{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,19]],"date-time":"2025-10-19T15:41:40Z","timestamp":1760888500063},"reference-count":47,"publisher":"Springer Science and Business Media LLC","issue":"6","license":[{"start":{"date-parts":[[2011,2,22]],"date-time":"2011-02-22T00:00:00Z","timestamp":1298332800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Eur J Trauma Emerg Surg"],"published-print":{"date-parts":[[2011,12]]},"DOI":"10.1007\/s00068-011-0083-8","type":"journal-article","created":{"date-parts":[[2011,2,21]],"date-time":"2011-02-21T09:58:59Z","timestamp":1298282339000},"page":"645-654","source":"Crossref","is-referenced-by-count":2,"title":["Effects on the ubiquitin proteasome system after closed soft-tissue trauma in rat skeletal muscle"],"prefix":"10.1007","volume":"37","author":[{"given":"N.","family":"Ponelies","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"D.","family":"Gosenca","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"N.","family":"Ising","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M.","family":"Schoen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"K.","family":"Ruppel","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"B.","family":"Vollmar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"U.","family":"Obertacke","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2011,2,22]]},"reference":[{"issue":"Pt 3","key":"83_CR1","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1042\/bj3070631","volume":"307","author":"R Medina","year":"1995","unstructured":"Medina R, Wing SS, Goldberg AL. Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy. Biochem J. 1995;307(Pt 3):631\u20137.","journal-title":"Biochem J"},{"key":"83_CR2","first-page":"R1690","volume":"277","author":"XM Song","year":"1999","unstructured":"Song XM, Ryder JW, Kawano Y, Chibalin AV, Krook A, Zierath JR. Muscle fiber type specificity in insulin signal transduction. Am J Physiol. 1999;277:R1690\u20136.","journal-title":"Am J Physiol"},{"key":"83_CR3","first-page":"31","volume":"39","author":"AL Goldberg","year":"1980","unstructured":"Goldberg AL, Tischler M, DeMartino G, Griffin G. Hormonal regulation of protein degradation and synthesis in skeletal muscle. Fed Proc. 1980;39:31\u20136.","journal-title":"Fed Proc"},{"key":"83_CR4","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1152\/ajplegacy.1976.231.2.441","volume":"231","author":"JB Li","year":"1976","unstructured":"Li JB, Goldberg AL. Effects of food deprivation on protein synthesis and degradation in rat skeletal muscles. Am J Physiol. 1976;231:441\u20138.","journal-title":"Am J Physiol"},{"key":"83_CR5","doi-asserted-by":"crossref","first-page":"R1423","DOI":"10.1152\/ajpregu.00545.2004","volume":"288","author":"MB Reid","year":"2005","unstructured":"Reid MB. Response of the ubiquitin\u2013proteasome pathway to changes in muscle activity. Am J Physiol Regul Integr Comp Physiol. 2005;288:R1423\u201331.","journal-title":"Am J Physiol Regul Integr Comp Physiol"},{"issue":"Pt 1","key":"83_CR6","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1042\/bj2730021","volume":"273","author":"PH Sugden","year":"1991","unstructured":"Sugden PH, Fuller SJ. Regulation of protein turnover in skeletal and cardiac muscle. Biochem J. 1991;273(Pt 1):21\u201337.","journal-title":"Biochem J"},{"key":"83_CR7","doi-asserted-by":"crossref","first-page":"227S","DOI":"10.1093\/jn\/129.1.227S","volume":"129","author":"SH Lecker","year":"1999","unstructured":"Lecker SH, Solomon V, Mitch WE, Goldberg AL. Muscle protein breakdown and the critical role of the ubiquitin\u2013proteasome pathway in normal and disease states. J Nutr. 1999;129:227S\u201337S.","journal-title":"J Nutr"},{"key":"83_CR8","doi-asserted-by":"crossref","first-page":"1897","DOI":"10.1056\/NEJM199612193352507","volume":"335","author":"WE Mitch","year":"1996","unstructured":"Mitch WE, Goldberg AL. Mechanisms of muscle wasting. The role of