{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,17]],"date-time":"2026-09-17T02:52:11Z","timestamp":1789613531452,"version":"build-2803163510"},"reference-count":136,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2019,9,30]],"date-time":"2019-09-30T00:00:00Z","timestamp":1569801600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003407","name":"Ministero dell\u2019Istruzione, dell\u2019Universit\u00e0 e della Ricerca","doi-asserted-by":"publisher","award":["2017A5TXC3"],"award-info":[{"award-number":["2017A5TXC3"]}],"id":[{"id":"10.13039\/501100003407","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nutrients"],"abstract":"<jats:p>Glutathione (GSH) is the main non-enzymatic antioxidant playing an important role in detoxification, signal transduction by modulation of protein thiols redox status and direct scavenging of radicals. The latter function is not only performed against reactive oxygen species (ROS) but GSH also has a fundamental role in buffering nitric oxide (NO), a physiologically-produced molecule having-multifaceted functions. The efficient rate of GSH synthesis and high levels of GSH-dependent enzymes are characteristic features of healthy skeletal muscle where, besides the canonical functions, it is also involved in muscle contraction regulation. Moreover, NO production in skeletal muscle is a direct consequence of contractile activity and influences several metabolic myocyte pathways under both physiological and pathological conditions. In this review, we will consider the homeostasis and intersection of GSH with NO and then we will restrict the discussion on their role in processes related to skeletal muscle function and degeneration.<\/jats:p>","DOI":"10.3390\/nu11102318","type":"journal-article","created":{"date-parts":[[2019,9,30]],"date-time":"2019-09-30T13:16:41Z","timestamp":1569849401000},"page":"2318","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":81,"title":["Glutathione and Nitric Oxide: Key Team Players in Use and Disuse of Skeletal Muscle"],"prefix":"10.3390","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7003-3172","authenticated-orcid":false,"given":"Sara","family":"Baldelli","sequence":"first","affiliation":[{"name":"IRCCS San Raffaele Pisana, Department of Human Sciences and Promotion of the Quality of Life, San Raffaele Roma Open University, 00166 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fabio","family":"Ciccarone","sequence":"additional","affiliation":[{"name":"IRCCS San Raffaele Pisana, Department of Human Sciences and Promotion of the Quality of Life, San Raffaele Roma Open University, 00166 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2095-8112","authenticated-orcid":false,"given":"Dolores","family":"Limongi","sequence":"additional","affiliation":[{"name":"IRCCS San Raffaele Pisana, Department of Human Sciences and Promotion of the Quality of Life, San Raffaele Roma Open University, 00166 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7518-5730","authenticated-orcid":false,"given":"Paola","family":"Checconi","sequence":"additional","affiliation":[{"name":"IRCCS San Raffaele Pisana, Department of Human Sciences and Promotion of the Quality of Life, San Raffaele Roma Open University, 00166 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna Teresa","family":"Palamara","sequence":"additional","affiliation":[{"name":"IRCCS San Raffaele \u2018La Pisana\u2019, 00166 Rome, Italy"},{"name":"Department of Public Health and Infectious Diseases, Sapienza University of Rome, 00185 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria Rosa","family":"Ciriolo","sequence":"additional","affiliation":[{"name":"IRCCS San Raffaele \u2018La Pisana\u2019, 00166 Rome, Italy"},{"name":"Department of Biology, University of Rome \u201cTor Vergata\u201d, 00133 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2019,9,30]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.mam.2008.05.005","article-title":"Regulation of Glutathione Synthesis","volume":"30","author":"Lu","year":"2009","journal-title":"Mol. Asp. Med."},{"key":"ref_2","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"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1096\/fasebj.13.10.1169","article-title":"Regulation of hepatic glutathione synthesis: Current concepts and controversies","volume":"13","author":"Lu","year":"1999","journal-title":"FASEB J."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1089\/ars.2010.3540","article-title":"S-glutathionylation: From molecular mechanisms to health outcomes","volume":"15","author":"Xiong","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"21021","DOI":"10.3390\/ijms141021021","article-title":"Impaired glutathione synthesis in neurodegeneration","volume":"14","author":"Aoyama","year":"2013","journal-title":"Int. J. Mol. Sci."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"972913","DOI":"10.1155\/2013\/972913","article-title":"Role of glutathione in cancer progression and chemoresistance","volume":"2013","author":"Traverso","year":"2013","journal-title":"Oxid. Med. Cell. Longev."