Runx1 prevents wasting, myofibrillar disorganization, and autophagy of skeletal muscle

Repertoires of Autophagy in the Pathogenesis of Ocular Diseases

Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351 · see citing works

Calcium's Role in Mechanotransduction during Muscle Development

Damm, T. B., & Egli, M. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000356667 · Cited by 14,548 · see citing works

Osf2/Cbfa1: A Transcriptional Activator of Osteoblast Differentiation

Ducy, P., Zhang, R., Geoffroy, V., Ridall, A. L., & Karsenty, G. (1997) · Cell · doi:10.1016/s0092-8674(00)80257-3 · Cited by 4,246 · see citing works

Targeted Disruption of Results in a Complete Lack of Bone Formation owing to Maturational Arrest of Osteoblasts

Komori, T., Yagi, H., Nomura, S., Yamaguchi, A., Sasaki, K., Deguchi, K., Shimizu, Y., Bronson, R. T., Gao, Y.-H., Inada, M., et al. (1997) · Cell · doi:10.1016/s0092-8674(00)80258-5 · Cited by 4,244 · see citing works

Autophagy as a regulated pathway of cellular degradation.

Klionsky, D., & Emr, S. (2000) · Science · doi:10.1126/science.290.5497.1717 · Cited by 3,794 · 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

Autophagy in Health and Disease: A Double-Edged Sword

Shintani, T., & Klionsky, D. J. (2004) · Science · doi:10.1126/science.1099993 · Cited by 2,531 · see citing works

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

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

AML1, the target of multiple chromosomal translocations in human leukemia, is essential for normal fetal liver hematopoiesis.

Okuda, T., van Deursen, J., Hiebert, S. W., Grosveld, G., & Downing, J. R. (1996) · Cell · doi:10.1016/s0092-8674(00)80986-1 · Cited by 1,856 · 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

Autophagy as a cell death and tumor suppressor mechanism

Gözüaçık, D., & Kimchi, A. (2004) · Oncogene · doi:10.1038/sj.onc.1207521 · Cited by 1,386 · 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

A Muscle-Specific Insulin Receptor Knockout Exhibits Features of the Metabolic Syndrome of NIDDM without Altering Glucose Tolerance

Brüning, J. C., Michael, M. D., Winnay, J. N., Hayashi, T., Hörsch, D., Accili, D., Goodyear, L. J., & Kahn, C. R. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80155-0 · Cited by 1,183 · see citing works

Disruption of the Cbfa2 gene causes necrosis and hemorrhaging in the central nervous system and blocks definitive hematopoiesis.

Wang, Q., Stacy, T., Binder, M., Marin-Padilla, M., Sharpe, A. H., & Speck, N. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.8.3444 · Cited by 1,178 · see citing works

A missense mutation in the αB-crystallin chaperone gene causes a desmin-related myopathy

Vicart, P., Caron, A., Guicheney, P., Li, Z., Prévost, M., Faure, A., Château, D., Chapon, F., Tomé, F. M. S., Dupret, J., et al. (1998) · Nature Genetics · doi:10.1038/1765 · Cited by 1,077 · see citing works

Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease)

Nishino, I., Fu, J., Tanji, K., Yamada, T., Shimojo, S., Koori, T., Mora, M., Riggs, J. E., Oh, S. J., Koga, Y., et al. (2000) · Nature · doi:10.1038/35022604 · Cited by 959 · see citing works

Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice

Tanaka, Y., Guhde, G., Suter, A., Eskelinen, E.-L., Hartmann, D., Lüllmann-Rauch, R., Janssen, P. M. L., Blanz, J., von Figura, K., & Saftig, P. (2000) · Nature · doi:10.1038/35022595 · Cited by 925 · see citing works

Differential Requirements for Runx Proteins in CD4 Repression and Epigenetic Silencing during T Lymphocyte Development

Taniuchi, I., Osato, M., Egawa, T., Sunshine, M. J., Bae, S., Komori, T., Ito, Y., & Littman, D. R. (2002) · Cell · doi:10.1016/s0092-8674(02)01111-x · Cited by 732 · see citing works

Signalling pathways that mediate skeletal muscle hypertrophy and atrophy

Glass, D. J. (2003) · Nature Cell Biology · doi:10.1038/ncb0203-87 · Cited by 694 · see citing works

IGF-1 induces skeletal myocyte hypertrophy through calcineurin in association with GATA-2 and NF-ATc1

Musarò, A., McCullagh, K. J. A., Naya, F. J., Olson, E. N., & Rosenthal, N. A. (1999) · Nature · doi:10.1038/23060 · Cited by 652 · see citing works

The Analysis of Gene Expression Data: Methods and Software

Boyle, T. (2005) · Journal of Statistical Software · doi:10.18637/jss.v014.b01 · Cited by 514 · see citing works

Missense mutations in desmin associated with familial cardiac and skeletal myopathy

Goldfarb, L. G., Park, K., Červen̆áková, L., Gorokhova, S., Lee, H.-S., Vasconcelos, O. M., Nagle, J. W., Semino-Mora, C., Sivakumar, K., & Dalakas, M. C. (1998) · Nature Genetics · doi:10.1038/1300 · Cited by 504 · see citing works

Changes in muscle mass and phenotype and the expression of autocrine and systemic growth factors by muscle in response to stretch and overload

GOLDSPINK, G. (1999) · Journal of Anatomy · doi:10.1046/j.1469-7580.1999.19430323.x · Cited by 435 · see citing works

Hormones, Growth Factors, and Myogenic Differentiation

Florini, J. R., Ewton, D. Z., & Magri, K. A. (1991) · Annual Review of Physiology · doi:10.1146/annurev.ph.53.030191.001221 · Cited by 419 · 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

Myofibrillar myopathy: clinical, morphological and genetic studies in 63 patients

Selcen, D. (2004) · Brain · doi:10.1093/brain/awh052 · Cited by 299 · see citing works

Mutations in myotilin cause myofibrillar myopathy

Selcen, D., & Engel, A. G. (2004) · Neurology · doi:10.1212/01.wnl.0000123576.74801.75 · Cited by 295 · see citing works

Myofibrillar myopathy caused by novel dominant negative αB‐crystallin mutations

Selcen, D., & Engel, A. G. (2003) · Annals of Neurology · doi:10.1002/ana.10767 · Cited by 259 · see citing works

A dysfunctional desmin mutation in a patient with severe generalized myopathy

Muñoz-Mármol, A. M., Strasser, G. A., Isamat, M., Coulombe, P. A., Yang, Y., Roca, X., Vela, E., Mate, J. L., Coll, J., Fernández‐Figueras, M. T., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.19.11312 · Cited by 255 · see citing works

Transcriptional autoregulation of the bone related CBFA1/RUNX2 gene

Drissi, H., Luc, Q., Shakoori, R., Lopes, S. M. C. D. S., Choi, J., Terry, A., Hu, M., Jones, S. N., Neil, J. C., Lian, J. B., et al. (2000) · Journal of Cellular Physiology · doi:10.1002/1097-4652(200009)184:3 · Cited by 251 · see citing works

Core-binding factors in hematopoiesis and immune function

Bruijn, M. F. T. R. D., & Speck, N. A. (2004) · Oncogene · doi:10.1038/sj.onc.1207763 · Cited by 231 · see citing works

Ras is involved in nerve-activity-dependent regulation of muscle genes

Murgia, M., Serrano, A. L., Calabria, E., Pallafacchina, G., Lømo, T., & Schiaffino, S. (2000) · Nature Cell Biology · doi:10.1038/35004013 · Cited by 218 · see citing works

Role of RUNX family members in transcriptional repression and gene silencing

Durst, K. L., & Hiebert, S. W. (2004) · Oncogene · doi:10.1038/sj.onc.1207122 · Cited by 184 · see citing works

Autophagic vacuolar myopathies

Nishino, I. (2003) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-003-0040-y · Cited by 123 · see citing works

The Analysis of Gene Expression Data: An Overview of Methods and Software

Parmigiani, G., Garrett, E. S., Irizarry, R. A., & Zeger, S. L. (2003) · Statistics for biology and health · doi:10.1007/0-387-21679-0_1 · Cited by 96 · see citing works

Epigenetic gene silencing by Runx proteins

Taniuchi, I., & Littman, D. R. (2004) · Oncogene · doi:10.1038/sj.onc.1207671 · Cited by 68 · see citing works

AML1 Is Expressed in Skeletal Muscle and Is Regulated by Innervation

Zhu, X., Yeadon, J. E., & Burden, S. J. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.12.8051-8057.1994 · Cited by 62 · see citing works

Cloning and Characterization of Cytokeratins 8 and 19 in Adult Rat Striated Muscle

Ursitti, J. A., Lee, P. C., Resneck, W. G., McNally, M. M., Bowman, A. L., O’Neill, A., Stone, M. R., & Bloch, R. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400128200 · Cited by 59 · see citing works

Direct activation of Sex-lethal transcription by the Drosophila Runt protein

Kramer, S. G., Jinks, T., Schedl, P. D., & Gergen, J. P. (1999) · Development · doi:10.1242/dev.126.1.191 · Cited by 51 · see citing works

Differences in the Function of Three Conserved E-boxes of the Muscle Creatine Kinase Gene in Cultured Myocytes and in Transgenic Mouse Skeletal and Cardiac Muscle

Nguyen, Q.-G. V., Buskin, J. N., Himeda, C. L., Shield, M. A., & Hauschka, S. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308194200 · Cited by 26 · see citing works

Accelerated Response of the myogenin Gene to Denervation in Mutant Mice Lacking Phosphorylation of Myogenin at Threonine 87

Blagden, C. S., Fromm, L., & Burden, S. J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.5.1983-1989.2004 · Cited by 16 · see citing works

Axonal loss in multiple sclerosis lesions: magnetic resonance imaging insights substrates of disability

Sperfeld (1999) · Pure Amsterdam UMC · doi:10.1002/1531-8249(199911)46:5 · Cited by 2 · see citing works

Autophagy is required to maintain muscle mass.

Masiero, E., Agatea, L., Mammucari, C., Blaauw, B., Loro, E., Komatsu, M., Metzger, D., Reggiani, C., Schiaffino, S., & Sandri, M. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.10.008 · Cited by 1,282 · see citing works

Skeletal muscle atrophy and the E3 ubiquitin ligases MuRF1 and MAFbx/atrogin-1

Bodine, S. C., & Baehr, L. M. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00204.2014 · Cited by 1,117 · see citing works

Signaling in Muscle Atrophy and Hypertrophy

Sandri, M. (2008) · Physiology · doi:10.1152/physiol.00041.2007 · Cited by 830 · see citing works

Signaling Pathways in Skeletal Muscle Remodeling

Bassel‐Duby, R., & Olson, E. N. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142622 · Cited by 799 · see citing works

Autophagy as a Stress-Response and Quality-Control Mechanism: Implications for Cell Injury and Human Disease

Murrow, L. M., & Debnath, J. (2012) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-020712-163918 · Cited by 526 · see citing works

Autophagy: Basic Principles and Relevance to Disease

Kundu, M., & Thompson, C. B. (2008) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathmechdis.2.010506.091842 · Cited by 523 · see citing works

Autophagy in skeletal muscle

Sandri, M. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.056 · Cited by 451 · see citing works

The Sick and the Weak: Neuropathies/Myopathies in the Critically Ill

Friedrich, O., Reid, M. B., den Berghe, G. V., Vanhorebeek, I., Hermans, G., Rich, M. M., & Larsson, L. (2015) · Physiological Reviews · doi:10.1152/physrev.00028.2014 · Cited by 394 · see citing works

Mitochondrial pathways in sarcopenia of aging and disuse muscle atrophy

Calvani, R., Joseph, A.-M., Adhihetty, P. J., Miccheli, A., Bossola, M., Leeuwenburgh, C., Bernabei, R., & Marzetti, E. (2013) · bchm · doi:10.1515/hsz-2012-0247 · Cited by 328 · see citing works

Dual roles of autophagy in the survival of <i>Caenorhabditis elegans</i> during starvation

Kang, C., You, Y.-J., & Avery, L. (2007) · Genes &amp; Development · doi:10.1101/gad.1573107 · Cited by 294 · see citing works

Generation of cell lines with tetracycline‐regulated autophagy and a role for autophagy in controlling cell size

Hosokawa, N., Hara, Y., & Mizushima, N. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.04.008 · Cited by 262 · see citing works

A transcriptional map of the impact of endurance exercise training on skeletal muscle phenotype

Keller, P., