Patterns of gene expression in atrophying skeletal muscles: response to food deprivation

Identification of ubiquitin ligases required for skeletal muscle atrophy.

Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., et al. (2001) · Science · doi:10.1126/science.1065874 · Cited by 3,521

Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo

Bodine, S. C., Stitt, T. N., Gonzalez, M., Kline, W. O., Stover, G. L., Bauerlein, R., Zlotchenko, E., Scrimgeour, A., Lawrence, J. C., Glass, D. J., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1014 · Cited by 2,752

Obesity and the regulation of energy balance

Spiegelman, B. M., & Flier, J. S. (2001) · Cell · doi:10.1016/s0092-8674(01)00240-9 · Cited by 2,398

Aggresomes, inclusion bodies and protein aggregation

Kopito, R. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01852-3 · Cited by 1,942

Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy

Gomes, M. D., Lecker, S. H., Jagoe, R. T., Navon, A., & Goldberg, A. L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251541198 · Cited by 1,774

Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways

Rommel, C., Bodine, S. C., Clarke, B. A., Rossman, R., Nunez, L., Stitt, T. N., Yancopoulos, G. D., & Glass, D. J. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1009 · Cited by 1,583

Regulation of translation initiation by FRAP/mTOR

Gingras, A.-C., Raught, B., & Sonenberg, N. (2001) · Genes & Development · doi:10.1101/gad.887201 · Cited by 1,545

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

Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A

Richard, I., Broux, O., Allamand, V., Fougerousse, F., Chiannilkulchai, N., Bourg, N., Brenguier, L., Devaud, C., Pasturaud, P., Roudaut, C., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90368-2 · Cited by 998

Importance of replication in microarray gene expression studies: Statistical methods and evidence from repetitive cDNA hybridizations

Lee, M. T., Kuo, F. C., Whitmore, G. A., & Sklar, J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.18.9834 · Cited by 861

Pathways from glutamine to apoptosis

Matés, J. M. (2006) · Frontiers in bioscience · doi:10.2741/2040 · Cited by 75

Gene expression changes controlling distinct adaptations in the heart and skeletal muscle of a hibernating mammal

Vermillion, K. L., Anderson, K. J., Hampton, M. E., & Andrews, M. T. (2015) · Physiological Genomics · doi:10.1152/physiolgenomics.00108.2014 · Cited by 77

Transcriptional reprogramming and ultrastructure during atrophy and recovery of mouse soleus muscle

Däpp, C., Schmutz, S., Hoppeler, H. H., & Flück, M. (2004) · Physiological Genomics · doi:10.1152/physiolgenomics.00100.2004 · Cited by 73

Denervation in murine fast-twitch muscle: short-term physiological changes and temporal expression profiling

Raffaello, A., Laveder, P., Romualdi, C., Bean, C., Toniolo, L., Germinario, E., Megighian, A., Danieli‐Betto, D., Reggiani, C., & Lanfranchi, G. (2005) · Physiological Genomics · doi:10.1152/physiolgenomics.00051.2005 · Cited by 75

Cisplatin triggers atrophy of skeletal C2C12 myotubes via impairment of Akt signalling pathway and subsequent increment activity of proteasome and autophagy systems

Fanzani, A., Zanola, A., Rovetta, F., Rossi, S., & Aleo, M. F. (2010) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2010.11.003 · Cited by 73

Comparative proteomic profile of rat sciatic nerve and gastrocnemius muscle tissues in ageing by 2‐D DIGE

Capitanio, D., Vasso, M., Fania, C., Moriggi, M., Viganò, A., Procacci, P., Magnaghi, V., & Gelfi, C. (2009) · PROTEOMICS · doi:10.1002/pmic.200701162 · Cited by 72

Increased expression of Myosin binding protein H in the skeletal muscle of amyotrophic lateral sclerosis patients

Conti, A., Riva, N., Pesca, M., Iannaccone, S., Cannistraci, C. V., Corbo, M., Previtali, S. C., Quattrini, A., & Alessio, M. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.10.013 · Cited by 68

17β-Estradiol Represses Myogenic Differentiation by Increasing Ubiquitin-specific Peptidase 19 through Estrogen Receptor α

Ogawa, M., Yamaji, R., Higashimura, Y., Harada, N., Ashida, H., Nakano, Y., & Inui, H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.276824 · Cited by 71

Ubiquitin-protein ligases in muscle wasting: multiple parallel pathways?

Lecker, S. H. (2003) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/01.mco.0000068963.34812.e5 · Cited by 71

Skeletal muscle subsarcolemmal mitochondrial dysfunction in high-fat fed rats exhibiting impaired glucose homeostasis

Lionetti, L., Mollica, M. P., Crescenzo, R., D’Andrea, E., Ferraro, M., Bianco, F., Liverini, G., & Iossa, S. (2007) · International Journal of Obesity · doi:10.1038/sj.ijo.0803636 · Cited by 71

AMP-Activated Protein Kinase Regulates E3 Ligases in Rodent Heart

Baskin, K. K., & Taegtmeyer, H. (2011) · Circulation Research · doi:10.1161/circresaha.111.252742 · Cited by 71

Relationships between circadian rhythms and modulation of gene expression by glucocorticoids in skeletal muscle

Almon, R. R., Yang, E., Lai, W., Androulakis, I. P., Ghimbovschi, S. D., Hoffman, E. P., Jusko, W. J., & DuBois, D. C. (2008) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.90399.2008 · Cited by 70

Regrowth of Skeletal Muscle Atrophied from Inactivity

Machida, S., & Booth, F. W. (2004) · Medicine & Science in Sports & Exercise · doi:10.1249/01.mss.0000106175.24978.84 · Cited by 70

Transcriptional profile of a myotube starvation model of atrophy

Stevenson, E. J., Koncarevic, A., Giresi, P. G., Jackman, R. W., & Kandarian, S. C. (2004) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01055.2004 · Cited by 71

Differential network analysis for the identification of condition-specific pathway activity and regulation

Gambardella, G., Moretti, M. N., Cegli, R. D., Cardone, L., Peron, A., & di Bernardo, D. (2013) · Bioinformatics · doi:10.1093/bioinformatics/btt290 · Cited by 69

Meta-analysis of expression signatures of muscle atrophy: gene interaction networks in early and late stages

Calura, E., Cagnin, S., Raffaello, A., Laveder, P., Lanfranchi, G., & Romualdi, C. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-630 · Cited by 67

Skeletal muscle atrogenes: From rodent models to human pathologies

Taillandier, D., & Polge, C. (2019) · Biochimie · doi:10.1016/j.biochi.2019.07.014 · Cited by 66

Integrated genomic and proteomic analyses identify stimulus-dependent molecular changes associated with distinct modes of skeletal muscle atrophy

Hunt, L. C., Graça, F. A., Pagala, V., Wang, Y., Li, Y., Yuan, Z., Fan, Y., Labelle, M., Peng, J., & Demontis, F. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109971 · Cited by 74

A hypoxia complement differentiates the muscle response to endurance exercise

Schmutz, S., Däpp, C., Wittwer, M., Durieux, A., Müeller, M., Weinstein, F. V., Vogt, M., Hoppeler, H. H., & Flück, M. (2010) · Experimental Physiology · doi:10.1113/expphysiol.2009.051029 · Cited by 66

Combined cDNA array/RT‐PCR analysis of gene expression profile in rat gastrocnemius muscle: relation to its adaptive function in energy metabolism during fasting

de Lange, P., Ragni, M., Silvestri, E., Moreno, M., Schiavo, L., Lombardi, A., Farina, P., Feola, A., Goglia, F., & Lanni, A. (2003) · The FASEB Journal · doi:10.1096/fj.03-0342fje · Cited by 67

Age-Related Dysfunction in Proteostasis and Cellular Quality Control in the Development of Sarcopenia

Paez, H. G., Pitzer, C. R., & Alway, S. E. (2023) · Cells · doi:10.3390/cells12020249 · Cited by 71

Cigarette smoke‐induced skeletal muscle atrophy is associated with up‐regulation of USP‐19 via p38 and ERK MAPKs