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1515\/BC.2009.033","article-title":"Glutathione dysregulation and the etiology and progression of human diseases","volume":"390","author":"Ballatori","year":"2009","journal-title":"Biol. Chem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"2139","DOI":"10.1113\/jphysiol.2011.206623","article-title":"Age-related changes in skeletal muscle reactive oxygen species generation and adaptive responses to reactive oxygen species","volume":"589","author":"Jackson","year":"2011","journal-title":"J. Physiol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1080\/10715760000300231","article-title":"Regulation of iNOS mRNA levels in endothelial cells by glutathione, a double-edged sword","volume":"32","author":"Chen","year":"2000","journal-title":"Free Radic. Res."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"762","DOI":"10.1124\/jpet.300.3.762","article-title":"Nitric oxide synthase expression in hypertension induced by inhibition of glutathione synthase","volume":"300","author":"Zhou","year":"2002","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1242\/jcs.077149","article-title":"Nitric oxide is the primary mediator of cytotoxicity induced by GSH depletion in neuronal cells","volume":"124","author":"Aquilano","year":"2011","journal-title":"J. Cell. Sci."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1038\/nrd2466","article-title":"The nitrate-nitrite-nitric oxide pathway in physiology and therapeutics","volume":"7","author":"Lundberg","year":"2008","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.1096\/fasebj.9.13.7557022","article-title":"Molecular mechanisms and therapeutic strategies related to nitric oxide","volume":"9","author":"Moncada","year":"1995","journal-title":"FASEB J."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1002\/jemt.1165","article-title":"NO message from muscle","volume":"55","author":"Grozdanovic","year":"2001","journal-title":"Microsc. Res. Tech."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1007\/s10787-007-0013-x","article-title":"Role of nitric oxide in inflammatory diseases","volume":"15","author":"Sharma","year":"2007","journal-title":"Inflammopharmacology"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"7130","DOI":"10.1158\/0008-5472.CAN-08-0410","article-title":"Nitric Oxide Is a Key Component in Inflammation-Accelerated Tumorigenesis","volume":"68","author":"Hussain","year":"2008","journal-title":"Cancer Res."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S0076-6879(08)36001-7","article-title":"Chemistry of nitric oxide and related species","volume":"436","author":"Hughes","year":"2008","journal-title":"Meth. Enzymol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/j.molmed.2009.06.007","article-title":"Protein S-nitrosylation in health and disease: A current perspective","volume":"15","author":"Foster","year":"2009","journal-title":"Trends Mol. Med."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"2660","DOI":"10.1016\/j.biocel.2008.05.013","article-title":"Glutathione and copper, zinc superoxide dismutase are modulated by overexpression of neuronal nitric oxide synthase","volume":"40","author":"Baldelli","year":"2008","journal-title":"Int. J. Biochem. Cell. Biol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1016\/S0014-5793(99)00371-3","article-title":"The induction of GSH synthesis by nanomolar concentrations of NO in endothelial cells: A role for gamma-glutamylcysteine synthetase and gamma-glutamyl transpeptidase","volume":"448","author":"Moellering","year":"1999","journal-title":"FEBS Lett."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1555","DOI":"10.1038\/sj.cdd.4401754","article-title":"Disulfide relays and phosphorylative cascades: Partners in redox-mediated signaling pathways","volume":"12","author":"Filomeni","year":"2005","journal-title":"Cell. Death Differ."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1111\/j.1474-9726.2006.00198.x","article-title":"Free radical generation by skeletal muscle of adult and old mice: Effect of contractile activity","volume":"5","author":"Vasilaki","year":"2006","journal-title":"Aging Cell."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1152\/physrev.2001.81.1.209","article-title":"Physiology of Nitric Oxide in Skeletal Muscle","volume":"81","author":"Stamler","year":"2001","journal-title":"Physiol. Rev."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1854","DOI":"10.1152\/jappl.1992.73.5.1854","article-title":"Glutathione and antioxidant enzymes in skeletal muscle: Effects of fiber type and exercise intensity","volume":"73","author":"Ji","year":"1992","journal-title":"J. Appl. Physiol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/0014-5793(85)80919-4","article-title":"Changes in the glutathione status of plasma, liver and muscle following exhaustive exercise in rats","volume":"185","author":"Lew","year":"1985","journal-title":"FEBS Lett."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.bbrc.2018.05.045","article-title":"Mini-Review: Oxidative stress, redox stress or redox success?","volume":"502","author":"Gutteridge","year":"2018","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1515\/BC.2004.001","article-title":"The chemistry of nitrosative stress induced by nitric oxide and reactive nitrogen oxide species. Putting perspective on stressful biological situations","volume":"385","author":"Ridnour","year":"2005","journal-title":"Biol. Chem."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1111\/bph.14533","article-title":"Nitric oxide synthase enzymology in the 20 years after the Nobel Prize","volume":"176","author":"Stuehr","year":"2019","journal-title":"Br. J. Pharmac."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.1161\/01.HYP.23.6.1121","article-title":"Nitric oxide synthase isozymes. Characterization, purification, molecular cloning, and functions","volume":"23","author":"Closs","year":"1994","journal-title":"Hypertension"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1006\/bbrc.1998.9578","article-title":"Isolation and Characterization of a Novel, Human Neuronal Nitric Oxide Synthase cDNA","volume":"251","author":"Larsson","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"11204","DOI":"10.1074\/jbc.271.19.11204","article-title":"Neuronal Nitric-oxide Synthase-, an Alternatively Spliced Isoform Expressed in Differentiated Skeletal Muscle","volume":"271","author":"Silvagno","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1016\/j.freeradbiomed.2014.10.575","article-title":"Regulation of iNOS function and cellular redox state by macrophage Gch1 reveals specific requirements for tetrahydrobiopterin in NRF2 activation","volume":"79","author":"McNeill","year":"2015","journal-title":"Free Rad. Biol. Med."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"38079","DOI":"10.1074\/jbc.M205256200","article-title":"Biochemistry of Mitochondrial Nitric-oxide Synthase","volume":"277","author":"Elfering","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1016\/j.mito.2011.05.010","article-title":"Functional evidence for nitric oxide production by skeletal-muscle mitochondria from lipopolysaccharide-treated mice","volume":"12","author":"Aguirre","year":"2012","journal-title":"Mitochondrion"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/j.freeradbiomed.2010.04.004","article-title":"Subcellular and cellular locations of nitric-oxide synthase isoforms as determinants of health and disease","volume":"49","author":"Villanueva","year":"2010","journal-title":"Free Rad. Biol. Med."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"618","DOI":"10.1016\/j.redox.2017.09.009","article-title":"Fundamentals on the biochemistry of peroxynitrite and protein tyrosine nitration","volume":"14","author":"Bartesaghi","year":"2018","journal-title":"Redox Biol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"7904","DOI":"10.1074\/jbc.RA119.007810","article-title":"Mechanism and regulation of ferrous heme-nitric oxide (NO) oxidation in NO synthases","volume":"294","author":"Tejero","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/j.molcel.2018.01.022","article-title":"Protein S-Nitrosylation: Enzymatically Controlled, but Intrinsically Unstable, Post-translational Modification","volume":"69","author":"Gusarov","year":"2018","journal-title":"Mol. Cell."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.cardiores.2004.01.013","article-title":"S-nitrosylation: A potential new paradigm in signal transduction","volume":"62","author":"Lamas","year":"2004","journal-title":"Cardiovasc. Res."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1038\/nrm1569","article-title":"Protein S nitrosylation: Purview and parameters","volume":"6","author":"Hess","year":"2005","journal-title":"Nat. Rev. Mol. Cell. Biol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/j.freeradbiomed.2004.05.031","article-title":"Inhibition of the yeast metal reductase heme protein fre1 by nitric oxide (NO): A model for inhibition of NADPH oxidase by NO","volume":"37","author":"Shinyashiki","year":"2004","journal-title":"Free Radic. Biol. Med."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1152\/ajpcell.1998.274.3.C827","article-title":"Nitric oxide inhibits superoxide production by inflammatory polymorphonuclear leukocytes","volume":"274","author":"Mitjavila","year":"1998","journal-title":"Am. J. Physiol. Cell. Phys."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"25239","DOI":"10.1016\/S0021-9258(18)47236-5","article-title":"Nitric oxide reduces early growth response-1 gene expression in rat lung macrophages treated with interferon-gamma and lipopolysaccharide","volume":"269","author":"Henderson","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_44","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_45","doi-asserted-by":"crossref","first-page":"3450","DOI":"10.18632\/aging.101139","article-title":"Altered S-nitrosylation of p53 is responsible for impaired antioxidant response in skeletal muscle during aging","volume":"8","author":"Baldelli","year":"2016","journal-title":"Aging"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Tan, B.L., Norhaizan, M.E., Liew, W.-P.-P., and Sulaiman Rahman, H. (2018). Antioxidant and Oxidative Stress: A Mutual Interplay in Age-Related Diseases. Front. Pharmacol., 9.","DOI":"10.3389\/fphar.2018.01162"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1006\/mcne.2000.0873","article-title":"Nitric Oxide Synthase (NOS-1) Coclustered With Agrin-Induced AChR-Specializations on Cultured Skeletal Myotubes","volume":"16","author":"Hoch","year":"2000","journal-title":"Mol. Cell. Neurosci."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Loureiro, A.C.C., do R\u00eago-Monteiro, I.C., Louzada, R.A., Ortenzi, V.H., de Aguiar, A.P., de Abreu, E.S., Cavalcanti-de-Albuquerque, J.P.A., Hecht, F., de Oliveira, A.C., and Ceccatto, V.M. (2016). Differential Expression of NADPH Oxidases Depends on Skeletal Muscle Fiber Type in Rats. Oxid. Med. Cell. Longev., 2016.","DOI":"10.1155\/2016\/6738701"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1174","DOI":"10.1016\/j.freeradbiomed.2006.07.005","article-title":"Glutathione-peroxidase-1 null muscle progenitor cells are globally defective","volume":"41","author":"Lee","year":"2006","journal-title":"Free Radic. Biol. Med."},{"key":"ref_50","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_51","doi-asserted-by":"crossref","first-page":"1484","DOI":"10.1152\/jappl.1996.81.4.1484","article-title":"Effect of sprint cycle training on activities of antioxidant enzymes in human skeletal muscle","volume":"81","author":"Hellsten","year":"1996","journal-title":"J. Appl. Physiol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1837","DOI":"10.1016\/j.biocel.2009.03.013","article-title":"Capacity of oxidative phosphorylation in human skeletal muscle: New perspectives of mitochondrial physiology","volume":"41","author":"Gnaiger","year":"2009","journal-title":"Int. J. Biochem. Cell. Biol."},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Wang, P., Li, C.G., Qi, Z., Cui, D., and Ding, S. (2019, September 06). Acute Exercise Induced Mitochondrial H2O2 Production in Mouse Skeletal Muscle: Association with p66Shc and FOXO3a Signaling and Antioxidant Enzymes. Available online: https:\/\/www.hindawi.com\/journals\/omcl\/2015\/536456\/.","DOI":"10.1155\/2015\/536456"},{"key":"ref_54","first-page":"1833","article-title":"Alteration of Glutathione and Antioxidant Status with Exercise in Unfed and Refed Rats","volume":"126","author":"Leeuwenburgh","year":"1996","journal-title":"J. Nutr."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"4709","DOI":"10.1021\/acs.analchem.9b00149","article-title":"Characterization of the Human Skeletal Muscle Metabolome for Elucidating the Mechanisms of Bicarbonate Ingestion on Strenuous Interval Exercise","volume":"91","author":"Saoi","year":"2019","journal-title":"Anal. Chem."},{"key":"ref_56","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_57","doi-asserted-by":"crossref","first-page":"20845","DOI":"10.3390\/ijms141020845","article-title":"Protein Glutathionylation in Cardiovascular Diseases","volume":"14","author":"Pastore","year":"2013","journal-title":"Int. J. Mol. Sci."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1235","DOI":"10.1016\/j.cell.2014.01.056","article-title":"S-Glutathionylation of Cryptic Cysteines Enhances Titin Elasticity by Blocking Protein Folding","volume":"156","author":"Kosuri","year":"2014","journal-title":"Cell"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1443","DOI":"10.1113\/jphysiol.2011.224535","article-title":"S-Glutathionylation of troponin I (fast) increases contractile apparatus Ca2+ sensitivity in fast-twitch muscle fibres of rats and humans","volume":"590","author":"Mollica","year":"2012","journal-title":"J. Physiol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1152\/ajpcell.00334.2016","article-title":"S-nitrosylation and S-glutathionylation of Cys134 on troponin I have opposing competitive actions on Ca2+ sensitivity in rat fast-twitch muscle fibers","volume":"312","author":"Dutka","year":"2016","journal-title":"Am. J. Physiol. Cell. Physiol."},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"Gill, R.M., O\u2019Brien, M., Young, A., Gardiner, D., and Mailloux, R.J. (2018). Protein S-glutathionylation lowers superoxide\/hydrogen peroxide release from skeletal muscle mitochondria through modification of complex I and inhibition of pyruvate uptake. PLoS ONE, 13.","DOI":"10.1371\/journal.pone.0192801"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1186\/s13395-014-0022-6","article-title":"Deficient nitric oxide signalling impairs skeletal muscle growth and performance: Involvement of mitochondrial dysregulation","volume":"4","author":"Morisi","year":"2014","journal-title":"Skelet. Muscle"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/0014-5793(96)00003-8","article-title":"Inhibition of the skeletal muscle ryanodine receptor calcium release channel by nitric oxide","volume":"380","author":"Minarovic","year":"1996","journal-title":"FEBS Lett."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1007\/s000180050359","article-title":"Effects of nitric oxide on the contraction of skeletal muscle","volume":"55","author":"Gailly","year":"1999","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"607","DOI":"10.3389\/fphys.2017.00607","article-title":"NO-sGC Pathway Modulates Ca2+ Release and Muscle Contraction in Zebrafish Skeletal Muscle","volume":"8","author":"Xiyuan","year":"2017","journal-title":"Front Physiol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/S0014-5793(98)01460-4","article-title":"Inhibition of skeletal muscle sarcoplasmic reticulum Ca2+-ATPase by nitric oxide","volume":"440","author":"Ishii","year":"1998","journal-title":"FEBS Lett."