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Malignant hyperthermia. <i>Mo. Med.<\/i>, <b>116<\/b>, 154\u2013159 (2019)."},{"key":"2","doi-asserted-by":"crossref","unstructured":"2) Miyoshi H, Yasuda T, Otsuki S, Kondo T, Haraki T, Mukaida K, Nakamura R, Hamada H, Kawamoto M. Several ryanodine receptor type 1 gene mutations of p.Arg2508 are potential sources of malignant hyperthermia. <i>Anesth. Analg.<\/i>, <b>121<\/b>, 994\u20131000 (2015).","DOI":"10.1213\/ANE.0000000000000886"},{"key":"3","doi-asserted-by":"crossref","unstructured":"3) Louis CF, Balog EM, Fruen BR. Malignant hyperthermia: an inherited disorder of skeletal muscle Ca<sup>2+<\/sup> regulation. <i>Biosci. Rep.<\/i>, <b>21<\/b>, 155\u2013168 (2001).","DOI":"10.1023\/A:1013644107519"},{"key":"4","doi-asserted-by":"crossref","unstructured":"4) Protasi F, Paolini C, Dainese M. Calsequestrin-1: a new candidate gene for malignant hyperthermia and exertional\/environmental heat stroke. <i>J. Physiol.<\/i>, <b>587<\/b>, 3095\u20133100 (2009).","DOI":"10.1113\/jphysiol.2009.171967"},{"key":"5","doi-asserted-by":"crossref","unstructured":"5) Woo JS, Jeong SY, Park JH, Choi JH, Lee EH. Calsequestrin: a well-known but curious protein in skeletal muscle. <i>Exp. Mol. Med.<\/i>, <b>52<\/b>, 1908\u20131925 (2020).","DOI":"10.1038\/s12276-020-00535-1"},{"key":"6","doi-asserted-by":"crossref","unstructured":"6) Protasi F, Paolini C, Canato M, Reggiani C, Quarta M. Lessons from calsequestrin-1 ablation <i>in vivo<\/i>: much more than a Ca<sup>2+<\/sup> buffer after all. <i>J. Muscle Res. Cell Motil.<\/i>, <b>32<\/b>, 257\u2013270 (2011).","DOI":"10.1007\/s10974-011-9277-2"},{"key":"7","doi-asserted-by":"crossref","unstructured":"7) Sun Z, Wang L, Han L, Wang Y, Zhou Y, Li Q, Wu Y, Talabieke S, Hou Y, Wu L, Liu R, Fu Z, You H, Li BY, Zheng Y, Luo D. Functional calsequestrin-1 is expressed in the heart and its deficiency is causally related to malignant hyperthermia-like arrhythmia. <i>Circulation<\/i>, <b>144<\/b>, 788\u2013804 (2021).","DOI":"10.1161\/CIRCULATIONAHA.121.053255"},{"key":"8","doi-asserted-by":"crossref","unstructured":"8) Tanwar J, Singh JB, Motiani RK. Molecular machinery regulating mitochondrial calcium levels: the nuts and bolts of mitochondrial calcium dynamics. <i>Mitochondrion<\/i>, <b>57<\/b>, 9\u201322 (2021).","DOI":"10.1016\/j.mito.2020.12.001"},{"key":"9","doi-asserted-by":"crossref","unstructured":"9) Liu ZJ, Zhao W, Lei HY, Xu HL, Lai LY, Xu R, Xu SY. High glucose enhances bupivacaine-induced neurotoxicity <i>via<\/i> MCU-mediated oxidative stress in SH-SY5Y cells. <i>Oxid. Med. Cell. Longev.<\/i>, <b>2019<\/b>, 7192798 (2019).","DOI":"10.1155\/2019\/7192798"},{"key":"10","doi-asserted-by":"crossref","unstructured":"10) Tan X, Zeng Y, Tu Z, Li P, Chen H, Cheng L, Tu S, Jiang L. TRPV1 contributes to the neuroprotective effect of dexmedetomidine in pilocarpine-induced status epilepticus juvenile rats. <i>BioMed Res. Int.<\/i>, <b>2020<\/b>, 7623635 (2020).","DOI":"10.1155\/2020\/7623635"},{"key":"11","doi-asserted-by":"crossref","unstructured":"11) Rizzuto R, De Stefani D, Raffaello A, Mammucari C. Mitochondria as sensors and regulators of calcium signalling. <i>Nat. Rev. Mol. Cell Biol.<\/i>, <b>13<\/b>, 566\u2013578 (2012).","DOI":"10.1038\/nrm3412"},{"key":"12","doi-asserted-by":"crossref","unstructured":"12) Kirichok Y, Krapivinsky G, Clapham DE. The mitochondrial calcium uniporter is a highly selective ion channel. <i>Nature<\/i>, <b>427<\/b>, 360\u2013364 (2004).","DOI":"10.1038\/nature02246"},{"key":"13","doi-asserted-by":"crossref","unstructured":"13) Kamer KJ, Mootha VK. The molecular era of the mitochondrial calcium uniporter. <i>Nat. Rev. Mol. Cell Biol.<\/i>, <b>16<\/b>, 545\u2013553 (2015).","DOI":"10.1038\/nrm4039"},{"key":"14","doi-asserted-by":"crossref","unstructured":"14) Fan M, Zhang J, Tsai C-W, Orlando BJ, Rodriguez M, Xu Y, Liao M, Tsai M-F, Feng L. Structure and mechanism of the mitochondrial Ca<sup>2+<\/sup> uniporter holocomplex. <i>Nature<\/i>, <b>582<\/b>, 129\u2013133 (2020).","DOI":"10.1038\/s41586-020-2309-6"},{"key":"15","doi-asserted-by":"crossref","unstructured":"15) Zhao Q, Li H, Chang L, Wei C, Yin Y, Bei H, Wang Z, Liang J, Wu Y. Qiliqiangxin attenuates oxidative stress-induced mitochondrion-dependent apoptosis in cardiomyocytes <i>via<\/i> PI3K\/AKT\/GSK3<i>\u03b2<\/i> signaling pathway. <i>Biol. Pharm. Bull.<\/i>, <b>42<\/b>, 1310\u20131321 (2019).","DOI":"10.1248\/bpb.b19-00050"},{"key":"16","doi-asserted-by":"crossref","unstructured":"16) Namekata I, Odaka R, Hamaguchi S, Tanaka H. KB-R7943 inhibits the mitochondrial Ca<sup>2+<\/sup> Uniporter but Not Na<sup>+<\/sup>-Ca<sup>2+<\/sup> exchanger in cardiomyocyte-derived H9c2 cells. <i>Biol. Pharm. Bull.<\/i>, <b>43<\/b>, 1993\u20131996 (2020).","DOI":"10.1248\/bpb.b20-00747"},{"key":"17","doi-asserted-by":"crossref","unstructured":"17) Nakamura S, Matsui A, Akabane S, Tamura Y, Hatano A, Miyano Y, Omote H, Kajikawa M, Maenaka K, Moriyama Y, Endo T, Oka T. The mitochondrial inner membrane protein LETM1 modulates cristae organization through its LETM domain. <i>Commun. Biol.<\/i>, <b>3<\/b>, 99 (2020).","DOI":"10.1038\/s42003-020-0832-5"},{"key":"18","doi-asserted-by":"crossref","unstructured":"18) Paolini C, Quarta M, Wei-LaPierre L, Michelucci A, Nori A, Reggiani C, Dirksen RT, Protasi F. Oxidative stress, mitochondrial damage, and cores in muscle from calsequestrin-1 knockout mice. <i>Skelet. Muscle<\/i>, <b>5<\/b>, 10 (2015).","DOI":"10.1186\/s13395-015-0035-9"},{"key":"19","doi-asserted-by":"crossref","unstructured":"19) Paolini C, Quarta M, Nori A, Boncompagni S, Canato M, Volpe P, Allen PD, Reggiani C, Protasi F. Reorganized stores and impaired calcium handling in skeletal muscle of mice lacking calsequestrin-1. <i>J. Physiol.<\/i>, <b>583<\/b>, 767\u2013784 (2007).","DOI":"10.1113\/jphysiol.2007.138024"},{"key":"20","doi-asserted-by":"crossref","unstructured":"20) Seng C, Pearce L, Meizoso-Huesca A, Singh DP, Murphy RM, Lamboley CR, Launikonis BS. Tiny changes in cytoplasmic [Ca<sup>2+<\/sup>] cause large changes in mitochondrial Ca<sup>2+<\/sup>: what are the triggers and functional implications? <i>Am. J. Physiol. Cell Physiol.<\/i>, <b>323<\/b>, C1285\u2013c9 (2022).","DOI":"10.1152\/ajpcell.00092.2022"},{"key":"21","doi-asserted-by":"crossref","unstructured":"21) Peoples JN, Saraf A, Ghazal N, Pham TT, Kwong JQ. Mitochondrial dysfunction and oxidative stress in heart disease. <i>Exp. Mol. Med.<\/i>, <b>51<\/b>, 1\u201313 (2019).","DOI":"10.1038\/s12276-019-0355-7"},{"key":"22","doi-asserted-by":"crossref","unstructured":"22) Tawfik I, Gottschalk B, Jarc A, Bresilla D, Rost R, Obermayer-Pietsch B, Graier WF, Madreiter-Sokolowski CT. T3-induced enhancement of mitochondrial Ca<sup>2+<\/sup> uptake as a boost for mitochondrial metabolism. <i>Free Radic. Biol. Med.<\/i>, <b>181<\/b>, 197\u2013208 (2022).","DOI":"10.1016\/j.freeradbiomed.2022.01.024"},{"key":"23","doi-asserted-by":"crossref","unstructured":"23) Protasi F, Girolami B, Serano M, Pietrangelo L, Paolini C. Ablation of calsequestrin-1, Ca<sup>2+<\/sup> unbalance, and susceptibility to heat stroke. <i>Front. Physiol.<\/i>, <b>13<\/b>, 1033300 (2022).","DOI":"10.3389\/fphys.2022.1033300"},{"key":"24","doi-asserted-by":"crossref","unstructured":"24) Wirth C, Brandt U, Hunte C, Zickermann V. Structure and function of mitochondrial complex I. <i>Biochim. Biophys. Acta Bioenerg.<\/i>, <b>1857<\/b>, 902\u2013914 (2016).","DOI":"10.1016\/j.bbabio.2016.02.013"},{"key":"25","doi-asserted-by":"crossref","unstructured":"25) Chen Q, Vazquez EJ, Moghaddas S, Hoppel CL, Lesnefsky EJ. Production of reactive oxygen species by mitochondria: central role of complex III*. <i>J. Biol. Chem.<\/i>, <b>278<\/b>, 36027\u201336031 (2003).","DOI":"10.1074\/jbc.M304854200"},{"key":"26","doi-asserted-by":"crossref","unstructured":"26) Rodr\u00edguez-Nuevo A, Torres-Sanchez A, Duran JM, De Guirior C, Mart\u00ednez-Zamora MA, B\u00f6ke E. Oocytes maintain ROS-free mitochondrial metabolism by suppressing complex I. <i>Nature<\/i>, <b>607<\/b>, 756\u2013761 (2022).","DOI":"10.1038\/s41586-022-04979-5"},{"key":"27","doi-asserted-by":"crossref","unstructured":"27) Yang Y, Du J, Xu R, Shen Y, Yang D, Li D, Hu H, Pei H, Yang Y. Melatonin alleviates angiotensin-II-induced cardiac hypertrophy <i>via<\/i> activating MICU1 pathway. <i>Aging (Albany NY)<\/i>, <b>13<\/b>, 493\u2013515 (2020).","DOI":"10.18632\/aging.202159"},{"key":"28","doi-asserted-by":"crossref","unstructured":"28) Liu Y, Jin M, Wang Y, Zhu J, Tan R, Zhao J, Ji X, Jin C, Jia Y, Ren T, Xing J. MCU-induced mitochondrial calcium uptake promotes mitochondrial biogenesis and colorectal cancer growth. <i>Signal Transduct. Target. Ther.<\/i>, <b>5<\/b>, 59 (2020).","DOI":"10.1038\/s41392-020-0155-5"},{"key":"29","doi-asserted-by":"crossref","unstructured":"29) Banavath HN, Roman B, Mackowski N, Biswas D, Afzal J, Nomura Y, Solhjoo S, O\u2019Rourke B, Kohr M, Murphy E, Steenbergen C, Das S. miR-181c activates mitochondrial calcium uptake by regulating MICU1 in the heart. <i>J. Am. Heart Assoc.<\/i>, <b>8<\/b>, e012919 (2019).","DOI":"10.1161\/JAHA.119.012919"},{"key":"30","doi-asserted-by":"crossref","unstructured":"30) Leng Y, Ge Q, Zhao Z, Wang K, Yao G. MICU1 may be a promising intervention target for gut-derived sepsis induced by intra-abdominal hypertension. <i>Cell Death Discov.<\/i>, <b>2<\/b>, 16080 (2016).","DOI":"10.1038\/cddiscovery.2016.80"},{"key":"31","doi-asserted-by":"crossref","unstructured":"31) Singh R, Bartok A, Paillard M, Tyburski A, Elliott M, Hajn\u00f3czky G. Uncontrolled mitochondrial calcium uptake underlies the pathogenesis of neurodegeneration in MICU1-deficient mice and patients. <i>Sci. Adv.<\/i>, <b>8<\/b>, eabj4716 (2022).","DOI":"10.1126\/sciadv.abj4716"},{"key":"32","doi-asserted-by":"crossref","unstructured":"32) Rosenberg H, Davis M, James D, Pollock N, Stowell K. Malignant hyperthermia. <i>Orphanet J. Rare Dis.<\/i>, <b>2<\/b>, 21 (2007).","DOI":"10.1186\/1750-1172-2-21"},{"key":"33","doi-asserted-by":"crossref","unstructured":"33) Hern\u00e1ndez-Ochoa EO, Pratt SJP, Lovering RM, Schneider MF. Critical role of intracellular RyR1 calcium release channels in skeletal muscle function and disease. <i>Front. Physiol.<\/i>, <b>6<\/b>, 420 (2016).","DOI":"10.3389\/fphys.2015.00420"},{"key":"34","doi-asserted-by":"crossref","unstructured":"34) Eu JP, Sun J, Xu L, Stamler JS, Meissner G. The skeletal muscle calcium release channel: coupled O<sub>2<\/sub> Sensor and NO signaling functions. <i>Cell<\/i>, <b>102<\/b>, 499\u2013509 (2000).","DOI":"10.1016\/S0092-8674(00)00054-4"},{"key":"35","doi-asserted-by":"crossref","unstructured":"35) Chen X, Ji Y, Liu R, Zhu X, Wang K, Yang X, Liu B, Gao Z, Huang Y, Shen Y, Liu H, Sun H. Mitochondrial dysfunction: roles in skeletal muscle atrophy. <i>J. Transl. Med.<\/i>, <b>21<\/b>, 503 (2023).","DOI":"10.1186\/s12967-023-04369-z"},{"key":"36","doi-asserted-by":"crossref","unstructured":"36) Gan Z, Fu T, Kelly DP, Vega RB. Skeletal muscle mitochondrial remodeling in exercise and diseases. <i>Cell Res.<\/i>, <b>28<\/b>, 969\u2013980 (2018).","DOI":"10.1038\/s41422-018-0078-7"},{"key":"37","doi-asserted-by":"crossref","unstructured":"37) Gliyazova NS, Huh EY, Ibeanu GC. A novel phenoxy thiophene sulphonamide molecule protects against glutamate evoked oxidative injury in a neuronal cell model. <i>BMC Neurosci.<\/i>, <b>14<\/b>, 93 (2013).","DOI":"10.1186\/1471-2202-14-93"},{"key":"38","doi-asserted-by":"crossref","unstructured":"38) Michelucci A, De Marco A, Guarnier FA, Protasi F, Boncompagni S. Antioxidant treatment reduces formation of structural cores and improves muscle function in RYR1Y522S\/WT mice. <i>Oxid. Med. Cell. Longev.<\/i>, <b>2017<\/b>, 6792694 (2017).","DOI":"10.1155\/2017\/6792694"},{"key":"39","doi-asserted-by":"crossref","unstructured":"39) Michelucci A, Paolini C, Canato M, Wei-Lapierre L, Pietrangelo L, De Marco A, Reggiani C, Dirksen RT, Protasi F. Antioxidants protect calsequestrin-1 knockout mice from halothane- and heat-induced sudden death. <i>Anesthesiology<\/i>, <b>123<\/b>, 603\u2013617 (2015).","DOI":"10.1097\/ALN.0000000000000748"},{"key":"40","doi-asserted-by":"crossref","unstructured":"40) Lu S, Liao Z, Lu X, Katschinski DM, Mercola M, Chen J, Heller Brown J, Molkentin JD, Bossuyt J, Bers DM. Hyperglycemia acutely increases cytosolic reactive oxygen species <i>via<\/i> O-linked GlcNAcylation and CaMKII activation in mouse ventricular myocytes. <i>Circ. Res.<\/i>, <b>126<\/b>, e80\u2013e96 (2020).","DOI":"10.1161\/CIRCRESAHA.119.316288"},{"key":"41","doi-asserted-by":"crossref","unstructured":"41) Li A, Yi J, Li X, Zhou J. Physiological Ca<sup>2+<\/sup> transients versus pathological steady-state Ca<sup>2+<\/sup> elevation, who flips the ros coin in skeletal muscle mitochondria. <i>Front. Physiol.<\/i>, <b>11<\/b>, 595800 (2020).","DOI":"10.3389\/fphys.2020.595800"},{"key":"42","doi-asserted-by":"crossref","unstructured":"42) Fanczal J, Pallagi P, G\u00f6r\u00f6g M, Diszh\u00e1zi G, Alm\u00e1ssy J, Mad\u00e1csy T, Varga \u00c1, Csernay-Bir\u00f3 P, Katona X, T\u00f3th E, Moln\u00e1r R, Rakonczay ZJr, Hegyi P, Mal\u00e9th J. TRPM2-mediated extracellular Ca<sup>2+<\/sup> entry promotes acinar cell necrosis in biliary acute pancreatitis. <i>J. Physiol.<\/i>, <b>598<\/b>, 1253\u20131270 (2020).","DOI":"10.1113\/JP279047"},{"key":"43","doi-asserted-by":"crossref","unstructured":"43) Li Y, Wang Y, Ma L. An association study of CASQ1 gene polymorphisms and heat stroke. <i>Genomics Proteomics Bioinformatics<\/i>, <b>12<\/b>, 127\u2013132 (2014).","DOI":"10.1016\/j.gpb.2014.03.004"},{"key":"44","doi-asserted-by":"crossref","unstructured":"44) Zhao X, Min CK, Ko JK, Parness J, Kim DH, Weisleder N, Ma J. Increased store-operated Ca<sup>2+<\/sup> entry in skeletal muscle with reduced calsequestrin-1 expression. <i>Biophys. J.<\/i>, <b>99<\/b>, 1556\u20131564 (2010).","DOI":"10.1016\/j.bpj.2010.06.050"},{"key":"45","doi-asserted-by":"crossref","unstructured":"45) Guarnier FA, Michelucci A, Serano M, Pietrangelo L, Pecorai C, Boncompagni S, Protasi F. Aerobic training prevents heatstrokes in calsequestrin-1 knockout mice by reducing oxidative stress. <i>Oxid. Med. Cell. Longev.<\/i>, <b>2018<\/b>, 4652480 (2018).","DOI":"10.1155\/2018\/4652480"},{"key":"46","doi-asserted-by":"crossref","unstructured":"46) Michelucci A, Boncompagni S, Canato M, Reggiani C, Protasi F. Estrogens protect calsequestrin-1 knockout mice from lethal hyperthermic episodes by reducing oxidative stress in muscle. <i>Oxid. Med. Cell. Longev.<\/i>, <b>2017<\/b>, 6936897 (2017).","DOI":"10.1155\/2017\/6936897"},{"key":"47","doi-asserted-by":"crossref","unstructured":"47) Wei L, Salahura G, Kang SH, Kasischke KA, Protasi F, Sheu SS, Dirksen RT. Mitochondrial superoxide flashes: metabolic biomarkers of skeletal muscle activity and disease. <i>FASEB J.<\/i>, <b>25<\/b>, 3068\u20133078 (2011).","DOI":"10.1096\/fj.11-187252"},{"key":"48","doi-asserted-by":"crossref","unstructured":"48) O-Uchi J, Porter Jr. G, Kang SH, Boncompagni S, Sokolova N, Gross P, Jhun BS, Beutner G, Brookes P, Blaxall B, Dirksen R, Protasi F, Pan S, Sheu S-S. RyR1 mutation associated with malignant hyperthermia facilitates catecholaminergic stress-included arrhythmia <i>via<\/i> mitochondrial injury and oxidative stress (893.8). <i>FASEB J<\/i>., <b>28<\/b>, 893.8 (2014).","DOI":"10.1096\/fasebj.28.1_supplement.893.8"},{"key":"49","doi-asserted-by":"crossref","unstructured":"49) Yarotskyy V, Protasi F, Dirksen RT. Accelerated activation of SOCE current in myotubes from two mouse models of anesthetic- and heat-induced sudden death. <i>PLOS ONE<\/i>, <b>8<\/b>, e77633 (2013).","DOI":"10.1371\/journal.pone.0077633"},{"key":"50","doi-asserted-by":"crossref","unstructured":"50) Wang L, Yang X, Li S, Wang Z, Liu Y, Feng J, Zhu Y, Shen Y. Structural and mechanistic insights into MICU1 regulation of mitochondrial calcium uptake. <i>EMBO J.<\/i>, <b>33<\/b>, 594\u2013604 (2014).","DOI":"10.1002\/embj.201386523"},{"key":"51","doi-asserted-by":"crossref","unstructured":"51) Katsenelson M, Shapira I, Abbas E, Jevdokimenko K, Styr B, Ruggiero A, A\u00efd S, Fornasiero EF, Holzenberger M, Rizzoli SO, Slutsky I. IGF-1 receptor regulates upward firing rate homeostasis <i>via<\/i> the mitochondrial calcium uniporter. <i>Proc. Natl. Acad. Sci. U.S.A.<\/i>, <b>119<\/b>, e2121040119 (2022).","DOI":"10.1073\/pnas.2121040119"},{"key":"52","doi-asserted-by":"crossref","unstructured":"52) Nakamura T, Ogawa M, Kojima K, Takayanagi S, Ishihara S, Hattori K, Naguro I, Ichijo H. The mitochondrial Ca<sup>2+<\/sup> uptake regulator, MICU1, is involved in cold stress-induced ferroptosis. <i>EMBO Rep.<\/i>, <b>22<\/b>, e51532 (2021).","DOI":"10.15252\/embr.202051532"},{"key":"53","doi-asserted-by":"crossref","unstructured":"53) Xue Q, Pei H, Liu Q, Zhao M, Sun J, Gao E, Ma X, Tao L. MICU1 protects against myocardial ischemia\/reperfusion injury and its control by the importer receptor Tom70. <i>Cell Death Dis.<\/i>, <b>8<\/b>, e2923 (2017).","DOI":"10.1038\/cddis.2017.280"},{"key":"54","doi-asserted-by":"crossref","unstructured":"54) Ji L, Liu F, Jing Z, Huang Q, Zhao Y, Cao H, Li J, Yin C, Xing J, Li F. MICU1 alleviates diabetic cardiomyopathy through mitochondrial Ca<sup>2+<\/sup>-dependent antioxidant response. <i>Diabetes<\/i>, <b>66<\/b>, 1586\u20131600 (2017).","DOI":"10.2337\/db16-1237"},{"key":"55","doi-asserted-by":"crossref","unstructured":"55) Wilton KM, Morales-Rosado JA, Selcen D, Muthusamy K, Ewing S, Agre K, Nickels K, Klee EW, Ho ML, Morava E. Developmental brain abnormalities and acute encephalopathy in a patient with myopathy with extrapyramidal signs secondary to pathogenic variants in MICU1. <i>JIMD Rep.<\/i>, <b>53<\/b>, 22\u201328 (2020).","DOI":"10.1002\/jmd2.12114"},{"key":"56","unstructured":"56) Fu P, Jia J, Gong L. Effect of chronic intermittent hypoxia exposure: differences on soleus muscle and musculi tibialis anterior. <i>Journal of Army Medical University<\/i>, <b>44<\/b>, 432\u2013440 (2022)."},{"key":"57","doi-asserted-by":"crossref","unstructured":"57) Wang H, Li B, Li A, An C, Liu S, Zhuang Z. Integrative metabolomics, enzymatic activity, and gene expression analysis provide insights into the metabolic profile differences between the slow-twitch muscle and fast-twitch muscle of <i>Pseudocaranx dentex<\/i>. <i>Int. J. Mol. Sci.<\/i>, <b>25<\/b>, 6131 (2024).","DOI":"10.3390\/ijms25116131"},{"key":"58","doi-asserted-by":"crossref","unstructured":"58) Lloyd EM, Pinniger GJ, Murphy RM, Grounds MD. Slow or fast: implications of myofibre type and associated differences for manifestation of neuromuscular disorders. <i>Acta Physiol. (Oxf.)<\/i>, <b>238<\/b>,  e14012 (2023).","DOI":"10.1111\/apha.14012"},{"key":"59","doi-asserted-by":"crossref","unstructured":"59) Fung TKH, Cheung KK, Wang X, Lau BWM, Ngai SPC. Transcriptomic profiling reveals differences in slow-twitch and fast-twitch muscles of a cigarette smoke-exposed rat model. <i>J. Cachexia Sarcopenia Muscle<\/i>, <b>16<\/b>, e13633 (2025).","DOI":"10.1002\/jcsm.13633"}],"container-title":["Biological and Pharmaceutical Bulletin"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/bpb\/48\/7\/48_b24-00829\/_pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,7,26]],"date-time":"2025-07-26T03:58:38Z","timestamp":1753502318000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/bpb\/48\/7\/48_b24-00829\/_article"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,7,24]]},"references-count":59,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2025]]}},"URL":"https:\/\/doi.org\/10.1248\/bpb.b24-00829","relation":{},"ISSN":["0918-6158","1347-5215"],"issn-type":[{"value":"0918-6158","type":"print"},{"value":"1347-5215","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,7,24]]},"article-number":"b24-00829"}}