{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T13:36:21Z","timestamp":1790775381167,"version":"4.1.0"},"reference-count":147,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2023,2,17]],"date-time":"2023-02-17T00:00:00Z","timestamp":1676592000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["NA 1565\/2-1"],"award-info":[{"award-number":["NA 1565\/2-1"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Mobility is an intrinsic feature of the animal kingdom that stimulates evolutionary processes and determines the biological success of animals. Skeletal muscle is the primary driver of voluntary movements. Besides, skeletal muscles have an immense impact on regulating glucose, amino acid, and lipid homeostasis. Muscle atrophy\/wasting conditions are accompanied by a drastic effect on muscle function and disrupt steady-state muscle physiology. Cachexia is a complex multifactorial muscle wasting syndrome characterized by extreme loss of skeletal muscle mass, resulting in a dramatic decrease in life quality and reported mortality in more than 30% of patients with advanced cancers. The lack of directed treatments to prevent or relieve muscle loss indicates our inadequate knowledge of molecular mechanisms involved in muscle cell organization and the molecular etiology of cancer-induced cachexia (CIC). This review highlights the latest knowledge of regulatory mechanisms involved in maintaining muscle function and their deregulation in wasting syndromes, particularly in cachexia. Recently, protein posttranslational modification by the small ubiquitin-like modifier (SUMO) has emerged as a key regulatory mechanism of protein function with implications for different aspects of cell physiology and diseases. We also review an atypical association of SUMO-mediated pathways in this context and deliberate on potential treatment strategies to alleviate muscle atrophy.<\/jats:p>","DOI":"10.3390\/cells12040644","type":"journal-article","created":{"date-parts":[[2023,2,17]],"date-time":"2023-02-17T02:27:24Z","timestamp":1676600844000},"page":"644","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["Emerging Mechanisms of Skeletal Muscle Homeostasis and Cachexia: The SUMO Perspective"],"prefix":"10.3390","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2833-4961","authenticated-orcid":false,"given":"Bushra","family":"Khan","sequence":"first","affiliation":[{"name":"Institute of Molecular and Cell Physiology, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luis Vincens","family":"Gand","sequence":"additional","affiliation":[{"name":"Institute of Molecular and Cell Physiology, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mamta","family":"Amrute-Nayak","sequence":"additional","affiliation":[{"name":"Institute of Molecular and Cell Physiology, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arnab","family":"Nayak","sequence":"additional","affiliation":[{"name":"Institute of Molecular and Cell Physiology, Hannover Medical School, Carl-Neuberg-Str. 1, 30625 Hannover, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,2,17]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1152\/physrev.1997.77.3.731","article-title":"Cellular energy utilization and molecular origin of standard metabolic rate in mammals","volume":"77","author":"Rolfe","year":"1997","journal-title":"Physiol. Rev."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1038\/173971a0","article-title":"Structural changes in muscle during contraction; interference microscopy of living muscle fibres","volume":"173","author":"Huxley","year":"1954","journal-title":"Nature"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"599S","DOI":"10.3945\/an.113.005405","article-title":"Keeping older muscle \u201cyoung\u201d through dietary protein and physical activity","volume":"5","author":"Moore","year":"2014","journal-title":"Adv. Nutr."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1172\/JCI111938","article-title":"Effects of insulin on peripheral and splanchnic glucose metabolism in noninsulin-dependent (type II) diabetes mellitus","volume":"76","author":"DeFronzo","year":"1985","journal-title":"J. Clin. Investig."},{"key":"ref_5","first-page":"177","article-title":"Clinical definition of sarcopenia","volume":"11","author":"Santilli","year":"2014","journal-title":"Clin. Cases Miner. Bone Metab."},{"key":"ref_6","first-page":"46","article-title":"Reversing sarcopenia: How weight training can build strength and vitality","volume":"51","author":"Evans","year":"1996","journal-title":"Geriatrics"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1159\/000356760","article-title":"Sarcopenia, cachexia and aging: Diagnosis, mechanisms and therapeutic options\u2014A mini-review","volume":"60","author":"Ali","year":"2014","journal-title":"Gerontology"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1038\/s41568-020-0251-4","article-title":"Understanding cachexia in the context of metastatic progression","volume":"20","author":"Biswas","year":"2020","journal-title":"Nat. Rev. Cancer"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.cmet.2012.06.011","article-title":"Cancer cachexia: Mediators, signaling, and metabolic pathways","volume":"16","author":"Fearon","year":"2012","journal-title":"Cell Metab."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1007\/s13539-012-0096-0","article-title":"Cancer cachexia prevention via physical exercise: Molecular mechanisms","volume":"4","author":"Gould","year":"2013","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"4979","DOI":"10.1113\/JP283569","article-title":"Impact of cancer cachexia on respiratory muscle function and the therapeutic potential of exercise","volume":"600","author":"Murphy","year":"2022","journal-title":"J. Physiol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1002\/jcsm.12360","article-title":"Cachexia induced by cancer and chemotherapy yield distinct perturbations to energy metabolism","volume":"10","author":"Pin","year":"2019","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1158\/0008-5472.CAN-13-1052","article-title":"Cancer usurps skeletal muscle as an energy repository","volume":"74","author":"Luo","year":"2014","journal-title":"Cancer Res."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/j.cell.2010.07.011","article-title":"Reversal of cancer cachexia and muscle wasting by ActRIIB antagonism leads to prolonged survival","volume":"142","author":"Zhou","year":"2010","journal-title":"Cell"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"7590","DOI":"10.4081\/ejtm.2018.7590","article-title":"Chemotherapy-induced muscle wasting: Association with NF-kappaB and cancer cachexia","volume":"28","author":"Damrauer","year":"2018","journal-title":"Eur. J. Transl. Myol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1136\/hrt.24.3.257","article-title":"Diseases of the heart in the works of Hippocrates","volume":"24","author":"Katz","year":"1962","journal-title":"Br. Heart J."},{"key":"ref_17","first-page":"257","article-title":"What is cancer anorexia-cachexia syndrome? A historical perspective","volume":"39","author":"Walsh","year":"2009","journal-title":"J. R. Coll Physicians Edinb."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1016\/S1470-2045(10)70218-7","article-title":"Definition and classification of cancer cachexia: An international consensus","volume":"12","author":"Fearon","year":"2011","journal-title":"Lancet Oncol."},{"key":"ref_19","first-page":"159","article-title":"Chemotherapy triggers cachexia by deregulating synergetic function of histone-modifying enzymes","volume":"12","author":"Pegoli","year":"2020","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1007\/s13539-014-0164-8","article-title":"Prevalence, incidence and clinical impact of cachexia: Facts and numbers-update 2014","volume":"5","author":"Anker","year":"2014","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1152\/physrev.00016.2008","article-title":"Mechanisms of cancer cachexia","volume":"89","author":"Tisdale","year":"2009","journal-title":"Physiol. Rev."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1038\/nrm.2016.81","article-title":"A comprehensive compilation of SUMO proteomics","volume":"17","author":"Hendriks","year":"2016","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"597675","DOI":"10.3389\/fphys.2020.597675","article-title":"Inflammation and Skeletal Muscle Wasting During Cachexia","volume":"11","author":"Webster","year":"2020","journal-title":"Front. Physiol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1038\/385540a0","article-title":"MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and IL-1","volume":"385","author":"Malinin","year":"1997","journal-title":"Nature"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/j.cell.2004.09.027","article-title":"IKKbeta\/NF-kappaB activation causes severe muscle wasting in mice","volume":"119","author":"Cai","year":"2004","journal-title":"Cell"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1016\/j.cmet.2007.09.009","article-title":"The E3 Ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle","volume":"6","author":"Clarke","year":"2007","journal-title":"Cell Metab."},{"key":"ref_27","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_28","doi-asserted-by":"crossref","first-page":"1704","DOI":"10.1126\/science.1065874","article-title":"Identification of ubiquitin ligases required for skeletal muscle atrophy","volume":"294","author":"Bodine","year":"2001","journal-title":"Science"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1172\/JCI200420174","article-title":"Cancer cachexia is regulated by selective targeting of skeletal muscle gene products","volume":"114","author":"Acharyya","year":"2004","journal-title":"J. Clin. Investig."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1093\/ajcn\/nqz347","article-title":"The autophagic-lysosomal and ubiquitin proteasome systems are simultaneously activated in the skeletal muscle of gastric cancer patients with cachexia","volume":"111","author":"Zhang","year":"2020","journal-title":"Am. J. Clin. Nutr."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1707","DOI":"10.1038\/s41467-017-01645-7","article-title":"Epigenetic targeting of bromodomain protein BRD4 counteracts cancer cachexia and prolongs survival","volume":"8","author":"Segatto","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1038\/sj.bjc.6602402","article-title":"NF-kappaB mediates proteolysis-inducing factor induced protein degradation and expression of the ubiquitin-proteasome system in skeletal muscle","volume":"92","author":"Wyke","year":"2005","journal-title":"Br. J. Cancer"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1038\/sj.bjc.6602780","article-title":"Expression of the ubiquitin-proteasome pathway and muscle loss in experimental cancer cachexia","volume":"93","author":"Khal","year":"2005","journal-title":"Br. J. Cancer"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1023\/A:1006806103675","article-title":"Expression of subunits of the 19S complex and of the PA28 activator in rat skeletal muscle","volume":"24","author":"Attaix","year":"1997","journal-title":"Mol. Biol. Rep."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"2847","DOI":"10.1074\/jbc.M411346200","article-title":"Degradation of MyoD mediated by the SCF (MAFbx) ubiquitin ligase","volume":"280","author":"Tintignac","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1565","DOI":"10.1002\/jcsm.12968","article-title":"Targeting MuRF1 by small molecules in a HFpEF rat model improves myocardial diastolic function and skeletal muscle contractility","volume":"13","author":"Adams","year":"2022","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1002\/jcsm.12233","article-title":"Small-molecule inhibition of MuRF1 attenuates skeletal muscle atrophy and dysfunction in cardiac cachexia","volume":"8","author":"Bowen","year":"2017","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Adams, V., Gussen, V., Zozulya, S., Cruz, A., Moriscot, A., Linke, A., and Labeit, S. (2020). Small-Molecule Chemical Knockdown of MuRF1 in Melanoma Bearing Mice Attenuates Tumor Cachexia Associated Myopathy. Cells, 9.","DOI":"10.3390\/cells9102272"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"e2200215119","DOI":"10.1073\/pnas.2200215119","article-title":"UBR2 targets myosin heavy chain IIb and IIx for degradation: Molecular mechanism essential for cancer-induced muscle wasting","volume":"119","author":"Gao","year":"2022","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1002\/(SICI)1097-0142(19980101)82:1<42::AID-CNCR5>3.0.CO;2-M","article-title":"Effects of cachexia due to cancer on whole body and skeletal muscle protein turnover","volume":"82","author":"Dworzak","year":"1998","journal-title":"Cancer"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1038\/ncb839","article-title":"TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling","volume":"4","author":"Inoki","year":"2002","journal-title":"Nat. Cell Biol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1216","DOI":"10.1038\/sj.bjc.6603704","article-title":"Attenuation of muscle atrophy in a murine model of cachexia by inhibition of the dsRNA-dependent protein kinase","volume":"96","author":"Eley","year":"2007","journal-title":"Br. J. Cancer"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1186\/2044-5040-1-4","article-title":"Regulation of skeletal muscle growth by the IGF1-Akt\/PKB pathway: Insights from genetic models","volume":"1","author":"Schiaffino","year":"2011","journal-title":"Skelet Muscle"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1002\/jcsm.12854","article-title":"Activation of Akt-mTORC1 signalling reverts cancer-dependent muscle wasting","volume":"13","author":"Geremia","year":"2022","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/S0092-8674(04)00400-3","article-title":"Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy","volume":"117","author":"Sandri","year":"2004","journal-title":"Cell"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1016\/j.cmet.2007.11.001","article-title":"FoxO3 controls autophagy in skeletal muscle in vivo","volume":"6","author":"Mammucari","year":"2007","journal-title":"Cell Metab."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1016\/j.cmet.2007.11.004","article-title":"FoxO3 coordinately activates protein degradation by the autophagic\/lysosomal and proteasomal pathways in atrophying muscle cells","volume":"6","author":"Zhao","year":"2007","journal-title":"Cell Metab."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"1946","DOI":"10.1210\/me.2013-1194","article-title":"Smad3 induces atrogin-1, inhibits mTOR and protein synthesis, and promotes muscle atrophy in vivo","volume":"27","author":"Goodman","year":"2013","journal-title":"Mol. Endocrinol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1016\/j.bbagen.2008.06.004","article-title":"Branched-chain amino acids and arginine suppress MaFbx\/atrogin-1 mRNA expression via mTOR pathway in C2C12 cell line","volume":"1780","author":"Herningtyas","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"E488","DOI":"10.1152\/ajpendo.00094.2002","article-title":"Reduced amino acid availability inhibits muscle protein synthesis and decreases activity of initiation factor eIF2B","volume":"284","author":"Kobayashi","year":"2003","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.aninu.2022.04.010","article-title":"L-Arginine\/nitric oxide regulates skeletal muscle development via muscle fibre-specific nitric oxide\/mTOR pathway in chickens","volume":"10","author":"Wang","year":"2022","journal-title":"Anim. Nutr."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"998","DOI":"10.1096\/fj.13-240580","article-title":"Skeletal muscle glycoprotein 130\u2019s role in Lewis lung carcinoma-induced cachexia","volume":"28","author":"Puppa","year":"2014","journal-title":"FASEB J."},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"White, J.P., Baynes, J.W., Welle, S.L., Kostek, M.C., Matesic, L.E., Sato, S., and Carson, J.A. (2011). The regulation of skeletal muscle protein turnover during the progression of cancer cachexia in the Apc(Min\/+) mouse. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0024650"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1016\/j.cmet.2013.10.001","article-title":"mTORC1 controls mitochondrial activity and biogenesis through 4E-BP-dependent translational regulation","volume":"18","author":"Morita","year":"2013","journal-title":"Cell Metab."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1007\/s13539-011-0051-5","article-title":"The role of insulin resistance in the development of muscle wasting during cancer cachexia","volume":"3","author":"Honors","year":"2012","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1002\/ijc.24784","article-title":"Evidence for the contribution of insulin resistance to the development of cachexia in tumor-bearing mice","volume":"126","author":"Asp","year":"2010","journal-title":"Int. J. Cancer"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1007\/s10552-009-9492-y","article-title":"Longitudinal associations of blood markers of insulin and glucose metabolism and cancer mortality in the third National Health and Nutrition Examination Survey","volume":"21","author":"Parekh","year":"2010","journal-title":"Cancer Causes Control"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"957","DOI":"10.4161\/cbt.12.11.18134","article-title":"Rosiglitazone delayed weight loss and anorexia while attenuating adipose depletion in mice with cancer cachexia","volume":"12","author":"Asp","year":"2011","journal-title":"Cancer Biol. Ther."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"2939","DOI":"10.2337\/diabetes.54.10.2939","article-title":"Tumor necrosis factor-alpha induces skeletal muscle insulin resistance in healthy human subjects via inhibition of Akt substrate 160 phosphorylation","volume":"54","author":"Plomgaard","year":"2005","journal-title":"Diabetes"},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Mannelli, M., Gamberi, T., Magherini, F., and Fiaschi, T. (2021). A Metabolic Change towards Fermentation Drives Cancer Cachexia in Myotubes. Biomedicines, 9.","DOI":"10.3390\/biomedicines9060698"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1177\/0967772019866954","article-title":"Carl and Gerty Cori: A collaboration that changed the face of biochemistry","volume":"29","author":"Rubin","year":"2021","journal-title":"J. Med. Biogr."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/j.cell.2008.08.021","article-title":"Cancer cell metabolism: Warburg and beyond","volume":"134","author":"Hsu","year":"2008","journal-title":"Cell"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1186\/1743-7075-8-75","article-title":"Is there a role for carbohydrate restriction in the treatment and prevention of cancer?","volume":"8","author":"Klement","year":"2011","journal-title":"Nutr. Metab."},{"key":"ref_64","first-page":"1098","article-title":"Effects of 2-deoxyglucose on carbohydrate metablism: Review of the literature and studies in the rat","volume":"11","author":"Brown","year":"1962","journal-title":"Metabolism"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"7023","DOI":"10.1158\/0008-5472.CAN-05-0453","article-title":"2-Deoxyglucose as an energy restriction mimetic agent: Effects on mammary carcinogenesis and on mammary tumor cell growth in vitro","volume":"65","author":"Zhu","year":"2005","journal-title":"Cancer Res."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"14825","DOI":"10.1074\/jbc.272.23.14825","article-title":"Identification and localization of a skeletal muscle secrotonin 5-HT2A receptor coupled to the Jak\/STAT pathway","volume":"272","author":"Burnol","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"500","DOI":"10.3389\/fphys.2019.00500","article-title":"The JAK\/STAT Pathway in Skeletal Muscle Pathophysiology","volume":"10","author":"Moresi","year":"2019","journal-title":"Front. Physiol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1083\/jcb.200703184","article-title":"JAK1-STAT1-STAT3, a key pathway promoting proliferation and preventing premature differentiation of myoblasts","volume":"179","author":"Sun","year":"2007","journal-title":"J. Cell Biol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1038\/cr.2010.144","article-title":"Oncostatin M inhibits myoblast differentiation and regulates muscle regeneration","volume":"21","author":"Xiao","year":"2011","journal-title":"Cell Res."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"34029","DOI":"10.1074\/jbc.M803012200","article-title":"JAK2\/STAT2\/STAT3 are required for myogenic differentiation","volume":"283","author":"Wang","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"11177","DOI":"10.1074\/jbc.M115.641514","article-title":"Inhibition of Stat3 activation suppresses caspase-3 and the ubiquitin-proteasome system, leading to preservation of muscle mass in cancer cachexia","volume":"290","author":"Silva","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Judge, S.M., Wu, C.L., Beharry, A.W., Roberts, B.M., Ferreira, L.F., Kandarian, S.C., and Judge, A.R. (2014). Genome-wide identification of FoxO-dependent gene networks in skeletal muscle during C26 cancer cachexia. BMC Cancer, 14.","DOI":"10.1186\/1471-2407-14-997"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.21037\/atm-20-7269","article-title":"Inhibition of IL-6\/JAK\/STAT3 pathway rescues denervation-induced skeletal muscle atrophy","volume":"8","author":"Huang","year":"2020","journal-title":"Ann. Transl. Med."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"18636","DOI":"10.1073\/pnas.0709307104","article-title":"Aberrant expression of zinc transporter ZIP4 (SLC39A4) significantly contributes to human pancreatic cancer pathogenesis and progression","volume":"104","author":"Li","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1053\/j.gastro.2018.10.026","article-title":"ZIP4 Promotes Muscle Wasting and Cachexia in Mice with Orthotopic Pancreatic Tumors by Stimulating RAB27B-Regulated Release of Extracellular Vesicles From Cancer Cells","volume":"156","author":"Yang","year":"2019","journal-title":"Gastroenterology"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1038\/s41591-018-0054-2","article-title":"Metastatic cancers promote cachexia through ZIP14 upregulation in skeletal muscle","volume":"24","author":"Wang","year":"2018","journal-title":"Nat. Med."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"6766","DOI":"10.1002\/cam4.3242","article-title":"Aberrant Zip14 expression in muscle is associated with cachexia in a Bard1-deficient mouse model of breast cancer metastasis","volume":"9","author":"Shakri","year":"2020","journal-title":"Cancer Med."},{"key":"ref_78","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_79","doi-asserted-by":"crossref","first-page":"1356","DOI":"10.1158\/1078-0432.CCR-06-2307","article-title":"Cancer cachexia signaling pathways continue to emerge yet much still points to the proteasome","volume":"13","author":"Acharyya","year":"2007","journal-title":"Clin. Cancer Res."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"2363","DOI":"10.1126\/science.289.5488.2363","article-title":"NF-kappaB-induced loss of MyoD messenger RNA: Possible role in muscle decay and cachexia","volume":"289","author":"Guttridge","year":"2000","journal-title":"Science"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1083\/jcb.140.2.259","article-title":"Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association","volume":"140","author":"Mahajan","year":"1998","journal-title":"J. Cell Biol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"1457","DOI":"10.1083\/jcb.135.6.1457","article-title":"A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex","volume":"135","author":"Matunis","year":"1996","journal-title":"J. Cell Biol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1038\/msb.2011.81","article-title":"Deep proteome and transcriptome mapping of a human cancer cell line","volume":"7","author":"Nagaraj","year":"2011","journal-title":"Mol. Syst. Biol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1186\/s13059-014-0422-2","article-title":"SUMO-specific proteases\/isopeptidases: SENPs and beyond","volume":"15","author":"Nayak","year":"2014","journal-title":"Genome Biol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"878","DOI":"10.15252\/embr.201438534","article-title":"SUMO2 is essential while SUMO3 is dispensable for mouse embryonic development","volume":"15","author":"Wang","year":"2014","journal-title":"EMBO Rep."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1016\/j.devcel.2005.10.007","article-title":"The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice","volume":"9","author":"Nacerddine","year":"2005","journal-title":"Dev. Cell"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1038\/s41580-022-00500-y","article-title":"Signalling mechanisms and cellular functions of SUMO","volume":"23","author":"Vertegaal","year":"2022","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1016\/j.ccell.2017.10.002","article-title":"Acute Promyelocytic Leukemia: A Paradigm for Oncoprotein-Targeted Cure","volume":"32","author":"Pandolfi","year":"2017","journal-title":"Cancer Cell"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1038\/nrm.2017.7","article-title":"Biomolecular condensates: Organizers of cellular biochemistry","volume":"18","author":"Banani","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1038\/s41580-020-00303-z","article-title":"A framework for understanding the functions of biomolecular condensates across scales","volume":"22","author":"Lyon","year":"2021","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1016\/j.cell.2012.10.021","article-title":"Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair","volume":"151","author":"Psakhye","year":"2012","journal-title":"Cell"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"3110","DOI":"10.1111\/febs.15319","article-title":"Sumoylation on its 25th anniversary: Mechanisms, pathology, and emerging concepts","volume":"287","author":"Celen","year":"2020","journal-title":"FEBS J."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1515\/bmc-2016-0030","article-title":"SUMO conjugation\u2014A mechanistic view","volume":"8","author":"Pichler","year":"2017","journal-title":"Biomol. Concepts"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1146\/annurev-biochem-061909-093311","article-title":"Sumoylation: A regulatory protein modification in health and disease","volume":"82","author":"Flotho","year":"2013","journal-title":"Annu. Rev. Biochem."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.molcel.2005.03.012","article-title":"SUMO: A history of modification","volume":"18","author":"Hay","year":"2005","journal-title":"Mol. Cell"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1073\/pnas.97.3.1125","article-title":"The sentrin-conjugating enzyme mUbc9 interacts with GLUT4 and GLUT1 glucose transporters and regulates transporter levels in skeletal muscle cells","volume":"97","author":"Giorgino","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"19783","DOI":"10.1074\/jbc.M110294200","article-title":"The insulin-sensitive glucose transporter, GLUT4, interacts physically with Daxx. Two proteins with capacity to bind Ubc9 and conjugated to SUMO1","volume":"277","author":"Lalioti","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"10208","DOI":"10.1074\/jbc.M710604200","article-title":"Functional role of sortilin in myogenesis and development of insulin-responsive glucose transport system in C2C12 myocytes","volume":"283","author":"Ariga","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"2420","DOI":"10.2337\/db15-0115","article-title":"SUMO-Specific Protease 2 (SENP2) Is an Important Regulator of Fatty Acid Metabolism in Skeletal Muscle","volume":"64","author":"Koo","year":"2015","journal-title":"Diabetes"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.metabol.2019.03.004","article-title":"SUMO-specific protease 2 mediates leptin-induced fatty acid oxidation in skeletal muscle","volume":"95","author":"Koo","year":"2019","journal-title":"Metabolism"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1111\/j.1582-4934.2006.tb00295.x","article-title":"SUMO-1 modification of MEF2A regulates its transcriptional activity","volume":"10","author":"Riquelme","year":"2006","journal-title":"J. Cell Mol. Med."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"2273","DOI":"10.1128\/MCB.25.6.2273-2287.2005","article-title":"Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors","volume":"25","author":"Gregoire","year":"2005","journal-title":"Mol. Cell Biol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1073\/pnas.0503698102","article-title":"PDSM, a motif for phosphorylation-dependent SUMO modification","volume":"103","author":"Hietakangas","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"2132","DOI":"10.1016\/j.yexcr.2006.03.016","article-title":"Ubc9 expression is essential for myotube formation in C2C12","volume":"312","author":"Riquelme","year":"2006","journal-title":"Exp. Cell Res."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1007\/s10974-021-09605-x","article-title":"2-D08 treatment regulates C2C12 myoblast proliferation and differentiation via the Erk1\/2 and proteasome signaling pathways","volume":"42","author":"Liu","year":"2021","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1002\/1097-4652(200101)186:1<104::AID-JCP1015>3.0.CO;2-0","article-title":"ERK1\/2 is required for myoblast proliferation but is dispensable for muscle gene expression and cell fusion","volume":"186","author":"Jones","year":"2001","journal-title":"J. Cell Physiol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"3430","DOI":"10.1038\/sj.emboj.7600346","article-title":"Pax7 directs postnatal renewal and propagation of myogenic satellite cells but not their specification","volume":"23","author":"Oustanina","year":"2004","journal-title":"EMBO J."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1793","DOI":"10.1007\/s00018-012-1220-1","article-title":"SUMOylation of Pax7 is essential for neural crest and muscle development","volume":"70","author":"Luan","year":"2013","journal-title":"Cell Mol. Life Sci."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1038\/s41419-019-1465-9","article-title":"SUMOylation of G9a regulates its function as an activator of myoblast proliferation","volume":"10","author":"Srinivasan","year":"2019","journal-title":"Cell Death Dis."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"1447","DOI":"10.1152\/physrev.00031.2010","article-title":"Fiber types in mammalian skeletal muscles","volume":"91","author":"Schiaffino","year":"2011","journal-title":"Physiol. Rev."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1074\/mcp.M116.066159","article-title":"A Proteomic Approach to Identify Alterations in the Small Ubiquitin-like Modifier (SUMO) Network during Controlled Mechanical Ventilation in Rat Diaphragm Muscle","volume":"16","author":"Namuduri","year":"2017","journal-title":"Mol. Cell. Proteomics"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"2269","DOI":"10.1096\/fj.201901913R","article-title":"Expression of SUMO enzymes is fiber type dependent in skeletal muscles and is dysregulated in muscle disuse","volume":"34","author":"Namuduri","year":"2020","journal-title":"FASEB J."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"9397","DOI":"10.1038\/s41598-019-45821-9","article-title":"Skeletal muscle in MuRF1 null mice is not spared in low-gravity conditions, indicating atrophy proceeds by unique mechanisms in space","volume":"9","author":"Cadena","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"69","DOI":"10.3389\/fphys.2014.00069","article-title":"Muscle hypertrophy is associated with increases in proteasome activity that is independent of MuRF1 and MAFbx expression","volume":"5","author":"Baehr","year":"2014","journal-title":"Front. Physiol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1353","DOI":"10.1093\/hmg\/ddp036","article-title":"Deficiency of the E3 ubiquitin ligase TRIM32 in mice leads to a myopathy with a neurogenic component","volume":"18","author":"Kudryashova","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"2725","DOI":"10.1016\/j.celrep.2019.04.107","article-title":"Regulation of SETD7 Methyltransferase by SENP3 Is Crucial for Sarcomere Organization and Cachexia","volume":"27","author":"Nayak","year":"2019","journal-title":"Cell Rep."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"17105","DOI":"10.1038\/nrdp.2017.105","article-title":"Cancer-associated cachexia","volume":"4","author":"Baracos","year":"2018","journal-title":"Nat. Rev. Dis. Primers"},{"key":"ref_118","doi-asserted-by":"crossref","unstructured":"Campelj, D.G., Goodman, C.A., and Rybalka, E. (2021). Chemotherapy-Induced Myopathy: The Dark Side of the Cachexia Sphere. Cancers, 13.","DOI":"10.3390\/cancers13143615"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"2449","DOI":"10.1084\/jem.20111020","article-title":"Central nervous system inflammation induces muscle atrophy via activation of the hypothalamic-pituitary-adrenal axis","volume":"208","author":"Braun","year":"2011","journal-title":"J. Exp. Med."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"C195","DOI":"10.1152\/ajpcell.00217.2011","article-title":"Doxorubicin acts via mitochondrial ROS to stimulate catabolism in C2C12 myotubes","volume":"302","author":"Gilliam","year":"2012","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"e14052","DOI":"10.14814\/phy2.14052","article-title":"Chronic doxorubicin administration impacts satellite cell and capillary abundance in a muscle-specific manner","volume":"7","author":"Fry","year":"2019","journal-title":"Physiol. Rep."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1002\/jcsm.12265","article-title":"Prevention of chemotherapy-induced cachexia by ACVR2B ligand blocking has different effects on heart and skeletal muscle","volume":"9","author":"Hulmi","year":"2018","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"1597","DOI":"10.1002\/jcsm.12795","article-title":"Loss of REDD1 prevents chemotherapy-induced muscle atrophy and weakness in mice","volume":"12","author":"Hain","year":"2021","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"3401","DOI":"10.1200\/JCO.2005.04.5724","article-title":"Double-blind, placebo-controlled, randomized study of eicosapentaenoic acid diester in patients with cancer cachexia","volume":"24","author":"Fearon","year":"2006","journal-title":"J. Clin. Oncol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1080\/01635581.2019.1634746","article-title":"Safety and Tolerability of Targeted Medical Nutrition for Cachexia in Non-Small-Cell Lung Cancer: A Randomized, Double-Blind, Controlled Pilot Trial","volume":"72","author":"Laviano","year":"2020","journal-title":"Nutr. Cancer"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1158\/0008-5472.277.65.1","article-title":"Attenuation of proteasome-induced proteolysis in skeletal muscle by [148]-hydroxy-[148]-methylbutyrate in cancer-induced muscle loss","volume":"65","author":"Smith","year":"2005","journal-title":"Cancer Res."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1016\/S0002-9610(02)00823-1","article-title":"Reversal of cancer-related wasting using oral supplementation with a combination of beta-hydroxy-beta-methylbutyrate, arginine, and glutamine","volume":"183","author":"May","year":"2002","journal-title":"Am. J. Surg."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"1623","DOI":"10.1002\/jcsm.12952","article-title":"Effects of beta-hydroxy beta-methylbutyrate (HMB) supplementation on muscle mass, function, and other outcomes in patients with cancer: A systematic review","volume":"13","author":"Prado","year":"2022","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"5425619","DOI":"10.1155\/2022\/5425619","article-title":"Efficacy of Curcumin on Treating Cancer Anorexia-Cachexia Syndrome in Locally or Advanced Head and Neck Cancer: A Double-Blind, Placebo-Controlled Randomised Phase IIa Trial (CurChexia)","volume":"2022","author":"Thambamroong","year":"2022","journal-title":"J. Nutr. Metab."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1177\/1534735416651968","article-title":"A Prospective Randomized Controlled Trial to Study the Impact of a Nutrition-Sensitive Intervention on Adult Women With Cancer Cachexia Undergoing Palliative Care in India","volume":"16","author":"Kapoor","year":"2017","journal-title":"Integr. Cancer Ther."