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1006\/abbi.1996.0146","article-title":"Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles","volume":"328","author":"Poderoso","year":"1996","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1016\/j.freeradbiomed.2015.08.024","article-title":"Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects","volume":"89","author":"Iglesias","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1007\/s10863-008-9166-6","article-title":"The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulfide: Chemical mechanism and physiological significance","volume":"40","author":"Cooper","year":"2008","journal-title":"J. Bioenerg. Biomembr."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1152\/ajpendo.00045.2007","article-title":"Nitric oxide increases GLUT4 expression and regulates AMPK signaling in skeletal muscle","volume":"293","author":"Lira","year":"2007","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"7427","DOI":"10.1113\/JP275133","article-title":"Nitric oxide is required for the insulin sensitizing effects of contraction in mouse skeletal muscle","volume":"595","author":"Zhang","year":"2017","journal-title":"J. Physiol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"3551","DOI":"10.1113\/jphysiol.2010.194035","article-title":"Nitric oxide and AMPK cooperatively regulate PGC-1 in skeletal muscle cells","volume":"588","author":"Lira","year":"2010","journal-title":"J. Physiol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1152\/ajpendo.00755.2009","article-title":"PGC-1alpha regulation by exercise training and its influences on muscle function and insulin sensitivity","volume":"299","author":"Lira","year":"2010","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_74","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-1alpha","volume":"104","author":"Handschin","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_75","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_76","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1074\/jbc.M113.506733","article-title":"Nuclear recruitment of neuronal nitric-oxide synthase by \u03b1-syntrophin is crucial for the induction of mitochondrial biogenesis","volume":"289","author":"Aquilano","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.jphs.2015.09.002","article-title":"Vascular nitric oxide: Beyond eNOS","volume":"129","author":"Zhao","year":"2015","journal-title":"J. Pharmacol. Sci."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"1399","DOI":"10.1152\/ajpregu.00004.2010","article-title":"Endothelial nitric oxide synthase is central to skeletal muscle metabolic regulation and enzymatic signaling during exercise in vivo","volume":"298","author":"Ayala","year":"2010","journal-title":"Am. J. Physiol. Regul. Integr. Comparat. Physiol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1089\/ars.2016.6787","article-title":"Tyrosine-Nitrated Proteins: Proteomic and Bioanalytical Aspects","volume":"26","author":"Bartesaghi","year":"2017","journal-title":"Antioxid. Redox Signal."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1277","DOI":"10.1093\/gerona\/63.12.1277","article-title":"Principal component analysis reveals age-related and muscle-type-related differences in protein carbonyl profiles of muscle mitochondria","volume":"63","author":"Feng","year":"2008","journal-title":"J. Gerontol. A Biol. Sci. Med. Sci."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.exger.2011.11.007","article-title":"Cumulative 3-nitrotyrosine in specific muscle proteins is associated with muscle loss during aging","volume":"47","author":"Murakami","year":"2012","journal-title":"Exp. Gerontol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/S0009-9120(02)00407-1","article-title":"Relation of aging with oxidative protein damage parameters in the rat skeletal muscle","volume":"36","author":"Cakatay","year":"2003","journal-title":"Clin. Biochem."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1093\/gerona\/gls334","article-title":"Long-term supplementation with a cystine-based antioxidant delays loss of muscle mass in aging","volume":"68","author":"Parveen","year":"2013","journal-title":"J. Gerontol. A Biol. Sci. Med. Sci."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.lfs.2013.11.009","article-title":"Alanyl-glutamine and glutamine plus alanine supplements improve skeletal redox status in trained rats: Involvement of heat shock protein pathways","volume":"94","author":"Petry","year":"2014","journal-title":"Life Sci."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"842","DOI":"10.1139\/apnm-2016-0049","article-title":"l-glutamine and l-alanine supplementation increase glutamine-glutathione axis and muscle HSP-27 in rats trained using a progressive high-intensity resistance exercise","volume":"41","author":"Leite","year":"2016","journal-title":"Appl. Physiol. Nutr. Metab."