{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,31]],"date-time":"2026-10-31T07:52:40Z","timestamp":1793433160627,"version":"4.5.0"},"reference-count":195,"publisher":"Springer Science and Business Media LLC","issue":"3","license":[{"start":{"date-parts":[[2021,11,8]],"date-time":"2021-11-08T00:00:00Z","timestamp":1636329600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2021,11,8]],"date-time":"2021-11-08T00:00:00Z","timestamp":1636329600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Rev Nephrol"],"published-print":{"date-parts":[[2022,3]]},"DOI":"10.1038\/s41581-021-00498-0","type":"journal-article","created":{"date-parts":[[2021,11,8]],"date-time":"2021-11-08T10:05:49Z","timestamp":1636365949000},"page":"138-152","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":163,"title":["Pathophysiological mechanisms leading to muscle loss in chronic kidney disease"],"prefix":"10.1038","volume":"18","author":[{"given":"Xiaonan H.","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William E.","family":"Mitch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0893-0723","authenticated-orcid":false,"given":"S. Russ","family":"Price","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2021,11,8]]},"reference":[{"key":"498_CR1","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1152\/jappl.2000.89.1.81","volume":"89","author":"I Janssen","year":"2000","unstructured":"Janssen, I., Heymsfield, S. B., Wang, Z. M. & Ross, R. Skeletal muscle mass and distribution in 468 men and women aged 18-88 yr. J. Appl. Physiol. 89, 81\u201388 (2000).","journal-title":"J. Appl. Physiol."},{"key":"498_CR2","doi-asserted-by":"publisher","first-page":"456","DOI":"10.1016\/S0899-9007(96)00141-4","volume":"12","author":"RD Griffiths","year":"1996","unstructured":"Griffiths, R. D. Muscle mass, survival, and the elderly ICU patient. Nutrition 12, 456\u2013458 (1996).","journal-title":"Nutrition"},{"key":"498_CR3","doi-asserted-by":"publisher","first-page":"1897","DOI":"10.1056\/NEJM199612193352507","volume":"335","author":"WE Mitch","year":"1996","unstructured":"Mitch, W. E. & Goldberg, A. L. Mechanisms of muscle wasting. The role of the ubiquitin-proteasome pathway. N. Engl. J. Med. 335, 1897\u20131905 (1996).","journal-title":"N. Engl. J. Med."},{"key":"498_CR4","doi-asserted-by":"publisher","first-page":"202","DOI":"10.1159\/000504240","volume":"49","author":"RM Hanna","year":"2020","unstructured":"Hanna, R. M., Ghobry, L., Wassef, O., Rhee, C. M. & Kalantar-Zadeh, K. A practical approach to nutrition, protein-energy wasting, sarcopenia, and cachexia in patients with chronic kidney disease. Blood Purif. 49, 202\u2013211 (2020).","journal-title":"Blood Purif."},{"key":"498_CR5","doi-asserted-by":"publisher","first-page":"219","DOI":"10.1097\/MNH.0000000000000318","volume":"26","author":"RN Moorthi","year":"2017","unstructured":"Moorthi, R. N. & Avin, K. G. Clinical relevance of sarcopenia in chronic kidney disease. Curr. Opin. Nephrol. Hyperten. 26, 219\u2013228 (2017).","journal-title":"Curr. Opin. Nephrol. Hyperten."},{"key":"498_CR6","doi-asserted-by":"publisher","first-page":"1296","DOI":"10.1056\/NEJMoa041031","volume":"351","author":"AS Go","year":"2004","unstructured":"Go, A. S., Chertow, G. M., Fan, D., McCulloch, C. E. & Hsu, C. Y. Chronic kidney disease and the risks of death, cardiovascular events, and hospitalization. N. Engl. J. Med. 351, 1296\u20131305 (2004).","journal-title":"N. Engl. J. Med."},{"key":"498_CR7","doi-asserted-by":"publisher","first-page":"1347","DOI":"10.1007\/s40620-020-00840-y","volume":"34","author":"A Sabatino","year":"2020","unstructured":"Sabatino, A., Cuppari, L., Stenvinkel, P., Lindholm, B. & Avesani, C. M. Sarcopenia in chronic kidney disease: what have we learned so far? J. Nephrol. 34, 1347\u20131372 (2020).","journal-title":"J. Nephrol."},{"key":"498_CR8","doi-asserted-by":"publisher","first-page":"458","DOI":"10.1016\/S0272-6386(12)70364-5","volume":"15","author":"EG Lowrie","year":"1990","unstructured":"Lowrie, E. G. & Lew, N. L. Death risk in hemodialysis patients: the predictive value of commonly measured variables and an evaluation of death rate differences between facilities. Am. J. Kidney Dis. 15, 458\u2013482 (1990).","journal-title":"Am. J. Kidney Dis."},{"key":"498_CR9","doi-asserted-by":"publisher","first-page":"380","DOI":"10.1053\/j.jrn.2018.08.006","volume":"28","author":"JJ Carrero","year":"2018","unstructured":"Carrero, J. J. et al. Global prevalence of protein-energy wasting in kidney disease: a meta-analysis of contemporary observational studies from the International Society of Renal Nutrition and Metabolism. J. Ren. Nutr. 28, 380\u2013392 (2018).","journal-title":"J. Ren. Nutr."},{"key":"498_CR10","doi-asserted-by":"publisher","first-page":"337","DOI":"10.1681\/ASN.2012010047","volume":"24","author":"JC Kim","year":"2013","unstructured":"Kim, J. C., Kalantar-Zadeh, K. & Kopple, J. D. Frailty and protein-energy wasting in elderly patients with end stage kidney disease. J. Am. Soc. Nephrol. 24, 337\u2013351 (2013).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR11","doi-asserted-by":"publisher","first-page":"898","DOI":"10.2215\/CJN.03340410","volume":"6","author":"DM Zelle","year":"2011","unstructured":"Zelle, D. M. et al. Low physical activity and risk of cardiovascular and all-cause mortality in renal transplant recipients. Clin. J. Am. Soc. Nephrol. 6, 898\u2013905 (2011).","journal-title":"Clin. J. Am. Soc. Nephrol."},{"key":"498_CR12","doi-asserted-by":"publisher","first-page":"3050","DOI":"10.1093\/ndt\/gfq138","volume":"25","author":"F Tentori","year":"2010","unstructured":"Tentori, F. et al. Physical exercise among participants in the Dialysis Outcomes and Practice Patterns Study (DOPPS): correlates and associated outcomes. Nephrol. Dial. Transpl. 25, 3050\u20133062 (2010).","journal-title":"Nephrol. Dial. Transpl."},{"key":"498_CR13","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1016\/j.semnephrol.2008.10.002","volume":"29","author":"CP Kovesdy","year":"2009","unstructured":"Kovesdy, C. P. & Kalantar-Zadeh, K. Why is protein-energy wasting associated with mortality in chronic kidney disease? Sem. Nephrol. 29, 3\u201314 (2009).","journal-title":"Sem. Nephrol."},{"key":"498_CR14","doi-asserted-by":"publisher","first-page":"1447","DOI":"10.1172\/JCI118566","volume":"97","author":"JL Bailey","year":"1996","unstructured":"Bailey, J. L. et al. The acidosis of chronic renal failure activates muscle proteolysis in rats by augmenting transcription of genes encoding proteins of the ATP-dependent ubiquitin-proteasome pathway. J. Clin. Invest. 97, 1447\u20131453 (1996).","journal-title":"J. Clin. Invest."},{"key":"498_CR15","doi-asserted-by":"publisher","first-page":"1070","DOI":"10.1093\/ndt\/gfv122","volume":"31","author":"P Stenvinkel","year":"2016","unstructured":"Stenvinkel, P., Carrero, J. J., von Walden, F., Ikizler, T. A. & Nader, G. A. Muscle wasting in end-stage renal disease promulgates premature death: established, emerging and potential novel treatment strategies. Nephrol. Dial. Transpl. 31, 1070\u20131077 (2016).","journal-title":"Nephrol. Dial. Transpl."},{"key":"498_CR16","doi-asserted-by":"publisher","first-page":"S1","DOI":"10.1053\/j.ajkd.2020.05.006","volume":"76","author":"TA Ikizler","year":"2020","unstructured":"Ikizler, T. A. et al. KDOQI clinical practice guideline for nutrition in CKD: 2020 update. Am. J. Kidney Dis. 76, S1\u2013S107 (2020).","journal-title":"Am. J. Kidney Dis."},{"key":"498_CR17","doi-asserted-by":"publisher","DOI":"10.1038\/emm.2015.97","volume":"48","author":"IY Kim","year":"2016","unstructured":"Kim, I. Y., Suh, S. H., Lee, I. K. & Wolfe, R. R. Applications of stable, nonradioactive isotope tracers in in vivo human metabolic research. Exp. Mol. Med. 48, e203 (2016).","journal-title":"Exp. Mol. Med."},{"key":"498_CR18","doi-asserted-by":"publisher","first-page":"649","DOI":"10.1042\/bj2120649","volume":"212","author":"AS Clark","year":"1983","unstructured":"Clark, A. S. & Mitch, W. E. Comparison of protein synthesis and degradation in incubated and perfused muscle. Biochem. J. 212, 649\u2013653 (1983).","journal-title":"Biochem. J."},{"key":"498_CR19","doi-asserted-by":"publisher","first-page":"751","DOI":"10.1038\/ki.2009.260","volume":"76","author":"XH Wang","year":"2009","unstructured":"Wang, X. H., Du, J., Klein, J. D., Bailey, J. L. & Mitch, W. E. Exercise ameliorates chronic kidney disease-induced defects in muscle protein metabolism and progenitor cell function. Kidney Int. 76, 751\u2013759 (2009).","journal-title":"Kidney Int."},{"key":"498_CR20","first-page":"403","volume":"66","author":"CF Chen","year":"2011","unstructured":"Chen, C. F., You, Z. H., Yang, W. C. & Lin, C. C. Hypokalaemic paralysis with seemingly pH-neutralized blood gas: liquorice-induced mineralocorticoid effect superimposed on renal tubular acidosis. Acta Clin. Belg. 66, 403 (2011).","journal-title":"Acta Clin. Belg."},{"key":"498_CR21","doi-asserted-by":"publisher","DOI":"10.1172\/jci.insight.95185","volume":"2","author":"SM Deger","year":"2017","unstructured":"Deger, S. M. et al. Systemic inflammation is associated with exaggerated skeletal muscle protein catabolism in maintenance hemodialysis patients. JCI Insight 2, e95185 (2017).","journal-title":"JCI Insight"},{"key":"498_CR22","doi-asserted-by":"publisher","first-page":"1419","DOI":"10.1038\/ki.2015.247","volume":"88","author":"G Garibotto","year":"2015","unstructured":"Garibotto, G. et al. Insulin sensitivity of muscle protein metabolism is altered in patients with chronic kidney disease and metabolic acidosis. Kidney Int. 88, 1419\u20131426 (2015).","journal-title":"Kidney Int."},{"key":"498_CR23","doi-asserted-by":"publisher","first-page":"E219","DOI":"10.1152\/ajpendo.2000.278.2.E219","volume":"278","author":"D Adey","year":"2000","unstructured":"Adey, D., Kumar, R., McCarthy, J. T. & Nair, K. S. Reduced synthesis of muscle proteins in chronic renal failure. Am. J. Physiol. Endocrinol. Metab. 278, E219\u2013E225 (2000).","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"498_CR24","doi-asserted-by":"publisher","first-page":"E658","DOI":"10.1152\/ajpendo.00444.2003","volume":"286","author":"DS Raj","year":"2004","unstructured":"Raj, D. S. et al. Coordinated increase in albumin, fibrinogen, and muscle protein synthesis during hemodialysis: role of cytokines. Am. J. Physiol. Endocrinol. Metab. 286, E658\u2013E664 (2004).","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"498_CR25","doi-asserted-by":"publisher","first-page":"1403","DOI":"10.1016\/j.ekir.2018.08.001","volume":"3","author":"S van Vliet","year":"2018","unstructured":"van Vliet, S. et al. Dysregulated handling of dietary protein and muscle protein synthesis after mixed-meal ingestion in maintenance hemodialysis patients. Kidney Int. Rep. 3, 1403\u20131415 (2018).","journal-title":"Kidney Int. Rep."},{"key":"498_CR26","doi-asserted-by":"publisher","first-page":"1027","DOI":"10.1002\/cphy.c140068","volume":"5","author":"NA Dumont","year":"2015","unstructured":"Dumont, N. A., Bentzinger, C. F., Sincennes, M. C. & Rudnicki, M. A. Satellite cells and skeletal muscle regeneration. Comp. Physiol. 5, 1027\u20131059 (2015).","journal-title":"Comp. Physiol."},{"key":"498_CR27","doi-asserted-by":"publisher","first-page":"1099","DOI":"10.1172\/JCI112924","volume":"79","author":"RC May","year":"1987","unstructured":"May, R. C., Kelly, R. A. & Mitch, W. E. Mechanisms for defects in muscle protein metabolism in rats with chronic uremia. Influence of metabolic acidosis. J. Clin. Invest. 79, 1099\u20131103 (1987).","journal-title":"J. Clin. Invest."},{"key":"498_CR28","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1096\/fj.03-0610com","volume":"18","author":"SH Lecker","year":"2004","unstructured":"Lecker, S. H. et al. Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression. FASEB J. 18, 39\u201351 (2004).","journal-title":"FASEB J."},{"key":"498_CR29","doi-asserted-by":"publisher","first-page":"19661","DOI":"10.1074\/jbc.M907258199","volume":"275","author":"J Du","year":"2000","unstructured":"Du, J., Mitch, W. E., Wang, X. & Price, S. R. Glucocorticoids induce proteasome C3 subunit expression in L6 muscle cells by opposing the suppression of its transcription by NF-\u03baB. J. Biol. Chem. 275, 19661\u201319666 (2000).","journal-title":"J. Biol. Chem."},{"key":"498_CR30","doi-asserted-by":"publisher","first-page":"393","DOI":"10.1038\/s41581-019-0148-1","volume":"15","author":"C Meyer-Schwesinger","year":"2019","unstructured":"Meyer-Schwesinger, C. The ubiquitin-proteasome system in kidney physiology and disease. Nat. Rev. Nephrol. 15, 393\u2013411 (2019).","journal-title":"Nat. Rev. Nephrol."},{"key":"498_CR31","doi-asserted-by":"publisher","first-page":"C512","DOI":"10.1152\/ajpcell.00402.2011","volume":"303","author":"S Lokireddy","year":"2012","unstructured":"Lokireddy, S. et al. Identification of atrogin-1-targeted proteins during the myostatin-induced skeletal muscle wasting. Am. J. Physiol. Cell Physiol. 303, C512\u2013C529 (2012).","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"498_CR32","doi-asserted-by":"publisher","first-page":"1083","DOI":"10.1083\/jcb.200901052","volume":"185","author":"S Cohen","year":"2009","unstructured":"Cohen, S. et al. During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation. J. Cell Biol. 185, 1083\u20131095 (2009).","journal-title":"J. Cell Biol."},{"key":"498_CR33","doi-asserted-by":"publisher","first-page":"1058","DOI":"10.1172\/JCI200422220","volume":"114","author":"HH Li","year":"2004","unstructured":"Li, H. H. et al. Atrogin-1\/muscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex. J. Clin. Invest. 114, 1058\u20131071 (2004).","journal-title":"J. Clin. Invest."},{"key":"498_CR34","doi-asserted-by":"crossref","unstructured":"Rom, O., Kaisari, S., Reznick, A. Z. & Aizenbud, D. in Oxidative Stress and Cardiorespiratory Function (ed. Pokorski M.) 1\u20138 (Springer, 2014).","DOI":"10.1007\/5584_2014_9"},{"key":"498_CR35","doi-asserted-by":"publisher","first-page":"575","DOI":"10.1083\/jcb.201110067","volume":"198","author":"S Cohen","year":"2012","unstructured":"Cohen, S., Zhai, B., Gygi, S. P. & Goldberg, A. L. Ubiquitylation by Trim32 causes coupled loss of desmin, Z-bands, and thin filaments in muscle atrophy. J. Cell Biol. 198, 575\u2013589 (2012).","journal-title":"J. Cell Biol."},{"key":"498_CR36","doi-asserted-by":"publisher","first-page":"1453","DOI":"10.1016\/S0006-2952(03)00497-0","volume":"66","author":"C Schwerk","year":"2003","unstructured":"Schwerk, C. & Schulze-Osthoff, K. Non-apoptotic functions of caspases in cellular proliferation and differentiation. Biochem. Pharmacol. 66, 1453\u20131458 (2003).","journal-title":"Biochem. Pharmacol."},{"key":"498_CR37","doi-asserted-by":"publisher","first-page":"1887","DOI":"10.3389\/fphys.2018.01887","volume":"9","author":"LM Schwartz","year":"2018","unstructured":"Schwartz, L. M. Skeletal muscles do not undergo apoptosis during either atrophy or programmed cell death\u2013revisiting the myonuclear domain hypothesis. Front. Physiol. 9, 1887 (2018).","journal-title":"Front. Physiol."},{"key":"498_CR38","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1172\/JCI18330","volume":"113","author":"J Du","year":"2004","unstructured":"Du, J. et al. Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions. J. Clin. Invest. 113, 115\u2013123 (2004).","journal-title":"J. Clin. Invest."},{"key":"498_CR39","doi-asserted-by":"publisher","first-page":"21249","DOI":"10.1074\/jbc.M109.041707","volume":"285","author":"XH Wang","year":"2010","unstructured":"Wang, X. H. et al. Caspase-3 cleaves specific 19 S proteasome subunits in skeletal muscle stimulating proteasome activity. J. Biol. Chem. 285, 21249\u201321257 (2010).","journal-title":"J. Biol. Chem."},{"key":"498_CR40","doi-asserted-by":"publisher","first-page":"3233","DOI":"10.1681\/ASN.2006020131","volume":"17","author":"BT Workeneh","year":"2006","unstructured":"Workeneh, B. T. et al. Development of a diagnostic method for detecting increased muscle protein degradation in patients with catabolic conditions. J. Am. Soc. Nephrol. 17, 3233\u20133239 (2006).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR41","doi-asserted-by":"publisher","first-page":"1174","DOI":"10.1681\/ASN.2009101011","volume":"21","author":"J Hu","year":"2010","unstructured":"Hu, J. et al. XIAP reduces muscle proteolysis induced by CKD. J. Am. Soc. Nephrol. 21, 1174\u20131183 (2010).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR42","doi-asserted-by":"publisher","first-page":"F1128","DOI":"10.1152\/ajprenal.00600.2016","volume":"312","author":"Z Su","year":"2017","unstructured":"Su, Z. et al. Chronic kidney disease induces autophagy leading to dysfunction of mitochondria in skeletal muscle. Am. J. Physiol. Ren. Physiol. 312, F1128\u2013F1140 (2017).","journal-title":"Am. J. Physiol. Ren. Physiol."},{"key":"498_CR43","doi-asserted-by":"publisher","first-page":"375","DOI":"10.1146\/annurev-pharmtox-010716-104936","volume":"57","author":"E Morel","year":"2017","unstructured":"Morel, E. et al. Autophagy: a druggable process. Ann. Rev. Pharmacol. Toxicol. 57, 375\u2013398 (2017).","journal-title":"Ann. Rev. Pharmacol. Toxicol."},{"key":"498_CR44","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1016\/j.cell.2018.09.048","volume":"176","author":"B Levine","year":"2019","unstructured":"Levine, B. & Kroemer, G. Biological functions of autophagy genes: a disease perspective. Cell 176, 11\u201342 (2019).","journal-title":"Cell"},{"key":"498_CR45","doi-asserted-by":"publisher","first-page":"1470","DOI":"10.1161\/CIRCRESAHA.110.227371","volume":"107","author":"N Hariharan","year":"2010","unstructured":"Hariharan, N. et al. Deacetylation of FoxO by Sirt1 plays an essential role in mediating starvation-induced autophagy in cardiac myocytes. Circ. Res. 107, 1470\u20131482 (2010).","journal-title":"Circ. Res."},{"key":"498_CR46","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-018-30977-7","volume":"8","author":"M Jang","year":"2018","unstructured":"Jang, M. et al. AMPK contributes to autophagosome maturation and lysosomal fusion. Sci. Rep. 8, 12637 (2018).","journal-title":"Sci. Rep."},{"key":"498_CR47","doi-asserted-by":"publisher","first-page":"e00303","DOI":"10.1128\/MCB.00303-18","volume":"38","author":"AF Corona Velazquez","year":"2018","unstructured":"Corona Velazquez, A. F. & Jackson, W. T. So many roads: the multifaceted regulation of autophagy induction. Mol. Cell Biol. 38, e00303\u2013e00318 (2018).","journal-title":"Mol. Cell Biol."},{"key":"498_CR48","doi-asserted-by":"publisher","first-page":"950","DOI":"10.1038\/s41430-018-0381-x","volume":"73","author":"YY Zhang","year":"2019","unstructured":"Zhang, Y. Y. et al. CKD autophagy activation and skeletal muscle atrophy\u2013a preliminary study of mitophagy and inflammation. Eur. J. Clin. Nutr. 73, 950\u2013960 (2019).","journal-title":"Eur. J. Clin. Nutr."