The Molecular Basis of Skeletal Muscle Atrophy

THE UBIQUITIN SYSTEM

Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840 · see citing works

THE NF-κB AND IκB PROTEINS: New Discoveries and Insights

Baldwin, A. S. (1996) · Annual Review of Immunology · doi:10.1146/annurev.immunol.14.1.649 · Cited by 5,882 · see citing works

NF-κB AND REL PROTEINS: Evolutionarily Conserved Mediators of Immune Responses

Ghosh, S., May, M. J., & Kopp, E. B. (1998) · Annual Review of Immunology · doi:10.1146/annurev.immunol.16.1.225 · Cited by 5,182 · see citing works

The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction

Glickman, M. H., & Ciechanover, A. J. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,216 · see citing works

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

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 · 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

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 · see citing works

Translational control of gene expression

Sonenberg, N., Hershey, J. W. B., & Mathews, M. B. (2000) · Cold Spring Harbor Laboratory eBooks · Cited by 1,379 · 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

Regulation of Membrane Protein Transport by Ubiquitin and Ubiquitin-Binding Proteins

Hicke, L., & Dunn, R. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.110701.154617 · Cited by 1,106 · see citing works

NF-κB-Induced Loss of MyoD Messenger RNA: Possible Role in Muscle Decay and Cachexia

D, D. C. G., Mayo, M. W., Madrid, L. V., Wang, C., & Baldwin, A. S. (2000) · Science · doi:10.1126/science.289.5488.2363 · Cited by 922 · see citing works

Handbook of Physiology. Section 12. Exercise: Regulation and Integration of Multiple Systems

Coast, J. R. (1997) · Medicine & Science in Sports & Exercise · doi:10.1097/00005768-199703000-00021 · Cited by 915 · see citing works

Induction of Cachexia in Mice by Systemically Administered Myostatin

Zimmers, T. A., Davies, M. V., Koniaris, L. G., Haynes, P. A., Esquela‐Kerscher, A., Tomkinson, K. N., McPherron, A. C., Wolfman, N. M., & Lee, S. (2002) · Science · doi:10.1126/science.1069525 · Cited by 908 · see citing works

Regulation of elongation factor 2 kinase by p90RSK1 and p70 S6 kinase

Wang, X.-M., Li, W., Williams, M. R., Terada, N., Alessi, D., & Proud, C. G. (2001) · EMBO Journal · doi:10.1093/emboj/20.16.4370 · Cited by 862 · see citing works

Functional improvement of dystrophic muscle by myostatin blockade

Bogdanovich, S., Krag, T. O. B., Barton, E. R., Morris, L. D., Whittemore, L.-A., Ahima, R. S., & Khurana, T. S. (2002) · Nature · doi:10.1038/nature01154 · Cited by 831 · see citing works

Exercise : regulation and integration of multiple systems

Rowell, L. B., & Shepherd, J. T. (1996) · Medical Entomology and Zoology · Cited by 810 · see citing works

Muscle Protein Breakdown and the Critical Role of the Ubiquitin-Proteasome Pathway in Normal and Disease States

Lecker, S. H., Solomon, V., Mitch, W. E., & Goldberg, A. L. (1999) · Journal of Nutrition · doi:10.1093/jn/129.1.227s · Cited by 732 · see citing works

Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions

Du, J., Wang, X., Miereles, C., Bailey, J. L., Debigaré, R., Zheng, B., Price, S. R., & Mitch, W. E. (2004) · Journal of Clinical Investigation · doi:10.1172/jci18330 · Cited by 730 · see citing works

Atrophy of the soleus muscle by hindlimb unweighting

Thomason, D. B., & Booth, F. W. (1990) · Journal of Applied Physiology · doi:10.1152/jappl.1990.68.1.1 · Cited by 631 · see citing works

Organization of the human myostatin gene and expression in healthy men and HIV-infected men with muscle wasting

Gonzalez-Cadavid, N. F., Taylor, W. E., Yarasheski, K., Sinha-Hikim, I., Ma, K., Ezzat, S., Shen, R., Lalani, R., Asa, S., Mamita, M., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.25.14938 · Cited by 571 · see citing works

<i>Physiology of a Microgravity Environment</i> Invited Review: Microgravity and skeletal muscle

Fitts, R. H., Riley, D. R., & Widrick, J. J. (2000) · Journal of Applied Physiology · doi:10.1152/jappl.2000.89.2.823 · Cited by 548 · see citing works

Skeletal muscle myocytes undergo protein loss and reactive oxygen-mediated NF-κB activation in response to tumor necrosis factor α

Li, Y., Schwartz, R. J., Waddell, I. D., Holloway, B. R., & Reid, M. B. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.10.871 · Cited by 502 · see citing works

Gettin’ down with ubiquitin: turning off cell-surface receptors, transporters and channels

Hicke, L. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01491-3 · Cited by 467 · see citing works

NF-κB mediates the protein loss induced by TNF-α in differentiated skeletal muscle myotubes

Li, Y., & Reid, M. B. (2000) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.2000.279.4.r1165 · Cited by 443 · see citing works

Glucocorticoid-induced skeletal muscle atrophy is associated with upregulation of myostatin gene expression

Ma, K., Mallidis, C., Bhasin, S., Mahabadi, V., Artaza, J., González-Cadavid, N. F., Arias, J., & Salehian, B. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00487.2002 · Cited by 416 · see citing works

Myostatin inhibits cell proliferation and protein synthesis in C2C12 muscle cells

Taylor, W. E., Bhasin, S., Artaza, J., Byhower, F., Azam, M., Willard, D. H., Kull, F. C., & González-Cadavid, N. F. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.280.2.e221 · Cited by 410 · see citing works

The candidate proto-oncogene bcl-3 encodes a transcriptional coactivator that activates through NF-kappa B p50 homodimers.

Fujita, T., Nolan, G. P., Liou, H. C., Scott, M. L., & Baltimore, D. (1993) · Genes &amp; Development · doi:10.1101/gad.7.7b.1354 · Cited by 409 · 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

What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?

Jagoe, R. T., & Goldberg, A. L. (2001) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/00075197-200105000-00003 · Cited by 399 · see citing works

Intracellular signaling during skeletal muscle atrophy

Kandarian, S. C., & Jackman, R. W. (2005) · Muscle & Nerve · doi:10.1002/mus.20442 · Cited by 393 · see citing works

Hindlimb unloading increases oxidative stress and disrupts antioxidant capacity in skeletal muscle

Lawler, J. M. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00186-2 · Cited by 370 · see citing works

Skeletal muscle myostatin mRNA expression is fiber-type specific and increases during hindlimb unloading

Carlson, C. J., Booth, F. W., & Gordon, S. E. (1999) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1999.277.2.r601 · Cited by 358 · see citing works

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

Jagoe, R. T., Lecker, S. H., Gomes, M., & Goldberg, A. L. (2002) · The FASEB Journal · doi:10.1096/fj.02-0312com · Cited by 344 · see citing works

Role of calpain in skeletal-muscle protein degradation

Huang, J., & Forsberg, N. E. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.21.12100 · Cited by 333 · 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

Spherical reflector as an electromagnetic-missile launcher

Shen, H.-M. (1990) · Journal of Applied Physics · doi:10.1063/1.347115 · Cited by 307 · see citing works

Glucocorticoids and muscle catabolism

Hasselgren, P.-O. (1999) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-199905000-00002 · Cited by 297 · see citing works

Effect of glucocorticoid administration on the rate of muscle protein breakdown in vivo in rats, as measured by urinary excretion of Nτ-methylhistidine

Tomas, F. M., Munro, H. N., & Young, V. R. (1979) · Biochemical Journal · doi:10.1042/bj1780139 · Cited by 293 · see citing works

Activation of an alternative NF‐ΚB pathway in skeletal muscle during disuse atrophy

Hunter, R. B., Stevenson, E. J., Koncarevic, A., Mitchell-Felton, H., Essig, D. A., & Kandarian, S. C. (2002) · The FASEB Journal · doi:10.1096/fj.01-0866com · Cited by 281 · see citing works

Muscle Cachexia: Current Concepts of Intracellular Mechanisms and Molecular Regulation

Hasselgren, P.-O., & Fischer, J. E. (2001) · Annals of Surgery · doi:10.1097/00000658-200101000-00003 · Cited by 278 · see citing works

Coordinate activation of lysosomal, Ca2+-activated and ATP-ubiquitin-dependent proteinases in the unweighted rat soleus muscle

Taillandier, D., AUROUSSEAU, E., Meynial‐Denis, D., Béchet, D., Ferrara, M., Cottin, P., Ducastaing, A., Bigard, X. A., Guezennec, C. Y., Schmid, H.-P., et al. (1996) · Biochemical Journal · doi:10.1042/bj3160065 · Cited by 272 · see citing works

FOXO Forkhead Transcription Factors Induce G2-M Checkpoint in Response to Oxidative Stress

Furukawa‐Hibi, Y., Yoshida-Araki, K., Ohta, T., Ikeda, K., & Motoyama, N. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200256200 · Cited by 271 · see citing works

Global analysis of gene expression patterns during disuse atrophy in rat skeletal muscle

Stevenson, E. J., Giresi, P. G., Koncarevic, A., & Kandarian, S. C. (2003) · The Journal of Physiology · doi:10.1111/j.1469-7793.2003.00033.x · Cited by 270 · see citing works

Control of Ser2448 Phosphorylation in the Mammalian Target of Rapamycin by Insulin and Skeletal Muscle Load

Reynolds, T., Bodine, S. C., & Lawrence, J. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201142200 · Cited by 268 · see citing works

The Grb10/Nedd4 Complex Regulates Ligand-Induced Ubiquitination and Stability of the Insulin-Like Growth Factor I Receptor

Vecchione, A. M., Marchese, A., Henry, P., Rotin, D., & Morrione, A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.9.3363-3372.2003 · Cited by 251 · see citing works

Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy

Hunter, R. B., & Kandarian, S. C. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21696 · Cited by 249 · see citing works

Induction of protein catabolism and the ubiquitin-proteasome pathway by mild oxidative stress

Gomes‐Marcondes, M. C. C., & Tisdale, M. J. (2002) · Cancer Letters · doi:10.1016/s0304-3835(02)00006-x · Cited by 249 · see citing works

TNF‐α increases ubiquitin‐conjugating activity in skeletal muscle by up‐regulating UbcH2/E2 20k

LI, Y.-P., Lecker, S. H., Chen, Y., Waddell, I. D., Goldberg, A. L., & Reid, M. B. (2003) · The FASEB Journal · doi:10.1096/fj.02-0759com · Cited by 243 · see citing works

Overexpression of interleukin-15 induces skeletal muscle hypertrophy in vitro: implications for treatment of muscle wasting disorders

Quinn, L. S., Anderson, B. G., Drivdahl, R. H., Alvarez, B., & Argilés, J. M. (2002) · Experimental Cell Research · doi:10.1006/excr.2002.5624 · Cited by 226 · 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

Mdm2-dependent ubiquitination and degradation of the insulin-like growth factor 1 receptor

Girnita, L., Girnita, A., & Larsson, O. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1431613100 · Cited by 223 · 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

Expression of a calpastatin transgene slows muscle wasting and obviates changes in myosin isoform expression during murine muscle disuse

Tidball, J. G., & Spencer, M. J. (2002) · The Journal of Physiology · doi:10.1113/jphysiol.2002.024935 · Cited by 210 · see citing works

NF‐κB p105 is a target of IκB kinases and controls signal induction of Bcl‐3–p50 complexes

Heissmeyer, V., Krappmann, D., Wulczyn, F. G., & Scheidereit, C. (1999) · The EMBO Journal · doi:10.1093/emboj/18.17.4766 · Cited by 197 · see citing works

The IκB Kinase (IKK) Inhibitor, NEMO-binding Domain Peptide, Blocks Osteoclastogenesis and Bone Erosion in Inflammatory Arthritis

Dai, S., Hirayama, T., Abbas, S., & Abu‐Amer, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400258200 · Cited by 196 · see citing works

IGF-binding protein-5: flexible player in the IGF system and effector on its own

Schneider, M. R., Wolf, E., Hoeflich, A., & Lahm, H. (2002) · Journal of Endocrinology · doi:10.1677/joe.0.1720423 · Cited by 190 · see citing works

Sepsis stimulates release of myofilaments in skeletal muscle by a calcium‐dependent mechanism

Williams, A. B., deCourten-Myers, G., Fischer, J. E., Luo, G., Sun, X., & Hasselgren, P.-O. J. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.11.1435 · Cited by 189 · see citing works

Space shuttle flight (STS‐90) enhances degradation of rat myosin heavy chain in association with activation of ubiquitin‐proteasome pathway

Ikemoto‐Uezumi, M., Nikawa, T., Takeda, S., Watanabe, C., Kitano, T., Baldwin, K. M., Izumi, R., Nonaka, I., Towatari, T., Teshima, S., et al. (2001) · The FASEB Journal · doi:10.1096/fj.00-0629fje · Cited by 186 · see citing works

Identification of cathepsin L as a differentially expressed message associated with skeletal muscle wasting

Deval, C., Mordier, S. B., Obled, C., Béchet, D., Combaret, L., Attaix, D., & Ferrara, M. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3600143 · Cited by 184 · see citing works

Modulating skeletal muscle mass by postnatal, muscle‐specific inactivation of the myostatin gene

Grobet, L., Pirottin, D., Farnir, F., Poncelet, D. A., Royo, L. J., Brouwers, B., Christians, E., Desmecht, D. J.-M., Coignoul, F. L., Kahn, R., et al. (2003) · genesis · doi:10.1002/gene.10188 · Cited by 182 · see citing works

Myostatin and insulin-like growth factor-I and -II expression in the muscle of rats exposed to the microgravity environment of the NeuroLab space shuttle flight

Lalani, R., Bhasin, S., Byhower, F., Tarnuzzer, R. W., Grant, M. B., Shen, R., Asa, S. L., Ezzat, S., & González-Cadavid, N. F. (2000) · Journal of Endocrinology · doi:10.1677/joe.0.1670417 · Cited by 178 · see citing works

Muscle Plasticity: Energy Demand and Supply Processes

Booth, F. W., & Baldwin, K. M. (1996) · Comprehensive physiology · doi:10.1002/cphy.cp120124 · Cited by 165 · see citing works

Atrophy responses to muscle inactivity. II. Molecular markers of protein deficits

Haddad, F., Roy, R. R., Zhong, H., Edgerton, V. R., & Baldwin, K. M. (2003) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01113.2002 · Cited by 164 · see citing works

Myogenic Akt Signaling Regulates Blood Vessel Recruitment during Myofiber Growth

Takahashi, A., Kureishi, Y., Jiang, Y., Luo, Z., Guo, K. Y., Mukhopadhyay, D., Ivashchenko, Y., Branellec, D., & Walsh, K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4803-4814.2002 · Cited by 159 · see citing works

Rates of ubiquitin conjugation increase when muscles atrophy, largely through activation of the N-end rule pathway

Solomon, V., Baracos, V. E., Sarraf, P., & Goldberg, A. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.21.12602 · Cited by 153 · see citing works

Construction and Analysis of Mouse Strains Lacking the Ubiquitin Ligase UBR1 (E3α) of the N-End Rule Pathway

Kwon, Y. T., Xia, Z., Davydov, I. V., Lecker, S. H., & Varshavsky, A. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.23.8007-8021.2001 · Cited by 153 · see citing works

Regulation of translation factors during hindlimb unloading and denervation of skeletal muscle in rats.

Hornberger, T., Hunter, R. B., Kandarian, S. C., & Esser, K. A. (2001) · American Journal of Physiology - Cell Physiology · doi:10.1152/ajpcell.2001.281.1.c179 · Cited by 153 · see citing works

Molecular regulation of muscle cachexia: it may be more than the proteasome.

Hasselgren, P.-O., Wray, C., & Mammen, J. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5849 · Cited by 146 · see citing works

Increased expression of the ubiquitin – proteasome pathway in murine myotubes by proteolysis-inducing factor (PIF) is associated with activation of the transcription factor NF-κB

Whitehouse, A., & Tisdale, M. J. (2003) · British Journal of Cancer · doi:10.1038/sj.bjc.6601132 · Cited by 136 · see citing works

Cardiac Ankyrin Repeat Protein Is a Novel Marker of Cardiac Hypertrophy

Aihara, Y., Kurabayashi, M., Saito, Y., Ohyama, Y., Tanaka, T., Takeda, S., Tomaru, K., Sekiguchi, K., Arai, M., Nakamura, T., et al. (2000) · Hypertension · doi:10.1161/01.hyp.36.1.48 · Cited by 135 · see citing works

Trafficking and cell surface stability of ENaC

Rotin, D., Kanelis, V., & Schild, L. (2001) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.2001.281.3.f391 · Cited by 135 · see citing works

Glucocorticoids Induce Proteasome C3 Subunit Expression in L6 Muscle Cells by Opposing the Suppression of Its Transcription by NF-κB

Du, J., Mitch, W. E., Wang, X., & Price, S. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m907258199 · Cited by 134 · see citing works

The effect of hypokinesia and hypodynamia on protein turnover and the growth of four skeletal muscles of the rat

Goldspink, D. F., Morton, A. J., Loughna, P. T., & Goldspink, G. (1986) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/bf00585311 · Cited by 132 · see citing works

Effect of inactivity and passive stretch on protein turnover in phasic and postural rat muscles

Loughna, P. T., Goldspink, G., & Goldspink, D. F. (1986) · Journal of Applied Physiology · doi:10.1152/jappl.1986.61.1.173 · Cited by 125 · see citing works

Identification of cathepsin L as a differentially expressed message associated with skeletal muscle wasting

Deval, C., Mordier, S. B., Obled, C., et al. (2001) · Biochemical Journal · doi:10.1042/bj3600143 · Cited by 124 · see citing works

The activation of protein degradation in muscle by Ca2+ or muscle injury does not involve a lysosomal mechanism

Furuno, K., & Goldberg, A. L. (1986) · Biochemical Journal · doi:10.1042/bj2370859 · Cited by 123 · see citing works

Intratumoral injection of oligonucleotides to the NFκB binding site inhibits cachexia in a mouse tumor model

Kawamura, I., Morishita, R., Tomita, N., Lacey, E., Aketa, M., Tsujimoto, S., Manda, T., Tomoi, M., Kida, I., Higaki, J., et al. (1999) · Gene Therapy · doi:10.1038/sj.gt.3300819 · Cited by 117 · see citing works

Cleavage of caspases-1, -3, -6, -8 and -9 substrates by proteases in skeletal muscles from mice undergoing cancer cachexia

Belizário, J. E., Lorite, M. J., & Tisdale, M. J. (2001) · British Journal of Cancer · doi:10.1054/bjoc.2001.1700 · Cited by 116 · see citing works

Regulation of NFKB1 proteins by the candidate oncoprotein BCL‐3: generation of NF‐κB homodimers from the cytoplasmic pool of p50–p105 and nuclear translocation

Watanabe, N., Iwamura, T., Shinoda, T., & Fujita, T. (1997) · The EMBO Journal · doi:10.1093/emboj/16.12.3609 · Cited by 109 · see citing works

Complement activation promotes muscle inflammation during modified muscle use.

Frenette, J., Cai, B.-Y., & Tidball, J. (2000) · American Journal of Pathology · doi:10.1016/s0002-9440(10)65081-x · Cited by 108 · see citing works

Patterns of global gene expression in rat skeletal muscle during unloading and low-intensity ambulatory activity

Bey, L., Akunuri, N., Zhao, P., Hoffman, E. P., Hamilton, D. G., & Hamilton, M. T. (2003) · Physiological Genomics · doi:10.1152/physiolgenomics.00001.2002 · Cited by 106 · see citing works

The Transcription Factors NF-κB and AP-1 Are Differentially Regulated in Skeletal Muscle during Sepsis

Penner, C. G., Gang, G., Wray, C. J., Fischer, J. E., & Hasselgren, P. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4497 · Cited by 99 · see citing works

Ectopic expression of IGF‐I and Shh by skeletal muscle inhibits disuse‐mediated skeletal muscle atrophy and bone osteopenia in vivo

Al‐Zghoul, M. B., Gerrard, D. E., Watkins, B. A., & Hannon, K. (2003) · The FASEB Journal · doi:10.1096/fj.03-0293fje · Cited by 96 · see citing works

Myostatin-deficient mice lose more skeletal muscle mass than wild-type controls during hindlimb suspension

McMahon, C. D., Popović, L., Oldham, J. M., Jeanplong, F., Smith, H. K., Kambadur, R., Sharma, M., Maxwell, L., & Bass, J. J. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00275.2002 · Cited by 96 · see citing works

Regulation of IGF‐I, IGFBP‐4 and IGFBP‐5 gene expression by loading in mouse skeletal muscle

Awede, B. L., Thissen, J., Gailly, P. L., & Lebacq, J. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01469-6 · Cited by 96 · see citing works

Different mechanisms of increased proteolysis in atrophy induced by denervation or unweighting of rat soleus muscle

Tischler, M. E., Rosenberg, S. B., Satarug, S., Henriksen, E. J., Kirby, C. R., Tome, M. E., & Chase, P. (1990) · Metabolism · doi:10.1016/0026-0495(90)90113-q · Cited by 94 · see citing works

Prolonged unloading of rat soleus muscle causes distinct adaptations of the gene profile

Wittwer, M., Flück, M., Hoppeler, H. H., Müller, S., Dominique Desplanches, C., & Billeter-Clark, R. (2002) · The FASEB Journal · doi:10.1096/fj.01-0792fje · Cited by 91 · see citing works

Mitochondria Mediate Tumor Necrosis Factor- α /NF- κ B Signaling in Skeletal Muscle Myotubes

Li, Y., Atkins, C. M., Sweatt, J. D., & Reid, M. B. (1999) · Antioxidants and Redox Signaling · doi:10.1089/ars.1999.1.1-97 · Cited by 90 · see citing works

Direct Inhibition of NF-κB Blocks Bone Erosion Associated with Inflammatory Arthritis

Clohisy, J. C. F., Roy, B. C., Biondo, C., Frazier, E. P., Willis, D., Teitelbaum, S. L., & Abu‐Amer, Y. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.10.5547 · Cited by 90 · see citing works

Effects of zero gravity on myofibril content and isomyosin distribution in rodent skeletal muscle

Baldwin, K. M., Herrick, R. E., Ilyina‐Kakueva, E. I., & Oganov, V. S. (1990) · The FASEB Journal · doi:10.1096/fasebj.4.1.2136840 · Cited by 84 · see citing works

Myostatin in Muscle Growth and Repair

Sharma, M., Langley, B. C., Bass, J. J., & Kambadur, R. (2001) · Exercise and Sport Sciences Reviews · doi:10.1097/00003677-200110000-00004 · Cited by 84 · see citing works

Interaction between corticosterone and tumor necrosis factor stimulated protein breakdown in rat skeletal muscle, similar to sepsis.

Hall-Angerås, M., Angerås, U., Zamir, O., Hasselgren, P. O., & Je, F. (1990) · PubMed · Cited by 79 · see citing works

Torbafylline (HWA 448) inhibits enhanced skeletal muscle ubiquitin‒proteasome-dependent proteolysis in cancer and septic rats

Combaret, L., Tilignac, T., Claustre, A., Voisin, L., Taillandier, D., Obled, C., TANAKA, K., & Attaix, D. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3610185 · Cited by 76 · see citing works

Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions

Du, J., Wang, X., Miereles, C., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200418330 · Cited by 76 · see citing works

Age-related changes in bone formation, osteoblastic cell proliferation, and differentiation during postnatal osteogenesis in human calvaria

de Pollak, C., Arnaud, É., Rénier, D., & Marie, P. J. (1997) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(199701)64:1 · Cited by 72 · see citing works

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 · see citing works

Translational control: implications for skeletal muscle hypertrophy.

Nader, G., Hornberger, T., & Esser, K. (2002) · Clinical Orthopaedics and Related Research · doi:10.1097/00003086-200210001-00021 · Cited by 70 · see citing works

Energy metabolism pathways in rat muscle under conditions of simulated microgravity

Stein, T. P., Schluter, M. D., Galante, A. T., Soteropoulos, P., Tolias, P. P., Grindeland, R. E., Moran, M., Wang, T. J., Polansky, M., & Wade, C. E. (2002) · The Journal of Nutritional Biochemistry · doi:10.1016/s0955-2863(02)00195-x · Cited by 70 · 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

The meteoric rise of regulated intracellular proteolysis

Mayer, R. J. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35040090 · Cited by 66 · see citing works

DANTROLENE REDUCES SERUM TNFα AND CORTICOSTERONE LEVELS AND MUSCLE CALCIUM, CALPAIN GENE EXPRESSION, AND PROTEIN BREAKDOWN IN SEPTIC RATS

Fischer, D. R., Sun, X., Williams, A. B., Gang, G., Pritts, T. A., James, H. J., Molloy, M. P., Fischer, J. E., Paul, R. J., & Hasselgren, P.-O. J. (2001) · Shock · doi:10.1097/00024382-200115030-00007 · Cited by 65 · see citing works

Gene therapy using SV40-derived vectors: What does the future hold?

Strayer, D. S. (1999) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(199912)181:3 · Cited by 61 · see citing works

Dantrolene ameliorates the metabolic hallmarks of sepsis in rats and improves survival in a mouse model of endotoxemia.

Hotchkiss, R. S., & Karl, I. E. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.8.3039 · Cited by 59 · see citing works

Signalling Pathways Regulating Protein Turnover in Skeletal Muscle

Thompson, M. G., & Palmer, R. M. (1998) · Cellular Signalling · doi:10.1016/s0898-6568(97)00076-4 · Cited by 53 · see citing works

Effect of glycogen synthase overexpression on insulin-stimulated muscle glucose uptake and storage

Fogt, D. L., Pan, S., Lee, S., Ding, Z., Scrimgeour, A. G., Lawrence, J. C., & Ivy, J. L. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00115.2003 · Cited by 48 · see citing works

Interaction of Glucocorticoid Hormones with Rat Skeletal Muscle: Catabolic Effects and Hormone Binding

Mayer, M., Shafrir, E., Kaiser, N., Milholland, R. J., & Rosen, F. (1976) · Metabolism · doi:10.1016/0026-0495(76)90046-9 · Cited by 47 · see citing works

Skeletal Muscle-Specific Calpain, p94, and Connectin/Titin: Their Physiological Functions and Relationship to Limb-Girdle Muscular Dystrophy Type 2A

Sorimachi, H., Ono, Y., & Suzuki, K. (2000) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-4267-4_23 · Cited by 47 · see citing works

Skeletal muscle cell hypertrophy induced by inhibitors of metalloproteases; myostatin as a potential mediator

Huet, C., Li, Z., Liu, H., Black, R. A., Galliano, M., & Engvall, E. (2001) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2001.281.5.c1624 · Cited by 47 · see citing works

Disuse atrophy, plasma corticosterone, and muscle glucocorticoid receptor levels.

Steffen, J. M., & Musacchia, X. J. (1987) · PubMed · Cited by 44 · see citing works

Time course of the response of myofibrillar and sarcoplasmic protein metabolism to unweighting of the soleus muscle

Muñoz, K. A., Satarug, S., & Tischler, M. E. (1993) · Metabolism · doi:10.1016/0026-0495(93)90014-f · Cited by 43 · see citing works

Torbafylline (HWA 448) inhibits enhanced skeletal muscle ubiquitin–proteasome-dependent proteolysis in cancer and septic rats

Combaret, L., TILIGNAC, T., Claustre, A., et al. (2002) · Biochemical Journal · doi:10.1042/bj3610185 · Cited by 43 · see citing works

Role of glucocorticoids in the response of rat leg muscles to reduced activity

Jaspers, S. R., & Tischler, M. E. (1986) · Muscle & Nerve · doi:10.1002/mus.880090613 · Cited by 39 · see citing works

Signal transduction pathways involved in proteolysis-inducing factor induced proteasome expression in murine myotubes

Smith, H. J., & Tisdale, M. J. (2003) · British Journal of Cancer · doi:10.1038/sj.bjc.6601328 · Cited by 38 · see citing works

Error-correcting microarray design

Khan, A. H., Ossadtchi, A. E., Leahy, R. M., & Smith, D. (2003) · Genomics · doi:10.1016/s0888-7543(02)00032-0 · Cited by 30 · see citing works

Effect of tumor necrosis factor or interleukin-1 on muscle amino acid uptake and the role of glucocorticoids.

Zamir, O., Hasselgren, P., James, H. J., Higashiguchi, T., & Fischer, J. E. (1993) · PubMed · Cited by 22 · see citing works

Effect of the antiglucocorticoid RU38486 on protein metabolism in unweighted soleus muscle

Tischler, M. E. (1994) · Metabolism · doi:10.1016/0026-0495(94)90044-2 · Cited by 18 · see citing works

Influence of performance on gene expression in skeletal muscle: effects of forced inactivity.

Thomason, D. B., & Booth, F. W. (1989) · PubMed · Cited by 10 · see citing works

Regulation of protein degradation in skeletal muscle

Goldberg, A. L., Tischler, M., & Libby, P. (1980) · Biochemical Society Transactions · doi:10.1042/bst0080497 · Cited by 5 · see citing works

Untitled work

(1997) · doi:10.1002/(sici)1097-0142(19970501)79:9

Myocardial Substrate Metabolism in the Normal and Failing Heart

Stanley, W. C., Recchia, F. A., & Lopaschuk, G. D. (2005) · Physiological Reviews · doi:10.1152/physrev.00006.2004 · Cited by 2,042 · 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

PGC-1α protects skeletal muscle from atrophy by suppressing FoxO3 action and atrophy-specific gene transcription

Sandri, M., Lin, J., Handschin, C., Yang, W., Arany, Z. P., Lecker, S. H., Goldberg, A. L., & Spiegelman, B. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607795103 · Cited by 974 · see citing works

The Molecular Bases of Training Adaptation

Coffey, V. G., & Hawley, J. A. (2007) · Sports Medicine · doi:10.2165/00007256-200737090-00001 · Cited by 756 · see citing works

Rapidly Progressive Diaphragmatic Weakness and Injury during Mechanical Ventilation in Humans

Jaber, S., Petrof, B. J., Jung, B., Chanques, G., Berthet, J., Rabuel, C., Bouyabrine, H., Courouble, P., Koechlin‐Ramonatxo, C., Sebbane, M., et al. (2010) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201004-0670oc · Cited by 709 · see citing works

Skeletal muscle: A review of molecular structure and function, in health and disease

Mukund, K., & Subramaniam, S. (2019) · Wiley Interdisciplinary Reviews: Systems Biology and Medicine · doi:10.1002/wsbm.1462 · Cited by 601 · see citing works

The COVID-19 pandemic and physical activity

Woods, J. A., Hutchinson, N. T., Powers, S. K., Roberts, W. O., Gómez‐Cabrera, M. C., Radak, Z. O., Berkes, I., Boros, A., Boldogh, I. R., Leeuwenburgh, C., et al. (2020) · Sports Medicine and Health Science · doi:10.1016/j.smhs.2020.05.006 · Cited by 647 · see citing works

During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation

Cohen, S., Brault, J. J., Gygi, S. P., Glass, D. J., Valenzuela, D. M., Gartner, C. A., Latres, E., & Goldberg, A. L. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200901052 · Cited by 584 · see citing works

Positive and Negative Regulation of Insulin Signaling by Reactive Oxygen and Nitrogen Species

Bashan, N., Kovsan, J., Kachko, I., Ovadia, H., & Rudich, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00014.2008 · Cited by 542 · 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

Oxidative stress and disuse muscle atrophy

Powers, S. K., Kavazis, A. N., & McClung, J. M. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01202.2006 · Cited by 471 · see citing works

Impact of sedentarism due to the COVID‐19 home confinement on neuromuscular, cardiovascular and metabolic health: Physiological and pathophysiological implications and recommendations for physical and nutritional countermeasures

Narici, M. V., VITO, G. D., Franchi, M. V., Paoli, A., Moro, T., Marcolin, G., Grassi, B., Baldassarre, G., Zuccarelli, L., Biolo, G., et al. (2020) · European Journal of Sport Science · doi:10.1080/17461391.2020.1761076 · Cited by 470 · see citing works

Infection, inflammation, height, and longevity

Crimmins, E. M., & Finch, C. E. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501470103 · Cited by 468 · see citing works

Role of changes in cardiac metabolism in development of diabetic cardiomyopathy

An, D., & Rodrigues, B. B. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00278.2006 · Cited by 443 · see citing works

Nuclear factor-kappa B signaling in skeletal muscle atrophy

Li, H., Malhotra, S., & Kumar, A. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0373-8 · Cited by 442 · see citing works

Reactive Oxygen Species Are Signalling Molecules for Skeletal Muscle Adaptation

Powers, S. K., Duarte, J., Kavazis, A. N., & Talbert, E. E. (2010) · Experimental Physiology · doi:10.1113/expphysiol.2009.050526 · Cited by 440 · see citing works

New fundamental resistance exercise determinants of molecular and cellular muscle adaptations

Toigo, M., & Boutellier, U. (2006) · European Journal of Applied Physiology · doi:10.1007/s00421-006-0238-1 · Cited by 437 · see citing works

Macrophage migration inhibitory factor stimulates AMP-activated protein kinase in the ischaemic heart

Miller, E. J., Li, J., Leng, L., McDonald, C., Atsumi, T., Bucala, R., & Young, L. H. (2008) · Nature · doi:10.1038/nature06504 · Cited by 429 · see citing works

Oxidative Stress, Chronic Disease, and Muscle Wasting

Moylan, J. S., & Reid, M. B. (2007) · Muscle &amp; Nerve · doi:10.1002/mus.20743 · Cited by 416 · see citing works

Sarcopenia, frailty and their prevention by exercise

Nascimento, C. M., Ingles, M., Salvador-Pascual, A., Cominetti, M. R., Gomez-Cabrera, M. C., & Viña, J. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.08.035 · Cited by 396 · see citing works

Intracellular signaling during skeletal muscle atrophy

Kandarian, S. C., & Jackman, R. W. (2005) · Muscle & Nerve · doi:10.1002/mus.20442 · Cited by 393 · see citing works

Exercise, MAPK, and NF-κB signaling in skeletal muscle

Kramer, H. F., & Goodyear, L. J. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00085.2007 · Cited by 375 · see citing works

Inflammation and Skeletal Muscle Wasting During Cachexia

Webster, J. M., Kempen, L. J. A. P., Hardy, R. S., & Langen, R. C. J. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.597675 · Cited by 372 · see citing works

Molecular and cellular mechanisms of skeletal muscle atrophy: an update

Fanzani, A., Conraads, V. M., Penna, F., & Martinet, W. (2012) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-012-0074-6 · Cited by 372 · see citing works

Denervation-Induced Skeletal Muscle Atrophy Is Associated with Increased Mitochondrial Ros Production

Muller, F. L., Song, W., Jang, Y. C., Liu, Y., Sabia, M., Richardson, A., & Van Remmen, H. (2007) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00767.2006 · Cited by 355 · see citing works