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/S1470-2045(14)71154-4","article-title":"Anamorelin for patients with cancer cachexia: An integrated analysis of two phase 2, randomised, placebo-controlled, double-blind trials","volume":"16","author":"Garcia","year":"2015","journal-title":"Lancet Oncol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1002\/cncr.31128","article-title":"Anamorelin (ONO-7643) for the treatment of patients with non-small cell lung cancer and cachexia: Results from a randomized, double-blind, placebo-controlled, multicenter study of Japanese patients (ONO-7643-04)","volume":"124","author":"Katakami","year":"2018","journal-title":"Cancer"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"1949","DOI":"10.1093\/annonc\/mdx192","article-title":"ROMANA 3: A phase 3 safety extension study of anamorelin in advanced non-small-cell lung cancer (NSCLC) patients with cachexia","volume":"28","author":"Currow","year":"2017","journal-title":"Ann. Oncol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"4633","DOI":"10.1038\/s41467-022-32135-0","article-title":"Blocking ActRIIB and restoring appetite reverses cachexia and improves survival in mice with lung cancer","volume":"13","author":"Queiroz","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"1387","DOI":"10.1249\/MSS.0000000000001916","article-title":"Combined Exercise Training Positively Affects Muscle Wasting in Tumor-Bearing Mice","volume":"51","author":"Ranjbar","year":"2019","journal-title":"Med. Sci. Sports Exerc."},{"key":"ref_136","doi-asserted-by":"crossref","unstructured":"Ballaro, R., Penna, F., Pin, F., Gomez-Cabrera, M.C., Vina, J., and Costelli, P. (2019). Moderate Exercise Improves Experimental Cancer Cachexia by Modulating the Redox Homeostasis. Cancers, 11.","DOI":"10.3390\/cancers11030285"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1139\/apnm-2016-0436","article-title":"Resistance exercise attenuates skeletal muscle oxidative stress, systemic pro-inflammatory state, and cachexia in Walker-256 tumor-bearing rats","volume":"42","author":"Padilha","year":"2017","journal-title":"Appl. Physiol. Nutr. Metab."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"7852","DOI":"10.1096\/fj.201802430R","article-title":"Preventive effects of low-intensity exercise on cancer cachexia-induced muscle atrophy","volume":"33","author":"Tanaka","year":"2019","journal-title":"FASEB J."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"113938","DOI":"10.18632\/oncotarget.23044","article-title":"Modulating the metabolism by trimetazidine enhances myoblast differentiation and promotes myogenesis in cachectic tumor-bearing c26 mice","volume":"8","author":"Gatta","year":"2017","journal-title":"Oncotarget"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"954","DOI":"10.1002\/jcsm.12226","article-title":"The mitochondrial metabolic reprogramming agent trimetazidine as an \u2018exercise mimetic\u2019 in cachectic C26-bearing mice","volume":"8","author":"Molinari","year":"2017","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1002\/jcb.23399","article-title":"AMPK promotes skeletal muscle autophagy through activation of forkhead FoxO3a and interaction with Ulk1","volume":"113","author":"Sanchez","year":"2012","journal-title":"J. Cell Biochem."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"26991","DOI":"10.1038\/srep26991","article-title":"Aerobic Exercise and Pharmacological Treatments Counteract Cachexia by Modulating Autophagy in Colon Cancer","volume":"6","author":"Pigna","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_143","first-page":"CD010804","article-title":"Exercise for cancer cachexia in adults","volume":"3","author":"Grande","year":"2021","journal-title":"Cochrane Database Syst. Rev."},{"key":"ref_144","doi-asserted-by":"crossref","unstructured":"Bourdel-Marchasson, I., Blanc-Bisson, C., Doussau, A., Germain, C., Blanc, J.F., Dauba, J., Lahmar, C., Terrebonne, E., Lecaille, C., and Ceccaldi, J. (2014). Nutritional advice in older patients at risk of malnutrition during treatment for chemotherapy: A two-year randomized controlled trial. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0108687"},{"key":"ref_145","doi-asserted-by":"crossref","unstructured":"Clemente-Suarez, V.J., Redondo-Florez, L., Rubio-Zarapuz, A., Martinez-Guardado, I., Navarro-Jimenez, E., and Tornero-Aguilera, J.F. (2022). Nutritional and Exercise Interventions in Cancer-Related Cachexia: An Extensive Narrative Review. Int. J. Environ. Res. Public Health, 19.","DOI":"10.3390\/ijerph19084604"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"3106","DOI":"10.1002\/jcsm.13094","article-title":"Engineered skeletal muscle recapitulates human muscle development, regeneration and dystrophy","volume":"13","author":"Shahriyari","year":"2022","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"2176","DOI":"10.1111\/febs.15263","article-title":"SUMO system\u2014A key regulator in sarcomere organization","volume":"287","author":"Nayak","year":"2020","journal-title":"FEBS J."}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/12\/4\/644\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T18:39:05Z","timestamp":1760121545000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/12\/4\/644"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,2,17]]},"references-count":147,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2023,2]]}},"alternative-id":["cells12040644"],"URL":"https:\/\/doi.org\/10.3390\/cells12040644","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,2,17]]}}}