated p38 in HK-2 Cells","volume":"7","author":"Choi","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_276","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fgene.2019.00435","article-title":"Regulation of Mitochondrial Biogenesis as a Way for Active Longevity: Interaction between the Nrf2 and PGC-1\u03b1 Signaling Pathways","volume":"10","author":"Gureev","year":"2019","journal-title":"Front. Genet."},{"key":"ref_277","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1002\/hipo.20934","article-title":"Acetyl-L-carnitine-mediated neuroprotection during hypoxia is attributed to ERK1\/2-Nrf2-regulated mitochondrial biosynthesis","volume":"22","author":"Hota","year":"2011","journal-title":"Hippocampus"},{"key":"ref_278","doi-asserted-by":"crossref","first-page":"2554","DOI":"10.1073\/pnas.1312570111","article-title":"Loss of the tumor suppressor LKB1 promotes metabolic reprogramming of cancer cells via HIF-1","volume":"111","author":"Faubert","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_279","doi-asserted-by":"crossref","first-page":"E960","DOI":"10.1152\/ajpendo.00237.2005","article-title":"Endurance training increases skeletal muscle LKB1 and PGC-1\u03b1 protein abundance: Effects of time and intensity","volume":"289","author":"Taylor","year":"2005","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_280","doi-asserted-by":"crossref","first-page":"e13800","DOI":"10.14814\/phy2.13800","article-title":"Lactate administration activates the ERK1\/2, mTORC1, and AMPK pathways differentially according to skeletal muscle type in mouse","volume":"6","author":"Casas","year":"2018","journal-title":"Physiol. Rep."},{"key":"ref_281","doi-asserted-by":"crossref","first-page":"5195","DOI":"10.1113\/JP271957","article-title":"Nuclear factor erythroid-derived 2-like 2 (NFE2L2, Nrf2) mediates exercise-induced mitochondrial biogenesis and the anti-oxidant response in mice","volume":"594","author":"Merry","year":"2016","journal-title":"J. Physiol."},{"key":"ref_282","doi-asserted-by":"crossref","unstructured":"\u017bo\u0142\u0105d\u017a, J., Koziel, A., Broniarek, I., Woyda-Ploszczyca, A., Ogrodna, K., Majerczak, J., Celichowski, J., Szkutnik, Z., and Jarmuszkiewicz, W. (2017). Effect of temperature on fatty acid metabolism in skeletal muscle mitochondria of untrained and endurance-trained rats. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0189456"},{"key":"ref_283","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1007\/s11064-015-1709-8","article-title":"Moderate-Intensity Physical Exercise Protects Against Experimental 6-Hydroxydopamine-Induced Hemiparkinsonism Through Nrf2-Antioxidant Response Element Pathway","volume":"41","author":"Aguiar","year":"2015","journal-title":"Neurochem. Res."},{"key":"ref_284","doi-asserted-by":"crossref","first-page":"jcs225698","DOI":"10.1242\/jcs.225698","article-title":"ERK1\/2 phosphorylates HIF-2\u03b1 and regulates its activity by controlling its CRM1-dependent nuclear shuttling","volume":"132","author":"Gkotinakou","year":"2019","journal-title":"J. Cell Sci."},{"key":"ref_285","first-page":"680","article-title":"Erythropoietin Administration Modulates Pulmonary Nrf2 Signaling Pathway After Traumatic Brain Injury in Mice","volume":"71","author":"Jin","year":"2011","journal-title":"J. Trauma Inj. Infect. Crit. Care"},{"key":"ref_286","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1007\/s12031-017-0885-1","article-title":"The Anti-Aging Effect of Erythropoietin via the ERK\/Nrf2-ARE Pathway in Aging Rats","volume":"61","author":"Wu","year":"2017","journal-title":"J. Mol. Neurosci."},{"key":"ref_287","doi-asserted-by":"crossref","first-page":"215","DOI":"10.5847\/wjem.j.issn.1920-8642.2013.03.011","article-title":"Cardioprotective effect of erythropoietin on sepsis-induced myocardial injury in rats","volume":"4","author":"Qin","year":"2013","journal-title":"World J. Emerg. Med."},{"key":"ref_288","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1016\/j.biocel.2013.03.007","article-title":"Erythropoietin contributes to slow oxidative muscle fiber specification via PGC-1\u03b1 and AMPK activation","volume":"45","author":"Wang","year":"2013","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_289","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1007\/s10522-009-9234-2","article-title":"Origin and evolution of the free radical theory of aging: A brief personal history, 1954\u20132009","volume":"10","author":"Harman","year":"2009","journal-title":"Biogerontology"},{"key":"ref_290","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/j.tibs.2014.02.003","article-title":"FOXO transcription factors: Key regulators of cellular quality control","volume":"39","author":"Webb","year":"2014","journal-title":"Trends Biochem. Sci."},{"key":"ref_291","doi-asserted-by":"crossref","first-page":"R956","DOI":"10.1152\/ajpregu.00187.2014","article-title":"Autophagy is essential to support skeletal muscle plasticity in response to endurance exercise","volume":"307","author":"Sanchez","year":"2014","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"ref_292","first-page":"772","article-title":"Exercise-mediated modulation of autophagy in skeletal muscle","volume":"28","author":"Calbet","year":"2017","journal-title":"Scand. J. Med. Sci. Sports"},{"key":"ref_293","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1096\/fj.15-276337","article-title":"Molecular mechanisms for mitochondrial adaptation to exercise training in skeletal muscle","volume":"30","author":"Drake","year":"2015","journal-title":"FASEB J."