the ubiquitin\u2013proteasome pathway. N Engl J Med. 1996;335:1897\u2013905.","journal-title":"N Engl J Med"},{"key":"83_CR9","doi-asserted-by":"crossref","first-page":"2156","DOI":"10.1016\/j.biocel.2005.01.017","volume":"37","author":"PO Hasselgren","year":"2005","unstructured":"Hasselgren PO, Menconi MJ, Fareed MU, Yang H, Wei W, Evenson A. Novel aspects on the regulation of muscle wasting in sepsis. Int J Biochem Cell Biol. 2005;37:2156\u201368.","journal-title":"Int J Biochem Cell Biol"},{"key":"83_CR10","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1006\/bbrc.2001.5849","volume":"290","author":"PO Hasselgren","year":"2002","unstructured":"Hasselgren PO, Wray C, Mammen J. Molecular regulation of muscle cachexia: it may be more than the proteasome. Biochem Biophys Res Commun. 2002;290:1\u201310.","journal-title":"Biochem Biophys Res Commun"},{"key":"83_CR11","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1038\/sj.bjc.6602780","volume":"93","author":"J Khal","year":"2005","unstructured":"Khal J, Wyke SM, Russell ST, Hine AV, Tisdale MJ. Expression of the ubiquitin\u2013proteasome pathway and muscle loss in experimental cancer cachexia. Br J Cancer. 2005;93:774\u201380.","journal-title":"Br J Cancer"},{"key":"83_CR12","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1096\/fj.03-0610com","volume":"18","author":"SH Lecker","year":"2004","unstructured":"Lecker SH, Jagoe RT, Gilbert A, Gomes M, Baracos V, Bailey J, et al. Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression. FASEB J. 2004;18:39\u201351.","journal-title":"FASEB J"},{"key":"83_CR13","doi-asserted-by":"crossref","first-page":"1610","DOI":"10.1172\/JCI118586","volume":"97","author":"L Voisin","year":"1996","unstructured":"Voisin L, Breuille D, Combaret L, Pouyet C, Taillandier D, Aurousseau E, et al. Muscle wasting in a rat model of long-lasting sepsis results from the activation of lysosomal, Ca2+-activated, and ubiquitin\u2013proteasome proteolytic pathways. J Clin Invest. 1996;97:1610\u20137.","journal-title":"J Clin Invest"},{"key":"83_CR14","first-page":"209","volume":"3","author":"MJ Tisdale","year":"2005","unstructured":"Tisdale MJ. The ubiquitin\u2013proteasome pathway as a therapeutic target for muscle wasting. J Support Oncol. 2005;3:209\u201317.","journal-title":"J Support Oncol"},{"key":"83_CR15","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1042\/EB0410173","volume":"41","author":"D Attaix","year":"2005","unstructured":"Attaix D, Ventadour S, Codran A, Bechet D, Taillandier D, Combaret L. The ubiquitin\u2013proteasome system and skeletal muscle wasting. Essays Biochem. 2005;41:173\u201386.","journal-title":"Essays Biochem"},{"key":"83_CR16","doi-asserted-by":"crossref","first-page":"1807","DOI":"10.1681\/ASN.2006010083","volume":"17","author":"SH Lecker","year":"2006","unstructured":"Lecker SH, Goldberg AL, Mitch WE. Protein degradation by the ubiquitin\u2013proteasome pathway in normal and disease states. J Am Soc Nephrol. 2006;17:1807\u201319.","journal-title":"J Am Soc Nephrol"},{"key":"83_CR17","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1042\/CS20010042","volume":"101","author":"D Larbaud","year":"2001","unstructured":"Larbaud D, Balage M, Taillandier D, Combaret L, Grizard J, Attaix D. Differential regulation of the lysosomal, Ca2+-dependent and ubiquitin\/proteasome-dependent proteolytic pathways in fast-twitch and slow-twitch rat muscle following hyperinsulinaemia. Clin Sci (Lond). 2001;101:551\u20138.","journal-title":"Clin Sci (Lond)"},{"key":"83_CR18","doi-asserted-by":"crossref","first-page":"1537","DOI":"10.1097\/01.ASN.0000127211.86206.E1","volume":"15","author":"SW Lee","year":"2004","unstructured":"Lee SW, Dai G, Hu Z, Wang X, Du J, Mitch WE. Regulation of muscle protein degradation: coordinated control of apoptotic and ubiquitin\u2013proteasome systems by phosphatidylinositol 3 kinase. J Am Soc Nephrol. 