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"233","DOI":"10.3945\/ajcn.112.049163","article-title":"Thiol-based antioxidant supplementation alters human skeletal muscle signaling and attenuates its inflammatory response and recovery after intense eccentric exercise","volume":"98","author":"Michailidis","year":"2013","journal-title":"Am. J. Clin. Nutr."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.3109\/10715762.2014.937341","article-title":"Vitamin E supplementation modifies adaptive responses to training in rat skeletal muscle","volume":"48","author":"Venditti","year":"2014","journal-title":"Free Radic. Res."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"852","DOI":"10.1016\/j.freeradbiomed.2015.10.412","article-title":"Vitamin C and E supplementation prevents some of the cellular adaptations to endurance-training in humans","volume":"89","author":"Morrison","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.freeradbiomed.2015.04.006","article-title":"Redox modulation of mitochondriogenesis in exercise. Does antioxidant supplementation blunt the benefits of exercise training?","volume":"86","author":"Cabo","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"7569127","DOI":"10.1155\/2018\/7569127","article-title":"L-Arginine Enhances Protein Synthesis by Phosphorylating mTOR (Thr 2446) in a Nitric Oxide-Dependent Manner in C2C12 Cells","volume":"2018","author":"Wang","year":"2018","journal-title":"Oxid. Med. Cell. Longev."},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Ham, D.J., Gleeson, B.G., Chee, A., Baum, D.M., Caldow, M.K., Lynch, G.S., and Koopman, R. (2015). L-Citrulline Protects Skeletal Muscle Cells from Cachectic Stimuli through an iNOS-Dependent Mechanism. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0141572"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1093\/gerona\/glu057","article-title":"Chronic inflammation (inflammaging) and its potential contribution to age-associated diseases","volume":"69","author":"Franceschi","year":"2014","journal-title":"J. Gerontol. A Biol. Sci. Med. Sci."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1940","DOI":"10.3945\/jn.116.230912","article-title":"Inflammaging and Skeletal Muscle: Can Protein Intake Make a Difference?","volume":"146","author":"Draganidis","year":"2016","journal-title":"J. Nutr."},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Szentesi, P., Csernoch, L., Dux, L., and Keller-Pint\u00e9r, A. (2019, September 09). Changes in Redox Signaling in the Skeletal Muscle with Aging. Available online: https:\/\/www.hindawi.com\/journals\/omcl\/2019\/4617801\/.","DOI":"10.1155\/2019\/4617801"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"1767","DOI":"10.4049\/jimmunol.1202903","article-title":"Requirement of inducible nitric oxide synthase for skeletal muscle regeneration after acute damage","volume":"190","author":"Rigamonti","year":"2013","journal-title":"J. Immunol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1753","DOI":"10.1002\/j.1460-2075.1996.tb00524.x","article-title":"Muscle wasting and dedifferentiation induced by oxidative stress in a murine model of cachexia is prevented by inhibitors of nitric oxide synthesis and antioxidants","volume":"15","author":"Buck","year":"1996","journal-title":"EMBO J."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1007\/s12035-012-8311-8","article-title":"Nitric oxide in myogenesis and therapeutic muscle repair","volume":"46","author":"Clementi","year":"2012","journal-title":"Mol. Neurobiol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1002\/jlb.64.4.427","article-title":"Nitric oxide synthase inhibition reduces muscle inflammation and necrosis in modified muscle use","volume":"64","author":"Pizza","year":"1998","journal-title":"J. Leukoc. Biol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1126\/scisignal.2005375","article-title":"Inflammatory stimuli induce inhibitory S-nitrosylation of the deacetylase SIRT1 to increase acetylation and activation of p53 and p65","volume":"7","author":"Shinozaki","year":"2014","journal-title":"Sci. Signal."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"155","DOI":"10.3389\/fimmu.2019.00155","article-title":"GSH-C4 Acts as Anti-inflammatory Drug in Different Models of Canonical and Cell Autonomous Inflammation Through NF\u03baB Inhibition","volume":"10","author":"Limongi","year":"2019","journal-title":"Front. Immunol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"23019","DOI":"10.18632\/oncotarget.8552","article-title":"Adipose triglyceride lipase decrement affects skeletal muscle homeostasis during aging through FAs-PPAR\u03b1-PGC-1\u03b1 antioxidant response","volume":"7","author":"Aquilano","year":"2016","journal-title":"Oncotarget"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1007\/s00418-008-0386-y","article-title":"Adipose triglyceride lipase (ATGL) expression in human skeletal muscle is type I (oxidative) fiber specific","volume":"129","author":"Jocken","year":"2008","journal-title":"Histochem. Cell. Biol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1038\/s41419-018-0345-z","article-title":"Hints on ATGL implications in cancer: Beyond bioenergetic clues","volume":"9","author":"Vegliante","year":"2018","journal-title":"Cell. Death Dis."