},{"key":"ref_294","first-page":"1","article-title":"Tomatidine enhances lifespan and healthspan in C. elegans through mitophagy induction via the SKN-1\/Nrf2 pathway","volume":"7","author":"Fang","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_295","first-page":"1","article-title":"Resistance exercise initiates mechanistic target of rapamycin (mTOR) translocation and protein complex co-localisation in human skeletal muscle","volume":"7","author":"Song","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_296","doi-asserted-by":"crossref","first-page":"3506","DOI":"10.4161\/cc.9.17.12731","article-title":"Ketones and lactate \u201cfuel\u201d tumor growth and metastasis","volume":"9","author":"Bonuccelli","year":"2010","journal-title":"Cell Cycle"},{"key":"ref_297","doi-asserted-by":"crossref","first-page":"2504","DOI":"10.4161\/cc.10.15.16585","article-title":"Cancer cells metabolically \u201cfertilize\u201d the tumor microenvironment with hydrogen peroxide, driving the Warburg effect","volume":"10","author":"Lin","year":"2011","journal-title":"Cell Cycle"},{"key":"ref_298","doi-asserted-by":"crossref","first-page":"57813","DOI":"10.18632\/oncotarget.18175","article-title":"The reverse Warburg effect is likely to be an Achilles\u2019 heel of cancer that can be exploited for cancer therapy","volume":"8","author":"Fu","year":"2017","journal-title":"Oncotarget"},{"key":"ref_299","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41419-019-1877-6","article-title":"Lactate and pyruvate promote oxidative stress resistance through hormetic ROS signaling","volume":"10","author":"Tauffenberger","year":"2019","journal-title":"Cell Death Dis."},{"key":"ref_300","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/j.redox.2018.08.014","article-title":"Identification of a functional antioxidant response element at the HIF1A locus","volume":"19","author":"Lacher","year":"2018","journal-title":"Redox Biol."},{"key":"ref_301","doi-asserted-by":"crossref","first-page":"R911","DOI":"10.1016\/j.cub.2015.07.055","article-title":"Endosymbiosis and Eukaryotic Cell Evolution","volume":"25","author":"Archibald","year":"2015","journal-title":"Curr. Biol."},{"key":"ref_302","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.2337\/db13-1614","article-title":"Exercise Prevents Maternal High-Fat Diet\u2013Induced Hypermethylation of thePgc-1\u03b1 Gene and Age-Dependent Metabolic Dysfunction in the Offspring","volume":"63","author":"Laker","year":"2014","journal-title":"Diabetes"},{"key":"ref_303","doi-asserted-by":"crossref","first-page":"1366","DOI":"10.1093\/ajh\/hpw088","article-title":"Adverse Effect of High-Fat Diet on Metabolic Programming in Offspring Born to a Murine Model of Maternal Hypertension","volume":"29","author":"Longo","year":"2016","journal-title":"Am. J. Hypertens."},{"key":"ref_304","doi-asserted-by":"crossref","first-page":"2530","DOI":"10.2337\/db18-0667","article-title":"Paternal Exercise Improves Glucose Metabolism in Adult Offspring","volume":"67","author":"Stanford","year":"2018","journal-title":"Diabetes"},{"key":"ref_305","doi-asserted-by":"crossref","unstructured":"Engineer, A., Saiyin, T., Greco, E., and Feng, Q. (2019). Say NO to ROS: Their Roles in Embryonic Heart Development and Pathogenesis of Congenital Heart Defects in Maternal Diabetes. Antioxidants, 8.","DOI":"10.3390\/antiox8100436"},{"key":"ref_306","doi-asserted-by":"crossref","first-page":"e000890","DOI":"10.1136\/bmjdrc-2019-000890","article-title":"Maternal and paternal exercise regulate offspring metabolic health and beta cell phenotype","volume":"8","author":"Zheng","year":"2020","journal-title":"Bmj Open Diabetes Res. Care"},{"key":"ref_307","doi-asserted-by":"crossref","first-page":"101867","DOI":"10.1016\/j.redox.2021.101867","article-title":"Oxidative eustress: On constant alert for redox homeostasis","volume":"41","author":"Sies","year":"2021","journal-title":"Redox Biol."},{"key":"ref_308","doi-asserted-by":"crossref","unstructured":"Silva, L., Tromm, C., Doyenart, R., Thirupathi, A., Silveira, P., and Pinho, R. (2018). Effects of different frequencies of physical training on electron transport chain and oxidative damage in healthy mice. Mot. Rev. Educ. F\u00edsica, 24.","DOI":"10.1590\/s1980-6574201800040008"}],"container-title":["Antioxidants"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-3921\/10\/4\/609\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T05:48:25Z","timestamp":1760161705000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-3921\/10\/4\/609"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,4,15]]},"references-count":308,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2021,4]]}},"alternative-id":["antiox10040609"],"URL":"https:\/\/doi.org\/10.3390\/antiox10040609","relation":{},"ISSN":["2076-3921"],"issn-type":[{"value":"2076-3921","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,4,15]]}}}