Cardiac cachexia: A systematic overview

von Haehling, S., Lainščak, M., Springer, J., & Anker, S. D. (2008) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2008.09.009 · Cited by 351 · see citing works

Reactive oxygen and nitrogen species as intracellular signals in skeletal muscle

Powers, S. K., Talbert, E. E., & Adhihetty, P. J. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2010.201327 · Cited by 340 · see citing works

Irisin is a pro-myogenic factor that induces skeletal muscle hypertrophy and rescues denervation-induced atrophy

Reza, M. M., Subramaniyam, N., Sim, C. M., Ge, X., Sathiakumar, D., McFarlane, C., Sharma, M., & Kambadur, R. (2017) · Nature Communications · doi:10.1038/s41467-017-01131-0 · Cited by 335 · see citing works

AMPK promotes skeletal muscle autophagy through activation of forkhead FoxO3a and interaction with Ulk1

Sanchez, A. M. J., Csibi, A., Raibon, A., Cornille, K., Gay, S., Bernardi, H., & Candau, R. B. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23399 · Cited by 329 · see citing works

Quercetin and related polyphenols: new insights and implications for their bioactivity and bioavailability

Kawabata, K., Mukai, R., & Ishisaka, A. (2015) · Food & Function · doi:10.1039/c4fo01178c · Cited by 327 · see citing works

Diagnostic and Therapeutic Challenges in Patients With Coexistent Chronic Obstructive Pulmonary Disease and Chronic Heart Failure

Jemtel, T. H. L., Padeletti, M., & Jelić, S. (2006) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2006.08.046 · Cited by 320 · see citing works

Dystrophin glycoprotein complex dysfunction: A regulatory link between muscular dystrophy and cancer cachexia

Acharyya, S., Butchbach, M. E. R., Sahenk, Z., Wang, H., Saji, M., Carathers, M., Ringel, M. D., Skipworth, R. J. E., Fearon, K. C. H., Hollingsworth, M. A., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.10.004 · Cited by 316 · see citing works

Bench-to-bedside review: Mobilizing patients in the intensive care unit – from pathophysiology to clinical trials

Truong, A. D., Fan, E., Brower, R. G., & Needham, D. M. (2009) · Critical Care · doi:10.1186/cc7885 · Cited by 307 · see citing works

Sepsis-induced myopathy

Callahan, L. A., & Supinski, G. S. (2009) · Critical Care Medicine · doi:10.1097/ccm.0b013e3181b6e439 · Cited by 299 · see citing works

Leucine and mTORC1: a complex relationship

Dodd, K. M., & Tee, A. R. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00525.2011 · Cited by 294 · see citing works

Sleep and muscle recovery: Endocrinological and molecular basis for a new and promising hypothesis

Dattilo, M., Antunes, H. K. M., Medeiros, A., Mônico Neto, M., Souza, H. S., Tufik, S., & de Mello, M. T. (2011) · Medical Hypotheses · doi:10.1016/j.mehy.2011.04.017 · Cited by 290 · see citing works

The muscle fiber type–fiber size paradox: hypertrophy or oxidative metabolism?

Wessel, T. V., HAAN, A. D., van der Laarse, W. J., & Jaspers, R. T. (2010) · European Journal of Applied Physiology · doi:10.1007/s00421-010-1545-0 · Cited by 287 · see citing works

Down-Regulation of Akt/Mammalian Target of Rapamycin Signaling Pathway in Response to Myostatin Overexpression in Skeletal Muscle

Amirouche, A., Durieux, A., Banzet, S., Koulmann, N., Bonnefoy, R., Mouret, C., Bigard, X. A., Peinnequin, A., & Freyssenet, D. G. (2008) · Endocrinology · doi:10.1210/en.2008-0959 · Cited by 282 · see citing works

The involvement of the ubiquitin proteasome system in human skeletal muscle remodelling and atrophy

Murton, A. J., Constantin, D., & Greenhaff, P. L. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.10.011 · Cited by 265 · see citing works

Mitochondrial-targeted antioxidants protect skeletal muscle against immobilization-induced muscle atrophy

Min, K., Smuder, A. J., Kwon, O.-S., Kavazis, A. N., Szeto, H. H., & Powers, S. K. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00591.2011 · Cited by 265 · see citing works

Effect of an unstable shoe construction on lower extremity gait characteristics

Nigg, B. M., Hintzen, S., & Ferber, R. (2005) · Clinical Biomechanics · doi:10.1016/j.clinbiomech.2005.08.013 · Cited by 263 · see citing works

NF-κB Regulation of YY1 Inhibits Skeletal Myogenesis through Transcriptional Silencing of Myofibrillar Genes

Wang, H., Hertlein, E. K., Bakkar, N., Sun, H., Acharyya, S., Wang, J., Carathers, M., Davuluri, R. V., & D, D. C. G. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02020-06 · Cited by 259 · 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

The ubiquitin–proteasome system and skeletal muscle wasting

Attaix, D., Ventadour, S., Codran, A., Béchet, D., Taillandier, D., & Combaret, L. (2005) · Essays in Biochemistry · doi:10.1042/eb0410173 · Cited by 253 · see citing works

Mitochondrial signaling contributes to disuse muscle atrophy

Powers, S. K., Wiggs, M. P., Duarte, J. A., Zergeroğlu, A. M., & Demirel, H. A. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00609.2011 · Cited by 244 · see citing works

Gene expression profiling in the early phases of DMD: a constant molecular signature characterizes DMD muscle from early postnatal life throughout disease progression

Pescatori, M., Broccolini, A., Minetti, C., Bertini, E., Bruno, C., D’Amico, A., Bernardini, C., Massimiliano Mirabella, A., Silvestri, G., Giglio, V., et al. (2007) · The FASEB Journal · doi:10.1096/fj.06-7285com · Cited by 243 · see citing works

TNF‐related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle‐wasting cytokine

Dogra, C., Changoua, H., Wedhas, N., Qin, X., Wergedal, J. E., & Kumar, A. (2007) · The FASEB Journal · doi:10.1096/fj.06-7537com · Cited by 244 · see citing works

Effect of denervation on mitochondrially mediated apoptosis in skeletal muscle.

Adhihetty, P. J., O'Leary, M. F. N., Chabi, B., Wicks, K. L., & Hood, D. A. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00768.2006 · Cited by 240 · 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

Targeted ablation of TRAF6 inhibits skeletal muscle wasting in mice

Paul, P. K., Gupta, S. K., Bhatnagar, S., Panguluri, S. K., Darnay, B. G., Choi, Y., & Kumar, A. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201006098 · Cited by 226 · see citing works

What determines growth potential and juvenile quality of farmed fish species?

