The E3 Ligase MuRF1 Degrades Myosin Heavy Chain Protein in Dexamethasone-Treated Skeletal Muscle

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 · see citing works

Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy.

Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2004) · Cell · doi:10.1016/s0092-8674(04)00400-3 · Cited by 3,012 · see citing works

Function and regulation of cullin–RING ubiquitin ligases

Petroski, M. D., & Deshaies, R. J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1547 · Cited by 2,148 · see citing works

The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors.

Stitt, T. N., Drujan, D., Clarke, B. A., Panaro, F., Timofeyva, Y., Kline, W. O., Gonzalez, M., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00211-4 · Cited by 1,964 · see citing works

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 · see citing works

IKKβ/NF-κB Activation Causes Severe Muscle Wasting in Mice

Cai, D., Frantz, J. D., Tawa, N. E., Melendez, P. A., Oh, B.-C., Lidov, H. G. W., Hasselgren, P.-O., Frontera, W. R., Lee, J., Glass, D. J., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.027 · Cited by 1,367 · see citing works

Skeletal muscle hypertrophy and atrophy signaling pathways

Glass, D. J. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.04.018 · Cited by 1,106 · see citing works

Differentiation Stage-Specific Inhibition of the Raf-MEK-ERK Pathway by Akt

Rommel, C., Clarke, B. A., Zimmermann, S., Nuñez, L., Rossman, R., Reid, K., Moelling, K., Yancopoulos, G. D., & Glass, D. J. (1999) · Science · doi:10.1126/science.286.5445.1738 · Cited by 759 · see citing works

IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1

Sacheck, J. M., Ohtsuka, A., McLary, S. C., & Goldberg, A. L. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00073.2004 · Cited by 606 · see citing works

TNF‐α acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle

Li, Y.-P., Chen, Y., John, J., Moylan, J. S., Jin, B., Mann, D. L., & Reid, M. B. (2005) · The FASEB Journal · doi:10.1096/fj.04-2364com · Cited by 601 · see citing works

The Kinase Domain of Titin Controls Muscle Gene Expression and Protein Turnover

Lange, S., Xiang, F., Yakovenko, A. R., Vihola, A., Hackman, P., Rostkova, E. V., Kristensen, J., Brandmeier, B., Franzen, G., Hedberg, B., et al. (2005) · Science · doi:10.1126/science.1110463 · Cited by 594 · see citing works

Cancer cachexia is regulated by selective targeting of skeletal muscle gene products

Acharyya, S., Ladner, K. J., Nelsen, L., Damrauer, J. S., Reiser, P. J., Swoap, S. J., & D, D. C. G. (2004) · Journal of Clinical Investigation · doi:10.1172/jci20174 · Cited by 541 · see citing works

Insulin-like Growth Factor-1 (IGF-1) Inversely Regulates Atrophy-induced Genes via the Phosphatidylinositol 3-Kinase/Akt/Mammalian Target of Rapamycin (PI3K/Akt/mTOR) Pathway*

Latres, E., Amini, A. R., Amini, A. A., Griffiths, J. S., Martin, F. J., Wei, Y., Lin, H. C., Yancopouloš, G., & Glass, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m407517200 · Cited by 514 · see citing works

Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain

Centner, T., Yano, J., Kimura, E., McElhinny, A., Pelin, K., Witt, C. C., Bang, M., Trombitás, K., Granzier, H., Gregorio, C. C., et al. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4448 · Cited by 402 · see citing works

A family of mammalian F-box proteins

Winston, J. T., Koepp, D. M., Zhu, C., Elledge, S. J., & Harper, J. W. (1999) · Current Biology · doi:10.1016/s0960-9822(00)80021-4 · Cited by 357 · see citing works

Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I

Kedar, V., McDonough, H., Arya, R., Li, H., Rockman, H. A., & Patterson, C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404341102 · Cited by 347 · 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

Regulation of Muscle Protein Degradation

Lee, S. W., Dai, G., Hu, Z., Wang, X., Du, J., & Mitch, W. E. (2004) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000127211.86206.e1 · Cited by 324 · 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

Hydrogen peroxide stimulates ubiquitin-conjugating activity and expression of genes for specific E2 and E3 proteins in skeletal muscle myotubes

Li, Y.-P., Chen, Y., Li, A. S., & Reid, M. B. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00129.2003 · Cited by 313 · see citing works

MURF-1 and MURF-2 Target a Specific Subset of Myofibrillar Proteins Redundantly: Towards Understanding MURF-dependent Muscle Ubiquitination

Witt, S. H., Granzier, H. L. M., Witt, C. C., & Labeit, S. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.05.021 · Cited by 310 · see citing works

Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1

McElhinny, A., Kakinuma, K., Sorimachi, H., Labeit, S., & Gregorio, C. C. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200108089 · Cited by 262 · see citing works

Sepsis upregulates the gene expression of multiple ubiquitin ligases in skeletal muscle

Wray, C. J., Mammen, J. M. V., Hershko, D., & Hasselgren, P. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(02)00341-2 · Cited by 218 · see citing works

Hindlimb casting decreases muscle mass in part by proteasome-dependent proteolysis but independent of protein synthesis

Krawiec, B. J., Frost, R. A., Vary, T. C., Jefferson, L. S., & Lang, C. H. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00126.2005 · Cited by 198 · see citing works

Tumor Necrosis Factor and Steroid Metabolism in Chronic Heart Failure: Possible Relation to Muscle Wasting

Anker, S. D., Clark, A. L., Kemp, M., Salsbury, C., Teixeira, M. M., Hellewell, P. G., & Coats, A. J. S. (1997) · Journal of the American College of Cardiology · doi:10.1016/s0735-1097(97)00262-3 · Cited by 190 · see citing works

Induction of MafBx and Murf ubiquitin ligase mRNAs in rat skeletal muscle after LPS injection

Dehoux, M., Beneden, R. V., Fernández-Celemı́n, L., Lause, P., & Thissen, J. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00505-2 · Cited by 146 · see citing works

Transgenic Mouse Proteomics Identifies New 14-3-3-associated Proteins Involved in Cytoskeletal Rearrangements and Cell Signaling

Angrand, P., Segura, I., Völkel, P., Ghidelli, S., Terry, R. L., Brajenovic, M., Vintersten, K., Klein, R., Superti‐Furga, G., Drewes, G., et al. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600147-mcp200 · Cited by 146 · see citing works

Transgenic Overexpression of Locally Acting Insulin-Like Growth Factor-1 Inhibits Ubiquitin-Mediated Muscle Atrophy in Chronic Left-Ventricular Dysfunction

Schulze, P. C., Fang, J. S., Kassik, K. A., Gannon, J., Cupesi, M., MacGillivray, C., Lee, R. T., & Rosenthal, N. A. (2005) · Circulation Research · doi:10.1161/01.res.0000179580.72375.c2 · Cited by 133 · see citing works

The deleterious effects of bed rest on human skeletal muscle fibers are exacerbated by hypercortisolemia and ameliorated by dietary supplementation

Fitts, R. H., Romatowski, J. G., Peters, J., Paddon‐Jones, D., Wolfe, R. R., & Ferrando, A. A. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00573.2006 · Cited by 113 · see citing works

Effects of dexamethasone on protein degradation and protease gene expression in rat L8 myotube cultures

Hong, D.-H., & Forsberg, N. E. (1995) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(95)03476-n · Cited by 88 · see citing works

Ubiquitin System: Selectivity and Timing of Protein Destruction

Yamao, F. (1999) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022277 · Cited by 64 · see citing works

Functional properties of the titin/connectin-associated proteins, the muscle-specific RING finger proteins (MURFs), in striated muscle

Gregorio, C. C., Perry, C. N., & McElhinny, A. (2006) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-005-9021-x · Cited by 62 · see citing works

Glucocorticoid-induced skeletal muscle atrophy in vitro is attenuated by mechanical stimulation

Chromiak, J. A., & Vandenburgh, H. H. (1992) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1992.262.6.c1471 · Cited by 37 · see citing works

Burns and Metabolism

Hasselgren, P.-O. (1999) · Journal of the American College of Surgeons · doi:10.1016/s1072-7515(98)00297-x · Cited by 18 · see citing works

A 31P‐magnetic resonance spectroscopy and biochemical study of the movbr mouse: Potential model for the mitochondrial encephalomyopathies

Tracey, I., Dunn, J. F., & Radda, G. K. (1997) · Muscle & Nerve · doi:10.1002/(sici)1097-4598(199711)20:11 · Cited by 9 · see citing works

Fiber Types in Mammalian Skeletal Muscles

Schiaffino, S., & Reggiani, C. (2011) · Physiological Reviews · doi:10.1152/physrev.00031.2010 · Cited by 3,022 · see citing works

Exercise Metabolism and the Molecular Regulation of Skeletal Muscle Adaptation

Egan, B., & Zierath, J. R. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2012.12.012 · Cited by 2,084 · see citing works

Cancer-associated cachexia

Baracos, V. E., Martin, L., Korc, M., Guttridge, D. C., & Fearon, K. C. H. (2018) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2017.105 · Cited by 1,738 · see citing works

Mechanisms regulating skeletal muscle growth and atrophy

Schiaffino, S., Dyar, K. A., Ciciliot, S., Blaauw, B., & Sandri, M. (2013) · The FEBS Journal · doi:10.1111/febs.12253 · Cited by 1,492 · see citing works

Cellular and molecular mechanisms of muscle atrophy

Bonaldo, P., & Sandri, M. (2013) · Disease Models & Mechanisms · doi:10.1242/dmm.010389 · Cited by 1,284 · see citing works

Muscle wasting in disease: molecular mechanisms and promising therapies

Cohen, S., Nathan, J. A., & Goldberg, A. L. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4467 · Cited by 1,089 · see citing works

Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models

Schiaffino, S., & Mammucari, C. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-4 · Cited by 816 · see citing works

Protein breakdown in muscle wasting: Role of autophagy-lysosome and ubiquitin-proteasome

Sandri, M. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.04.023 · Cited by 689 · see citing works

Glucocorticoid-Induced Skeletal Muscle Atrophy

Schakman, O., Kalista, S., Barbé, C., Loumaye, A., & Thissen, J. P. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.05.036 · Cited by 705 · see citing works

A review on the mechanisms of blood-flow restriction resistance training-induced muscle hypertrophy

Pearson, S. J., & Hussain, S. R. (2015) · Sports Medicine · doi:10.1007/s40279-014-0264-9 · Cited by 592 · see citing works

Signaling pathways controlling skeletal muscle mass

Egerman, M. A., & Glass, D. J. (2014) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.857291 · Cited by 555 · see citing works

Skeletal muscle autophagy and apoptosis during aging: Effects of calorie restriction and life-long exercise

Wohlgemuth, S. E., Seo, A. Y., Marzetti, E., Lees, H. A., & Leeuwenburgh, C. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2009.11.002 · Cited by 397 · see citing works

Signaling pathways perturbing muscle mass.

Glass, D. J. (2010) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/mco.0b013e32833862df · Cited by 359 · see citing works

An Antibody Blocking Activin Type II Receptors Induces Strong Skeletal Muscle Hypertrophy and Protects from Atrophy

Lach-Trifilieff, E., Minetti, G. C., Sheppard, K., Ibebunjo, C., Feige, J. N., Hartmann, S., Brachat, S., Rivet, H., Koelbing, C., Morvan, F., et al. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01307-13 · Cited by 306 · see citing works

Restoring Specific Lactobacilli Levels Decreases Inflammation and Muscle Atrophy Markers in an Acute Leukemia Mouse Model

Bindels, L. B., Beck, R., Schakman, O., Martin, J. C., De Backer, F., Sohet, F. M., Dewulf, E. M., Pachikian, B. D., Neyrinck, A. M., Thissen, J.-P., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037971 · Cited by 278 · see citing works

The regulation of muscle mass by endogenous glucocorticoids

Braun, T. P., & Marks, D. L. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00012 · Cited by 273 · see citing works

The TWEAK–Fn14 system is a critical regulator of denervation-induced skeletal muscle atrophy in mice

