The DOI matches its Crossref record; 227 of the 231 references it cites were found in a registry or an index.
Myostatin/activin pathway antagonism: Molecular basis and therapeutic potential
Abstract
Muscle wasting is associated with a wide range of catabolic diseases. This debilitating loss of muscle mass and functional capacity reduces the quality of life and increases the risks of morbidity and mortality. Major progress has been made in understanding the biochemical mechanisms and signaling pathways regulating muscle protein balance under normal conditions and the enhanced protein loss in atrophying muscles. It is now clear that activation of myostatin/activin signaling is critical in triggering the accelerated muscle catabolism that causes muscle loss in multiple disease states. Binding of myostatin and activin to the ActRIIB receptor complex on muscle cell membrane leads to activation of Smad2/3-mediated transcription, which in turn stimulates FoxO-dependent transcription and enhanced muscle protein breakdown via ubiquitin-proteasome system and autophagy. In addition, Smad activation inhibits muscle protein synthesis by suppressing Akt signaling. Pharmacological blockade of the myostatin/activin-ActRIIB pathway has been shown to prevent or reverse the loss of muscle mass and strength in various disease models including cancer cachexia and renal failure. Moreover, it can markedly prolong the lifespan of animals with cancer-associated muscle loss. Furthermore, inhibiting myostatin/activin actions also improves insulin sensitivity, reduces excessive adiposity, attenuates systemic inflammation, and accelerates bone fracture healing in disease models. Based on these exciting advances, the potential therapeutic benefits of myostatin/activin antagonism are now being tested in multiple clinical settings. This article is part of a Directed Issue entitled: Molecular basis of muscle wasting.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“In addition to the ability to modulate the Smad, FOXO and AKT pathways, the interaction between myostatin and physical exercise also appears to occur through the transcription factor peroxisome proliferator-activated receptor gamma co-activator 1-alpha (PGC-1α) in muscle, which in turn is stimulated by exercise (Han et al., 2013).”
From Physical Exercise-Induced Myokines and Muscle-Adipose Tissue Crosstalk: A Review of Current Knowledge and the Implications for Health and Metabolic Diseases (2018) · cites this paper as Han et al., 2013
In the citing paper
“TGFβ-like ligands myostatin (GDF-8) and Activin A are negative regulators of skeletal muscle mass.”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [14]
In the citing paper
“The PI3K/Akt/mTOR signaling axis is well known to regulate anabolic processes, including increasing protein synthesis to support muscle hypertrophy [14].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [14]
In the citing paper
“These ligands signal via the activin type II A and B receptors (ActRII) which complex with transmembrane type I activin receptor-like kinases (ALK4 or ALK5) [14].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [14]
In the citing paper
“Engagement of these receptors leads to phosphorylation of Smad proteins downstream regulation of gene expression, and decreased IGF-1 signaling via Akt [14].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [14]
In the citing paper
“Mechanistically, ActRII inhibition is thought to induce skeletal muscle hypertrophy by reducing Smad2/3 activity and elevating Akt signaling [14,16].”
From Antibody blockade of activin type II receptors preserves skeletal muscle mass and enhances fat loss during GLP-1 receptor agonism (2024) · cites this paper as [14]
Citations
Cites
1 retracted
Lokireddy, S., Wijesoma, I. W., Teng, S., Bonala, S., Gluckman, P. D., McFarlane, C., Sharma, M., & Kambadur, R. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.10.005 · Cited by 154
RetractedDefinition and classification of cancer cachexia: an international consensus
Fearon, K., Strasser, F., Anker, S. D., Bosaeus, I. G., Bruera, E. D., Fainsinger, R. L., Jatoi, A., Loprinzi, C. L., Macdonald, N., Mantovani, G., et al. (2011) · The Lancet Oncology · doi:10.1016/s1470-2045(10)70218-7 · Cited by 6,020
Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member
McPherron, A. C., Lawler, A. M., & Lee, S.-J. (1997) · Nature · doi:10.1038/387083a0 · Cited by 4,013
SATELLITE CELL OF SKELETAL MUSCLE FIBERS
Mauro, A. (1961) · The Journal of Cell Biology · doi:10.1083/jcb.9.2.493 · Cited by 3,683
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
Fielding, R. A., Vellas, B., Evans, W. J., Bhasin, S., Morley, J. E., Newman, A. B., Abellan van Kan, G., Andrieu, S., Bauer, J., Breuille, D., et al. (2011) · Journal of the American Medical Directors Association · doi:10.1016/j.jamda.2011.01.003 · Cited by 3,256
Massagué, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3434 · Cited by 3,239
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
Self-citationPax7 Is Required for the Specification of Myogenic Satellite Cells
Seale, P., Sabourin, L. A., Girgis-Gabardo, A., Mansouri, A., Gruß, P., & Rudnicki, M. A. (2000) · Cell · doi:10.1016/s0092-8674(00)00066-0 · Cited by 2,345
Evans, W., Morley, J., Argilés, J., Bales, C., Baracos, V., Guttridge, D., Jatoi, A., Kalantar-zadeh, K., Lochs, H., Mantovani, G., et al. (2008) · Clinical Nutrition · doi:10.1016/j.clnu.2008.06.013 · Cited by 2,341
Self-citationDouble muscling in cattle due to mutations in the myostatin gene
McPherron, A. C., & Lee, S.-J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12457 · Cited by 2,039
Fouque, D. P., Kalantar‐Zadeh, K., Kopple, J. D., Cano, N., Chauveau, P., Cuppari, L., Franch, H. A., Guarnieri, G., Ikizler, T. A., Kaysen, G. A., et al. (2007) · Kidney International · doi:10.1038/sj.ki.5002585 · Cited by 2,004
Self-citationStitt, 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
FoxO3 Controls Autophagy in Skeletal Muscle In Vivo