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"32048","DOI":"10.1074\/jbc.274.45.32048","article-title":"Peroxisome proliferator-activated receptor alpha negatively regulates the vascular inflammatory gene response by negative cross-talk with transcription factors NF-kappaB and AP-1","volume":"274","author":"Delerive","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1865","DOI":"10.1096\/fj.201500153","article-title":"Disruption of nuclear factor (erythroid-derived-2)-like 2 antioxidant signaling: A mechanism for impaired activation of stem cells and delayed regeneration of skeletal muscle","volume":"30","author":"Shelar","year":"2016","journal-title":"FASEB J."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"e13998","DOI":"10.14814\/phy2.13998","article-title":"Effects of Nrf2 deficiency on mitochondrial oxidative stress in aged skeletal muscle","volume":"7","author":"Kitaoka","year":"2019","journal-title":"Physiol. Rep."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"287","DOI":"10.3389\/fphys.2019.00287","article-title":"Exercise-Induced Myokines With Therapeutic Potential for Muscle Wasting","volume":"10","author":"Piccirillo","year":"2019","journal-title":"Front. Physiol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.coph.2017.05.005","article-title":"Muscle as a paracrine and endocrine organ","volume":"34","author":"Giudice","year":"2017","journal-title":"Curr. Opin. Pharmacol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"372","DOI":"10.3389\/fphys.2019.00372","article-title":"A Short-Term High-Fat Diet Alters Glutathione Levels and IL-6 Gene Expression in Oxidative Skeletal Muscles of Young Rats","volume":"10","author":"Andrich","year":"2019","journal-title":"Front Physiol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1152\/japplphysiol.00735.2002","article-title":"Antioxidants attenuate the plasma cytokine response to exercise in humans","volume":"94","author":"Vassilakopoulos","year":"2003","journal-title":"J. Appl. Physiol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"2683","DOI":"10.1096\/fj.06-7477com","article-title":"Nitric oxide production is a proximal signaling event controlling exercise-induced mRNA expression in human skeletal muscle","volume":"21","author":"Steensberg","year":"2007","journal-title":"FASEB J."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"373","DOI":"10.2165\/00007256-200636050-00001","article-title":"Trauma-Induced Systemic Inflammatory Response versus Exercise-Induced Immunomodulatory Effects","volume":"36","author":"Fehrenbach","year":"2006","journal-title":"Sports Med."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1089\/ars.2007.1792","article-title":"Regulation of proliferation of skeletal muscle precursor cells by NADPH oxidase","volume":"10","author":"Mofarrahi","year":"2008","journal-title":"Antioxid. Redox Signal."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1152\/ajpcell.00355.2007","article-title":"Recovery of skeletal muscle mass after extensive injury: Positive effects of increased contractile activity","volume":"294","author":"Serrurier","year":"2008","journal-title":"Am. J. Physiol. Cell. Physiol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1016\/j.cmet.2015.05.011","article-title":"Understanding the Cellular and Molecular Mechanisms of Physical Activity-Induced Health Benefits","volume":"22","author":"Neufer","year":"2015","journal-title":"Cell. Metab."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"F700","DOI":"10.1152\/ajprenal.90548.2008","article-title":"Moderate exercise attenuates caspase-3 activity, oxidative stress, and inhibits progression of diabetic renal disease in db\/db mice","volume":"296","author":"Ghosh","year":"2009","journal-title":"Am. J. Physiol. Renal Physiol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1097\/MCO.0000000000000335","article-title":"The effects of exercise on muscle strength, body composition, physical functioning and the inflammatory profile of older adults: A systematic review","volume":"20","author":"Liberman","year":"2017","journal-title":"Curr. Opin. Clin. Nutr. Metab. Care"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"1869","DOI":"10.1249\/MSS.0b013e3181a645a6","article-title":"In vivo alterations in skeletal muscle form and function after disuse atrophy","volume":"41","author":"Clark","year":"2009","journal-title":"Med. Sci. Sports Exerc."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.bone.2015.03.015","article-title":"Inflammation induced loss of skeletal muscle","volume":"80","author":"Londhe","year":"2015","journal-title":"Bone"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1482","DOI":"10.1152\/japplphysiol.00925.2012","article-title":"Calpain and caspase-3 play required roles in immobilization-induced limb muscle atrophy","volume":"114","author":"Talbert","year":"2013","journal-title":"J. Appl. Physiol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.jot.2017.05.006","article-title":"Inflammation and age-associated skeletal muscle deterioration (sarcopaenia)","volume":"10","author":"Wang","year":"2017","journal-title":"J. Orthop. Translat."