Valente, L. M. P., Moutou, K. A., Conceição, L. E. C., Engrola, S. A. D., Fernandes, J. M. O., & Johnston, I. A. (2013) · Reviews in Aquaculture · doi:10.1111/raq.12020 · Cited by 225 · see citing works

Role of Oxidative Stress as Key Regulator of Muscle Wasting during Cachexia

Ábrigo, J., Elorza, Á. A., Riedel, C. A., Vilos, C., Simón, F., Cabrera, D., Estrada, L. D., & Cabello‐Verrugio, C. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2063179 · Cited by 221 · see citing works

AMP-activated protein kinase and the regulation of glucose transport

FUJII, N. L., Jessen, N., & Goodyear, L. J. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00207.2006 · Cited by 218 · see citing works

Mitochondrial dysfunction induces muscle atrophy during prolonged inactivity: A review of the causes and effects

Hyatt, H. W., Deminice, R., Yoshihara, T., & Powers, S. K. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.11.005 · Cited by 219 · see citing works

Oxidation enhances myofibrillar protein degradation via calpain and caspase-3

Smuder, A. J., Kavazis, A. N., Hudson, M. B., Nelson, W. B., & Powers, S. K. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.06.025 · Cited by 217 · see citing works

The impact of sleep on age-related sarcopenia: Possible connections and clinical implications

Piovezan, R. D., Abucham, J., dos Santos, R. V. T., de Mello, M. T., Tufik, S., & Poyares, D. R. (2015) · Ageing Research Reviews · doi:10.1016/j.arr.2015.07.003 · Cited by 215 · see citing works

Smoking-induced Skeletal Muscle Dysfunction. From Evidence to Mechanisms

Degens, H., Gayan‐Ramirez, G., & van Hees, H. W. H. (2015) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201410-1830pp · Cited by 212 · 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

Mechanical ventilation induces diaphragmatic mitochondrial dysfunction and increased oxidant production

Kavazis, A. N., Talbert, E. E., Smuder, A. J., Hudson, M. B., Nelson, W. B., & Powers, S. K. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.01.002 · Cited by 205 · see citing works

Calpains in muscle wasting

Bartoli, M., & Richard, I. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.12.012 · Cited by 198 · see citing works

Clinical review: Ventilator-induced diaphragmatic dysfunction - human studies confirm animal model findings!

Jaber, S., Jung, B., Matecki, S., & Petrof, B. J. (2011) · Critical Care · doi:10.1186/cc10023 · Cited by 193 · see citing works

The time course of the adaptations of human muscle proteome to bed rest and the underlying mechanisms

Brocca, L., Cannavino, J., Coletto, L., Biolo, G., Sandri, M., Bottinelli, R., & Pellegrino, M. A. (2012) · The Journal of Physiology · doi:10.1113/jphysiol.2012.240267 · Cited by 190 · see citing works

Transforming growth factor‐beta induces skeletal muscle atrophy and fibrosis through the induction of atrogin‐1 and scleraxis

Mendias, C. L., Gumucio, J. P., Davis, M. E., Bromley, C. W., Davis, C. S., & Brooks, S. V. (2011) · Muscle & Nerve · doi:10.1002/mus.22232 · Cited by 188 · see citing works

The association between COPD and heart failure risk: a review

de Miguel‐Díez, J., Morgan, C., & Jiménez‐García, R. (2013) · International Journal of COPD · doi:10.2147/copd.s31236 · Cited by 188 · see citing works

The Impact of Insulin Resistance and Inflammation on the Association Between Sarcopenic Obesity and Physical Functioning

Levine, M. E., & Crimmins, E. M. (2012) · Obesity · doi:10.1038/oby.2012.20 · Cited by 186 · see citing works

Molecular determinants of skeletal muscle mass: getting the “AKT” together

Nader, G. A. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.02.026 · Cited by 182 · see citing works

Does skeletal muscle have an ‘epi’-memory? The role of epigenetics in nutritional programming, metabolic disease, aging and exercise

Sharples, A. P., Stewart, C. E., & Seaborne, R. A. (2016) · Aging Cell · doi:10.1111/acel.12486 · Cited by 180 · see citing works

Ventilator-induced diaphragmatic dysfunction

Petrof, B. J., Jaber, S., & Matecki, S. (2009) · Current Opinion in Critical Care · doi:10.1097/mcc.0b013e328334b166 · Cited by 180 · see citing works

Mice lacking COX10 in skeletal muscle recapitulate the phenotype of progressive mitochondrial myopathies associated with cytochrome c oxidase deficiency

Díaz, F., Thomas, C. K., García, S., Hernandez, D., & Moraes, C. T. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi307 · Cited by 179 · see citing works

Effect of pulmonary rehabilitation on muscle remodelling in cachectic patients with COPD

Vogiatzis, I., Simoes, D. C. M., Stratakos, G. K., Kourepini, E., Terzis, G. D., Manta, P., Athanasopoulos, D., Roussos, C., Wagner, P. D., & Zakynthinos, S. G. (2010) · European Respiratory Journal · doi:10.1183/09031936.00112909 · Cited by 173 · see citing works

Prevention of unloading-induced atrophy by vitamin E supplementation: Links between oxidative stress and soleus muscle proteolysis?

Servais, S., Letexier, D., Favier, R. J. M., Duchamp, C., & Dominique Desplanches, C. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.12.001 · Cited by 170 · see citing works

Exercise Training Prevents Oxidative Stress and Ubiquitin-Proteasome System Overactivity and Reverse Skeletal Muscle Atrophy in Heart Failure

Cunha, T. F., Bacurau, A. V. N., Moreira, J. B. N., da Paixão, N. A., Campos, J. C., Ferreira, J. C. B., Leal, M. L., Negrão, C. E., Moriscot, A. S., Wisløff, U., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041701 · Cited by 169 · see citing works

Gut microbiota–bile acid–skeletal muscle axis

Mancin, L., Wu, G. D., & Paoli, A. (2022) · Trends in Microbiology · doi:10.1016/j.tim.2022.10.003 · Cited by 176 · see citing works

Renin‐Angiotensin System: An Old Player with Novel Functions in Skeletal Muscle

Cabello‐Verrugio, C., Morales, M. G., Rivera, J. C. A., Cabrera, D., & Simón, F. (2015) · Medicinal Research Reviews · doi:10.1002/med.21343 · Cited by 164 · see citing works

Tumor Necrosis Factor Alpha-Mediated Reduction of KLF2 Is Due to Inhibition of MEF2 by NF-κB and Histone Deacetylases

Kumar, A., Lin, Z., SenBanerjee, S., & Jain, M. K. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.14.5893-5903.2005 · Cited by 165 · see citing works

In vivo time-lapse microscopy reveals no loss of murine myonuclei during weeks of muscle atrophy

Bruusgaard, J. C., & Gundersen, K. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34022 · Cited by 162 · see citing works

Doxorubicin acts via mitochondrial ROS to stimulate catabolism in C2C12 myotubes

Gilliam, L. A. A., Moylan, J. S., Patterson, E. W., Smith, J. D., Wilson, A. S., Rabbani, Z., & Reid, M. B. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00217.2011 · Cited by 162 · see citing works

Ectopic Expression of Myostatin Induces Atrophy of Adult Skeletal Muscle by Decreasing Muscle Gene Expression

Durieux, A., Amirouche, A., Banzet, S., Koulmann, N., Bonnefoy, R., Pasdeloup, M., Mouret, C., Bigard, X. A., Peinnequin, A., & Freyssenet, D. G. (2007) · Endocrinology · doi:10.1210/en.2006-1500 · Cited by 162 · see citing works