},{"key":"498_CR49","doi-asserted-by":"publisher","first-page":"611","DOI":"10.1007\/s00467-012-2380-9","volume":"28","author":"SS Gunta","year":"2013","unstructured":"Gunta, S. S. & Mak, R. H. Ghrelin and leptin pathophysiology in chronic kidney disease. Pediatr. Nephrol. 28, 611\u2013616 (2013).","journal-title":"Pediatr. Nephrol."},{"key":"498_CR50","doi-asserted-by":"publisher","first-page":"1388","DOI":"10.1681\/ASN.2004100842","volume":"17","author":"JL Bailey","year":"2006","unstructured":"Bailey, J. L., Zheng, B., Hu, Z., Price, S. R. & Mitch, W. E. Chronic kidney disease causes defects in signaling through the insulin receptor substrate\/phosphatidylinositol 3-kinase\/Akt pathway: implications for muscle atrophy. J. Am. Soc. Nephrol. 17, 1388\u20131394 (2006).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR51","doi-asserted-by":"publisher","first-page":"960","DOI":"10.1016\/j.cell.2017.02.004","volume":"168","author":"RA Saxton","year":"2017","unstructured":"Saxton, R. A. & Sabatini, D. M. mTOR signaling in growth, metabolism, and disease. Cell 168, 960\u2013976 (2017).","journal-title":"Cell"},{"key":"498_CR52","doi-asserted-by":"publisher","first-page":"569","DOI":"10.1016\/j.cell.2005.10.024","volume":"123","author":"MK Holz","year":"2005","unstructured":"Holz, M. K., Ballif, B. A., Gygi, S. P. & Blenis, J. mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events. Cell 123, 569\u2013580 (2005).","journal-title":"Cell"},{"key":"498_CR53","doi-asserted-by":"publisher","first-page":"C1061","DOI":"10.1152\/ajpcell.00209.2019","volume":"317","author":"N Hodson","year":"2019","unstructured":"Hodson, N., West, D. W. D., Philp, A., Burd, N. A. & Moore, D. R. Molecular regulation of human skeletal muscle protein synthesis in response to exercise and nutrients: a compass for overcoming age-related anabolic resistance. Am. Physiol. Cell Physiol. 317, C1061\u2013C1078 (2019).","journal-title":"Am. Physiol. Cell Physiol."},{"key":"498_CR54","doi-asserted-by":"publisher","first-page":"1704","DOI":"10.1126\/science.1065874","volume":"294","author":"SC Bodine","year":"2001","unstructured":"Bodine, S. C. et al. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 294, 1704\u20131708 (2001).","journal-title":"Science"},{"key":"498_CR55","doi-asserted-by":"publisher","first-page":"14440","DOI":"10.1073\/pnas.251541198","volume":"98","author":"MD Gomes","year":"2001","unstructured":"Gomes, M. D., Lecker, S. H., Jagoe, R. T., Navon, A. & Goldberg, A. L. Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc. Natl Acad. Sci. USA 98, 14440\u201314445 (2001).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"498_CR56","doi-asserted-by":"publisher","first-page":"556","DOI":"10.2337\/db18-0416","volume":"68","author":"BT O\u2019Neill","year":"2019","unstructured":"O\u2019Neill, B. T. et al. FoxO transcription factors are critical regulators of diabetes-related muscle atrophy. Diabetes 68, 556\u2013570 (2019).","journal-title":"Diabetes"},{"key":"498_CR57","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1152\/japplphysiol.00963.2018","volume":"127","author":"F von Walden","year":"2019","unstructured":"von Walden, F. Ribosome biogenesis in skeletal muscle: coordination of transcription and translation. J. Appl. Physiol. 127, 591\u2013598 (2019).","journal-title":"J. Appl. Physiol."},{"key":"498_CR58","doi-asserted-by":"publisher","first-page":"1305","DOI":"10.1007\/s00018-020-03662-0","volume":"78","author":"V Romanello","year":"2021","unstructured":"Romanello, V. & Sandri, M. The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass. Cell. Mol. Life Sci. 78, 1305\u20131328 (2021).","journal-title":"Cell. Mol. Life Sci."},{"key":"498_CR59","doi-asserted-by":"publisher","first-page":"1772","DOI":"10.1152\/japplphysiol.90636.2008","volume":"105","author":"Y Gao","year":"2008","unstructured":"Gao, Y., Ordas, R., Klein, J. D. & Price, S. R. Regulation of caspase-3 activity by insulin in skeletal muscle cells involves both PI3-kinase and MEK-1\/2. J. Appl. Physiol. 105, 1772\u20131778 (2008).","journal-title":"J. Appl. Physiol."},{"key":"498_CR60","doi-asserted-by":"publisher","first-page":"77","DOI":"10.1053\/j.jrn.2013.01.001","volume":"23","author":"JJ Carrero","year":"2013","unstructured":"Carrero, J. J. et al. Etiology of the protein-energy wasting syndrome in chronic kidney disease: a consensus statement from the International Society of Renal Nutrition and Metabolism (ISRNM). J. Ren. Nutr. 23, 77\u201390 (2013).","journal-title":"J. Ren. Nutr."},{"key":"498_CR61","doi-asserted-by":"publisher","first-page":"2075","DOI":"10.1681\/ASN.2008111205","volume":"20","author":"I de Brito-Ashurst","year":"2009","unstructured":"de Brito-Ashurst, I., Varagunam, M., Raftery, M. J. & Yaqoob, M. M. Bicarbonate supplementation slows progression of CKD and improves nutritional status. J. Am. Soc. Nephrol. 20, 2075\u20132084 (2009).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR62","first-page":"3059","volume":"119","author":"Z Hu","year":"2009","unstructured":"Hu, Z., Wang, H., Lee, I. H., Du, J. & Mitch, W. E. Endogenous glucocorticoids and impaired insulin signaling are both required to stimulate muscle wasting under pathophysiological conditions in mice. J. Clin. Invest. 119, 3059\u20133069 (2009).","journal-title":"J. Clin. Invest."},{"key":"498_CR63","doi-asserted-by":"publisher","first-page":"632","DOI":"10.1681\/ASN.V84632","volume":"8","author":"KA Graham","year":"1997","unstructured":"Graham, K. A., Reaich, D., Channon, S. M., Downie, S. & Goodship, T. H. Correction of acidosis in hemodialysis decreases whole-body protein degradation. J. Am. Soc. Nephrol. 8, 632\u2013637 (1997).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR64","first-page":"E230","volume":"265","author":"D Reaich","year":"1993","unstructured":"Reaich, D. et al. Correction of acidosis in humans with CRF decreases protein degradation and amino acid oxidation. Am. J. Physiol. 265, E230\u2013E235 (1993).","journal-title":"Am. J. Physiol."},{"key":"498_CR65","doi-asserted-by":"publisher","first-page":"289","DOI":"10.1053\/j.ackd.2017.06.005","volume":"24","author":"JA Kraut","year":"2017","unstructured":"Kraut, J. A. & Madias, N. E. Adverse deffects of the metabolic acidosis of chronic kidney disease. Adv. Chronic Kidney Dis. 24, 289\u2013297 (2017).","journal-title":"Adv. Chronic Kidney Dis."},{"key":"498_CR66","doi-asserted-by":"publisher","first-page":"F700","DOI":"10.1152\/ajprenal.00440.2003","volume":"287","author":"HA Franch","year":"2004","unstructured":"Franch, H. A. et al. Acidosis impairs insulin receptor substrate-1-associated phosphoinositide 3-kinase signaling in muscle cells: consequences on proteolysis. Am. J. Physiol. Ren. Physiol. 287, F700\u2013F706 (2004).","journal-title":"Am. J. Physiol. Ren. Physiol."},{"key":"498_CR67","doi-asserted-by":"publisher","first-page":"2127","DOI":"10.1172\/JCI117208","volume":"93","author":"WE Mitch","year":"1994","unstructured":"Mitch, W. E. et al. Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasomes. J. Clin. Invest. 93, 2127\u20132133 (1994).","journal-title":"J. Clin. Invest."},{"key":"498_CR68","doi-asserted-by":"publisher","first-page":"1967","DOI":"10.1073\/pnas.93.5.1967","volume":"93","author":"U Isozaki","year":"1996","unstructured":"Isozaki, U., Mitch, W. E., England, B. K. & Price, S. R. Protein degradation and increased mRNAs encoding proteins of the ubiquitin-proteasome proteolytic pathway in BC3H1 myocytes require an interaction between glucocorticoids and acidification. Proc. Natl Acad. Sci. USA 93, 1967\u20131971 (1996).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"498_CR69","doi-asserted-by":"publisher","first-page":"614","DOI":"10.1172\/JCI112344","volume":"77","author":"RC May","year":"1986","unstructured":"May, R. C., Kelly, R. A. & Mitch, W. E. Metabolic acidosis stimulates protein degradation in rat muscle by a glucocorticoid-dependent mechanism. J. Clin. Invest. 77, 614\u2013621 (1986).","journal-title":"J. Clin. Invest."},{"key":"498_CR70","doi-asserted-by":"publisher","first-page":"C955","DOI":"10.1152\/ajpcell.1994.267.4.C955","volume":"267","author":"SR Price","year":"1994","unstructured":"Price, S. R., England, B. K., Bailey, J. L., Van Vreede, K. & Mitch, W. E. Acidosis and glucocorticoids concomitantly increase ubiquitin and proteasome subunit mRNAs in rat muscle. Am. J. Physiol. Cell Physiol. 267, C955\u2013C960 (1994).","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"498_CR71","doi-asserted-by":"publisher","first-page":"1432","DOI":"10.1038\/ki.1994.187","volume":"45","author":"G Garibotto","year":"1994","unstructured":"Garibotto, G. et al. Skeletal muscle protein synthesis and degradation in patients with chronic renal failure. Kidney Int. 45, 1432\u20131439 (1994).","journal-title":"Kidney Int."},{"key":"498_CR72","doi-asserted-by":"publisher","first-page":"E668","DOI":"10.1152\/ajpendo.1993.264.4.E668","volume":"264","author":"SS Wing","year":"1993","unstructured":"Wing, S. S. & Goldberg, A. L. Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting. Am. J. Physiol. Endocrinol. Metab. 264, E668\u2013E676 (1993).","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"498_CR73","doi-asserted-by":"publisher","first-page":"2180373","DOI":"10.1155\/2018\/2180373","volume":"2018","author":"S Mihai","year":"2018","unstructured":"Mihai, S. et al. Inflammation-related mechanisms in chronic kidney disease prediction, progression, and outcome. J. Immunol. Res. 2018, 2180373 (2018).","journal-title":"J. Immunol. Res."},{"key":"498_CR74","doi-asserted-by":"publisher","first-page":"R1173","DOI":"10.1152\/ajpregu.00735.2009","volume":"298","author":"JG Tidball","year":"2010","unstructured":"Tidball, J. G. & Villalta, S. A. Regulatory interactions between muscle and the immune system during muscle regeneration. Am. J. Physiol. Regul. Integr. Comp. Physiol. 298, R1173\u2013R1187 (2010).","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"498_CR75","doi-asserted-by":"publisher","first-page":"989","DOI":"10.1177\/002215540104900807","volume":"49","author":"RA Collins","year":"2001","unstructured":"Collins, R. A. & Grounds, M. D. The role of tumor necrosis factor-alpha (TNF-\u03b1) in skeletal muscle regeneration. Studies in TNF-\u03b1(-\/-) and TNF-\u03b1(-\/-)\/LT-\u03b1(-\/-) mice. J. Histochem. Cytochem. 49, 989\u20131001 (2001).","journal-title":"J. Histochem. Cytochem."},{"key":"498_CR76","doi-asserted-by":"publisher","first-page":"626","DOI":"10.1681\/ASN.2014020144","volume":"26","author":"L Hu","year":"2015","unstructured":"Hu, L. et al. Low-frequency electrical stimulation attenuates muscle atrophy in CKD\u2013a potential treatment strategy. J. Am. Soc. Nephrol. 26, 626\u2013635 (2015).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR77","doi-asserted-by":"publisher","first-page":"1489","DOI":"10.1074\/jbc.M112.419788","volume":"288","author":"C Zhang","year":"2013","unstructured":"Zhang, C. et al. Interleukin-6\/signal transducer and activator of transcription 3 (STAT3) pathway is essential for macrophage infiltration and myoblast proliferation during muscle regeneration. J. Biol. Chem. 288, 1489\u20131499 (2013).","journal-title":"J. Biol. Chem."},{"key":"498_CR78","doi-asserted-by":"publisher","first-page":"1054","DOI":"10.1038\/ki.2008.21","volume":"73","author":"DS Raj","year":"2008","unstructured":"Raj, D. S. et al. Interleukin-6 modulates hepatic and muscle protein synthesis during hemodialysis. Kidney Int. 73, 1054\u20131061 (2008).","journal-title":"Kidney Int."},{"key":"498_CR79","doi-asserted-by":"crossref","unstructured":"Thoma, A. & Lightfoot, A. P. in Muscle Atrophy (ed. Xiao J.) 267\u2013279 (Springer, 2018).","DOI":"10.1007\/978-981-13-1435-3_12"},{"key":"498_CR80","doi-asserted-by":"publisher","first-page":"604","DOI":"10.1681\/ASN.2008060628","volume":"20","author":"L Zhang","year":"2009","unstructured":"Zhang, L. et al. IL-6 and serum amyloid A synergy mediates angiotensin II-induced muscle wasting. J. Am. Soc. Nephrol. 20, 604\u2013612 (2009).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR81","doi-asserted-by":"publisher","first-page":"168","DOI":"10.1097\/JES.0b013e3181f44f11","volume":"38","author":"JA Carson","year":"2010","unstructured":"Carson, J. A. & Baltgalvis, K. A. Interleukin 6 as a key regulator of muscle mass during cachexia. Exerc. Sport. Sci. Rev. 38, 168\u2013176 (2010).","journal-title":"Exerc. Sport. Sci. Rev."},{"key":"498_CR82","doi-asserted-by":"publisher","first-page":"2409","DOI":"10.1172\/JCI117936","volume":"95","author":"GS Hotamisligil","year":"1995","unstructured":"Hotamisligil, G. S., Arner, P., Caro, J. F., Atkinson, R. L. & Spiegelman, B. M. Increased adipose tissue expression of tumor necrosis factor-alpha in human obesity and insulin resistance. J. Clin. Invest. 95, 2409\u20132415 (1995).","journal-title":"J. Clin. Invest."},{"key":"498_CR83","doi-asserted-by":"publisher","first-page":"1096","DOI":"10.1038\/ki.2013.147","volume":"84","author":"TA Ikizler","year":"2013","unstructured":"Ikizler, T. A. et al. Prevention and treatment of protein energy wasting in chronic kidney disease patients: a consensus statement by the International Society of Renal Nutrition and Metabolism. Kidney Int. 84, 1096\u20131107 (2013).","journal-title":"Kidney Int."},{"key":"498_CR84","doi-asserted-by":"publisher","first-page":"1125","DOI":"10.1161\/CIRCRESAHA.116.308391","volume":"118","author":"RG Walker","year":"2016","unstructured":"Walker, R. G. et al. Biochemistry and biology of GDF11 and myostatin: similarities, differences, and questions for future investigation. Circ. Res. 118, 1125\u20131141 (2016).","journal-title":"Circ. Res."},{"key":"498_CR85","doi-asserted-by":"publisher","first-page":"506","DOI":"10.1016\/j.kint.2018.10.010","volume":"95","author":"D Verzola","year":"2019","unstructured":"Verzola, D., Barisione, C., Picciotto, D., Garibotto, G. & Koppe, L. Emerging role of myostatin and its inhibition in the setting of chronic kidney disease. Kidney Int. 95, 506\u2013517 (2019).","journal-title":"Kidney Int."},{"key":"498_CR86","doi-asserted-by":"publisher","first-page":"9306","DOI":"10.1073\/pnas.151270098","volume":"98","author":"SJ Lee","year":"2001","unstructured":"Lee, S. J. & McPherron, A. C. Regulation of myostatin activity and muscle growth. Proc. Natl Acad. Sci. USA 98, 9306\u20139311 (2001).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"498_CR87","doi-asserted-by":"publisher","first-page":"826","DOI":"10.1038\/bonekey.2016.48","volume":"5","author":"H Kaji","year":"2016","unstructured":"Kaji, H. Effects of myokines on bone. Bonekey Rep. 5, 826 (2016).","journal-title":"Bonekey Rep."},{"key":"498_CR88","doi-asserted-by":"publisher","first-page":"H1973","DOI":"10.1152\/ajpheart.00200.2011","volume":"300","author":"A Breitbart","year":"2011","unstructured":"Breitbart, A., Auger-Messier, M., Molkentin, J. D. & Heineke, J. Myostatin from the heart: local and systemic actions in cardiac failure and muscle wasting. Am. J. Physiol. Heart Circ. Physiol. 300, H1973\u2013H1982 (2011).","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"498_CR89","doi-asserted-by":"publisher","first-page":"1946","DOI":"10.1210\/me.2013-1194","volume":"27","author":"CA Goodman","year":"2013","unstructured":"Goodman, C. A., McNally, R. M., Hoffmann, F. M. & Hornberger, T. A. Smad3 induces atrogin-1, inhibits mTOR and protein synthesis, and promotes muscle atrophy in vivo. Mol. Endocrinol. 27, 1946\u20131957 (2013).","journal-title":"Mol. Endocrinol."},{"key":"498_CR90","doi-asserted-by":"publisher","first-page":"1653","DOI":"10.1096\/fj.10-176917","volume":"25","author":"L Zhang","year":"2011","unstructured":"Zhang, L. et al. Pharmacological inhibition of myostatin suppresses systemic inflammation and muscle atrophy in mice with chronic kidney disease. FASEB J. 25, 1653\u20131663 (2011).","journal-title":"FASEB J."},{"key":"498_CR91","doi-asserted-by":"publisher","first-page":"773","DOI":"10.1038\/ki.2010.494","volume":"79","author":"D Verzola","year":"2011","unstructured":"Verzola, D. et al. Apoptosis and myostatin mRNA are upregulated in the skeletal muscle of patients with chronic kidney disease. Kidney Int. 79, 773\u2013782 (2011).","journal-title":"Kidney Int."},{"key":"498_CR92","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0141035","volume":"10","author":"S Yano","year":"2015","unstructured":"Yano, S. et al. Relationship between blood myostatin levels and kidney function: Shimane CoHRE Study. PLoS ONE 10, e0141035 (2015).","journal-title":"PLoS ONE"},{"key":"498_CR93","doi-asserted-by":"publisher","first-page":"208","DOI":"10.1053\/j.jrn.2006.04.014","volume":"16","author":"WE Mitch","year":"2006","unstructured":"Mitch, W. E. Proteolytic mechanisms, not malnutrition, cause loss of muscle mass in kidney failure. J. Ren. Nutr. 16, 208\u2013211 (2006).","journal-title":"J. Ren. Nutr."},{"key":"498_CR94","doi-asserted-by":"publisher","first-page":"1476","DOI":"10.1172\/JCI25255","volume":"115","author":"WE Mitch","year":"2005","unstructured":"Mitch, W. E. Cachexia in chronic kidney disease: a link to defective central nervous system control of appetite. J. Clin. Invest. 115, 1476\u20131478 (2005).","journal-title":"J. Clin. Invest."},{"key":"498_CR95","doi-asserted-by":"publisher","first-page":"605","DOI":"10.1038\/88423","volume":"4","author":"AA Butler","year":"2001","unstructured":"Butler, A. A. et al. Melanocortin-4 receptor is required for acute homeostatic responses to increased dietary fat. Nat. Neurosci. 4, 605\u2013611 (2001).","journal-title":"Nat. Neurosci."},{"key":"498_CR96","doi-asserted-by":"publisher","first-page":"1423","DOI":"10.1681\/ASN.V891423","volume":"8","author":"O Heimburger","year":"1997","unstructured":"Heimburger, O., Lonnqvist, F., Danielsson, A., Nordenstrom, J. & Stenvinkel, P. Serum immunoreactive leptin concentration and its relation to the body fat content in chronic renal failure. J. Am. Soc. Nephrol. 8, 1423\u20131430 (1997).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR97","doi-asserted-by":"publisher","first-page":"1303","DOI":"10.1681\/ASN.V1171303","volume":"11","author":"P Stenvinkel","year":"2000","unstructured":"Stenvinkel, P., Lindholm, B., Lonnqvist, F., Katzarski, K. & Heimburger, O. Increases in serum leptin levels during peritoneal dialysis are associated with inflammation and a decrease in lean body mass. J. Am. Soc. Nephrol. 11, 1303\u20131309 (2000).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR98","first-page":"296","volume":"51","author":"M Nishikawa","year":"1999","unstructured":"Nishikawa, M. et al. Measurement of serum leptin in patients with chronic renal failure on hemodialysis. Clin. Nephrol. 51, 296\u2013303 (1999).","journal-title":"Clin. Nephrol."},{"key":"498_CR99","doi-asserted-by":"publisher","first-page":"643","DOI":"10.1093\/ndt\/gfn529","volume":"24","author":"AK Arbeiter","year":"2009","unstructured":"Arbeiter, A. K. et al. Ghrelin and other appetite-regulating hormones in paediatric patients with chronic renal failure during dialysis and following kidney transplantation. Nephrol. Dial. Transplant. 24, 643\u2013646 (2009).","journal-title":"Nephrol. Dial. Transplant."},{"key":"498_CR100","doi-asserted-by":"publisher","first-page":"2113","DOI":"10.1007\/s00467-018-4002-7","volume":"33","author":"N Canpolat","year":"2018","unstructured":"Canpolat, N. et al. Leptin and ghrelin in chronic kidney disease: their associations with protein-energy wasting. Pediatr. Nephrol. 33, 2113\u20132122 (2018).","journal-title":"Pediatr. Nephrol."},{"key":"498_CR101","doi-asserted-by":"publisher","first-page":"661","DOI":"10.1007\/s00467-017-3840-z","volume":"33","author":"A Monzani","year":"2018","unstructured":"Monzani, A. et al. Unacylated ghrelin and obestatin: promising biomarkers of protein energy wasting in children with chronic kidney disease. Pediatr. Nephrol. 33, 661\u2013672 (2018).","journal-title":"Pediatr. Nephrol."},{"key":"498_CR102","doi-asserted-by":"publisher","first-page":"2295","DOI":"10.1007\/s00467-010-1588-9","volume":"25","author":"AK Buscher","year":"2010","unstructured":"Buscher, A. K., Buscher, R., Hauffa, B. P. & Hoyer, P. F. Alterations in appetite-regulating hormones influence protein-energy wasting in pediatric patients with chronic kidney disease. Pediatr. Nephrol. 25, 2295\u20132301 (2010).","journal-title":"Pediatr. Nephrol."},{"key":"498_CR103","doi-asserted-by":"publisher","first-page":"258","DOI":"10.1053\/j.jrn.2011.07.005","volume":"22","author":"Y Caliskan","year":"2012","unstructured":"Caliskan, Y. et al. Comparison of markers of appetite and inflammation between hemodialysis patients with and without failed renal transplants. J. Ren. Nutr. 22, 258\u2013267 (2012).","journal-title":"J. Ren. Nutr."},{"key":"498_CR104","doi-asserted-by":"publisher","first-page":"F1315","DOI":"10.1152\/ajprenal.00341.2012","volume":"303","author":"WW Cheung","year":"2012","unstructured":"Cheung, W. W. & Mak, R. H. Melanocortin antagonism ameliorates muscle wasting and inflammation in chronic kidney disease. Am. J. Physiol. Ren. Physiol. 303, F1315\u2013F1324 (2012).","journal-title":"Am. J. Physiol. Ren. Physiol."},{"key":"498_CR105","doi-asserted-by":"publisher","first-page":"8928","DOI":"10.3390\/ijms21238928","volume":"21","author":"FM Chaves","year":"2020","unstructured":"Chaves, F. M., Mansano, N. S., Frazao, R. & Donato, J. Jr Tumor necrosis factor \u03b1 and interleukin-1\u03b2 acutely inhibit AgRP neurons in the arcuate nucleus of the hypothalamus. Int. J. Mol. Sci. 21, 8928 (2020).","journal-title":"Int. J. Mol. Sci."},{"key":"498_CR106","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1007\/s13539-011-0019-5","volume":"2","author":"RH Mak","year":"2011","unstructured":"Mak, R. H. et al. Wasting in chronic kidney disease. J. Cachexia Sarcopenia Muscle 2, 9\u201325 (2011).","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"498_CR107","doi-asserted-by":"publisher","first-page":"2147","DOI":"10.1016\/j.biocel.2013.05.039","volume":"45","author":"BS Gordon","year":"2013","unstructured":"Gordon, B. S., Kelleher, A. R. & Kimball, S. R. Regulation of muscle protein synthesis and the effects of catabolic states. Int. J. Biochem. Cell Biol. 45, 2147\u20132157 (2013).","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"498_CR108","doi-asserted-by":"publisher","first-page":"2573","DOI":"10.1681\/ASN.2019121277","volume":"31","author":"L Zhang","year":"2020","unstructured":"Zhang, L. et al. Mechanisms regulating muscle protein synthesis in chronic kidney disease. J. Am. Soc. Nephrol. 31, 2573\u20132587 (2020).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR109","doi-asserted-by":"publisher","first-page":"2068","DOI":"10.1681\/ASN.2010121278","volume":"22","author":"XH Wang","year":"2011","unstructured":"Wang, X. H. et al. Decreased miR-29 suppresses myogenesis in CKD. J. Am. Soc. Nephrol. 22, 2068\u20132076 (2011).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR110","doi-asserted-by":"publisher","first-page":"C551","DOI":"10.1152\/ajpcell.00266.2013","volume":"306","author":"MB Hudson","year":"2014","unstructured":"Hudson, M. B. et al. miR-23a is decreased during muscle atrophy by a mechanism that includes calcineurin signaling and exosome-mediated export. Am. J. Physiol. Cell Physiol. 306, C551\u2013C558 (2014).","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"498_CR111","doi-asserted-by":"publisher","first-page":"401","DOI":"10.1038\/ki.2012.84","volume":"82","author":"J Xu","year":"2012","unstructured":"Xu, J. et al. Transcription factor FoxO1, the dominant mediator of muscle wasting in chronic kidney disease, is inhibited by microRNA-486. Kidney Int. 82, 401\u2013411 (2012).","journal-title":"Kidney Int."},{"key":"498_CR112","doi-asserted-by":"publisher","first-page":"2631","DOI":"10.1681\/ASN.2016111213","volume":"28","author":"B Wang","year":"2017","unstructured":"Wang, B. et al. MicroRNA-23a and microRNA-27a mimic exercise by ameliorating CKD-induced muscle atrophy. J. Am. Soc. Nephrol. 28, 2631\u20132640 (2017).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR113","doi-asserted-by":"publisher","first-page":"C314","DOI":"10.1152\/ajpcell.00395.2013","volume":"307","author":"MB Hudson","year":"2014","unstructured":"Hudson, M. B. et al. miR-182 attenuates atrophy-related gene expression by targeting FoxO3 in skeletal muscle. Am. J. Physiol. Cell Physiol. 307, C314\u2013C319 (2014).","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"498_CR114","doi-asserted-by":"publisher","DOI":"10.14814\/phy2.12780","volume":"4","author":"JL Gamboa","year":"2016","unstructured":"Gamboa, J. L. et al. Mitochondrial dysfunction and oxidative stress in patients with chronic kidney disease. Physiol. Rep. 4, e12780 (2016).","journal-title":"Physiol. Rep."},{"key":"498_CR115","doi-asserted-by":"publisher","first-page":"658","DOI":"10.1053\/j.ajkd.2016.05.011","volume":"68","author":"B Roshanravan","year":"2016","unstructured":"Roshanravan, B. et al. CKD and muscle mitochondrial energetics. Am. J. Kidney Dis. 68, 658\u2013659 (2016).","journal-title":"Am. J. Kidney Dis."},{"key":"498_CR116","first-page":"532","volume":"6","author":"PG Yazdi","year":"2013","unstructured":"Yazdi, P. G., Moradi, H., Yang, J. Y., Wang, P. H. & Vaziri, N. D. Skeletal muscle mitochondrial depletion and dysfunction in chronic kidney disease. Int. J. Clin. Exp. Med. 6, 532\u2013539 (2013).","journal-title":"Int. J. Clin. Exp. Med."},{"key":"498_CR117","doi-asserted-by":"publisher","first-page":"419","DOI":"10.1681\/ASN.2009060571","volume":"21","author":"L Zhang","year":"2010","unstructured":"Zhang, L., Wang, X. H., Wang, H., Du, J. & Mitch, W. E. Satellite cell dysfunction and impaired IGF-1 signaling cause CKD-induced muscle atrophy. J. Am. Soc. Nephrol. 21, 419\u2013427 (2010).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR118","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1002\/jcp.22218","volume":"225","author":"L Heron-Milhavet","year":"2010","unstructured":"Heron-Milhavet, L., Mamaeva, D., LeRoith, D., Lamb, N. J. & Fernandez, A. Impaired muscle regeneration and myoblast differentiation in mice with a muscle-specific KO of IGF-IR. J. Cell. Physiol. 225, 1\u20136 (2010).","journal-title":"J. Cell. Physiol."},{"key":"498_CR119","doi-asserted-by":"publisher","first-page":"317","DOI":"10.1016\/j.yexcr.2007.09.012","volume":"314","author":"C McFarlane","year":"2008","unstructured":"McFarlane, C. et al. Myostatin signals through Pax7 to regulate satellite cell self-renewal. Exp. Cell Res. 314, 317\u2013329 (2008).","journal-title":"Exp. Cell Res."},{"key":"498_CR120","doi-asserted-by":"publisher","first-page":"1888","DOI":"10.1016\/S0140-6736(17)30788-2","volume":"390","author":"A Levin","year":"2017","unstructured":"Levin, A. et al. Global kidney health 2017 and beyond: a roadmap for closing gaps in care, research, and policy. Lancet 390, 1888\u20131917 (2017).","journal-title":"Lancet"},{"key":"498_CR121","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1038\/sj.ki.5001955","volume":"71","author":"V Bellizzi","year":"2007","unstructured":"Bellizzi, V. et al. Very low protein diet supplemented with ketoanalogs improves blood pressure control in chronic kidney disease. Kidney Int. 71, 245\u2013251 (2007).","journal-title":"Kidney Int."},{"key":"498_CR122","doi-asserted-by":"publisher","first-page":"718","DOI":"10.3390\/jcm8050718","volume":"8","author":"L Di Micco","year":"2019","unstructured":"Di Micco, L., Di Lullo, L., Bellasi, A. & Di Iorio, B. R. Very low protein diet for patients with chronic kidney disease: recent insights. J. Clin. Med. 8, 718 (2019).","journal-title":"J. Clin. Med."},{"key":"498_CR123","doi-asserted-by":"publisher","first-page":"1765","DOI":"10.1056\/NEJMra1700312","volume":"377","author":"K Kalantar-Zadeh","year":"2017","unstructured":"Kalantar-Zadeh, K. & Fouque, D. Nutritional management of chronic kidney disease. N. Engl. J. Med. 377, 1765\u20131776 (2017).","journal-title":"N. Engl. J. Med."},{"key":"498_CR124","doi-asserted-by":"publisher","first-page":"1351","DOI":"10.1007\/s10157-018-1591-1","volume":"22","author":"L Milovanova","year":"2018","unstructured":"Milovanova, L. et al. Effect of essential amino acid small ketoanalogues and protein restriction diet on morphogenetic proteins (FGF-23 and Klotho) in 3b-4 stages chronic small kidney disease patients: a randomized pilot study. Clin. Exp. Nephrol. 22, 1351\u20131359 (2018).","journal-title":"Clin. Exp. Nephrol."},{"key":"498_CR125","doi-asserted-by":"publisher","first-page":"2164","DOI":"10.1681\/ASN.2015040369","volume":"27","author":"L Garneata","year":"2016","unstructured":"Garneata, L., Stancu, A., Dragomir, D., Stefan, G. & Mircescu, G. Ketoanalogue-supplemented vegetarian very low-protein diet and CKD progression. J. Am. Soc. Nephrol. 27, 2164\u20132176 (2016).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR126","doi-asserted-by":"publisher","first-page":"243","DOI":"10.1159\/000485729","volume":"196","author":"H Hara","year":"2018","unstructured":"Hara, H. et al. Protein energy wasting and sarcopenia in dialysis patients. Cont. Nephrol. 196, 243\u2013249 (2018).","journal-title":"Cont. Nephrol."},{"key":"498_CR127","doi-asserted-by":"publisher","first-page":"1396","DOI":"10.1038\/ki.1996.196","volume":"49","author":"KA Graham","year":"1996","unstructured":"Graham, K. A. et al. Correction of acidosis in CAPD decreases whole body protein degradation. Kidney Int. 49, 1396\u20131400 (1996).","journal-title":"Kidney Int."},{"key":"498_CR128","doi-asserted-by":"publisher","first-page":"603","DOI":"10.1046\/j.1523-1755.1998.00023.x","volume":"54","author":"RH Mak","year":"1998","unstructured":"Mak, R. H. Effect of metabolic acidosis on insulin action and secretion in uremia. Kidney Int. 54, 603\u2013607 (1998).","journal-title":"Kidney Int."},{"key":"498_CR129","doi-asserted-by":"publisher","first-page":"E121","DOI":"10.1152\/ajpendo.1995.268.1.E121","volume":"268","author":"D Reaich","year":"1995","unstructured":"Reaich, D. et al. Insulin-mediated changes in PD and glucose uptake after correction of acidosis in humans with CRF. Am. J. Physiol. Endocrinol. Metab. 268, E121\u2013E126 (1995).","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"498_CR130","doi-asserted-by":"publisher","first-page":"515","DOI":"10.1681\/ASN.2014020205","volume":"26","author":"M Dobre","year":"2015","unstructured":"Dobre, M., Rahman, M. & Hostetter, T. H. Current status of bicarbonate in CKD. J. Am. Soc. Nephrol. 26, 515\u2013523 (2015).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR131","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/kisup.2012.1","volume":"2","author":"Kidney Disease: Improving Global Outcomes (KDIGO) CKD Work Group.","year":"2012","unstructured":"Kidney Disease: Improving Global Outcomes (KDIGO) CKD Work Group. KDIGO clinical practice guideline for the evaluation and management of chronic kidney disease. Kidney Int. Suppl. 2, 1\u2013138 (2012).","journal-title":"Kidney Int. Suppl."},{"key":"498_CR132","doi-asserted-by":"publisher","first-page":"529","DOI":"10.1038\/ki.2013.401","volume":"85","author":"I Loniewski","year":"2014","unstructured":"Loniewski, I. & Wesson, D. E. Bicarbonate therapy for prevention of chronic kidney disease progression. Kidney Int. 85, 529\u2013535 (2014).","journal-title":"Kidney Int."},{"key":"498_CR133","doi-asserted-by":"publisher","first-page":"28","DOI":"10.1249\/JES.0000000000000209","volume":"48","author":"KR Wilund","year":"2013","unstructured":"Wilund, K. R., Viana, J. L. & Perez, L. M. A critical review of exercise training in hemodialysis patients: personalized activity prescriptions are needed. Exerc. Sport. Sci. Rev. 48, 28\u201339 (2013).","journal-title":"Exerc. Sport. Sci. Rev."},{"key":"498_CR134","doi-asserted-by":"publisher","first-page":"250","DOI":"10.1681\/ASN.2017010020","volume":"29","author":"TA Ikizler","year":"2018","unstructured":"Ikizler, T. A. et al. Metabolic effects of diet and exercise in patients with moderate to severe CKD: a randomized clinical trial. J. Am. Soc. Nephrol. 29, 250\u2013259 (2018).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR135","first-page":"S1","volume":"45","author":"K\/DOQI Workgroup.","year":"2005","unstructured":"K\/DOQI Workgroup. K\/DOQI clinical practice guidelines for cardiovascular disease in dialysis patients. Am. J. Kidney Dis. 45, S1\u2013153 (2005).","journal-title":"Am. J. Kidney Dis."},{"key":"498_CR136","doi-asserted-by":"publisher","first-page":"822","DOI":"10.1093\/ckj\/sfy054","volume":"11","author":"JM Gollie","year":"2018","unstructured":"Gollie, J. M., Harris-Love, M. O., Patel, S. S. & Argani, S. Chronic kidney disease: considerations for monitoring skeletal muscle health and prescribing resistance exercise. Clin. Kidney J. 11, 822\u2013831 (2018).","journal-title":"Clin. Kidney J."},{"key":"498_CR137","doi-asserted-by":"publisher","first-page":"541","DOI":"10.3389\/fphys.2017.00541","volume":"8","author":"EL Watson","year":"2017","unstructured":"Watson, E. L. et al. The effect of resistance exercise on inflammatory and myogenic markers in patients with chronic kidney disease. Front. Physiol. 8, 541 (2017).","journal-title":"Front. Physiol."},{"key":"498_CR138","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1053\/j.jrn.2010.03.004","volume":"21","author":"J Dong","year":"2011","unstructured":"Dong, J. et al. The effect of resistance exercise to augment long-term benefits of intradialytic oral nutritional supplementation in chronic hemodialysis patients. J. Ren. Nutr. 21, 149\u2013159 (2011).","journal-title":"J. Ren. Nutr."},{"key":"498_CR139","doi-asserted-by":"publisher","first-page":"574","DOI":"10.1053\/j.ajkd.2007.07.005","volume":"50","author":"B Cheema","year":"2007","unstructured":"Cheema, B. et al. Randomized controlled trial of intradialytic resistance training to target muscle wasting in ESRD: the Progressive Exercise for Anabolism in Kidney Disease (PEAK) study. Am. J. Kidney Dis. 50, 574\u2013584 (2007).","journal-title":"Am. J. Kidney Dis."},{"key":"498_CR140","doi-asserted-by":"publisher","first-page":"132","DOI":"10.1053\/j.jrn.2012.06.007","volume":"23","author":"S Molsted","year":"2013","unstructured":"Molsted, S., Harrison, A. P., Eidemak, I. & Andersen, J. L. The effects of high-load strength training with protein- or non-protein-containing nutritional supplementation in patients undergoing dialysis. J. Ren. Nutr. 23, 132\u2013140 (2013).","journal-title":"J. Ren. Nutr."},{"key":"498_CR141","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0134511","volume":"10","author":"Z Su","year":"2015","unstructured":"Su, Z. et al. Acupuncture plus low-frequency electrical stimulation (Acu-LFES) attenuates diabetic myopathy by enhancing muscle regeneration. PLoS ONE 10, e0134511 (2015).","journal-title":"PLoS ONE"},{"key":"498_CR142","doi-asserted-by":"publisher","first-page":"434","DOI":"10.1016\/j.bbrc.2011.05.152","volume":"410","author":"A Onda","year":"2011","unstructured":"Onda, A. et al. Acupuncture ameliorated skeletal muscle atrophy induced by hindlimb suspension in mice. Biochem. Biophys. Res. Commun. 410, 434\u2013439 (2011).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"498_CR143","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1016\/j.jams.2018.11.001","volume":"12","author":"Y Liu","year":"2019","unstructured":"Liu, Y., Xiao, F. & Liang, X. Acupuncture improves the facial muscular function in a case of facioscapulohumeral muscular dystrophy. J. Acupunct. Meridian Stud. 12, 73\u201376 (2019).","journal-title":"J. Acupunct. Meridian Stud."},{"key":"498_CR144","doi-asserted-by":"publisher","first-page":"260","DOI":"10.1089\/acu.2017.1241","volume":"29","author":"P Sudhakaran","year":"2017","unstructured":"Sudhakaran, P. Amyotrophic lateral sclerosis: an acupuncture approach. Med. Acupunct. 29, 260\u2013268 (2017).","journal-title":"Med. Acupunct."},{"key":"498_CR145","doi-asserted-by":"publisher","first-page":"268","DOI":"10.1136\/acupmed-2015-011005","volume":"35","author":"J Yu","year":"2017","unstructured":"Yu, J., Wang, M., Liu, J., Zhang, X. & Yang, S. Effect of electroacupuncture on the expression of agrin and acetylcholine receptor subtypes in rats with tibialis anterior muscular atrophy induced by sciatic nerve injection injury. Acupunct. Med. 35, 268\u2013275 (2017).","journal-title":"Acupunct. Med."},{"key":"498_CR146","doi-asserted-by":"publisher","first-page":"426","DOI":"10.1152\/japplphysiol.00175.2015","volume":"120","author":"Z Su","year":"2016","unstructured":"Su, Z. et al. Acupuncture plus low-frequency electrical stimulation (Acu-LFES) attenuates denervation-induced muscle atrophy. J. Appl. Physiol. 120, 426\u2013436 (2016).","journal-title":"J. Appl. Physiol."},{"key":"498_CR147","doi-asserted-by":"publisher","first-page":"1912","DOI":"10.1093\/ndt\/gfh955","volume":"20","author":"C Che-Yi","year":"2005","unstructured":"Che-Yi, C., Wen, C. Y., Min-Tsung, K. & Chiu-Ching, H. Acupuncture in haemodialysis patients at the Quchi (LI11) acupoint for refractory uraemic pruritus. Nephrol. Dial. Transpl. 20, 1912\u20131915 (2005).","journal-title":"Nephrol. Dial. Transpl."},{"key":"498_CR148","doi-asserted-by":"publisher","first-page":"741","DOI":"10.1089\/acm.2010.0206","volume":"17","author":"KH Kim","year":"2011","unstructured":"Kim, K. H. et al. Acupuncture for symptom management in hemodialysis patients: a prospective, observational pilot study. J. Altern. Complement. Med. 17, 741\u2013748 (2011).","journal-title":"J. Altern. Complement. Med."