Mittal, A., Bhatnagar, S., Kumar, A., Lach-Trifilieff, E., Wauters, S., Li, H., Makonchuk, D. Y., Glass, D. J., & Kumar, A. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200909117 · Cited by 250 · see citing works

Muscle sparing in muscle RING finger 1 null mice: response to synthetic glucocorticoids

Baehr, L. M., Furlow, J. D., & Bodine, S. C. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2011.212845 · Cited by 234 · see citing works

Maps and legends: the quest for dissociated ligands of the glucocorticoid receptor

Clark, A. R., & Belvisi, M. G. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2011.12.004 · Cited by 209 · see citing works

Ubiquitylation by Trim32 causes coupled loss of desmin, Z-bands, and thin filaments in muscle atrophy

Cohen, S., Zhai, B., Gygi, S. P., & Goldberg, A. L. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201110067 · Cited by 205 · see citing works

Metastatic cancers promote cachexia through ZIP14 upregulation in skeletal muscle

Wang, G., Biswas, A. K., Ma, W., Kandpal, M., Coker, C., Grandgenett, P. M., Hollingsworth, M. A., Jain, R., Tanji, K., Lόpez-Pintado, S., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0054-2 · Cited by 188 · see citing works

Limb Immobilization Induces a Coordinate Down-Regulation of Mitochondrial and Other Metabolic Pathways in Men and Women

Abadi, A., Glover, E. I., Isfort, R. J., Raha, S., Safdar, A., Yasuda, N., Kaczor, J. J., Melov, S., Hubbard, A., Qu, X., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006518 · Cited by 189 · see citing works

Anabolic and catabolic pathways regulating skeletal muscle mass

McCarthy, J. J., & Esser, K. A. (2010) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/mco.0b013e32833781b5 · Cited by 148 · see citing works

Regulation of muscle atrophy in aging and disease

Vinciguerra, M., Musaro, A., & Rosenthal, N. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7002-2_15 · Cited by 149 · see citing works

Myricanol rescues dexamethasone-induced muscle dysfunction Via a sirtuin 1-dependent mechanism

Shen, S., Liao, Q., Liu, J., Pan, R., Lee, S. M., & Lin, L. (2019) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12393 · Cited by 142 · see citing works

Leptin Administration Favors Muscle Mass Accretion by Decreasing FoxO3a and Increasing PGC-1α in ob/ob Mice

Sáinz, N., Rodríguez, A., Catalán, V., Becerril, S., Ramírez, B., Gómez-Ambrosi, J., & Frühbeck, G. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006808 · Cited by 135 · see citing works

Protein breakdown in cancer cachexia

Sandri, M. (2016) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2015.11.002 · Cited by 134 · see citing works

The Transcription Factor ATF4 Promotes Skeletal Myofiber Atrophy during Fasting

Ebert, S. M., Monteys, A. M., Fox, D. K., Bongers, K. S., Shields, B. E., Malmberg, S. E., Davidson, B. L., Suneja, M., & Adams, C. M. (2010) · Molecular Endocrinology · doi:10.1210/me.2009-0345 · Cited by 130 · see citing works

HDAC1 activates FoxO and is both sufficient and required for skeletal muscle atrophy

Beharry, A. W., Sandesara, P. B., Roberts, B. M., Ferreira, L. F., Senf, S. M., & Judge, A. R. (2014) · Journal of Cell Science · doi:10.1242/jcs.136390 · Cited by 128 · see citing works

Regulation of Human Skin Pigmentation in situ by Repetitive UV Exposure: Molecular Characterization of Responses to UVA and/or UVB

Choi, W., Miyamura, Y., Wolber, R., Smuda, C., Reinhold, W., Liu, H., Kolbe, L., & Hearing, V. J. (2010) · Journal of Investigative Dermatology · doi:10.1038/jid.2010.5 · Cited by 117 · see citing works

High Fat Diet‐Induced Skeletal Muscle Wasting Is Decreased by Mesenchymal Stem Cells Administration: Implications on Oxidative Stress, Ubiquitin Proteasome Pathway Activation, and Myonuclear Apoptosis

Abrigo, J., Rivera, J. C., Aravena, J., Cabrera, D., Simon, F., Ezquer, F., Ezquer, M., & Cabello-Verrugio, C. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/9047821 · Cited by 109 · see citing works