Liu, Q., Xu, W., Luo, Y., Han, F., Yao, X., Yang, T., Zhang, Y., Pi, W., & Guo, X. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23151 · Cited by 66

Insulin-Like Growth Factor I: The Yin and Yang of Muscle Atrophy

Heszele, M. F. C., & Price, S. R. (2004) · Endocrinology · doi:10.1210/en.2004-1037 · Cited by 64

Molecular characterization of atrogin-1/F-box protein-32 (FBXO32) and F-box protein-25 (FBXO25) in rainbow trout (Oncorhynchus mykiss): Expression across tissues in response to feed deprivation

Cleveland, B. M., & Evenhuis, J. P. (2010) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2010.06.010 · Cited by 64

Myofibril breakdown during atrophy is a delayed response requiring the transcription factor PAX4 and desmin depolymerization

Volodin, A., Kosti, I., Goldberg, A. L., & Cohen, S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1612988114 · Cited by 62

Identification of 1- and 3-methylhistidine as biomarkers of skeletal muscle toxicity by nuclear magnetic resonance-based metabolic profiling

Aranı́bar, N., Vassallo, J. D., Rathmacher, J. A., Stryker, S. A., Zhang, Y., Dai, J., Janovitz, E. B., Robertson, D., Reily, M. D., Lowe‐Krentz, L. J., et al. (2010) · Analytical Biochemistry · doi:10.1016/j.ab.2010.11.023 · Cited by 60

Myostatin expression is increased by food deprivation in a muscle-specific manner and contributes to muscle atrophy during prolonged food deprivation in mice

Allen, D. L., Cleary, A. S., Lindsay, S. F., Loh, A. S., & Reed, J. M. (2010) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00504.2010 · Cited by 61

The Preventive Effect of β-Carotene on Denervation-Induced Soleus Muscle Atrophy in Mice

Ogawa, M., Kariya, Y., Kitakaze, T., Yamaji, R., Harada, N., Sakamoto, T., Hosotani, K., Nakano, Y., & Inui, H. (2013) · British Journal Of Nutrition · doi:10.1017/s0007114512003297 · Cited by 58

Fasting induces a biphasic adaptive metabolic response in murine small intestine

Sokolović, M., Wehkamp, D., Sokolović, A., Vermeulen, J. L. M., Gilhuijs-Pederson, L. A., van Haaften, R. I. M., Nikolsky, Y., Evelo, C. T., van Kampen, A. H. C., Hakvoort, T. B. M., et al. (2007) · BMC Genomics · doi:10.1186/1471-2164-8-361 · Cited by 58

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 60

Distinct protein degradation profiles are induced by different disuse models of skeletal muscle atrophy

Bialek, P., Morris, C., Parkington, J., St. Andre, M., Owens, J., Yaworsky, P., Seeherman, H., & Jelinsky, S. A. (2011) · Physiological Genomics · doi:10.1152/physiolgenomics.00247.2010 · Cited by 57

Interorgan Coordination of the Murine Adaptive Response to Fasting

Hakvoort, T. B. M., Moerland, P. D., Frijters, R., Sokolović, A., Labruyère, W. T., Vermeulen, J. L. M., van Themaat, E. V. L., Breit, T. M., Wittink, F. R. A., van Kampen, A. H. C., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.216986 · Cited by 56

Ubiquitin ligases MuRF1 and MAFbx in human skeletal muscle atrophy

de Palma, L., Marinelli, M., Pavan, M., & Orazi, A. (2007) · Joint Bone Spine · doi:10.1016/j.jbspin.2007.04.019 · Cited by 57

Insulin/IGF1 signalling mediates the effects of β2‐adrenergic agonist on muscle proteostasis and growth

Gonçalves, D. A., Silveira, W. A., Manfredi, L. H., Graça, F. A., Armani, A., Bertaggia, E., O´Neill, B. T., Lautherbach, N., Machado, J., Nogara, L., et al. (2019) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12395 · Cited by 56

Increased transcription of ubiquitin–proteasome system components: molecular responses associated with muscle atrophy

Price, S. R. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(02)00385-0 · Cited by 57

The role of TGF-β signaling in muscle atrophy, sarcopenia and cancer cachexia

Lan, X., Deng, C., Wang, Q., Zhao, L., Jiao, B., & Xiang, Y. (2024) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2024.114513 · Cited by 61

The possible role of myostatin in skeletal muscle atrophy and cachexia

Jespersen, J., Kjær, M., & Schjerling, P. (2005) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/j.1600-0838.2005.00498.x · Cited by 55

Ketogenic diet induces skeletal muscle atrophy via reducing muscle protein synthesis and possibly activating proteolysis in mice

Nakao, R., Abe, T., Yamamoto, S., & Oishi, K. (2019) · Scientific Reports · doi:10.1038/s41598-019-56166-8 · Cited by 55

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

Conditional over-expression of PITX1 causes skeletal muscle dystrophy in mice

Pandey, S. N., Cabotage, J., Shi, R., Dixit, M., Sutherland, M., Liu, J., Muger, S., Harper, S. Q., Nagaraju, K., & Chen, Y. (2012) · Biology Open · doi:10.1242/bio.20121305 · Cited by 54

Acute daily psychological stress causes increased atrophic gene expression and myostatin-dependent muscle atrophy

Allen, D. L., McCall, G. E., Loh, A. S., Madden, M. C., & Mehan, R. S. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00296.2010 · Cited by 55

CRISPR/Cas9-Mediated miR-29b Editing as a Treatment of Different Types of Muscle Atrophy in Mice

Li, J., Wang, L., Hua, X., Tang, H., Chen, R., Yang, T., Das, S., & Xiao, J. (2020) · Molecular Therapy · doi:10.1016/j.ymthe.2020.03.005 · Cited by 54

Microarray analysis of the temporal response of skeletal muscle to methylprednisolone: comparative analysis of two dosing regimens

Almon, R. R., DuBois, D. C., Yao, Z., Hoffman, E. P., Ghimbovschi, S. D., & Jusko, W. J. (2007) · Physiological Genomics · doi:10.1152/physiolgenomics.00242.2006 · Cited by 52

The inhibition of glutamine synthetase sensitizes human sarcoma cells to l-asparaginase

Tardito, S., Uggeri, J., Bozzetti, C., Bianchi, M. G., Rotoli, B. M., Franchi‐Gazzola, R., Gazzola, G. C., Gatti, R., & Bussolati, O. (2007) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-007-0421-z · Cited by 51

Daily Variations in Dietary Lysine Content Alter the Expression of Genes Related to Proteolysis in Chicken Pectoralis major Muscle

Tesseraud, S., Bouvarel, I., Collin, A., Cailleau-Audouin, E., Crochet, S., Seiliez, I., & Leterrier, C. (2008) · Journal of Nutrition · doi:10.3945/jn.108.095752 · Cited by 50

Avoidance of Skeletal Muscle Atrophy in Spontaneous and Facultative Hibernators

Cotton, C. J., & Harlow, H. J. (2010) · Physiological and Biochemical Zoology · doi:10.1086/650471 · Cited by 49

Molecular Insights into Muscle Homeostasis, Atrophy and Wasting

Scicchitano, B. M., Dobrowolny, G., Sica, G., & Musarò, A. (2018) · Current Genomics · doi:10.2174/1389202919666180101153911 · Cited by 52

Proteomic analysis of altered protein expression in skeletal muscle of rats in a hypermetabolic state induced by burn sepsis

Duan, X., Francois Berthiaume, B., Yarmush, D. M., & Yarmush, M. L. (2006) · Biochemical Journal · doi:10.1042/bj20051710 · Cited by 48

Foxo1 represses expression of musclin, a skeletal muscle-derived secretory factor

Yasui, A., Nishizawa, H., Okuno, Y., Morita, K., Kobayashi, H., Kawai, K., Matsuda, M., Kishida, K., Kihara, S., Kamei, Y., et al. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.10.013 · Cited by 46

Regulation of muscle atrophy-related genes by the opposing transcriptional activities of ZEB1/CtBP and FOXO3

Ninfali, C., Siles, L., Darling, D. S., & Postigo, A. A. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky835 · Cited by 45

Systemic responses to inhaled ozone in mice: cachexia and down-regulation of liver xenobiotic metabolizing genes

Last, J. A., Gohil, K., Mathrani, V. C., & Kenyon, N. J. (2005) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2005.02.001 · Cited by 45

Transcriptional reprogramming during reloading of atrophied rat soleus muscle

Flück, M., Schmutz, S., Wittwer, M., Hoppeler, H., & Desplanches, D. (2005) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00833.2004 · Cited by 44

Catabolic Signaling Pathways, Atrogenes, and Ubiquitinated Proteins Are Regulated by the Nutritional Status in the Muscle of the Fine Flounder

Fuentes, E. N., Ruíz, P., Valdés, J. A., & Molina, A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044256 · Cited by 44

Effects of energy deficit, dietary protein, and feeding on intracellular regulators of skeletal muscle proteolysis

Carbone, J. W., Margolis, L. M., McClung, J. P., Cao, J. J., Murphy, N. E., Sauter, E. R., Combs, G. F., Young, A. J., & Pasiakos, S. M. (2013) · The FASEB Journal · doi:10.1096/fj.13-239228 · Cited by 43

Identification of functional glucocorticoid response elements in the mouse FoxO1 promoter

Qin, W., Pan, J., Qin, Y., Lee, D. N., Bauman, W. A., & Cardozo, C. P. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.06.080 · Cited by 43

Hypoxia transiently affects skeletal muscle hypertrophy in a functional overload model

Chaillou, T., Koulmann, N., Simler, N., Meunier, A., Serrurier, B., Chapot, R., Peinnequin, A., Beaudry, M., & Bigard, X. A. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00262.2011 · Cited by 45

Supplementation of carnitine leads to an activation of the IGF-1/PI3K/Akt signalling pathway and down regulates the E3 ligase MuRF1 in skeletal muscle of rats

Keller, J., Couturier, A., Haferkamp, M., Most, E., & Eder, K. (2013) · Nutrition & Metabolism · doi:10.1186/1743-7075-10-28 · Cited by 43

Transcriptional profiling of tissue plasticity: role of shifts in gene expression and technical limitations

Flück, M., Däpp, C., Schmutz, S., Wit, E. C., & Hoppeler, H. H. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00050.2005 · Cited by 43

Small molecule adiponectin receptor agonist GTDF protects against skeletal muscle atrophy

Singh, A. K., Shree, S., Chattopadhyay, S., Kumar, S., Gurjar, A., Kushwaha, S., Kumar, H., Trivedi, A. K., Chattopadhyay, N., Maurya, R., et al. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.09.013 · Cited by 42

The clinical relevance and mechanism of skeletal muscle wasting

Duan, K., Gao, X., & Zhu, D. (2020) · Clinical Nutrition · doi:10.1016/j.clnu.2020.07.029 · Cited by 44

Caspase 1 deficiency reduces inflammation-induced brain transcription

Mastronardi, C. A., Whelan, F., Yildiz, O. A., Hannestad, J. O., Elashoff, D. A., McCann, S. M., Licinio, J., & Wong, M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701366104 · Cited by 42

Small Molecular Weight Soybean Protein-Derived Peptides Nutriment Attenuates Rat Burn Injury-Induced Muscle Atrophy by Modulation of Ubiquitin-Proteasome System and Autophagy Signaling Pathway

Zhao, F., Yu, Y., Liu, W., Zhang, J., Liu, X., Liu, L., & Yin, H. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b05387 · Cited by 41

Identification of cold-shock protein RBM3 as a possible regulator of skeletal muscle size through expression profiling

Dupont‐Versteegden, E. E., Nagarajan, R., Beggs, M. L., Bearden, E. D., Simpson, P. M., & Peterson, C. A. (2008) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.90455.2008 · Cited by 40

Transcriptional profiling of skeletal muscle reveals factors that are necessary to maintain satellite cell integrity during ageing