},{"key":"498_CR149","doi-asserted-by":"publisher","first-page":"215","DOI":"10.1142\/S0192415X09006783","volume":"37","author":"LH Su","year":"2009","unstructured":"Su, L. H., Wu, K. D., Lee, L. S., Wang, H. & Liu, C. F. Effects of far infrared acupoint stimulation on autonomic activity and quality of life in hemodialysis patients. Am. J. Chin. Med. 37, 215\u2013226 (2009).","journal-title":"Am. J. Chin. Med."},{"key":"498_CR150","doi-asserted-by":"publisher","first-page":"4131","DOI":"10.1111\/febs.12338","volume":"280","author":"P Munoz-Canoves","year":"2013","unstructured":"Munoz-Canoves, P., Scheele, C., Pedersen, B. K. & Serrano, A. L. Interleukin-6 myokine signaling in skeletal muscle: a double-edged sword? FEBS J. 280, 4131\u20134148 (2013).","journal-title":"FEBS J."},{"key":"498_CR151","doi-asserted-by":"publisher","first-page":"491497","DOI":"10.1155\/2013\/491497","volume":"2013","author":"Y Kharraz","year":"2013","unstructured":"Kharraz, Y., Guerra, J., Mann, C. J., Serrano, A. L. & Munoz-Canoves, P. Macrophage plasticity and the role of inflammation in skeletal muscle repair. Med. Inflamm. 2013, 491497 (2013).","journal-title":"Med. Inflamm."},{"key":"498_CR152","doi-asserted-by":"publisher","first-page":"129","DOI":"10.1152\/japplphysiol.00154.2016","volume":"121","author":"RW Morton","year":"2016","unstructured":"Morton, R. W. et al. Neither load nor systemic hormones determine resistance training-mediated hypertrophy or strength gains in resistance-trained young men. J. Appl. Physiol. 121, 129\u2013138 (2016).","journal-title":"J. Appl. Physiol."},{"key":"498_CR153","doi-asserted-by":"publisher","first-page":"251","DOI":"10.1016\/j.cmet.2013.06.017","volume":"18","author":"R Mounier","year":"2013","unstructured":"Mounier, R. et al. AMPK\u03b11 regulates macrophage skewing at the time of resolution of inflammation during skeletal muscle regeneration. Cell Metab. 18, 251\u2013264 (2013).","journal-title":"Cell Metab."},{"key":"498_CR154","doi-asserted-by":"publisher","first-page":"102","DOI":"10.1152\/physiolgenomics.00057.2006","volume":"30","author":"Y Takaoka","year":"2007","unstructured":"Takaoka, Y. et al. Electroacupuncture suppresses myostatin gene expression: cell proliferative reaction in mouse skeletal muscle. Physiol. Genomics 30, 102\u2013110 (2007).","journal-title":"Physiol. Genomics"},{"key":"498_CR155","doi-asserted-by":"publisher","first-page":"199","DOI":"10.1038\/ki.2009.114","volume":"76","author":"DR Ashby","year":"2009","unstructured":"Ashby, D. R. et al. Sustained appetite improvement in malnourished dialysis patients by daily ghrelin treatment. Kidney Int. 76, 199\u2013206 (2009).","journal-title":"Kidney Int."},{"key":"498_CR156","doi-asserted-by":"publisher","first-page":"2111","DOI":"10.1681\/ASN.2005010039","volume":"16","author":"K Wynne","year":"2005","unstructured":"Wynne, K. et al. Subcutaneous ghrelin enhances acute food intake in malnourished patients who receive maintenance peritoneal dialysis: a randomized, placebo-controlled trial. J. Am. Soc. Nephrol. 16, 2111\u20132118 (2005).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR157","doi-asserted-by":"publisher","first-page":"523","DOI":"10.1093\/ndt\/gfw474","volume":"33","author":"GA Campbell","year":"2018","unstructured":"Campbell, G. A., Patrie, J. T., Gaylinn, B. D., Thorner, M. O. & Bolton, W. K. Oral ghrelin receptor agonist MK-0677 increases serum insulin-like growth factor 1 in hemodialysis patients: a randomized blinded study. Nephrol. Dial. Transpl. 33, 523\u2013530 (2018).","journal-title":"Nephrol. Dial. Transpl."},{"key":"498_CR158","doi-asserted-by":"publisher","first-page":"2333","DOI":"10.1016\/j.biocel.2013.05.019","volume":"45","author":"HQ Han","year":"2013","unstructured":"Han, H. Q., Zhou, X., Mitch, W. E. & Goldberg, A. L. Myostatin\/activin pathway antagonism: molecular basis and therapeutic potential. Int. J. Biochem. Cell Biol. 45, 2333\u20132347 (2013).","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"498_CR159","doi-asserted-by":"publisher","first-page":"458","DOI":"10.1002\/mus.25268","volume":"55","author":"C Campbell","year":"2017","unstructured":"Campbell, C. et al. Myostatin inhibitor ACE-031 treatment of ambulatory boys with Duchenne muscular dystrophy: results of a randomized, placebo-controlled clinical trial. Muscle Nerve 55, 458\u2013464 (2017).","journal-title":"Muscle Nerve"},{"key":"498_CR160","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0191313","volume":"13","author":"BD Perry","year":"2018","unstructured":"Perry, B. D. et al. Palmitate-induced ER stress and inhibition of protein synthesis in cultured myotubes does not require Toll-like receptor 4. PLoS ONE 13, e0191313 (2018).","journal-title":"PLoS ONE"},{"key":"498_CR161","doi-asserted-by":"publisher","DOI":"10.14814\/phy2.13530","volume":"5","author":"ME Woodworth-Hobbs","year":"2017","unstructured":"Woodworth-Hobbs, M. E. et al. Docosahexaenoic acid counteracts palmitate-induced endoplasmic reticulum stress in C2C12 myotubes: impact on muscle atrophy. Physiol. Rep. 5, e13530 (2017).","journal-title":"Physiol. Rep."},{"key":"498_CR162","doi-asserted-by":"publisher","first-page":"868","DOI":"10.1016\/j.jnutbio.2014.03.017","volume":"25","author":"ME Woodworth-Hobbs","year":"2014","unstructured":"Woodworth-Hobbs, M. E. et al. Docosahexaenoic acid prevents palmitate-induced activation of proteolytic systems in C2C12 myotubes. J. Nutr. Biochem. 25, 868\u2013874 (2014).","journal-title":"J. Nutr. Biochem."},{"key":"498_CR163","doi-asserted-by":"publisher","first-page":"238","DOI":"10.1016\/j.bbrc.2008.08.004","volume":"375","author":"J Khal","year":"2008","unstructured":"Khal, J. & Tisdale, M. J. Downregulation of muscle protein degradation in sepsis by eicosapentaenoic acid (EPA). Biochem. Biophys. Res. Commun. 375, 238\u2013240 (2008).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"498_CR164","doi-asserted-by":"publisher","first-page":"266","DOI":"10.1093\/ndt\/gfu283","volume":"30","author":"AM Hung","year":"2015","unstructured":"Hung, A. M. et al. Omega-3 fatty acids inhibit the up-regulation of endothelial chemokines in maintenance hemodialysis patients. Nephrol. Dial. Transplant. 30, 266\u2013274 (2015).","journal-title":"Nephrol. Dial. Transplant."},{"key":"498_CR165","doi-asserted-by":"publisher","first-page":"1227","DOI":"10.2215\/CJN.04150415","volume":"11","author":"SM Deger","year":"2016","unstructured":"Deger, S. M. et al. High dose omega-3 fatty acid administration and skeletal muscle protein turnover in maintenance hemodialysis patients. Clin. J. Am. Soc. Nephrol. 11, 1227\u20131235 (2016).","journal-title":"Clin. J. Am. Soc. Nephrol."},{"key":"498_CR166","doi-asserted-by":"publisher","first-page":"702948","DOI":"10.1155\/2012\/702948","volume":"2012","author":"Y Ishikawa","year":"2012","unstructured":"Ishikawa, Y. et al. Effect of exercise on kidney function, oxidative stress, and inflammation in type 2 diabetic KK-A(y) mice. Exp. Diabetes Res. 2012, 702948 (2012).","journal-title":"Exp. Diabetes Res."},{"key":"498_CR167","doi-asserted-by":"publisher","first-page":"F700","DOI":"10.1152\/ajprenal.90548.2008","volume":"296","author":"S Ghosh","year":"2009","unstructured":"Ghosh, S. et al. Moderate exercise attenuates caspase-3 activity, oxidative stress, and inhibits progression of diabetic renal disease in db\/db mice. Am. J. Physiol. Ren. Physiol. 296, F700\u2013F708 (2009).","journal-title":"Am. J. Physiol. Ren. Physiol."},{"key":"498_CR168","doi-asserted-by":"publisher","first-page":"2800","DOI":"10.1681\/ASN.2013091025","volume":"25","author":"S Hanatani","year":"2014","unstructured":"Hanatani, S. et al. Akt1-mediated fast\/glycolytic skeletal muscle growth attenuates renal damage in experimental kidney disease. J. Am. Soc. Nephrol. 25, 2800\u20132811 (2014).","journal-title":"J. Am. Soc. Nephrol."},{"key":"498_CR169","doi-asserted-by":"publisher","first-page":"367","DOI":"10.1089\/hum.2019.287","volume":"31","author":"B Wang","year":"2020","unstructured":"Wang, B. et al. Exogenous miR-29a attenuates muscle atrophy and kidney fibrosis in unilateral ureteral obstruction in mice. Hum. Gene Ther. 31, 367\u2013375 (2020).","journal-title":"Hum. Gene Ther."},{"key":"498_CR170","doi-asserted-by":"publisher","first-page":"1864","DOI":"10.7150\/thno.29579","volume":"9","author":"B Wang","year":"2019","unstructured":"Wang, B. et al. miR-26a limits muscle wasting and cardiac fibrosis through exosome-mediated microRNA transfer in chronic kidney disease. Theranostics 9, 1864\u20131877 (2019).","journal-title":"Theranostics"},{"key":"498_CR171","doi-asserted-by":"publisher","first-page":"13590","DOI":"10.1096\/fj.201900884R","volume":"33","author":"A Zhang","year":"2019","unstructured":"Zhang, A. et al. Exogenous miR-26a suppresses muscle wasting and renal fibrosis in obstructive kidney disease. FASEB J. 33, 13590\u201313601 (2019).","journal-title":"FASEB J."},{"key":"498_CR172","doi-asserted-by":"publisher","first-page":"755","DOI":"10.1002\/jcsm.12296","volume":"9","author":"A Zhang","year":"2018","unstructured":"Zhang, A. et al. miRNA-23a\/27a attenuates muscle atrophy and renal fibrosis through muscle-kidney crosstalk. J. Cachexia Sarcopenia Muscle 9, 755\u2013770 (2018).","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"498_CR173","doi-asserted-by":"publisher","first-page":"571","DOI":"10.1016\/j.ymthe.2019.01.008","volume":"27","author":"H Wang","year":"2019","unstructured":"Wang, H. et al. Exosome-mediated miR-29 transfer reduces muscle atrophy and kidney fibrosis in mice. Mol. Ther. 27, 571\u2013583 (2019).","journal-title":"Mol. Ther."