Autophagy as a Potential Target for Sarcopenia: AUTOPHAGY REGULATION IN SARCOPENIA

Fan, J., Kou, X., Jia, S., Yang, X., Yang, Y., & Chen, N. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25260 · Cited by 101 · see citing works

Autophagy and Protein Turnover Signaling in Slow-Twitch Muscle during Exercise

PAGANO, A. F., PY, G., BERNARDI, H., CANDAU, R. B., & SANCHEZ, A. M. J. (2014) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000000237 · Cited by 96 · see citing works

Proteasome activation delays aging in vitro and in vivo

Chondrogianni, N., Sakellari, M., Lefaki, M., Papaevgeniou, N., & Gonos, E. S. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.03.031 · Cited by 94 · see citing works

Dietary fish oil alleviates soleus atrophy during immobilization in association with Akt signaling to p70s6k and E3 ubiquitin ligases in rats

You, J.-S., Park, M.-N., Song, W., & Lee, Y.-S. (2010) · Applied Physiology Nutrition and Metabolism · doi:10.1139/h10-022 · Cited by 88 · see citing works

Angiotensin-(1–7) decreases skeletal muscle atrophy induced by angiotensin II through a Mas receptor-dependent mechanism

Cisternas, F., Morales, M. G., Meneses, C., Simon, F., Brandan, E., Abrigo, J., Vazquez, Y., & Cabello-Verrugio, C. (2015) · Clinical Science · doi:10.1042/cs20140215 · Cited by 83 · see citing works

Apigenin Ameliorates the Obesity-Induced Skeletal Muscle Atrophy by Attenuating Mitochondrial Dysfunction in the Muscle of Obese Mice

Choi, W. H., Son, H. J., Jang, Y. J., Ahn, J., Jung, C. H., & Ha, T. Y. (2017) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201700218 · Cited by 81 · see citing works

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 · see citing works

Paradoxical sleep deprivation induces muscle atrophy

Dattilo, M., Antunes, H. K. M., Medeiros, A., Mônico‐neto, M., Souza, H. D. S., Lee, K. S., Tufik, S., & de Mello, M. T. (2012) · Muscle & Nerve · doi:10.1002/mus.22322 · Cited by 66 · see citing works

Skeletal muscle in MuRF1 null mice is not spared in low-gravity conditions, indicating atrophy proceeds by unique mechanisms in space

Cadena, S. M., Zhang, Y., Fang, J., Brachat, S., Kuss, P., Giorgetti, E., Stodieck, L. S., Kneissel, M., & Glass, D. J. (2019) · Scientific Reports · doi:10.1038/s41598-019-45821-9 · Cited by 61 · see citing works

Nutraceuticals in the Prevention and Treatment of the Muscle Atrophy

Wang, Y., Liu, Q., Quan, H., Kang, S.-G., Huang, K., & Tong, T. (2021) · Nutrients · doi:10.3390/nu13061914 · Cited by 61 · see citing works

Review article: the aetiology of fatigue in inflammatory bowel disease and potential therapeutic management strategies

McGing, J. J., Radford, S. J., Francis, S. T., Serres, S., Greenhaff, P. L., & Moran, G. W. (2021) · Alimentary Pharmacology & Therapeutics · doi:10.1111/apt.16465 · Cited by 60 · see citing works

Twist1 Activation in Muscle Progenitor Cells Causes Muscle Loss Akin to Cancer Cachexia

Parajuli, P., Kumar, S., Loumaye, A., Singh, P., Eragamreddy, S., Nguyen, T. L., Ozkan, S., Razzaque, M. S., Prunier, C., Thissen, J.-P., et al. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.05.026 · Cited by 58 · see citing works

Proteasome inhibition improves the muscle of laminin α2 chain-deficient mice.