Mammucari, C., Milan, G., Romanello, V., Masiero, E., Rudolf, R., Del Piccolo, P., Burden, S. J., Di Lisi, R., Sandri, C., Zhao, J., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.001 · Cited by 1,953
Self-citationMassagué, J. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35043051 · Cited by 1,925
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
Self-citationInvited Review: Aging and sarcopenia
Doherty, T. J. (2003) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00347.2003 · Cited by 1,764
Making sense of latent TGFβ activation
Annes, J. P., Munger, J. S., & Rifkin, D. B. (2002) · Journal of Cell Science · doi:10.1242/jcs.00229 · Cited by 1,624
Regulation of myostatin activity and muscle growth
Lee, S.-J., & McPherron, A. C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151270098 · Cited by 1,616
The healthcare costs of sarcopenia in the United States
Janssen, I., Shepard, D. S., Katzmarzyk, P. T., & Roubenoff, R. (2004) · Journal of the American Geriatrics Society · doi:10.1111/j.1532-5415.2004.52014.x · Cited by 1,546
Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression
Lecker, S. H., Jagoe, R. T., Gilbert, A., Gomes, M., Baracos, V., Bailey, J., Price, S. R., Mitch, W. E., & Goldberg, A. L. (2004) · The FASEB Journal · doi:10.1096/fj.03-0610com · Cited by 1,539
Self-citationZhao, J., Brault, J. J., Schild, A., Cao, P., Sandri, M., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.004 · Cited by 1,489
Self-citationTargeting the TGFβ signalling pathway in disease
Akhurst, R. J., & Hata, A. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3810 · Cited by 1,466
Wasting as independent risk factor for mortality in chronic heart failure
Anker, S. D., Ponikowski, P. P., Varney, S. J., Chua, T. P., Clark, A. L., Webb-Peploe, K., Harrington, D., Kox, W. J., Poole-Wilson, P. A., & Coats, A. J. S. (1997) · The Lancet · doi:10.1016/s0140-6736(96)07015-8 · Cited by 1,399
Myostatin Mutation Associated with Gross Muscle Hypertrophy in a Child
Schuelke, M., Wagner, K. R., Stolz, L. E., Hübner, C., Riebel, T., Kömen, W., Braun, T., Tobin, J. F., & Lee, S.-J. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa040933 · Cited by 1,399
Regulation of the mTOR Complex 1 Pathway by Nutrients, Growth Factors, and Stress
Sengupta, S., Peterson, T. R., & Sabatini, D. M. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.026 · Cited by 1,275
Clop, A., Marcq, F., Takeda, H., Pirottin, D., Tordoir, X., Bibé, B., Bouix, J., Caiment, F., Elsen, J.-M., Eychenne, F., et al. (2006) · Nature Genetics · doi:10.1038/ng1810 · Cited by 1,260
Protein degradation by the ubiquitin-proteasome pathway in normal and disease states
Lecker, S. H., Goldberg, A. L., & Mitch, W. E. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006010083 · Cited by 1,234
Self-citationTisdale, M. J. (2009) · Physiological Reviews · doi:10.1152/physrev.00016.2008 · Cited by 1,216
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
Self-citationSarcopenia with limited mobility: an international consensus
Morley, J. E., Abbatecola, A. M., Argiles, J. M., Baracos, V., Bauer, J., Bhasin, S., Cederholm, T., Stewart Coats, A. J., Cummings, S. R., Evans, W. J., et al. (2011) · Journal of the American Medical Directors Association · doi:10.1016/j.jamda.2011.04.014 · Cited by 1,125
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
Tisdale, M. J. (2002) · Nature reviews. Cancer · doi:10.1038/nrc927 · Cited by 993
Morley, J. E., Baumgartner, R., Roubenoff, R., Mayer, J., & Nair, K. S. (2001) · Journal of Laboratory and Clinical Medicine · doi:10.1067/mlc.2001.113504 · Cited by 964
Reversal of Cancer Cachexia and Muscle Wasting by ActRIIB Antagonism Leads to Prolonged Survival
Zhou, X., Wang, J. L., Lu, J., Song, Y., Kwak, K. S., Jiao, Q., Rosenfeld, R., Chen, Q., Boone, T. C., Simonet, W. S., et al. (2010) · Cell · doi:10.1016/j.cell.2010.07.011 · Cited by 960
Self-citationUnderstanding the mechanisms and treatment options in cancer cachexia
Fearon, K. C. H., Arends, J., & Baracos, V. E. (2012) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2012.209 · Cited by 952
Myostatin Inhibits Myoblast Differentiation by Down-regulating MyoD Expression
Langley, B. C., Thomas, M., Bishop, A., Sharma, M., Gilmour, S., & Kambadur, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204291200 · Cited by 910
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
Prevalence of sarcopenia and predictors of skeletal muscle mass in healthy, older men and women
Iannuzzi-Sucich, M., Prestwood, K. M., & Kenny, A. M. (2002) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/57.12.m772 · Cited by 890
Signaling in Muscle Atrophy and Hypertrophy
Sandri, M. (2008) · Physiology · doi:10.1152/physiol.00041.2007 · Cited by 866
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
Mosher, D. S., Quignon, P., Bustamante, C. D., Sutter, N. B., Mellersh, C. S., Parker, H. G., & Ostrander, E. A. (2007) · PLoS Genetics · doi:10.1371/journal.pgen.0030079 · Cited by 826
Body composition and mortality in chronic obstructive pulmonary disease
Schols, A. M. W. J., Broekhuizen, R., Weling-Scheepers, C. A., & Wouters, E. F. �. (2005) · American Journal of Clinical Nutrition · doi:10.1093/ajcn.82.1.53 · Cited by 820
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
Myostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size
Trendelenburg, A. U., Meyer, A., Rohner, D., Boyle, J., Hatakeyama, S., & Glass, D. J. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00105.2009 · Cited by 792
Sarcopenia: origins and clinical relevance
Rosenberg, I. H. (2011) · Clinics in Geriatric Medicine · doi:10.1016/j.cger.2011.03.003 · Cited by 786
Myostatin negatively regulates satellite cell activation and self-renewal
McCroskery, S., Thomas, M., Maxwell, L., Sharma, M., & Kambadur, R. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200207056 · Cited by 784
Hemmati‐Brivanlou, A., Kelly, O., & Melton, D. A. (1994) · Cell · doi:10.1016/0092-8674(94)90320-4 · Cited by 761
Skeletal muscle loss: cachexia, sarcopenia, and inactivity
Evans, W. J. (2010) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.2010.28608a · Cited by 758
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
Self-citationA mouse model for spinal muscular atrophy
Hsieh‐Li, H. M., Chang, J., Jong, Y., Wu, M.-H., Wang, N. M., Tsai, C. H., & Li, H. (2000) · Nature Genetics · doi:10.1038/71709 · Cited by 704
A PGC-1α isoform induced by resistance training regulates skeletal muscle hypertrophy
Ruas, J. L., White, J. P., Rao, R. R., Kleiner, S., Brannan, K. T., Harrison, B. C., Greene, N. P., Wu, J., Estall, J. L., Irving, B. A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.050 · Cited by 677
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 610
Self-citationSacheck, 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
Self-citationWang, X., Hu, Z., Hu, J., Du, J., & Mitch, W. E. (2006) · Endocrinology · doi:10.1210/en.2006-0251 · Cited by 600
Self-citationSacheck, J. M., Hyatt, J. K., Raffaello, A., Thomas Jagoe, R., Roy, R. R., Reggie Edgerton, V., Lecker, S. H., & Goldberg, A. L. (2007) · The FASEB Journal · doi:10.1096/fj.06-6604com · Cited by 585
Self-citationBetaglycan binds inhibin and can mediate functional antagonism of activin signalling
Lewis, K. A., Gray, P. C., Blount, A. L., MacConell, L., Wiater, E., Bilezikjian, L. M., & Vale, W. (2000) · Nature · doi:10.1038/35006129 · Cited by 585
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
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
Mechanisms of glucocorticoid-induced myopathy
Schakman, O., Gilson, H., & Thissen, J. P. (2008) · Journal of Endocrinology · doi:10.1677/joe-07-0606 · Cited by 521
Smad2 and 3 transcription factors control muscle mass in adulthood
Sartori, R., Milan, G., Patron, M., Mammucari, C., Blaauw, B., Abraham, R., & Sandri, M. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00104.2009 · Cited by 517
Niche Regulation of Muscle Satellite Cell Self-Renewal and Differentiation
Kuang, S., Gillespie, M. A., & Rudnicki, M. A. (2008) · Cell Stem Cell · doi:10.1016/j.stem.2007.12.012 · Cited by 507
Tumor necrosis factor-α and muscle wasting: a cellular perspective
Reid, M. B., & Li, Y. (2001) · Respiratory Research · doi:10.1186/rr67 · Cited by 467
Dhawan, J., & Rando, T. A. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.10.007 · Cited by 466
Bailey, J. L., Wang, X., England, B. K., Price, S. R., Ding, X., & Mitch, W. E. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118566 · Cited by 455
Self-citationActivation of latent myostatin by the BMP-1/tolloid family of metalloproteinases
Wolfman, N. M., McPherron, A. C., Pappano, W. N., Davies, M. V., Song, K., Tomkinson, K. N., Wright, J. F., Zhao, L., Sebald, S. M., Greenspan, D. S., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2534946100 · Cited by 454
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
Mitch, W. E., Medina, R., Grieber, S., May, R. C., England, B. K., Price, S. R., Bailey, J. L., & Goldberg, A. L. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117208 · Cited by 405
Self-citationDevelopment of cancer cachexia-like syndrome and adrenal tumors in inhibin-deficient mice.
Matzuk, M. M., Finegold, M. J., Mather, J. P., KRUMMEN, L. A., Lu, H., & Bradley, A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.19.8817 · Cited by 374
May, R. C., Kelly, R. A., & Mitch, W. E. (1986) · Journal of Clinical Investigation · doi:10.1172/jci112344 · Cited by 374
Self-citationSignaling pathways perturbing muscle mass.
Glass, D. J. (2010) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/mco.0b013e32833862df · Cited by 359
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
Muscle-specific expression of IGF-1 blocks angiotensin II–induced skeletal muscle wasting
Song, Y., Li, Y., Du, J., Mitch, W. E., Rosenthal, N. A., & Delafontaine, P. (2005) · Journal of Clinical Investigation · doi:10.1172/jci22324 · Cited by 352
Self-citationPrice, S. R., Bailey, J. L., Wang, X., Jurkovitz, C. T., England, B. K., Ding, X., Phillips, L. S., & Mitch, W. E. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118968 · Cited by 348
Self-citationLagirand-Cantaloube, J., Offner, N., Csibi, A., Leibovitch, M.-P., Batonnet‐Pichon, S., Tintignac, L. A. J., Segura, C. T., & Leibovitch, S. A. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.52 · Cited by 344
May, R. C., Kelly, R. A., & Mitch, W. E. (1987) · Journal of Clinical Investigation · doi:10.1172/jci112924 · Cited by 324
Self-citationRegulation 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
Self-citationZhang, L., Rajan, V., Lin, E., Hu, Z., Han, H. Q., Zhou, X., Song, Y., Min, H., Wang, X., Du, J., et al. (2011) · The FASEB Journal · doi:10.1096/fj.10-176917 · Cited by 323
Self-citationDownstream of Akt: FoxO3 and mTOR in the regulation of autophagy in skeletal muscle
Mammucari, C., Schiaffino, S., & Sandri, M. (2008) · Autophagy · doi:10.4161/auto.5905 · Cited by 303
Shan, T., Liang, X., Bi, P., & Kuang, S. (2013) · The FASEB Journal · doi:10.1096/fj.12-225755 · Cited by 301
Yarasheski, K. E., Bhasin, S., Sinha‐Hikim, I., Pak-Loduca, J., & González-Cadavid, N. F. (2002) · PubMed · Cited by 293
Activin A and inhibin A as possible endocrine markers for pre-eclampsia
Muttukrishna, S., Knight, P. G., Groome, N., Redman, C., & Ledger, W. J. (1997) · The Lancet · doi:10.1016/s0140-6736(96)09264-1 · Cited by 285
Review of muscle wasting associated with chronic kidney disease
Workeneh, B., & Mitch, W. E. (2010) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.2010.28608b · Cited by 285
Self-citationJones, K. L., Mansell, A. S., Patella, S., Scott, B. J., Hedger, M. P., de Kretser, D., & Phillips, D. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705971104 · Cited by 284
Wasting in chronic kidney disease
Mak, R. H., Ikizler, A. T., Kovesdy, C. P., Raj, D. S., Stenvinkel, P., & Kalantar-Zadeh, K. (2011) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1007/s13539-011-0019-5 · Cited by 281
Choi, C. S., Befroy, D. E., Codella, R., Kim, S., Reznick, R. M., Hwang, Y.-J., Liu, Z.-X., Lee, H.-Y., Distefano, A., Samuel, V. T., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810339105 · Cited by 279
The metabolic fates of amino acids and the formation of glutamine in skeletal muscle.