},{"key":"498_CR174","doi-asserted-by":"publisher","first-page":"267","DOI":"10.1038\/ng1180","volume":"34","author":"VK Mootha","year":"2003","unstructured":"Mootha, V. K. et al. PGC-1\u03b1-responsive genes involved in oxidative phosphorylation are coordinately downregulated in human diabetes. Nat. Genet. 34, 267\u2013273 (2003).","journal-title":"Nat. Genet."},{"key":"498_CR175","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0159181","volume":"11","author":"JA Rahnert","year":"2016","unstructured":"Rahnert, J. A., Zheng, B., Hudson, M. B., Woodworth-Hobbs, M. E. & Price, S. R. Glucocorticoids alter CRTC-CREB signaling in muscle cells: impact on PGC-1\u03b1 expression and atrophy markers. PLoS ONE 11, e0159181 (2016).","journal-title":"PLoS ONE"},{"key":"498_CR176","doi-asserted-by":"publisher","first-page":"960","DOI":"10.1016\/j.bbamcr.2010.03.019","volume":"1803","author":"TK Roberts-Wilson","year":"2010","unstructured":"Roberts-Wilson, T. K. et al. Calcineurin signaling and PGC-1\u03b1 expression are suppressed during muscle atrophy due to diabetes. Biochim. Biophys. Acta 1803, 960\u2013967 (2010).","journal-title":"Biochim. Biophys. Acta"},{"key":"498_CR177","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-017-01646-6","volume":"8","author":"H Peng","year":"2017","unstructured":"Peng, H. et al. Myokine mediated muscle-kidney crosstalk suppresses metabolic reprogramming and fibrosis in damaged kidneys. Nat. Commun. 8, 1493 (2017).","journal-title":"Nat. Commun."},{"key":"498_CR178","doi-asserted-by":"publisher","first-page":"495","DOI":"10.1007\/s00424-020-02367-4","volume":"472","author":"JS Chang","year":"2020","unstructured":"Chang, J. S. & Kong, I. D. Irisin prevents dexamethasone-induced atrophy in C2C12 myotubes. Pflug. Arch. 472, 495\u2013502 (2020).","journal-title":"Pflug. Arch."},{"key":"498_CR179","doi-asserted-by":"publisher","first-page":"2417","DOI":"10.1210\/en.2019-00257","volume":"160","author":"KL Walton","year":"2019","unstructured":"Walton, K. L. et al. Activin A-induced cachectic wasting Is attenuated by systemic delivery of Its cognate propeptide in male mice. Endocrinology 160, 2417\u20132426 (2019).","journal-title":"Endocrinology"},{"key":"498_CR180","doi-asserted-by":"publisher","first-page":"23942","DOI":"10.1073\/pnas.2014716117","volume":"117","author":"SJ Lee","year":"2020","unstructured":"Lee, S. J. et al. Targeting myostatin\/activin A protects against skeletal muscle and bone loss during spaceflight. Proc. Natl Acad. Sci. USA 117, 23942\u201323951 (2020).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"498_CR181","doi-asserted-by":"publisher","first-page":"1711","DOI":"10.1096\/fj.13-245894","volume":"28","author":"JL Chen","year":"2014","unstructured":"Chen, J. L. et al. Elevated expression of activins promotes muscle wasting and cachexia. FASEB J. 28, 1711\u20131723 (2014).","journal-title":"FASEB J."},{"key":"498_CR182","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms15153","volume":"8","author":"E Latres","year":"2017","unstructured":"Latres, E. et al. Activin A more prominently regulates muscle mass in primates than does GDF8. Nat. Commun. 8, 15153 (2017).","journal-title":"Nat. Commun."},{"key":"498_CR183","doi-asserted-by":"publisher","DOI":"10.1172\/JCI135821","volume":"131","author":"F Solagna","year":"2021","unstructured":"Solagna, F. et al. Pro-cachectic factors link experimental and human chronic kidney disease to skeletal muscle wasting programs. J. Clin. Invest. 131, e135821 (2021).","journal-title":"J. Clin. Invest."},{"key":"498_CR184","doi-asserted-by":"publisher","first-page":"1213","DOI":"10.1007\/s00467-011-1963-1","volume":"27","author":"S Kummer","year":"2012","unstructured":"Kummer, S., von Gersdorff, G., Kemper, M. J. & Oh, J. The influence of gender and sexual hormones on incidence and outcome of chronic kidney disease. Pediatr. Nephrol. 27, 1213\u20131219 (2012).","journal-title":"Pediatr. Nephrol."},{"key":"498_CR185","doi-asserted-by":"publisher","first-page":"328","DOI":"10.3390\/nu9040328","volume":"9","author":"G Jean","year":"2017","unstructured":"Jean, G., Souberbielle, J. C. & Chazot, C. Vitamin D in chronic kidney disease and dialysis patients. Nutrients 9, 328 (2017).","journal-title":"Nutrients"},{"key":"498_CR186","doi-asserted-by":"publisher","first-page":"1773","DOI":"10.3390\/ijerph15081773","volume":"15","author":"PH Franca Gois","year":"2018","unstructured":"Franca Gois, P. H., Wolley, M., Ranganathan, D. & Seguro, A. C. Vitamin D deficiency in chronic kidney disease: recent evidence and controversies. Int. J. Env. Res. Pub. Health 15, 1773 (2018).","journal-title":"Int. J. Env. Res. Pub. Health"},{"key":"498_CR187","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1007\/s00223-019-00583-4","volume":"106","author":"CM Girgis","year":"2020","unstructured":"Girgis, C. M. Vitamin D and skeletal muscle: emerging roles in development, anabolism and repair. Calcif. Tissue Int. 106, 47\u201357 (2020).","journal-title":"Calcif. Tissue Int."},{"key":"498_CR188","doi-asserted-by":"publisher","first-page":"423","DOI":"10.1053\/j.jrn.2011.10.006","volume":"22","author":"PL Gordon","year":"2012","unstructured":"Gordon, P. L., Doyle, J. W. & Johansen, K. L. Association of 1,25-dihydroxyvitamin D levels with physical performance and thigh muscle cross-sectional area in chronic kidney disease stage 3 and 4. J. Ren. Nutr. 22, 423\u2013433 (2012).","journal-title":"J. Ren. Nutr."},{"key":"498_CR189","doi-asserted-by":"publisher","first-page":"397","DOI":"10.1053\/j.jrn.2007.06.001","volume":"17","author":"PL Gordon","year":"2007","unstructured":"Gordon, P. L., Sakka, G. K., Doyle, J. W., Shubert, T. & Johansen, K. L. Relationship between vitamin D and muscle size and strength in patients on hemodialysis. J. Ren. Nutr. 17, 397\u2013407 (2007).","journal-title":"J. Ren. Nutr."},{"key":"498_CR190","doi-asserted-by":"publisher","first-page":"1143","DOI":"10.2215\/CJN.02840312","volume":"8","author":"NA Hewitt","year":"2013","unstructured":"Hewitt, N. A., O\u2019Connor, A. A., O\u2019Shaughnessy, D. V. & Elder, G. J. Effects of cholecalciferol on functional, biochemical, vascular, and quality of life outcomes in hemodialysis patients. Clin. J. Am. Soc. Nephrol. 8, 1143\u20131149 (2013).","journal-title":"Clin. J. Am. Soc. Nephrol."},{"key":"498_CR191","doi-asserted-by":"publisher","first-page":"686","DOI":"10.1016\/j.clnu.2016.05.012","volume":"36","author":"DR Mager","year":"2017","unstructured":"Mager, D. R., Jackson, S. T., Hoffman, M. R., Jindal, K. & Senior, P. A. Vitamin D supplementation, bone health and quality of life in adults with diabetes and chronic kideney disease: results of an open label randomized clinical trial. Clin. Nutr. 36, 686\u2013696 (2017).","journal-title":"Clin. Nutr."},{"key":"498_CR192","doi-asserted-by":"publisher","first-page":"12448","DOI":"10.1073\/pnas.1707925114","volume":"114","author":"F Morvan","year":"2017","unstructured":"Morvan, F. et al. Blockade of activin type II receptors with a dual anti-ActRIIA\/IIB antibody is critical to promote maximal skeletal muscle hypertrophy. Proc. Natl Acad. Sci. USA 114, 12448\u201312453 (2017).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"498_CR193","doi-asserted-by":"publisher","first-page":"434","DOI":"10.1038\/mt.2014.221","volume":"23","author":"JL Chen","year":"2015","unstructured":"Chen, J. L. et al. Development of novel activin-targeted therapeutics. Mol. Ther. 23, 434\u2013444 (2015).","journal-title":"Mol. Ther."},{"key":"498_CR194","doi-asserted-by":"publisher","first-page":"368","DOI":"10.1016\/j.cmet.2013.07.012","volume":"18","author":"L Zhang","year":"2013","unstructured":"Zhang, L. et al. Stat3 activation links a C\/EBPdelta to myostatin pathway to stimulate loss of muscle mass. Cell Metab. 18, 368\u2013379 (2013).","journal-title":"Cell Metab."},{"key":"498_CR195","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1038\/s41581-019-0248-y","volume":"16","author":"M Ruiz-Ortega","year":"2020","unstructured":"Ruiz-Ortega, M., Rayego-Mateos, S., Lamas, S., Ortiz, A. & Rodrigues-Diez, R. R. Targeting the progression of chronic kidney disease. Nat. Rev. Nephrol. 16, 269\u2013288 (2020).","journal-title":"Nat. Rev. Nephrol."}],"container-title":["Nature Reviews Nephrology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41581-021-00498-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41581-021-00498-0","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41581-021-00498-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,2,8]],"date-time":"2023-02-08T07:18:48Z","timestamp":1675840728000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41581-021-00498-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,11,8]]},"references-count":195,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2022,3]]}},"alternative-id":["498"],"URL":"https:\/\/doi.org\/10.1038\/s41581-021-00498-0","relation":{},"ISSN":["1759-5061","1759-507X"],"issn-type":[{"value":"1759-5061","type":"print"},{"value":"1759-507X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,11,8]]},"assertion":[{"value":"1 October 2021","order":1,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"8 November 2021","order":2,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}