Carmignac, V., Quéré, R., & Durbeej, M. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddq499 · Cited by 58 · see citing works

Small‐molecule‐mediated chemical knock‐down of MuRF1/MuRF2 and attenuation of diaphragm dysfunction in chronic heart failure

Adams, V., Bowen, T. S., Werner, S., Barthel, P., Amberger, C., Konzer, A., Graumann, J., Sehr, P., Lewis, J., Provaznik, J., et al. (2019) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12448 · Cited by 51 · see citing works

Delphinidin Prevents Muscle Atrophy and Upregulates miR-23a Expression

Murata, M., Nonaka, H., Komatsu, S., Goto, M., Morozumi, M., Yamada, S., Lin, I.-C., Yamashita, S., & Tachibana, H. (2017) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.6b03661 · Cited by 47 · see citing works

Ginsenoside Rg1 Prevents Starvation-Induced Muscle Protein Degradation Via Regulation of AKT/mTOR/FoxO Signaling in C2C12 Myotubes

Li, F., Li, X., Peng, X., Sun, L., Jia, S., Wang, P., Ma, S., Zhao, H., Yu, Q., & Huo, H. (2017) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2017.4615 · Cited by 40 · see citing works

High Altitude Mediated Skeletal Muscle Atrophy: Protective Role of Curcumin

Chaudhary, P., Sharma, Y. K., Sharma, S., Singh, S. N., & Suryakumar, G. (2019) · Biochimie · doi:10.1016/j.biochi.2018.10.012 · Cited by 35 · see citing works

Pyropia Yezoensis Peptide PYP1-5 Protects against Dexamethasone-Induced Muscle Atrophy through the Downregulation of Atrogin1/MAFbx and MuRF1 in Mouse C2C12 Myotubes

Lee, M.-K., Kim, Y.-M., Kim, I.-H., Choi, Y.-H., & Nam, T.-J. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.6443 · Cited by 28 · see citing works

Mountain Ginseng Inhibits Skeletal Muscle Atrophy by Decreasing Muscle Ring finger Protein-1 and Atrogin1 through Forkhead Box O3 in L6 Myotubes

Seok, Y. M., Yoo, J.-M., Nam, Y., Kim, J., Kim, J. S., Son, J.-H., & Kim, H. J. (2021) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.113557 · Cited by 27 · see citing works

Canadine from Corydalis turtschaninovii Stimulates Myoblast Differentiation and Protects against Myotube Atrophy

Lee, H., Lee, S.-J., Bae, G.-U., Baek, N.-I., & Ryu, J.-H. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122748 · Cited by 26 · see citing works

Effects of Fucoxanthin on the Inhibition of Dexamethasone-Induced Skeletal Muscle Loss in Mice

Yoshikawa, M., Hosokawa, M., Miyashita, K., Nishino, H., & Hashimoto, T. (2021) · Nutrients · doi:10.3390/nu13041079 · Cited by 25 · see citing works

Slow and fast myosin heavy chain content defines three types of myotubes in early muscle cell cultures.

Miller, J. B., Crow, M. T., & Stockdale, F. E. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.5.1643 · Cited by 193 · see citing works

E1B 55k-independent dissociation of the DNA ligase IV/XRCC4 complex by E4 34k during adenovirus infection

Jayaram, S., Gilson, T. D., Ehrlich, E. S., Yu, X.-F., Ketner, G. W., & Hanakahi, L. A. (2008) · Virology · doi:10.1016/j.virol.2008.08.045 · Cited by 20 · see citing works

Identification of the phosphorylation sites on the E3 ubiquitin ligase Pellino that are critical for activation by IRAK1 and IRAK4

Smith, H., Peggie, M. W., Campbell, D. G., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900774106 · Cited by 79 · see citing works

Activity-based E3 ligase profiling uncovers an E3 ligase with esterification activity

Pao, K., Wood, N. T., Knebel, A., Rafie, K., Stanley, M., Mabbitt, P. D., Sundaramoorthy, R., Hofmann, K., van Aalten, D. M. F., & Virdee, S. (2018) · Nature · doi:10.1038/s41586-018-0026-1 · Cited by 282 · see citing works

A Comprehensive Atlas of E3 Ubiquitin Ligase Mutations in Neurological Disorders

George, A. J., Hoffiz, Y. C., Charles, A. J., Zhu, Y., & Mabb, A. M. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00029 · Cited by 170 · see citing works