2004;15:1537\u201345.","journal-title":"J Am Soc Nephrol"},{"key":"83_CR19","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/0165-0270(91)90104-8","volume":"39","author":"CE Dixon","year":"1991","unstructured":"Dixon CE, Clifton GL, Lighthall JW, Yaghmai AA, Hayes RL. A controlled cortical impact model of traumatic brain injury in the rat. J Neurosci Methods. 1991;39:253\u201362.","journal-title":"J Neurosci Methods"},{"key":"83_CR20","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1002\/jor.1100170509","volume":"17","author":"KD Schaser","year":"1999","unstructured":"Schaser KD, Vollmar B, Menger MD, Schewior L, Kroppenstedt SN, Raschke M, et al. In vivo analysis of microcirculation following closed soft-tissue injury. J Orthop Res. 1999;17:678\u201385.","journal-title":"J Orthop Res"},{"key":"83_CR21","first-page":"111","volume":"85","author":"H Tscherne","year":"1982","unstructured":"Tscherne H, Oestern HJ. A new classification of soft-tissue damage in open and closed fractures (author\u2019s transl). Unfallheilkunde. 1982;85:111\u20135.","journal-title":"Unfallheilkunde"},{"key":"83_CR22","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1097\/01.shk.0000164692.04026.76","volume":"24","author":"N Ponelies","year":"2005","unstructured":"Ponelies N, Hirsch T, Krehmeier U, Denz C, Patel MB, Majetschak M. Cytosolic ubiquitin and ubiquitylation rates in human peripheral blood mononuclear cells during sepsis. Shock. 2005;24:20\u20135.","journal-title":"Shock"},{"key":"83_CR23","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1111\/j.1440-1711.2005.01399.x","volume":"84","author":"M Majetschak","year":"2006","unstructured":"Majetschak M, Ponelies N, Hirsch T. Targeting the monocytic ubiquitin system with extracellular ubiquitin. Immunol Cell Biol. 2006;84:59\u201365.","journal-title":"Immunol Cell Biol"},{"key":"83_CR24","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/j.orthres.2004.05.009","volume":"23","author":"KD Schaser","year":"2005","unstructured":"Schaser KD, Bail HJ, Schewior L, Stover JF, Melcher I, Haas NP, Mittlmeier T. Acute effects of N-acetylcysteine on skeletal muscle microcirculation following closed soft tissue trauma in rats. J Orthop Res. 2005;23:231\u201341.","journal-title":"J Orthop Res"},{"key":"83_CR25","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1016\/S1074-5521(01)00069-2","volume":"8","author":"BM Kessler","year":"2001","unstructured":"Kessler BM, Tortorella D, Altun M, Kisselev AF, Fiebiger E, Hekking BG, et al. Extended peptide-based inhibitors efficiently target the proteasome and reveal overlapping specificities of the catalytic beta-subunits. Chem Biol. 2001;8:913\u201329.","journal-title":"Chem Biol"},{"key":"83_CR26","doi-asserted-by":"crossref","first-page":"10403","DOI":"10.1073\/pnas.96.18.10403","volume":"96","author":"L Meng","year":"1999","unstructured":"Meng L, Mohan R, Kwok BH, Elofsson M, Sin N, Crews CM. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc Natl Acad Sci USA. 1999;96:10403\u20138.","journal-title":"Proc Natl Acad Sci USA"},{"key":"83_CR27","first-page":"R434","volume":"277","author":"SC Hobler","year":"1999","unstructured":"Hobler SC, Williams A, Fischer D, Wang JJ, Sun X, Fischer JE, et al. Activity and expression of the 20S proteasome are increased in skeletal muscle during sepsis. Am J Physiol. 1999;277:R434\u201340.","journal-title":"Am J Physiol"},{"key":"83_CR28","doi-asserted-by":"crossref","first-page":"C1132","DOI":"10.1152\/ajpcell.1999.276.5.C1132","volume":"276","author":"WE Mitch","year":"1999","unstructured":"Mitch WE, Bailey JL, Wang X, Jurkovitz C, Newby D, Price SR. Evaluation of signals activating ubiquitin\u2013proteasome proteolysis in a model of muscle wasting. Am J Physiol. 