Chang, T. W., & Goldberg, A. L. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34855-x · Cited by 274
Self-citationTries, R. S., Chen, T., Vies, M. V. D., Tomkinson, K. N., Pearson, A. A., Shakey, Q., & Wolfman, N. M. (2001) · Growth Factors · doi:10.3109/08977190109029114 · Cited by 265
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 265
Lysosomal proteolysis in skeletal muscle
Béchet, D., Tassa, A., Taillandier, D., Combaret, L., & Attaix, D. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.02.029 · Cited by 259
IL-6 and Serum Amyloid A Synergy Mediates Angiotensin II–Induced Muscle Wasting
Zhang, L., Du, J., Hu, Z., Han, G., Delafontaine, P., García, G., & Mitch, W. E. (2009) · Journal of the American Society of Nephrology · doi:10.1681/asn.2008060628 · Cited by 246
Self-citationMyostatin propeptide‐mediated amelioration of dystrophic pathophysiology
Bogdanovich, S., Perkins, K. J., Krag, T. O. B., Whittemore, L.-A., & Khurana, T. S. (2005) · The FASEB Journal · doi:10.1096/fj.04-2796com · Cited by 244
Modulation of myostatin expression during modified muscle use
Wehling, M., Cai, B.-Y., & Tidball, J. (2000) · The FASEB Journal · doi:10.1096/fasebj.14.1.103 · Cited by 238
Bailey, J. L., Zheng, B., Hu, Z., Price, S. R., & Mitch, W. E. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2004100842 · Cited by 238
Self-citationGenetic deletion of myostatin from the heart prevents skeletal muscle atrophy in heart failure
Heineke, J., Auger-Messier, M., Xu, J., Sargent, M., York, A., Welle, S., & Molkentin, J. D. (2010) · Circulation · doi:10.1161/circulationaha.109.882068 · Cited by 238
Evaluation of signals activating ubiquitin-proteasome proteolysis in a model of muscle wasting
Mitch, W. E., Bailey, J. L., Wang, X., Jurkovitz, C. T., Newby, D. E., & Price, S. R. (1999) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1999.276.5.c1132 · Cited by 237
Self-citationMorley, J. E. (2012) · Family Practice · doi:10.1093/fampra/cmr063 · Cited by 237
Vallet, S., Mukherjee, S., Vaghela, N., Hideshima, T., Fulciniti, M., Pozzi, S., Santo, L., Cirstea, D. D., Patel, K. J., Sohani, A. R., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911929107 · Cited by 231
Rosen, G., Wollner, N., Tan, C. R. C., Wu, S., Hajdu, S. I., Cham, W., D’Angio, G. J., & Murphy, M. L. (1974) · Cancer · doi:10.1002/1097-0142(197402)33:2 · Cited by 230
Klimek, M. B., Aydogdu, T., Link, M., Pons, M., Koniaris, L. G., & Zimmers, T. A. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.12.123 · Cited by 229
Reardon, K. A., Davis, J. A., Kapsa, R. M. I., Choong, P., & Byrne, E. (2001) · Muscle & Nerve · doi:10.1002/mus.1086 · Cited by 227
Effects of spaceflight on murine skeletal muscle gene expression
Allen, D. L., Bandstra, E. R., Harrison, B. C., Thorng, S., Stodieck, L., Kostenuik, P. J., Morony, S., Lacey, D. L., Hammond, T. G., Leinwand, L. A., et al. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.90780.2008 · Cited by 225
Brault, J. J., Jespersen, J. G., & Goldberg, A. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.113092 · Cited by 217
Self-citationSidis, Y., Mukherjee, A., Keutmann, H., Delbaere, A., Sadatsuki, M., & Schneyer, A. (2006) · Endocrinology · doi:10.1210/en.2006-0089 · Cited by 211
Satellite Cell Dysfunction and Impaired IGF-1 Signaling Cause CKD-Induced Muscle Atrophy
Zhang, L., Wang, X. H., Wang, H., Du, J., & Mitch, W. E. (2010) · Journal of the American Society of Nephrology · doi:10.1681/asn.2009060571 · Cited by 207
Self-citationCohen, S., Zhai, B., Gygi, S. P., & Goldberg, A. L. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201110067 · Cited by 205
Self-citationHu, Z., Wang, H., Lee, I. H., Du, J., & Mitch, W. E. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38770 · Cited by 205
Self-citationActivin signaling as an emerging target for therapeutic interventions
Tsuchida, K., Nakatani, M., Hitachi, K., Uezumi, A., Sunada, Y., Ageta, H., & Inokuchi, K. (2009) · Cell Communication and Signaling · doi:10.1186/1478-811x-7-15 · Cited by 202
Proinflammatory cytokines and skeletal muscle
te, U. S., & Schulze, P. C. (2004) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-200405000-00005 · Cited by 193
Zhang, C., McFarlane, C., Lokireddy, S., Masuda, S., Ge, X., Gluckman, P. D., Sharma, M., & Kambadur, R. (2012) · Diabetologia · doi:10.1007/s00125-011-2304-4 · Cited by 192
Cellular Markers of Muscle Atrophy in Chronic Obstructive Pulmonary Disease
Plant, P. J., Brooks, D., Faughnan, M., Bayley, T., Bain, J., Singer, L., Correa, J., Pearce, D., Binnie, M., & Batt, J. (2010) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2008-0382oc · Cited by 190
Nutrition in CAPD: Serum bicarbonate and the ubiquitin-proteasome system in muscle
Pickering, W. P., Price, S. R., Bircher, G., Marinovic, A. C., Mitch, W. E., & Walls, J. (2002) · Kidney International · doi:10.1046/j.1523-1755.2002.00276.x · Cited by 190
Self-citationMuscle myostatin signalling is enhanced in experimental cancer cachexia
Costelli, P., Muscaritoli, M., Bonetto, A., Penna, F., Reffo, P., Bossola, M., Bonelli, G., Doglietto, G. B., Baccino, F. M., & Fanelli, F. R. (2008) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2008.01970.x · Cited by 186
From muscle wasting to sarcopenia and myopenia: update 2012
von Haehling, S., Morley, J. E., & Anker, S. D. (2012) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-012-0089-z · Cited by 185
Huang, C., Tighiouart, H., Beddhu, S., Cheung, A. K., Dwyer, J. T., Eknoyan, G., Beck, G. J., Levey, A. S., & Sarnak, M. J. (2010) · Kidney International · doi:10.1038/ki.2009.524 · Cited by 183
Elevated Levels of Activin A in Heart Failure
Yndestad, A., Ueland, T., Øie, E., Florholmen, G., Halvorsen, B. L., Attramadal, H., Simonsen, S., Frøland, S. S., Gullestad, L. L., Christensen, G., et al. (2004) · Circulation · doi:10.1161/01.cir.0000120704.97934.41 · Cited by 181
Plank, L. D., & Hill, G. L. (2000) · World Journal of Surgery · doi:10.1007/s002689910104 · Cited by 180
LeBrasseur, N. K., Schelhorn, T. M., Bernardo, B. L., Cosgrove, P. G., Loria, P. M., & Brown, T. A. (2009) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glp068 · Cited by 180
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
Lee, S., Huynh, T. V., Lee, Y., Sebald, S. M., Wilcox‐Adelman, S. A., Iwamori, N., Lepper, C., Matzuk, M. M., & Fan, C. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206410109 · Cited by 177
Relationship between cortisone and muscle work in determining muscle size
Goldberg, A. L., & GOODMAN, H. M. (1969) · The Journal of Physiology · doi:10.1113/jphysiol.1969.sp008715 · Cited by 175
Self-citationMcIntyre, C. W., Selby, N. M., Sigrist, M. K., Pearce, L. E., Mercer, T. H., & Naish, P. (2006) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfl064 · Cited by 174
The role of insulin resistance in the development of muscle wasting during cancer cachexia
Honors, M. A., & Kinzig, K. P. (2011) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0051-5 · Cited by 171
Myostatin signals through Pax7 to regulate satellite cell self-renewal
McFarlane, C., Hennebry, A., Thomas, M., Plummer, E., Ling, N., Sharma, M., & Kambadur, R. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.09.012 · Cited by 171
Autocrine/paracrine regulation of pituitary function by activin, inhibin and follistatin
Bilezikjian, L. M., Blount, A. L., Leal, A. M. O., Donaldson, C., Fischer, W. H., & Vale, W. (2004) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2004.02.010 · Cited by 170
Koyama, S., Hata, S., Witt, C. C., Ono, Y., Lerche, S., Ojima, K., Chiba, T., Doi, N., Kitamura, F., Tanaka, K., et al. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.11.049 · Cited by 162
Kovesdy, C. P., George, S. M., Anderson, J. E., & Kalantar‐Zadeh, K. (2009) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.2008.27390 · Cited by 160
Identification of a Novel Pool of Extracellular Pro-myostatin in Skeletal Muscle
Anderson, S. B., Goldberg, A. L., & Whitman, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706678200 · Cited by 159
Self-citationZhang, C., McFarlane, C., Lokireddy, S., Bonala, S., Ge, X., Masuda, S., Gluckman, P. D., Sharma, M., & Kambadur, R. (2011) · Diabetologia · doi:10.1007/s00125-011-2079-7 · Cited by 158
Polge, C., Heng, A.-É., Jarzaguet, M., Ventadour, S., Claustre, A., Combaret, L., Béchet, D., Matondo, M., Uttenweiler‐Joseph, S., Monsarrat, B., et al. (2011) · The FASEB Journal · doi:10.1096/fj.11-180968 · Cited by 157
p53 expression and risk factors for cutaneous melanoma: A case-control study
Whiteman, D. C., Parsons, P. G., & Green, A. C. (1998) · International Journal of Cancer · doi:10.1002/(sici)1097-0215(19980911)77:6 · Cited by 154
Zheng, B., Ohkawa, S., Li, H., Roberts‐Wilson, T. K., & Price, S. R. (2010) · The FASEB Journal · doi:10.1096/fj.09-151480 · Cited by 145
Busquets, S., Toledo, M., Orpí, M., Massa, D., Porta, M. M., Capdevila, E., Padilla, N., Frailis, V., López-Soriano, F. J., Han, H. Q., et al. (2011) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-011-0049-z · Cited by 141
Self-citationThe effects of a soluble activin type IIB receptor on obesity and insulin sensitivity
Akpan, I., Goncalves, M. D., Dhir, R., Yin, X., Pistilli, E. E., Bogdanovich, S., Khurana, T. S., Ucran, J., Lachey, J., & Ahima, R. S. (2009) · International Journal of Obesity · doi:10.1038/ijo.2009.162 · Cited by 140
Lenk, K., Erbs, S., Höllriegel, R., Beck, E. B., Linke, A. H.-P., Gielen, S., Winkler, S. M., Sandri, M., Hambrecht, R., Schuler, G. C., et al. (2011) · European Journal of Preventive Cardiology · doi:10.1177/1741826711402735 · Cited by 140
Protein-Energy Wasting and Mortality in Chronic Kidney Disease
Bonanni, A., Mannucci, I., Verzola, D., Sofia, A., Saffioti, S., Gianetta, E., & Garibotto, G. (2011) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph8051631 · Cited by 139
Myostatin from the heart: local and systemic actions in cardiac failure and muscle wasting
Breitbart, A., Auger‐Messier, M., Molkentin, J. D., & Heineke, J. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00200.2011 · Cited by 139
Myostatin activation in patients with advanced heart failure and after mechanical unloading
George, I., Bish, L. T., Kamalakkannan, G., Petrilli, C. M., Oz, M. C., Naka, Y., Lee Sweeney, H., & Maybaum, S. (2010) · European Journal of Heart Failure · doi:10.1093/eurjhf/hfq039 · Cited by 136
Identification of atrogin-1-targeted proteins during the myostatin-induced skeletal muscle wasting
Lokireddy, S., Wijesoma, I. W., Sze, S. K., McFarlane, C., Kambadur, R., & Sharma, M. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00402.2011 · Cited by 135
The genetic origin and history of speed in the Thoroughbred racehorse
Bower, M. A., McGivney, B. A., Campana, M. G., Gu, J., Andersson, L. S., Barrett, E., Davis, C. R., Mikko, S., Stock, F., Воронкова, В. Н., et al. (2012) · Nature Communications · doi:10.1038/ncomms1644 · Cited by 133
Fournier, B., Murray, B., Gutzwiller, S., Marcaletti, S., Marcellin, D., Bergling, S., Brachat, S., Persohn, E., Pierrel, E., Bombard, F., et al. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06575-11 · Cited by 130
