Ubiquitin-proteasome-dependent proteolysis in skeletal muscle.

STRUCTURE AND FUNCTIONS OF THE 20S AND 26S PROTEASOMES

Coux, O., Tanaka, K., & Goldberg, A. L. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.004101 · Cited by 2,438 · see citing works

The Proteasome: Paradigm of a Self-Compartmentalizing Protease

Baumeister, W. P., Walz, J., Zühl, F., & Seemüller, E. (1998) · Cell · doi:10.1016/s0092-8674(00)80929-0 · Cited by 1,497 · see citing works

THE UBIQUITIN SYSTEM FOR PROTEIN DEGRADATION

Hershko, A., & Ciechanover, A. J. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.003553 · Cited by 1,419 · see citing works

Protein turnover in mammalian tissues and in the whole body

Waterlow, J. C., Garlick, P. J., & Millward, D. J. (1978) · Medical Entomology and Zoology · Cited by 1,238 · see citing works

Mechanisms of Muscle Wasting — The Role of the Ubiquitin–Proteasome Pathway

Mitch, W. E., & Goldberg, A. L. (1996) · New England Journal of Medicine · doi:10.1056/nejm199612193352507 · Cited by 1,163 · see citing works

A 26 S protease subunit that binds ubiquitin conjugates.

Deveraux, Q. L., Ustrell, V., Pickart, C. M., & Rechsteiner, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37244-7 · Cited by 763 · see citing works

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.

Bailey, J. L., Wang, X., England, B. K., Price, S. R., Ding, X., & Mitch, W. E. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118566 · Cited by 455 · see citing works

Interleukin 6 receptor antibody inhibits muscle atrophy and modulates proteolytic systems in interleukin 6 transgenic mice.

Tsujinaka, T., Fujita, J., Ebisui, C., Yano, M., Kominami, E., Suzuki, K., Tanaka, K., Katsume, A., Ohsugi, Y., Shiozaki, H., et al. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118398 · Cited by 421 · see citing works

Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasomes.

Mitch, W. E., Medina, R., Grieber, S., May, R. C., England, B. K., Price, S. R., Bailey, J. L., & Goldberg, A. L. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117208 · Cited by 405 · see citing works

Muscle wasting in insulinopenic rats results from activation of the ATP-dependent, ubiquitin-proteasome proteolytic pathway by a mechanism including gene transcription.

Price, S. R., Bailey, J. L., Wang, X., Jurkovitz, C. T., England, B. K., Ding, X., Phillips, L. S., & Mitch, W. E. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118968 · Cited by 348 · see citing works

Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting

Wing, S. S., & Goldberg, A. L. (1993) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1993.264.4.e668 · Cited by 345 · see citing works

The mechanism of ubiquitin activating enzyme. A kinetic and equilibrium analysis.

Haas, A. L., & Rose, I. A. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34024-9 · Cited by 330 · see citing works

Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles.

Tawa, N. E., Odessey, R., & Goldberg, A. L. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119513 · Cited by 322 · see citing works

Pathways of ubiquitin conjugation

Haas, A. L., & Siepmann, T. J. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.14.9409544 · Cited by 313 · see citing works

Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy.

Furuno, K., Goodman, M. N., & Goldberg, A. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38923-9 · Cited by 300 · see citing works

Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy

Medina, R., Wing, S. S., & Goldberg, A. L. (1995) · Biochemical Journal · doi:10.1042/bj3070631 · Cited by 294 · see citing works

Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma.

Baracos, V., DeVivo, C., Hoyle, D., & Goldberg, A. (1995) · American Journal of Physiology · doi:10.1152/ajpendo.1995.268.5.e996 · Cited by 275 · see citing works

Sepsis is associated with increased mRNAs of the ubiquitin-proteasome proteolytic pathway in human skeletal muscle.

Tiao, G. M., Hobler, S. C., Wang, J. J., Meyer, T. A., Luchette, F. A., Fischer, J. E., & Hasselgren, P.-O. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119143 · Cited by 264 · see citing works

Sepsis stimulates nonlysosomal, energy-dependent proteolysis and increases ubiquitin mRNA levels in rat skeletal muscle.

Tiao, G. M., Fagan, J. M., Samuels, N., James, J. H., Hudson, K., Lieberman, M. A., Fischer, J. E., & Hasselgren, P.-O. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117588 · Cited by 255 · see citing works

Energy-ubiquitin-dependent muscle proteolysis during sepsis in rats is regulated by glucocorticoids.

Tiao, G. M., Fagan, J. M., Roegner, V., Lieberman, M. A., Wang, J. J., Fischer, J. E., & Hasselgren, P. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118421 · Cited by 248 · see citing works

Muscle wasting in a rat model of long-lasting sepsis results from the activation of lysosomal, Ca2+ -activated, and ubiquitin-proteasome proteolytic pathways.

Voisin, L., Breuillé, D., Combaret, L., Pouyet, C., Taillandier, D., AUROUSSEAU, E., Obled, C., & Attaix, D. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118586 · Cited by 225 · see citing works

Evidence that lysosomes are not involved in the degradation of myofibrillar proteins in rat skeletal muscle

Lowell, B. B., Ruderman, N. B., & Goodman, M. N. (1986) · Biochemical Journal · doi:10.1042/bj2340237 · Cited by 222 · see citing works

Increase in ubiquitin-protein conjugates concomitant with the increase in proteolysis in rat skeletal muscle during starvation and atrophy denervation

Wing, S. S., Haas, A. L., & Goldberg, A. L. (1995) · Biochemical Journal · doi:10.1042/bj3070639 · Cited by 222 · see citing works

Increased mRNA levels for components of the lysosomal, Ca2+-activated, and ATP-ubiquitin-dependent proteolytic pathways in skeletal muscle from head trauma patients.

Mansoor, O., Beaufrère, B., Boirie‌, Y., Rallière, C., Taillandier, D., AUROUSSEAU, E., Schoeffler, P., Arnal, M., & Attaix, D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.7.2714 · Cited by 221 · see citing works

Increased ATP-ubiquitin-dependent proteolysis in skeletal muscles of tumor-bearing rats.

Temparis, S., Asensi, M., Taillandier, D., AUROUSSEAU, E., Larbaud, D., Obled, A., Béchet, D., Ferrara, M., Estrela, J. M., & Attaix, D. (1994) · PubMed · Cited by 214 · see citing works

Acidosis and glucocorticoids concomitantly increase ubiquitin and proteasome subunit mRNAs in rat muscle

Price, S. R., England, B. K., Bailey, J. L., Vreede, K. V., & Mitch, W. E. (1994) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1994.267.4.c955 · Cited by 182 · see citing works

Sensitivity and protein turnover response to glucocorticoids are different in skeletal muscle from adult and old rats. Lack of regulation of the ubiquitin-proteasome proteolytic pathway in aging.

Dardevet, D. P., Sornet, C., Taillandier, D., Savary‐Auzeloux, I., Attaix, D., & Grizard, J. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118264 · Cited by 174 · see citing works

Activation of the ubiquitin pathway in rat skeletal muscle by catabolic doses of glucocorticoids

Auclair, D., Garrel, D. R., Zerouala, A. C., & Ferland, L. H. (1997) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1997.272.3.c1007 · Cited by 161 · see citing works

Developmental Changes of the 26 S Proteasome in Abdominal Intersegmental Muscles of Manduca sexta during Programmed Cell Death

Reynolds, S. E., Billett, M. A., Gordon, C., Colleaux, L., Kloetzel, P. M., Tanaka, K., Dawson, S. P., Arnold, J. E., Mayer, N. J., & Mayer, R. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.4.1850 · Cited by 152 · see citing works

Ubiquitin gene expression is increased in skeletal muscle of tumour‐bearing rats

Llovera, M., Garcia‐Martínez, C., Agell, N., Marzábal, M., López-Soriano, F. J., & Argilés, J. M. A. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80290-4 · Cited by 133 · see citing works

Molecular cloning, sequence, and tissue distribution of the human ubiquitin-activating enzyme E1.

Handley, P., Mueckler, M. M., Siegel, N. R., Ciechanover, A. J., & Schwartz, A. L. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.1.258 · Cited by 130 · see citing works

14-kDa ubiquitin-conjugating enzyme: structure of the rat gene and regulation upon fasting and by insulin

Wing, S. S., & Banville, D. L. (1994) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1994.267.1.e39 · Cited by 123 · see citing works

Activation of the ubiquitin-ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy.

Medina, R., Wing, S. S., Haas, A., & Goldberg, A. L. (1991) · PubMed · Cited by 119 · see citing works

Burn injury stimulates multiple proteolytic pathways in skeletal muscle, including the ubiquitin-energy-dependent pathway.

Fang, C., Tiao, G. M., James, H. J., Ogle, C., Fischer, J. E., & Hasselgren, P. (1995) · PubMed · Cited by 100 · see citing works

The Ubiquitin System for Protein Degradation

Hershko, A. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.61.1.761 · Cited by 97 · see citing works

Sepsis-induced increase in muscle proteolysis is blocked by specific proteasome inhibitors

Hobler, S. C., Tiao, G. M., Fischer, J. E., Monaco, J. J., & Hasselgren, P.-O. (1998) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1998.274.1.r30 · Cited by 83 · see citing works

The Critical Role of the Ubiquitin-Proteasome Pathway in Muscle Wasting in Comparison to Lysosomal and Ca2+-Dependent Systems

Attaix, D., & Taillandier, D. (1998) · Advances in molecular and cell biology · doi:10.1016/s1569-2558(08)60463-4 · Cited by 69 · see citing works

Anti-TNF Treatment Reverts Increased Muscle Ubiquitin Gene Expression in Tumour-Bearing Rats

Llovera, M., Carbó, N., Garcia‐Martínez, C., Costelli, P., Tessitore, L., Baccino, F. M., Agell, N., Bagby, G. J., López-Soriano, F. J., & Argilés, J. M. A. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.0651 · Cited by 66 · see citing works

Insulin-like growth factor I stimulates degradation of an mRNA transcript encoding the 14 kDa ubiquitin-conjugating enzyme

Wing, S. S., & Bédard, N. (1996) · Biochemical Journal · doi:10.1042/bj3190455 · Cited by 55 · see citing works

Gastrointestinal tract protein synthesis and mRNA levels for proteolytic systems in adult fasted rats

Samuels, S. E., Taillandier, D., AUROUSSEAU, E., Cherel, Y., Maho, Y. L., Arnal, M., & Attaix, D. (1996) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1996.271.2.e232 · Cited by 51 · see citing works

No alteration in gene expression of components of the ubiquitin proteasome proteolytic pathway in dystrophin‐deficient muscles

Combaret, L., Taillandier, D., Voisin, L., Samuels, S., Boespflug‐Tanguy, O., & Attaix, D. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00910-6 · Cited by 45 · see citing works

Isolation, Characterization, and Partial Purification of a Novel Ubiquitin-Protein Ligase, E3

Gonen, H., Stancovski, I., Shkedy, D., Hadari, T., Bercovich, B., Bengal, E., Mesilati, S., Hatoum, O. A., Schwartz, A. L., & Ciechanover, A. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.1.302 · Cited by 39 · see citing works

Regulation of ATP-ubiquitin-dependent proteolysis in muscle wasting

Attaix, D., Taillandier, D., Temparis, S., Larbaud, D., AUROUSSEAU, E., Combaret, L., & Voisin, L. (1994) · annales de biologie animale biochimie biophysique · doi:10.1051/rnd:19940605 · Cited by 39 · see citing works

Euglycemic hyperinsulinemia and hyperaminoacidemia decrease skeletal muscle ubiquitin mRNA in goats

Larbaud, D., Debras, E., Taillandier, D., Samuels, S. E., Temparis, S., Champredon, C., Grizard, J., & Attaix, D. (1996) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1996.271.3.e505 · Cited by 31 · see citing works

Expression of subunits of the 19S complex and of the PA28 activator in rat skeletal muscle

Attaix, D., Taillandier, D., Combaret, L., Rallière, C., Larbaud, D., AUROUSSEAU, E., & Tanaka, K. (1997) · Molecular Biology Reports · doi:10.1023/a:1006806103675 · Cited by 30 · see citing works

Glucocorticoids Do Not Regulate the Expression of Proteolytic Genes in Skeletal Muscle from Cushing's Syndrome Patients

Rallière, C., Tauveron, I., Taillandier, D., Guy, L., Boiteux, J., Giraud, B., Attaix, D., & Thiéblot, P. (1997) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.82.9.4221 · Cited by 30 · see citing works

Differential Effects of Bovine PA28 on Six Peptidase Activities of the Lobster Muscle Proteasome (Multicatalytic Proteinase)

Mykles, D. L. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0009 · Cited by 27 · see citing works

Intracellular protein degradation.

Rivett, A. J. (1990) · PubMed · Cited by 24 · see citing works

Lobster Muscle Proteasome and the Degradation of Myofibrillar Proteins

Mykles, D. L. (2017) · Enzyme and Protein · doi:10.1159/000468681 · Cited by 17 · see citing works

A novel ATP-requiring protease from skeletal muscle that hydrolyzes non-ubiquitinated proteins

Fagan, J. M., & Waxman, L. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84653-7 · Cited by 14 · see citing works

Cancer cachexia: Developing multimodal therapy for a multidimensional problem

Fearon, K. C. H. (2008) · European Journal of Cancer · doi:10.1016/j.ejca.2008.02.033 · Cited by 444 · see citing works

Proteolytic and lipolytic responses to starvation

Finn, P. F., & Dice, J. F. (2006) · Nutrition · doi:10.1016/j.nut.2006.04.008 · Cited by 321 · see citing works

Trends in Postmortem Aging in Fish: Understanding of Proteolysis and Disorganization of the Myofibrillar Structure

Delbarre‐Ladrat, C., Chéret, R., Taylor, R. G., & Verrez‐Bagnis, V. (2006) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408390591000929 · Cited by 299 · see citing works

Modes of regulation of ubiquitin-mediated protein degradation

Kornitzer, D., & Ciechanover, A. J. (2000) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(200001)182:1 · Cited by 256 · see citing works

Mechanism of attenuation of skeletal muscle protein catabolism in cancer cachexia by eicosapentaenoic acid.

Whitehouse, A., Smith, H. J., Drake, J. L., & Tisdale, M. J. (2001) · PubMed · Cited by 226 · see citing works

Atrogin-1/MAFbx and MuRF1 are downregulated in aging-related loss of skeletal muscle

Edstrom, E., Altun, M., Hagglund, M., & Ulfhake, B. (2006) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/61.7.663 · Cited by 196 · see citing works

Inhibitors of the eukaryotic 20S proteasome core particle: a structural approach

Groll, M., & Huber, R. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.09.025 · Cited by 194 · see citing works

The Ubiquitin–Proteasome System in Regulation of the Skeletal Muscle Homeostasis and Atrophy: From Basic Science to Disorders

Kitajima, Y., Yoshioka, K., & Suzuki, N. (2020) · The Journal of Physiological Sciences · doi:10.1186/s12576-020-00768-9 · Cited by 171 · see citing works

Sarcopenia and cachexia: the adaptations of negative regulators of skeletal muscle mass

Sakuma, K., & Yamaguchi, A. (2012) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0052-4 · Cited by 137 · see citing works

NF-κB mediates proteolysis-inducing factor induced protein degradation and expression of the ubiquitin–proteasome system in skeletal muscle

Wyke, S. M., & Tisdale, M. J. (2005) · British Journal of Cancer · doi:10.1038/sj.bjc.6602402 · Cited by 130 · see citing works

Clenbuterol induces muscle-specific attenuation of atrophy through effects on the ubiquitin-proteasome pathway

Yimlamai, T., Dodd, S. L., Borst, S. E., & Park, S. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00448.2004 · Cited by 115 · see citing works

Proteasome Function in Aging and Oxidative Stress: Implications in Protein Maintenance Failure

Farout, L., & Friguet, B. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.205 · Cited by 112 · see citing works

Human protein metabolism: its measurement and regulation

Liu, Z., & Barrett, E. J. (2002) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00337.2002 · Cited by 112 · see citing works

Alterations in mRNA expression and protein products following spinal cord injury in humans

Urso, M. L., Chen, Y., Scrimgeour, A. G., Lee, P. C., Lee, K. F., & Clarkson, P. M. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2006.118042 · Cited by 111 · see citing works

Downregulation of ubiquitin-dependent proteolysis by eicosapentaenoic acid in acute starvation

Whitehouse, A. S., & Tisdale, M. J. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5209 · Cited by 100 · see citing works

p62/SQSTM1 but not LC3 is accumulated in sarcopenic muscle of mice

Sakuma, K., Kinoshita, M., Ito, Y., Aizawa, M., Aoi, W., & Yamaguchi, A. (2015) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12045 · Cited by 96 · see citing works

Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution 1 1Edited by P. E. Wright

Miura, T., Klaus, W., Gsell, B., Miyamoto, C., & Senn, H. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2859 · Cited by 93 · see citing works

Expression of the ubiquitin-proteasome pathway and muscle loss in experimental cancer cachexia

Khal, J., Wyke, S., Russell, S., Hine, A. V., & Tisdale, M. J. (2005) · British Journal of Cancer · doi:10.1038/sj.bjc.6602780 · Cited by 90 · see citing works

Development and evaluation of a sandwich ELISA for quantification of the 20S proteasome in human plasma

Dutaud, D., Aubry, L., Henry, L., Levieux, D., Hendil, K. B., Kuehn, L., Bureau, J. P., & Ouali, A. (2002) · Journal of Immunological Methods · doi:10.1016/s0022-1759(01)00555-5 · Cited by 85 · see citing works

Ubiquitin-proteasome-dependent proteolysis in rainbow trout ( Oncorhynchus mykiss ): effect of food deprivation

Martín, S., Blaney, S. M., Bowman, A. S., & Houlihan, D. F. (2002) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-002-0916-8 · Cited by 84 · see citing works

Epigallocatechin-3-gallate effectively attenuates skeletal muscle atrophy caused by cancer cachexia

Wang, H., Lai, Y.-J., Chan, Y.-L., Li, T., & Wu, C. (2011) · Cancer Letters · doi:10.1016/j.canlet.2011.02.023 · Cited by 83 · see citing works

The Ubiquitin-Proteasome System Is Indispensable for the Maintenance of Muscle Stem Cells

Kitajima, Y., Suzuki, N., Nunomiya, A., Osana, S., Yoshioka, K., Tashiro, Y., Takahashi, R., Ono, Y., Aoki, M., & Nagatomi, R. (2018) · Stem Cell Reports · doi:10.1016/j.stemcr.2018.10.009 · Cited by 75 · see citing works

Identification of the Immunoproteasome as a Novel Regulator of Skeletal Muscle Differentiation

Cui, Z., Hwang, S. M., & Gomes, A. V. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00622-13 · Cited by 69 · see citing works

Effects of Peripartum Propylene Glycol Supplementation on Nitrogen Metabolism, Body Composition, and Gene Expression for the Major Protein Degradation Pathways in Skeletal Muscle in Dairy Cows

Chibisa, G. E., Gozho, G. N., Kessel, A. G. V., Olkowski, A. A., & Mutsvangwa, T. (2008) · Journal of Dairy Science · doi:10.3168/jds.2007-0920 · Cited by 69 · see citing works

Myogenic and nonmyogenic cells differentially express proteinases, Hsc/Hsp70, and BAG-1 during skeletal muscle regeneration

Duguez, S., Bihan, M. L., Gouttefangeas, D., Féasson, L., & Freyssenet, D. G. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00331.2002 · Cited by 63 · see citing works

Molecular characterization of skeletal muscle atrophy in the R6/2 mouse model of Huntington's disease

She, P., Zhang, Z., Marchionini, D. M., Diaz, W. C., Jetton, T. J., Kimball, S. R., Vary, T. C., Lang, C. H., & Lynch, C. J. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00630.2010 · Cited by 59 · see citing works

Targeting the Ubiquitin E3 Ligase MuRF1 to Inhibit Muscle Atrophy

Eddins, M. J., Marblestone, J. G., Kumar, S., Leach, C. A., Sterner, D. E., Mattern, M. R., & Nicholson, B. (2011) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-011-9175-7 · Cited by 58 · see citing works

Basic Science Review: Nitric Oxide—Releasing Prosthetic Materials

Varu, V. N., Tsihlis, N. D., & Kibbe, M. R. (2008) · Vascular and Endovascular Surgery · doi:10.1177/1538574408322752 · Cited by 58 · see citing works

β-Sitosterol Attenuates Dexamethasone-Induced Muscle Atrophy via Regulating FoxO1-Dependent Signaling in C2C12 Cell and Mice Model

Hah, Y., Lee, W. K., Lee, S.-Y., Kim, E. J., Lee, J. H., Lee, S.-J., Ji, Y. H., Kim, S. G., Lee, H., Hong, S. Y., et al. (2022) · Nutrients · doi:10.3390/nu14142894 · Cited by 56 · see citing works

Role(s) of nucleoli and phosphorylation of ribosomal protein S6 and/or HSP27 in the regulation of muscle mass

Kawano, F., MATSUOKA, Y., Oke, Y., Higo, Y., Terada, M., Wang, X. D., Nakai, N., Fukuda, H., Imajoh‐Ohmi, S., & Ohira, Y. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00297.2006 · Cited by 56 · see citing works

Potential role of autophagy in modulation of lipid metabolism

Kovsan, J., Bashan, N., Greenberg, A. S., & Rudich, A. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00562.2009 · Cited by 54 · see citing works

Proteasome activity is altered in skeletal muscle tissue of tumour-bearing rats a leucine-rich diet

Ventrucci, G., de Mello, M. A. R., & Gomes‐Marcondes, M. C. C. (2004) · Endocrine Related Cancer · doi:10.1677/erc.1.00828 · Cited by 54 · see citing works

Reactive nitrogen species induce nuclear factor-κB-mediated protein degradation in skeletal muscle cells

Bar‐Shai, M., & Reznick, A. Z. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.02.009 · Cited by 53 · see citing works

Cancer cachexia syndrome in head and neck cancer patients: Part II. Pathophysiology

George, J. R., Cannon, T. Y., Lai, V., Richey, L., Zanation, A. M., Hayes, D. N., Shores, C., D, D. C. G., & Couch, M. E. (2007) · Head & Neck · doi:10.1002/hed.20630 · Cited by 49 · see citing works

Muscle protein turnover during early development in chickens divergently selected for growth rate

Tesseraud, S., Chagneau, A. M., & Grizard, J. (2000) · Poultry Science · doi:10.1093/ps/79.10.1465 · Cited by 48 · see citing works

Insulin-Like Growth Factor I Reduces Ubiquitin and Ubiquitin-Conjugating Enzyme Gene Expression but Does Not Inhibit Muscle Proteolysis in Septic Rats

Fang, C., Li, B.-G., Sun, X., & Hasselgren, P.-O. (2000) · Endocrinology · doi:10.1210/endo.141.8.7593 · Cited by 46 · see citing works

The Ubiquitin-Proteasome Proteolytic Pathway in Heart vs Skeletal Muscle: Effects of Acute Diabetes

Liu, Z., Miers, W. R., Wei, L., & Barrett, E. J. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3609 · Cited by 43 · see citing works

Genetic defects in acetylcholine signalling promote protein degradation in muscle cells of Caenorhabditis elegans

Szewczyk, N. J., Hartman, J. J., Barmada, S. J., & Jacobson, L. A. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.11.2003 · Cited by 43 · see citing works

Skeletal muscle protein mobilization during the progression of lactation

Clowes, E. J., AHERNE, F. X., & Baracos, V. E. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00198.2004 · Cited by 43 · see citing works

Modulation of intestinal protein synthesis and protease mRNA by luminal and systemic nutrients

Adegoke, O. A. J., McBurney, M. I., Samuels, S., & Baracos, V. E. (2003) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00402.2002 · Cited by 43 · see citing works

Insulin action on skeletal muscle protein metabolism during catabolic states

Grizard, J., Dardevet, D. P., Balage, M., Larbaud, D., Sinaud, S., Savary‐Auzeloux, I., Grzelkowska, K., Rochon, C., Tauveron, I., & Obled, C. (1999) · annales de biologie animale biochimie biophysique · doi:10.1051/rnd:19990104 · Cited by 38 · see citing works

Activation of Ras and the Mitogen-Activated Protein Kinase Pathway Promotes Protein Degradation in Muscle Cells of Caenorhabditis elegans

Szewczyk, N. J., Peterson, B. K., & Jacobson, L. A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.12.4181-4188.2002 · Cited by 36 · see citing works

Phosphodiesterase‐4 inhibition reduces proteolysis and atrogenes expression in rat skeletal muscles

Lira, E. C., Gonçalves, D. A. P., Parreiras‐e‐Silva, L. T., Zanon, N. M., Kettelhut, Í. D. C., & Navegantes, L. C. C. (2011) · Muscle & Nerve · doi:10.1002/mus.22066 · Cited by 32 · see citing works

Luminal Amino Acids Acutely Decrease Intestinal Mucosal Protein Synthesis and Protease mRNA in Piglets

Adegoke, O. A. J., McBurney, M. I., Samuels, S., & Baracos, V. E. (1999) · Journal of Nutrition · doi:10.1093/jn/129.10.1871 · Cited by 32 · see citing works

Alterations of proteasome activities in skeletal muscle tissue of diabetic rats

Merforth, S., Osmers, A., & Dahlmann, B. (1999) · Molecular Biology Reports · doi:10.1023/a:1006966005662 · Cited by 32 · see citing works

Does external pneumatic compression treatment between bouts of overreaching resistance training sessions exert differential effects on molecular signaling and performance-related variables compared to passive recovery? An exploratory study

Haun, C. T., Roberts, M. D., Romero, M. A., Osburn, S. C., Mobley, C. B., Anderson, R. G., Goodlett, M. D., Pascoe, D. D., & Martin, J. S. (2017) · PLoS ONE · doi:10.1371/journal.pone.0180429 · Cited by 31 · see citing works

Daily brief restraint stress alters signaling pathways and induces atrophy and apoptosis in rat skeletal muscle

Engelbrecht, A., Smith, C., Neethling, I., THOMAS, M. P., Ellis, B., Mattheyse, M., & Myburgh, K. H. (2009) · Stress · doi:10.3109/10253890903089834 · Cited by 31 · see citing works

Biomarkers for cancer cachexia: is there also a genetic component to cachexia?

Tan, B. H. L., Deans, D. A. C., Skipworth, R. J. E., Ross, J. A., & Fearon, K. C. H. (2007) · Supportive Care in Cancer · doi:10.1007/s00520-007-0367-z · Cited by 30 · see citing works

Peroxynitrite Induces an Alternative NF-κB Activation Pathway in L8 Rat Myoblasts

Bar‐Shai, M., & Reznick, A. Z. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.639 · Cited by 30 · see citing works

On our way to targeted therapy for cachexia in cancer?

Boddaert, M. S. A., Gerritsen, W. R., & Pinedo, H. M. (2006) · Current Opinion in Oncology · doi:10.1097/01.cco.0000228738.85626.ac · Cited by 30 · see citing works

Alteration of 20S proteasome-subtypes and proteasome activator PA28 in skeletal muscle of rat after induction of diabetes mellitus

Merforth, S., Kuehn, L., Osmers, A., & Dahlmann, B. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(02)00381-3 · Cited by 30 · see citing works

Therapeutic considerations of sarcopenia in heart failure patients

Saitoh, M., Ebner, N., von Haehling, S., Anker, S. D., & Springer, J. (2018) · Expert Review of Cardiovascular Therapy · doi:10.1080/14779072.2018.1424542 · Cited by 26 · see citing works

Eating for two: Consequences of parental methionine nutrition on offspring metabolism in rainbow trout (Oncorhynchus mykiss)

Seiliez, I., Vélez, E. J., Lutfi, E., Dias, K., Plagnes‐Juan, E., Marandel, L., Panserat, S., Geurden, I., & Cassy, S. (2017) · Aquaculture · doi:10.1016/j.aquaculture.2017.01.010 · Cited by 25 · see citing works

Lifelong Caloric Restriction and Interleukin-6 Secretion From Adipose Tissue: Effects on Physical Performance Decline in Aged Rats

You, T., Sonntag, W. E., Leng, X., & Carter, C. S. (2007) · The Journals of Gerontology Series A · doi:10.1093/gerona/62.10.1082 · Cited by 25 · see citing works

Down-regulation of the ubiquitin–proteasome proteolysis system by amino acids and insulin involves the adenosine monophosphate-activated protein kinase and mammalian target of rapamycin pathways in rat hepatocytes

Chotechuang, N., Azzout-Marniche, D., Bos, C., Chaumontet, C., Gaudichon, C., & Tomé, D. (2011) · Amino Acids · doi:10.1007/s00726-010-0765-2 · Cited by 24 · see citing works

Maternal vitamin D deficiency causes smaller muscle fibers and altered transcript levels of genes involved in protein degradation, myogenesis, and cytoskeleton organization in the newborn rat

Max, D., Brandsch, C., Schumann, S., Kühne, H., Frommhagen, M., Schutkowski, A., Hirche, F., Staege, M. S., & Stangl, G. I. (2013) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201300360 · Cited by 24 · see citing works

Effects of Fasting and Refeeding on Expression of Proteolytic-Related Genes in Skeletal Muscle of Chicks

Nakashima, K., Komatsu, T., Yamazaki, M., & Abé, H. (2005) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.51.248 · Cited by 24 · see citing works

The effects of age, energy and protein intake on protein turnover and the expression of proteolysis-related genes in the broiler breeder hen

Ekmay, R. D., Salas, C., England, J., Cerrate, S., & Coon, C. N. (2012) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2012.10.002 · Cited by 22 · see citing works

Activation of skeletal muscle protein breakdown following consumption of soyabean protein in pigs

Löhrke, B., Saggau, E., Schadereit, R., Beyer, M., Bellmann, O., Kuhla, S., & Hagemeister, H. (2001) · British Journal Of Nutrition · doi:10.1079/bjn2000291 · Cited by 22 · see citing works

Myofibril-bound serine protease and its endogenous inhibitor in mouse: extraction, partial characterization and effect on myofibrils

Sangorrín, M. P., Martone, C. B., & Sanchez, J. J. (2002) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/s1096-4959(01)00510-3 · Cited by 22 · see citing works

Chronic Metabolic Acidosis Increases mRNA Levels for Components of the Ubiquitin-Mediated Proteolytic Pathway in Skeletal Muscle of Dairy Cows

Gilmore, J., Squires, J. E., McBride, B. W., Mutsvangwa, T., & Lindinger, M. I. (2004) · Journal of Nutrition · doi:10.1093/jn/134.3.558 · Cited by 21 · see citing works

Roles and potential therapeutic targets of the ubiquitin proteasome system in muscle wasting

Nury, D., Doucet, C. M., & Coux, O. (2007) · BMC Biochemistry · doi:10.1186/1471-2091-8-s1-s7 · Cited by 21 · see citing works

A Leucine-Rich Diet Modulates the Tumor-Induced Down-Regulation of the MAPK/ERK and PI3K/Akt/mTOR Signaling Pathways and Maintains the Expression of the Ubiquitin-Proteasome Pathway in the Placental Tissue of NMRI Mice1

Viana, L. R., & Gomes‐Marcondes, M. C. C. (2014) · Biology of Reproduction · doi:10.1095/biolreprod.114.123307 · Cited by 20 · see citing works

High‐intensity interval training changes the expression of muscle RING‐finger protein‐1 and muscle atrophy F‐box proteins and proteins involved in the mechanistic target of rapamycin pathway and autophagy in rat skeletal muscle

Cui, X., Zhang, Y., Wang, Z., Yu, J., Kong, Z., & Ružić, L. (2019) · Experimental Physiology · doi:10.1113/ep087601 · Cited by 21 · see citing works

Impact of cancer cachexia on respiratory muscle function and the therapeutic potential of exercise

Murphy, B. T., Mackrill, J. J., & O’Halloran, K. D. (2022) · The Journal of Physiology · doi:10.1113/jp283569 · Cited by 20 · see citing works

Prosomes Form Sarcomere-like Banding Patterns in Skeletal, Cardiac, and Smooth Muscle Cells

Foucrier, J., Bassaglia, Y., Grand, M.-C., Rothen‐Rutishauser, B., Perriard, J., & Scherrer, K. (2001) · Experimental Cell Research · doi:10.1006/excr.2001.5212 · Cited by 16 · see citing works

Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy

Kitajima, Y., Suzuki, N., Yoshioka, K., Izumi, R., Tateyama, M., Tashiro, Y., Takahashi, R., Aoki, M., & Ono, Y. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00859 · Cited by 14 · see citing works

Identification of a myofibril-bound serine protease and its endogenous inhibitor in mouse skeletal muscle

Sangorrín, M. P., Martone, C. B., & Sanchez, J. J. (2000) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(00)00055-8 · Cited by 13 · see citing works

Anabolic and catabolic mediators of intestinal protein turnover: a new experimental approach

Baracos, V. E., Samuels, S., & Adegoke, O. A. J. (2000) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-200005000-00004 · Cited by 11 · see citing works

The 26S proteasome of the lignin-degrading Basidiomycete Phlebia radiata

Staszczak, M. (2006) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2006.05.005 · Cited by 11 · see citing works

Aging/Tenderization Mechanisms

BOWKER, B. C., Eastridge, J. S., PAROCZAY, E. W., CALLAHAN, J. A., & Solomon, M. B. (2010) · doi:10.1002/9780813820897.ch4 · Cited by 11 · see citing works

Ubiquitin gene expression and ubiquitin conjugation in chicken muscle do not reflect differences in growth rate between broiler and layer birds.

Harper, J. M. M., Mee, M., Arnold, J. E., Boorman, K. N., Mayer, R. J., & BUTTERY, P. J. (1999) · Journal of Animal Science · doi:10.2527/1999.7771702x · Cited by 10 · see citing works

Chapter 3 Whole animal and tissue proteolysis in growing animals

(2005) · Biology of growing animals · doi:10.1016/s1877-1823(09)70010-4 · Cited by 10 · see citing works

Ubiquitin- and proteasome-dependent pathway of protein degradation as an emerging therapeutic target

Wójcik, C. (2000) · Emerging Therapeutic Targets · doi:10.1517/14728222.4.1.89 · Cited by 10 · see citing works

Ultrastructural findings at the satellite cell-myofiber border in normal and diseased human muscle biopsy specimens

Laule, S., & Bornemann, A. (2001) · Acta Neuropathologica · doi:10.1007/s004010000302 · Cited by 9 · see citing works

Dietary Plant Extracts in Improving Skeletal Muscle Development and Metabolic Function

Xiang, J., Du, ‬., & Wang, H. (2022) · Food Reviews International · doi:10.1080/87559129.2022.2087669 · Cited by 8 · see citing works

Proteins and Amino Acids

(2007) · Nutrition in exercise and sport · doi:10.1201/9781420043815.ch1 · Cited by 7 · see citing works

Catabolism of Skeletal Muscle Proteins and Its Reversal in Cancer Cachexia

Tisdale, M. J. (2000) · KARGER eBooks · doi:10.1159/000061828 · Cited by 6 · see citing works

The Mouse Psma1 Gene Coding for the α-Type C2 Proteasome Subunit: Structural and Functional Analysis, Mapping, and Colocalization with Pde3b on Mouse Chromosome 7

Hopitzan, A. A., Himmelbauer, H., Spevak, W., & Castañón, M. J. (2000) · Genomics · doi:10.1006/geno.2000.6217 · Cited by 6 · see citing works

Diet-Induced Obesity and Insulin Resistance Spur Tumor Growth and Cancer Cachexia in Rats Bearing the Yoshida Sarcoma

Honors, M. A., & Kinzig, K. P. (2014) · Nutrition and Cancer · doi:10.1080/01635581.2014.916325 · Cited by 5 · see citing works

In Vitro Toxicological Assessment of Heavy Metals and Intracellular Mechanisms of Toxicity

Parris, W. E., & Adeli, K. (2002) · CRC Press eBooks · doi:10.1201/9780203909300.ch3 · Cited by 5 · see citing works

Interleukin-1 up-regulates the expression and activity of 26S proteasome in burned rat

Ni, B., Jianxin, Z., Dong, Y., Jiahe, P., Wu, X., Li, R., Chen, M., Zhou, C., Tan, Y., & Wu, Y. (2007) · Burns · doi:10.1016/j.burns.2006.08.019 · Cited by 5 · see citing works

Potential intracellular targets for anabolic/anti-catabolic therapies

Palmer, R. M., & Thompson, M. G. (1999) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-199905000-00004 · Cited by 4 · see citing works

Muscle Growth, Repair and Preservation

Erskine, R. M., & Degens, H. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-396454-0.00025-4 · Cited by 3 · see citing works

Cachexie cancéreuse : bases physiopathologiques

Lerebours, É., Déchelotte, P., & Michel, P. (2001) · Nutrition Clinique et Métabolisme · doi:10.1016/s0985-0562(01)00083-8 · Cited by 3 · see citing works

Is there a volume saturation point for muscle hypertrophy in resistance-trained individuals? A narrative review

Camargo, J. B. B., Bittencourt, D., da Silva, D. G., Bergamasco, J. G. A., Michel, J. M., Roberts, M. D., & Libardi, C. A. (2025) · European Journal of Applied Physiology · doi:10.1007/s00421-025-05959-z · Cited by 2 · see citing works

Assessment of Protein Status in Athletes

Phillips, S. M. (2002) · CRC Press eBooks · doi:10.1201/9781420041323.ch12 · Cited by 2 · see citing works

Muscle deteriorations become prominent within 24 hours after admission in severely burned adults

Martini, W. Z., Yu, Y., Chung, K. K., & Dubick, M. A. (2021) · The Journal of Trauma: Injury, Infection, and Critical Care · doi:10.1097/ta.0000000000003285 · Cited by 1 · see citing works

Assessment of Protein Status in Athletes

Driskell, J. A., & Wolinsky, I. (2002) · CRC Press eBooks · doi:10.1201/9781420041323-18 · Cited by 1 · see citing works

THE EFFECTS OF HINDLIMB UNWEIGHTING AND BETA 2-AGONIST ON THE UBIQUITIN-PROTEASOME PATHWAY AND INSULIN-LIKE GROWTH FACTOR I

Yimlamai, T. (2004) · Cited by 1 · see citing works

Old-age muscle atrophy : Cellular mechanisms and behavioral consequenses

Altun, M. (2007) · Figshare

The Effects of Aging on Muscle Loss and Nuclear Factor Kappa-B Levels in Rats Fed a Diet Containing Suboptimal Leucine Levels

Kohlen, C. R. (2009) · doi:10.15368/theses.2009.3

New Knowledge About Protein

Lifschitz, C. H. (2001) · CRC Press eBooks · doi:10.1201/b14018-4

Le contrôle de la protéolyse, régulation majeure qualitative et quantitative

Leverve, X. M. (2001) · Nutrition Clinique et Métabolisme · doi:10.1016/s0985-0562(00)00039-x

Facteurs lipolytiques et protéolytiques de la cachexie cancéreuse

Tisdale, M. J. (2001) · Nutrition Clinique et Métabolisme · doi:10.1016/s0985-0562(01)00086-3

Molecular Changes Following Skeletal Muscle Disuse in Humans

Reich, K. A. (2022) · ScholarWorks@UMassAmherst (University of Massachusetts Amherst) · doi:10.7275/1079181

Analysis of cell division in cardiomyocytes during development and disease

Ahuja, P. (2006) · Repository for Publications and Research Data (ETH Zurich) · doi:10.3929/ethz-a-005171711

Métabolisme énergétique au cours de la cachexie cancereuse

Johnson, G. (2007) · OpenGrey (Institut de l'Information Scientifique et Technique)

Major Processes for Muscle Gain and Loss

(2010) · CRC Press eBooks · doi:10.1201/ebk1439813621-c5

Protein Turnover in Rat Skeletal Muscle During In Vitro Hypo-Osmotic Stress

Darling, R. (2012) · Brock University Digital Repository (Brock University)

The Critical Role of the Ubiquitin-Proteasome Pathway in Muscle Wasting in Comparison to Lysosomal and Ca2+-Dependent Systems

Attaix, D., & Taillandier, D. (1998) · Advances in molecular and cell biology · doi:10.1016/s1569-2558(08)60463-4 · Cited by 69 · see citing works

The role of ubiquitin–proteasome-dependent proteolysis in the remodelling of skeletal muscle

Taillandier, D., Combaret, L., Pouch-Pélissier, M.-N., Samuels, S., Béchet, D., & Attaix, D. (2004) · Proceedings of The Nutrition Society · doi:10.1079/par2004358 · Cited by 86 · see citing works

Regulation of ATP-ubiquitin-dependent proteolysis in muscle wasting

Attaix, D., Taillandier, D., Temparis, S., Larbaud, D., AUROUSSEAU, E., Combaret, L., & Voisin, L. (1994) · annales de biologie animale biochimie biophysique · doi:10.1051/rnd:19940605 · Cited by 39 · see citing works

Mechanisms of ubiquitination and proteasome-dependent proteolysis in skeletal muscle.

Attaix, D., Combaret, L., Kee, A. J., & Taillandier, D. (2003) · CABI Publishing eBooks · doi:10.1079/9780851996790.0219 · Cited by 23 · see citing works

The ubiquitin-dependent proteolytic pathway in skeletal muscle: its role in pathological states

Argilés, J. M. A., & López-Soriano, F. J. (1996) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(96)10021-3 · Cited by 74 · see citing works