1999;276:C1132\u20138.","journal-title":"Am J Physiol"},{"key":"83_CR29","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1097\/00075197-200105000-00003","volume":"4","author":"RT Jagoe","year":"2001","unstructured":"Jagoe RT, Goldberg AL. What do we really know about the ubiquitin\u2013proteasome pathway in muscle atrophy? Curr Opin Clin Nutr Metab Care. 2001;4:183\u201390.","journal-title":"Curr Opin Clin Nutr Metab Care"},{"key":"83_CR30","doi-asserted-by":"crossref","first-page":"2714","DOI":"10.1073\/pnas.93.7.2714","volume":"93","author":"O Mansoor","year":"1996","unstructured":"Mansoor O, Beaufrere B, Boirie Y, Ralliere C, Taillandier D, Aurousseau E, et al. Increased mRNA levels for components of the lysosomal, Ca2+-activated, and ATP-ubiquitin-dependent proteolytic pathways in skeletal muscle from head trauma patients. Proc Natl Acad Sci USA. 1996;93:2714\u20138.","journal-title":"Proc Natl Acad Sci USA"},{"key":"83_CR31","doi-asserted-by":"crossref","first-page":"3141","DOI":"10.1210\/en.2004-0869","volume":"146","author":"CH Fang","year":"2005","unstructured":"Fang CH, Li BG, James JH, King JK, Evenson AR, Warden GD, Hasselgren PO. Protein breakdown in muscle from burned rats is blocked by insulin-like growth factor i and glycogen synthase kinase-3\u03b2 inhibitors. Endocrinology. 2005;146:3141\u20139.","journal-title":"Endocrinology"},{"key":"83_CR32","doi-asserted-by":"crossref","first-page":"227","DOI":"10.33549\/physiolres.930966","volume":"56","author":"M Seiffert","year":"2007","unstructured":"Seiffert M, Gosenca D, Ponelies N, Ising N, Patel MB, Obertacke U, Majetschak M. Regulation of the ubiquitin proteasome system in mechanically injured human skeletal muscle. Physiol Res. 2007;56:227\u201333.","journal-title":"Physiol Res"},{"key":"83_CR33","first-page":"185","volume":"22","author":"BD Fisher","year":"1990","unstructured":"Fisher BD, Baracos VE, Shnitka TK, Mendryk SW, Reid DC. Ultrastructural events following acute muscle trauma. Med Sci Sports Exerc. 1990;22:185\u201393.","journal-title":"Med Sci Sports Exerc"},{"key":"83_CR34","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1589\/jpts.18.57","volume":"18","author":"BD Fisher","year":"2006","unstructured":"Fisher BD, Rathgaber M. An overview of muscle regeneration following acute injury. J Phys Ther Sci. 2006;18:57\u201366.","journal-title":"J Phys Ther Sci"},{"key":"83_CR35","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1007\/s00423-003-0433-z","volume":"389","author":"P Gierer","year":"2004","unstructured":"Gierer P, Vollmar B, Schaser KD, Andreas C, Gradl G, Mittlmeier T. Efficiency of small-volume resuscitation in restoration of disturbed skeletal muscle microcirculation after soft-tissue trauma and haemorrhagic shock. Langenbecks Arch Surg. 2004;389:40\u20135.","journal-title":"Langenbecks Arch Surg"},{"key":"83_CR36","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1042\/CS20040192","volume":"107","author":"I Tjader","year":"2004","unstructured":"Tjader I, Essen P, Garlick PJ, McMnurlan MA, Rooyackers O, Wernerman J. Impact of surgical trauma on human skeletal muscle protein synthesis. Clin Sci (Lond). 2004;107:601\u20137.","journal-title":"Clin Sci (Lond)"},{"key":"83_CR37","first-page":"E359","volume":"275","author":"JL Luo","year":"1998","unstructured":"Luo JL, Hammarqvist F, Andersson K, Wernerman J. Surgical trauma decreases glutathione synthetic capacity in human skeletal muscle tissue. Am J Physiol. 1998;275:E359\u201365.","journal-title":"Am J Physiol"},{"key":"83_CR38","doi-asserted-by":"crossref","first-page":"E326","DOI":"10.1152\/ajpendo.00345.2001","volume":"282","author":"MC Farges","year":"2002","unstructured":"Farges MC, Balcerzak D, Fisher BD, Attaix D, Bechet D, Ferrara M, Baracos VE. Increased muscle proteolysis after local trauma mainly reflects macrophage-associated lysosomal proteolysis. Am J Physiol Endocrinol Metab. 2002;282:E326\u201335.","journal-title":"Am J Physiol Endocrinol Metab"},{"key":"83_CR39","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1172\/JCI119513","volume":"100","author":"NE Tawa Jr","year":"1997","unstructured":"Tawa NE Jr, Odessey R, Goldberg AL. Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles. J Clin Invest. 1997;100:197\u2013203.","journal-title":"J Clin Invest"},{"key":"83_CR40","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1016\/j.yexcr.2005.03.031","volume":"307","author":"Q Zhu","year":"2005","unstructured":"Zhu Q, Wani G, Wang QE, El-mahdy M, Snapka RM, Wani AA. Deubiquitination by proteasome is coordinated with substrate translocation for proteolysis in vivo. Exp Cell Res. 2005;307:436\u201351.","journal-title":"Exp Cell Res"},{"key":"83_CR41","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1093\/jb\/mvg107","volume":"134","author":"JH Kim","year":"2003","unstructured":"Kim JH, Park KC, Chung SS, Bang O, Chung CH. Deubiquitinating enzymes as cellular regulators. J Biochem (Tokyo). 2003;134:9\u201318.","journal-title":"J Biochem (Tokyo)"},{"key":"83_CR42","doi-asserted-by":"crossref","first-page":"E693","DOI":"10.1152\/ajpendo.00281.2004","volume":"288","author":"L Combaret","year":"2005","unstructured":"Combaret L, Adegoke OA, Bedard N, Baracos V, Attaix D, Wing SS. USP19 is a ubiquitin-specific protease regulated in rat skeletal muscle during catabolic states. Am J Physiol Endocrinol Metab. 2005;288:E693\u2013700.","journal-title":"Am J Physiol Endocrinol Metab"},{"key":"83_CR43","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1016\/j.clnu.2007.07.003","volume":"26","author":"G Fuster","year":"2007","unstructured":"Fuster G, Busquets S, Almendro V, Lopez-Soriano FJ, Argiles JM. Antiproteolytic effects of plasma from hibernating bears: a new approach for muscle wasting therapy? Clin Nutr. 2007;26:658\u201361.","journal-title":"Clin Nutr"},{"key":"83_CR44","doi-asserted-by":"crossref","first-page":"R166","DOI":"10.1152\/ajpcell.1993.265.1.C166","volume":"265","author":"RA Fielding","year":"1993","unstructured":"Fielding RA, Manfredi TJ, Ding W, Fiatarone MA, Evans WJ, Cannon JG. Acute phase response in exercise. III. Neutrophil and IL-1 beta accumulation in skeletal muscle. Am J Physiol. 1993;265:R166\u201372.","journal-title":"Am J Physiol"},{"key":"83_CR45","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1002\/jlb.65.4.492","volume":"65","author":"JG Tidball","year":"1999","unstructured":"Tidball JG, Berchenko E, Frenette J. Macrophage invasion does not contribute to muscle membrane injury during inflammation. J Leukoc Biol. 1999;65:492\u20138.","journal-title":"J Leukoc Biol"},{"key":"83_CR46","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1053\/j.otsm.2006.01.012","volume":"13","author":"C Gates","year":"2005","unstructured":"Gates C, Huard J. Management of skeletal muscle injuries in military personnel. Oper Tech Sports Med. 2005;13:247\u201356.","journal-title":"Oper Tech Sports Med"},{"key":"83_CR47","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1152\/physrev.00019.2003","volume":"84","author":"SB Charge","year":"2004","unstructured":"Charge SB, Rudnicki MA. Cellular and molecular regulation of muscle regeneration. Physiol Rev. 2004;84:209\u201338.","journal-title":"Physiol Rev"}],"container-title":["European Journal of Trauma and Emergency Surgery"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s00068-011-0083-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s00068-011-0083-8\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s00068-011-0083-8","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,19]],"date-time":"2021-11-19T05:44:03Z","timestamp":1637300643000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s00068-011-0083-8"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,2,22]]},"references-count":47,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2011,12]]}},"alternative-id":["83"],"URL":"https:\/\/doi.org\/10.1007\/s00068-011-0083-8","relation":{},"ISSN":["1863-9933","1863-9941"],"issn-type":[{"value":"1863-9933","type":"print"},{"value":"1863-9941","type":"electronic"}],"subject":[],"published":{"date-parts":[[2011,2,22]]}}}