Scimè, A., Desrosiers, J., Trensz, F., Palidwor, G., Caron, A. Z., Andrade-Navarro, M. A., & Grenier, G. (2009) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2009.11.001 · Cited by 40

Proteolysis inhibition by hibernating bear serum leads to increased protein content in human muscle cells

Chanon, S., Chazarin, B., Toubhans, B., Durand, C., Chery, I., Robert, M., Vieille‐Marchiset, A., Swenson, J. E., Zedrosser, A., Evans, A. L., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-23891-5 · Cited by 42

MTOR signaling and ubiquitin-proteosome gene expression in the preservation of fat free mass following high protein, calorie restricted weight loss

McIver, C. M., Wycherley, T. P., & Clifton, P. M. (2012) · Nutrition & Metabolism · doi:10.1186/1743-7075-9-83 · Cited by 39

Skeletal muscles of hibernating brown bears are unusually resistant to effects of denervation

Lin, D. C., Hershey, J. D., Mattoon, J. S., & Robbins, C. T. (2012) · Journal of Experimental Biology · doi:10.1242/jeb.066134 · Cited by 37

Live weight parameters and feed intake in Dorper, Damara and Australian Merino lambs exposed to restricted feeding

Scanlon, T. T., de Almeida, A. M., van Burgel, A., Kilminster, T., Milton, J. T. B., Greeff, J. C., & Oldham, C. (2012) · Small Ruminant Research · doi:10.1016/j.smallrumres.2012.08.004 · Cited by 37

Beneficial effects of metformin on muscle atrophy induced by obesity in rats

Hasan, M. M., Shalaby, S. M., El‐Gendy, J., & Abdelghany, E. M. A. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.27852 · Cited by 38

Insulin-like growth factor-1 and muscle wasting in chronic heart failure

Schulze, P. C., & Späte, U. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.04.017 · Cited by 37

Grape seed extract prevents skeletal muscle wasting in interleukin 10 knockout mice

Wang, B., Yang, G., Liang, X., Zhu, M. J., & Du, ‬. (2014) · BMC Complementary and Alternative Medicine · doi:10.1186/1472-6882-14-162 · Cited by 36

Regulation of Fasting Fuel Metabolism by Toll-Like Receptor 4

Pang, S., Tang, H., Zhuo, S., Zang, Y. Q., & Le, Y. (2010) · Diabetes · doi:10.2337/db10-0418 · Cited by 35

Up-Regulation of Genes Related to the Ubiquitin-Proteasome System in the Brown Adipose Tissue of 24-h-Fasted Rats

Nakai, Y., Hashida, H., Kadota, K., Minami, M., Shimizu, K., Matsumoto, I., Kato, H., & Abe, K. (2008) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.70508 · Cited by 35

Manganese‐induced downregulation of astroglial glutamine transporter SNAT3 involves ubiquitin‐mediated proteolytic system

Sidoryk‐Wȩgrzynowicz, M., Lee, E., Ni, M., & Aschner, M. (2010) · Glia · doi:10.1002/glia.21060 · Cited by 34

Mu RF ‐1 and p‐ GSK 3β expression in muscle atrophy of cirrhosis

Merli, M., Giusto, M., Molfino, A., Bonetto, A., Rossi, M., Corradini, S. G., Baccino, F. M., Fanelli, F. R., Costelli, P., & Muscaritoli, M. (2013) · Liver International · doi:10.1111/liv.12128 · Cited by 34

Slowing muscle atrophy: putting the brakes on protein breakdown

Lecker, S. H., & Goldberg, A. L. (2002) · The Journal of Physiology · doi:10.1113/jphysiol.2002.030429 · Cited by 34

Oral L-Glutamine Pretreatment Attenuates Skeletal Muscle Atrophy Induced by 24-h Fasting in Mice

de Vasconcelos, D. A. A., Giesbertz, P., de Souza, D. R., Vitzel, K. F., Abreu, P., Marzuca-Nassr, G. N., Fortes, M. A. S., Murata, G. M., Hirabara, S. M., Curi, R., et al. (2019) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2019.05.010 · Cited by 33

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