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1159\/000484679","article-title":"Mechanistic Links Underlying the Impact of C-Reactive Protein on Muscle Mass in Elderly","volume":"44","author":"Wilkinson","year":"2017","journal-title":"Cell. Physiol. Biochem."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1152\/ajpregu.00767.2006","article-title":"Denervation-induced skeletal muscle atrophy is associated with increased mitochondrial ROS production","volume":"293","author":"Muller","year":"2007","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"622","DOI":"10.15252\/emmm.201607052","article-title":"STAT3 promotes IFN\u03b3\/TNF\u03b1-induced muscle wasting in an NF-\u03baB-dependent and IL-6-independent manner","volume":"9","author":"Ma","year":"2017","journal-title":"EMBO Mol. Med."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"6533","DOI":"10.1128\/MCB.25.15.6533-6545.2005","article-title":"NF-kappa B-mediated MyoD decay during muscle wasting requires nitric oxide synthase mRNA stabilization, HuR protein, and nitric oxide release","volume":"25","author":"Mazroui","year":"2005","journal-title":"Mol. Cell. Biol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1152\/japplphysiol.00431.2011","article-title":"Deficiency of inducible nitric oxide synthase attenuates immobilization-induced skeletal muscle atrophy in mice","volume":"113","author":"Bae","year":"2012","journal-title":"J. Appl. Physiol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"1113","DOI":"10.1007\/s00109-008-0373-8","article-title":"Nuclear Factor-kappa B Signaling in Skeletal Muscle Atrophy","volume":"86","author":"Li","year":"2008","journal-title":"J. Mol. Med."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"5089","DOI":"10.1113\/jphysiol.2010.198283","article-title":"Effects of inactivity on human muscle glutathione synthesis by a double-tracer and single-biopsy approach","volume":"588","author":"Agostini","year":"2010","journal-title":"J. Physiol."},{"key":"ref_129","doi-asserted-by":"crossref","unstructured":"Derbre, F., Ferrando, B., Gomez-Cabrera, M.C., Sanchis-Gomar, F., Martinez-Bello, V.E., Olaso-Gonzalez, G., Diaz, A., Gratas-Delamarche, A., Cerda, M., and Vi\u00f1a, J. (2012). Inhibition of Xanthine Oxidase by Allopurinol Prevents Skeletal Muscle Atrophy: Role of p38 MAPKinase and E3 Ubiquitin Ligases. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0046668"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"2468","DOI":"10.1172\/JCI30654","article-title":"NO production results in suspension-induced muscle atrophy through dislocation of neuronal NOS","volume":"117","author":"Suzuki","year":"2007","journal-title":"J. Clin. Investig."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1134\/S0006297911050075","article-title":"Protective effect of L-Arginine administration on proteins of unloaded m. soleus","volume":"76","author":"Lomonosova","year":"2011","journal-title":"Biochem. Mosc."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"2950","DOI":"10.1073\/pnas.1307736110","article-title":"Reactive nitrogen species regulate autophagy through ATM-AMPK-TSC2-mediated suppression of mTORC1","volume":"110","author":"Tripathi","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1152\/ajpcell.00018.2004","article-title":"Stretch-induced nitric oxide modulates mechanical properties of skeletal muscle cells","volume":"287","author":"Zhang","year":"2004","journal-title":"Am. J. Physiol. Cell. Physiol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1152\/japplphysiol.00936.2005","article-title":"In vivo inhibition of nitric oxide synthase impairs upregulation of contractile protein mRNA in overloaded plantaris muscle","volume":"100","author":"Sellman","year":"2006","journal-title":"J. Appl. Physiol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"2909","DOI":"10.1091\/mbc.e02-01-0062","article-title":"Release of Hepatocyte Growth Factor from Mechanically Stretched Skeletal Muscle Satellite Cells and Role of pH and Nitric Oxide","volume":"13","author":"Tatsumi","year":"2002","journal-title":"Mol. Biol. Cell."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1006\/excr.2001.5252","article-title":"Mechanical stretch induces activation of skeletal muscle satellite cells in vitro","volume":"267","author":"Tatsumi","year":"2001","journal-title":"Exp. Cell. Res."}],"container-title":["Nutrients"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6643\/11\/10\/2318\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T13:26:14Z","timestamp":1760189174000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6643\/11\/10\/2318"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,9,30]]},"references-count":136,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2019,10]]}},"alternative-id":["nu11102318"],"URL":"https:\/\/doi.org\/10.3390\/nu11102318","relation":{},"ISSN":["2072-6643"],"issn-type":[{"value":"2072-6643","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,9,30]]}}}