Increased Proteolysis, Myosin Depletion, and Atrophic AKT-FOXO Signaling in Human Diaphragm Disuse

Levine, S., Biswas, C., Dierov, J. K., Barsotti, R., Shrager, J. B., Nguyen, T., Sonnad, S. S., Kucharchzuk, J. C., Kaiser, L. R., Singhal, S. K., et al. (2010) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200910-1487oc · Cited by 157 · see citing works

The central role of hypothalamic inflammation in the acute illness response and cachexia

Burfeind, K. G., Michaelis, K. A., & Marks, D. L. (2016) · Seminars in Cell &amp; Developmental Biology · doi:10.1016/j.semcdb.2015.10.038 · Cited by 156 · see citing works

Ubiquitin–protein ligases in muscle wasting

Cao, P., Kim, H. J., & Lecker, S. H. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.11.010 · Cited by 156 · see citing works

Build it up-Tear it down: protein quality control in the cardiac sarcomere

Willis, M. S., Schisler, J. C., Portbury, A. L., & Patterson, C. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn289 · Cited by 156 · see citing works

Adaptation of muscle size and myofascial force transmission: a review and some new experimental results

Huijing, P. A., & Jaspers, R. T. (2005) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/j.1600-0838.2005.00457.x · Cited by 157 · see citing works

Control of Muscle Size During Disuse, Disease, and Aging

Degens, H., & Alway, S. E. (2006) · International Journal of Sports Medicine · doi:10.1055/s-2005-837571 · Cited by 155 · see citing works

Diaphragm adaptations in patients with COPD

Ottenheijm, C. A. C., Heunks, L. M. A., & Dekhuijzen, R. P. N. (2008) · Respiratory Research · doi:10.1186/1465-9921-9-12 · Cited by 156 · see citing works

Response of the ubiquitin-proteasome pathway to changes in muscle activity

Reid, M. B. (2005) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00545.2004 · Cited by 154 · see citing works

Assessing the role of muscle protein breakdown in response to nutrition and exercise in humans.

Tipton, K. D., Hamilton, D. L., & Gallagher, I. J. (2018) · Sports Medicine · doi:10.1007/s40279-017-0845-5 · Cited by 152 · see citing works

Therapeutic approaches for muscle wasting disorders

Lynch, G. S., Schertzer, J. D., & Ryall, J. G. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2006.11.004 · Cited by 152 · see citing works

Effect of voluntary wheel running on circadian corticosterone release and on HPA axis responsiveness to restraint stress in Sprague-Dawley rats

Fediuc, S., Campbell, J. E., & Riddell, M. C. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01416.2005 · Cited by 148 · see citing works

Pressure support ventilation attenuates ventilator-induced protein modifications in the diaphragm

Futier, E., Constantin, J., Combaret, L., Mosoni, L., Roszyk, L., Sapin, V., Attaix, D., Jung, B., Jaber, S., & Bazin, J.-É. (2008) · Critical Care · doi:10.1186/cc7010 · Cited by 147 · see citing works

Reduced Skeletal Muscle Inhibitor of κBβ Content Is Associated With Insulin Resistance in Subjects With Type 2 Diabetes

Sriwijitkamol, A., Christ-Roberts, C. Y., Berria, R., Eagan, P. A., Pratipanawatr, T., DeFronzo, R. A., Mandarino, L. J., & Musi, N. (2006) · Diabetes · doi:10.2337/diabetes.55.03.06.db05-0677 · Cited by 144 · see citing works

The ubiquitin-proteasome pathway as a therapeutic target for muscle wasting.

Tisdale, M. J. (2005) · PubMed · Cited by 145 · see citing works

mTORC1 Promotes Denervation-Induced Muscle Atrophy Through a Mechanism Involving the Activation of FoxO and E3 Ubiquitin Ligases

Tang, H., Inoki, K., Lee, M. C., Wright, E., Khuong, A., Khuong, A., Sugiarto, S., Garner, M. S., Paik, J., DePinho, R. A., et al. (2014) · Science Signaling · doi:10.1126/scisignal.2004809 · Cited by 142 · see citing works

A Histone Deacetylase 4/Myogenin Positive Feedback Loop Coordinates Denervation-dependent Gene Induction and Suppression

Tang, H., Macpherson, P. C. D., Marvin, M. C., Meadows, E., Klein, W. H., Yang, X., & Goldman, D. J. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-07-0759 · Cited by 142 · see citing works

Nuclear domains during muscle atrophy: nuclei lost or paradigm lost?

Gundersen, K., & Bruusgaard, J. C. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2008.154369 · Cited by 140 · see citing works

Calorie restriction accelerates the catabolism of lean body mass during 2 wk of bed rest

Biolo, G., Ciocchi, B., Stulle, M., Bosutti, A., Barazzoni, R., Zanetti, M., Antonione, R., Lebenstedt, M., Platen, P., Heer, M. A., et al. (2007) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/86.2.366 · Cited by 139 · see citing works

miR-23a is decreased during muscle atrophy by a mechanism that includes calcineurin signaling and exosome-mediated export

Hudson, M. B., Woodworth-Hobbs, M. E., Zheng, B., Rahnert, J. A., Blount, M. A., Gooch, J. L., Searles, C. D., & Price, S. R. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00266.2013 · Cited by 137 · see citing works

Systems-Based Discovery of Tomatidine as a Natural Small Molecule Inhibitor of Skeletal Muscle Atrophy

Dyle, M. C., Ebert, S. M., Cook, D. P., Kunkel, S. D., Fox, D. K., Bongers, K. S., Bullard, S. A., Dierdorff, J. M., & Adams, C. M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.556241 · Cited by 138 · see citing works

Redox homeostasis, oxidative stress and disuse muscle atrophy

Pellegrino, M. A., Desaphy, J., Brocca, L., Pierno, S., Camerino, D. C., & Bottinelli, R. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2010.203232 · Cited by 137 · see citing works

Intensive Care Unit-Acquired Weakness: Not Just Another Muscle Atrophying Condition

Lad, H., Saumur, T. M., Herridge, M. S., dos Santos, C. C., Mathur, S., Batt, J. A. E., & Gilbert, P. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21217840 · Cited by 136 · see citing works

Nuclear factor‐κB signalling and transcriptional regulation in skeletal muscle atrophy

Jackman, R. W., Cornwell, E. W., Wu, C., & Kandarian, S. C. (2012) · Experimental Physiology · doi:10.1113/expphysiol.2011.063321 · Cited by 73 · see citing works

Molecular events and signalling pathways involved in skeletal muscle disuse‐induced atrophy and the impact of countermeasures

Chopard, A., Hillock, S., & Jasmin, B. J. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00864.x · Cited by 99 · see citing works

Signaling mechanisms involved in disuse muscle atrophy

Zhang, P., Chen, X., & Fan, M. (2007) · Medical Hypotheses · doi:10.1016/j.mehy.2006.11.043 · Cited by 204 · see citing works

An investigation into the P13-K/AKT signalling pathway in TNF-a-induced muscle proeolysis in L6 myotubes

Sishi, B. (2008) · SUNScholar (Stellenbosch University)

Regulation of the akt signalling in human skeletal muscle atrophy

Léger, B. (2008) · IRIS