Murphy, K. T., Koopman, R., Naim, T., Léger, B., Trieu, J., Ibebunjo, C., & Lynch, G. S. (2010) · The FASEB Journal · doi:10.1096/fj.10-159608 · Cited by 129
Anker, S. D., Steinborn, W., & Strassburg, S. (2004) · Annals of Medicine · doi:10.1080/07853890410017467 · Cited by 129
Pituitary actions of ligands of the TGF-β family: activins and inhibins
Bilezikjian, L. M., Blount, A. L., Donaldson, C., & Vale, W. (2006) · Reproduction · doi:10.1530/rep.1.01073 · Cited by 128
Lokireddy, S., Mouly, V., Butler-Browne, G. S., Gluckman, P. D., Sharma, M., Kambadur, R., & McFarlane, C. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00114.2011 · Cited by 126
Muscular atrophy of caveolin-3–deficient mice is rescued by myostatin inhibition
Ohsawa, Y., Hagiwara, H., Nakatani, M., Yasue, A., Moriyama, K., Murakami, T., Tsuchida, K., Noji, S., & Sunada, Y. (2006) · Journal of Clinical Investigation · doi:10.1172/jci28520 · Cited by 122
Binns, M. M., Boehler, D. A., & Lambert, D. H. (2010) · Animal Genetics · doi:10.1111/j.1365-2052.2010.02126.x · Cited by 121
Zugmaier, G., Paik, S., Wilding, G., Knabbe, C., Bano, M., Lupu, R., Deschauer, B., Simpson, S., Dickson, R. B., & Lippman, M. E. (1991) · PubMed · Cited by 121
Satellite cell senescence underlies myopathy in a mouse model of limb-girdle muscular dystrophy 2H
Kudryashova, E., Kramerova, I., & Spencer, M. J. (2012) · Journal of Clinical Investigation · doi:10.1172/jci59581 · Cited by 119
Serum myostatin levels and skeletal muscle wasting in chronic obstructive pulmonary disease
Ju, C., & Chen, R. (2011) · Respiratory Medicine · doi:10.1016/j.rmed.2011.07.016 · Cited by 118
Role of glucocorticoids in the molecular regulation of muscle wasting
Menconi, M. J., Fareed, M. U., O’Neal, P., Poylin, V. Y., Wei, W., & Hasselgren, P. (2007) · Critical Care Medicine · doi:10.1097/01.ccm.0000279194.11328.77 · Cited by 118
Pistilli, E. E., Bogdanovich, S., Goncalves, M. D., Ahima, R. S., Lachey, J. L., Seehra, J. S., & Khurana, T. S. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.11.071 · Cited by 116
Decreased inhibin tone and increased activin A secretion characterize reproductive aging in women
Santoro, N. F., Adel, T. E., & Skurnick, J. (1999) · Fertility and Sterility · doi:10.1016/s0015-0282(98)00529-9 · Cited by 116
Human myostatin negatively regulates human myoblast growth and differentiation
McFarlane, C., Hui, G. Z., Amanda, W. Z. W., Lau, H. Y., Lokireddy, S., XiaoJia, G., Mouly, V., Butler-Browne, G. S., Gluckman, P. D., Sharma, M., et al. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00012.2011 · Cited by 115
Kwak, K. S., Zhou, X., Solomon, V., Baracos, V. E., Davis, J. G., Bannon, A. W., Boyle, W. J., Lacey, D. L., & Han, H. Q. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-2102 · Cited by 112
Self-citationRose, F. F., Mattis, V. B., Rindt, H., & Lorson, C. L. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn426 · Cited by 112
Antibody-Directed Myostatin Inhibition Enhances Muscle Mass and Function in Tumor-Bearing Mice
Murphy, K. T., Chee, A., Gleeson, B. G., Naim, T., Swiderski, K., Koopman, R., & Lynch, G. S. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00121.2011 · Cited by 111
Terpos, E., Kastritis, E., Christoulas, D., Gkotzamanidou, M. A., Eleutherakis‐Papaiakovou, E., Kanellias, N., Παπαθεοδώρου, Α., & Dimopoulos, M. A. (2012) · Annals of Oncology · doi:10.1093/annonc/mds068 · Cited by 109
Increased Plasma Myostatin in Heart Failure
Gruson, D., Ahn, S. A., Ketelslegers, J., & Rousseau, M. F. (2011) · European Journal of Heart Failure · doi:10.1093/eurjhf/hfr024 · Cited by 105
Regulation of Myostatin by Glucocorticoids After Thermal Injury
Lang, C. H., Silvis, C., Nystrom, G. J., & Frost, R. A. (2001) · The FASEB Journal · doi:10.1096/fj.00-0849fje · Cited by 105
Myostatin inhibition slows muscle atrophy in rodent models of amyotrophic lateral sclerosis
Holzbaur, E. L. F., Howland, D., Weber, N., Wallace, K. E., She, Y., Kwak, S., Tchistiakova, L. A., Murphy, E. K., Hinson, J., Karim, R., et al. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.05.009 · Cited by 104
Parsons, S. A., Millay, D. P., Sargent, M. A., McNally, E. M., & Molkentin, J. D. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.051316 · Cited by 102
Serum immunoreactive activin A levels in normal subjects and patients with various diseases
Harada, K., Shintani, Y., Sakamoto, Y., WAKATSUKI, M., Shitsukawa, K., & Saito, S. (1996) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.81.6.8964839 · Cited by 101
Overexpression of activin A in stage IV colorectal cancer
Wildi, S., Kleeff, J. H., Maruyama, H., Maurer, C. A., Büchler, M. W., & Korc, M. (2001) · Gut · doi:10.1136/gut.49.3.409 · Cited by 101
Myostatin expression in ventricular myocardium in a rat model of volume‐overload heart failure
Shyu, K., Lu, M.-J., Wang, B. W., Sun, H.-Y., & Chang, H. (2006) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2006.01718.x · Cited by 100
Targeting the myostatin signaling pathway to treat muscle wasting diseases
Han, H. Q., & Mitch, W. E. (2011) · Current Opinion in Supportive and Palliative Care · doi:10.1097/spc.0b013e32834bddf9 · Cited by 96
Self-citationActivin A induces cell proliferation of fibroblast‐like synoviocytes in rheumatoid arthritis
Ota, F., Maeshima, A., Yamashita, S., Ikeuchi, H., Kaneko, Y., Kuroiwa, T., Hiromura, K., Ueki, K., Kojima, I., & Nojima, Y. (2003) · Arthritis & Rheumatism · doi:10.1002/art.11249 · Cited by 96
Muscle mass, survival, and the elderly ICU patient
Griffiths, R. D. (1996) · Nutrition · doi:10.1016/s0899-9007(96)00141-4 · Cited by 94
Activin A: a novel player and inflammatory marker in inflammatory bowel disease?
Hübner, G., Brauchle, M. A., Gregor, M., & Werner, S. (1997) · PubMed · Cited by 94
Control of Hepatic Differentiation by Activin/TGFβ Signaling
Clotman, F., & Lemaigre, F. P. (2005) · Cell Cycle · doi:10.4161/cc.5.2.2341 · Cited by 86
The p97/VCP ATPase is critical in muscle atrophy and the accelerated degradation of muscle proteins
Piccirillo, R., & Goldberg, A. L. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.178 · Cited by 85
Self-citationMorrison, B. M., Lachey, J. L., Warsing, L. C., Ting, B. L., Pullen, A. E., Underwood, K. W., Kumar, R., Sako, D., Grinberg, A. V., Wong, V. L., et al. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.02.017 · Cited by 85
Changes in Myostatin Signaling in Non-Weight-Losing Cancer Patients
Aversa, Z., Bonetto, A., Penna, F., Costelli, P., Rienzo, G. D., Lacitignola, A., Baccino, F. M., Ziparo, V., Mercantini, P., Fanelli, F. R., et al. (2011) · Annals of Surgical Oncology · doi:10.1245/s10434-011-1720-5 · Cited by 85
Activins and Inhibins and Their Signaling
Vale, W., Wiater, E., Gray, P. C., Harrison, C. A., Bilezikjian, L. M., & Choe, S. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1315.023 · Cited by 84
Regulation of Inhibin Synthesis in the Rat Ovary
Woodruff, T. K., & Mayo, K. E. (1990) · Annual Review of Physiology · doi:10.1146/annurev.ph.52.030190.004111 · Cited by 83
Bamberger, C., Schärer, A., Antsiferova, M. A., Tychsen, B., Pankow, S., Müller, M. R., Rülicke, T., Paus, R., & Werner, S. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)62047-0 · Cited by 81
Baccarelli, A., Morpurgo, P. S., Corsi, A. M., Vaghi, I., Fanelli, M., Cremonesi, G., Vaninetti, S., Beck‐Peccoz, P., & Spada, A. (2001) · Experimental Gerontology · doi:10.1016/s0531-5565(01)00117-6 · Cited by 79
Elevated levels of activin A in clinical and experimental pulmonary hypertension
Yndestad, A., Larsen, K., Øie, E., Ueland, T., Smith, C., Halvorsen, B. L., Sjaastad, I., Skjønsberg, O. H., Pedersen, T. M., Anfinsen, O.-G., et al. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.90719.2008 · Cited by 78
Thomas, T. Z., Wang, H., Niclasen, P., O’Bryan, M. K., Evans, L. W., Groome, N. P., Pedersen, J., & Risbridger, G. P. (1997) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.82.11.4374 · Cited by 78
Hamrick, M. W., Arounleut, P., Kellum, E., Cain, M. A., Immel, D., & Liang, L. (2010) · The Journal of Trauma: Injury, Infection, and Critical Care · doi:10.1097/ta.0b013e3181c451f4 · Cited by 78
The role of cytokines in muscle wasting: Its relation with cancer cachexia
Argilés, J. M. A., Garcia‐Martínez, C., Llovera, M., & López-Soriano, F. J. (1992) · Medicinal Research Reviews · doi:10.1002/med.2610120605 · Cited by 76
Antagonism of activin by inhibin and inhibin receptors: a functional role for betaglycan-glycan
Gray, P. C., Bilezikjian, L. M., & Vale, W. W. (2001) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(01)00515-9 · Cited by 76
D’Antona, D., dos Reis, F. M., Benedetto, C., Evans, L., Groome, N., de Kretser, D., Wallace, E. M., & Petraglia, F. (2000) · Journal of Endocrinology · doi:10.1677/joe.0.1650157 · Cited by 75
Work-induced changes in skeletal muscle IGF-1 and myostatin gene expression in uremia
Sun, D., Chen, Y., & Rabkin, R. (2006) · Kidney International · doi:10.1038/sj.ki.5001532 · Cited by 74
Inhibiting myostatin reverses muscle fibrosis through apoptosis
Li, Z. B., Zhang, J., & Wagner, K. R. (2012) · Journal of Cell Science · doi:10.1242/jcs.090365 · Cited by 74
Muttukrishna, S., Child, T. J., Lockwood, G. M., Groome, N. P., Barlow, D. H., & Ledger, W. J. (2000) · Human Reproduction · doi:10.1093/humrep/15.3.549 · Cited by 74
Morine, K., Bish, L. T., Selsby, J. T., Gazzara, J. A., Pendrak, K., Sleeper, M. M., Barton, E. R., Lee, S., & Sweeney, H. L. (2010) · Muscle & Nerve · doi:10.1002/mus.21743 · Cited by 73
Rajan, V., & Mitch, W. E. (2007) · Pediatric Nephrology · doi:10.1007/s00467-007-0594-z · Cited by 73
Self-citationActivin-A regulates follistatin secretion from cultured rat anterior pituitary cells
Bilezikjian, L. M., CORRIGAN, A. Z., Vaughan, J. M., & Vale, W. (1993) · Endocrinology · doi:10.1210/endo.133.6.8243277 · Cited by 72
Koncarevic, A., Cornwall-Brady, M., Pullen, A., Davies, M., Sako, D., Liu, J., Kumar, R., Tomkinson, K., Baker, T., Umiker, B., et al. (2010) · Endocrinology · doi:10.1210/en.2010-0134 · Cited by 71
Lawlor, M. W., Read, B., Edelstein, R., Yang, N. J., Pierson, C. R., Stein, M. J., Wermer-Colan, A., Buj‐Bello, A., Lachey, J. L., Seehra, J. S., et al. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.10.035 · Cited by 68
Bernardo, B. L., Wachtmann, T. S., Cosgrove, P. G., Kühn, M., Opsahl, A., Judkins, K. M., Freeman, T. B., Hadcock, J. R., & LeBrasseur, N. K. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011307 · Cited by 68
Zachwieja, J. J., Smith, S. R., Sinha‐Hikim, I., González-Cadavid, N. F., & Bhasin, S. (1999) · PubMed · Cited by 66
Murphy, K. T., Ryall, J. G., Snell, S. M., Nair, L., Koopman, R., Krasney, P. A., Ibebunjo, C., Holden, K. S., Loria, P. M., Salatto, C. T., et al. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090932 · Cited by 66
Atrophy of the Heart: A Correlative Study of Eighty-Five Proved Cases
Hellerstein, H. K., & Santiago-Stevenson, D. (1950) · Circulation · doi:10.1161/01.cir.1.1.93 · Cited by 66
Production of activin A and its roles in inflammation and hematopoiesis.
Yu, J. C. L., & Dolter, K. E. (1997) · PubMed · Cited by 64
Pires-Oliveira, M., Maragno, A. L., Parreiras‐e‐Silva, L. T., Chiavegatti, T., Gomes, M. D., & Godinho, R. O. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00490.2009 · Cited by 63
Inhibin Resistance Is Associated with Aggressive Tumorigenicity of Ovarian Cancer Cells
Steller, M. D., Shaw, T. J., Vanderhyden, B. C., & Éthier, J.-F. (2005) · Molecular Cancer Research · doi:10.1158/1541-7786.50.3.1 · Cited by 62
Acute antibody-directed myostatin inhibition attenuates disuse muscle atrophy and weakness in mice
Murphy, K. T., Cobani, V., Ryall, J. G., Ibebunjo, C., & Lynch, G. S. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01183.2010 · Cited by 59
Chang, K., Kao, H., Liang, Y. J., Cheng, M., Chang, Y., Liu, S.-C., Lin, Y., Ko, T. Y., Lee, Y., Tsai, C.-L., et al. (2010) · Annals of Surgical Oncology · doi:10.1245/s10434-010-0926-2 · Cited by 58
Flagged first, then by citations
4 of the 231 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
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
Self-citationMechanisms of muscle wasting in chronic kidney disease
Wang, X. H., & Mitch, W. E. (2014) · Nature Reviews Nephrology · doi:10.1038/nrneph.2014.112 · Cited by 630
Self-citationSarcopenia from mechanism to diagnosis and treatment in liver disease
Dasarathy, S., & Merli, M. (2016) · Journal of Hepatology · doi:10.1016/j.jhep.2016.07.040 · Cited by 608
Role of Myokines in Regulating Skeletal Muscle Mass and Function
Lee, J. H., & Jun, H.-S. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00042 · Cited by 432
Leal, L. G., Lopes, M. A., & Batista, M. L. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01307 · Cited by 382
“In addition to the ability to modulate the Smad, FOXO and AKT pathways, the interaction between myostatin and physical exercise also appears to occur through the transcription factor peroxisome proliferator-activated receptor gamma co-activator 1-alpha (PGC-1α) in muscle, which in turn is stimulated by exercise (Han e…”
Background
Metadata
- Authors
- Han, H. Q., Zhou, X., Mitch, W. E., & Goldberg, A. L.
- Affiliations
- Amgen (United States) (US)
- Baylor College of Medicine (US)
- Harvard University (US)
- Corresponding author
- Han, H.Q.
- Venue
- The International Journal of Biochemistry & Cell Biology
- Publisher
- Elsevier BV
- Published
- 2013-10
- Volume
- 45
- Issue
- 10
- Pages
- 2333-2347
- ISSN
- 1357-2725 (ISSN-L)
- OpenAlex
- W1971189666
- Cited by
- 314
- References
- 231
- Citations by year
- 2026: 25 · 2025: 27 · 2024: 25 · 2023: 12 · 2022: 26 · 2021: 26 · 2020: 32 · 2019: 29 · 2018: 21 · 2017: 20 · 2016: 22 · 2015: 17 · 2014: 23 · 2013: 9
- FWCI
- 2.23
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The International Journal of Biochemistry & Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- myostatin, activin, muscle atrophy, Smad2/3 signaling, ubiquitin-proteasome system, autophagy, Akt signaling, muscle protein synthesis, cancer cachexia, renal failure, lifespan extension, insulin sensitivity, adiposity, systemic inflammation, fracture healing
- MeSH terms
- Animals, Humans, Muscle Proteins, Muscular Diseases, Signal Transduction, Muscle, Skeletal, Ubiquitin, Activins, Ubiquitin-Protein Ligases, Proteasome Endopeptidase Complex, Myostatin, Molecular Targeted Therapy
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review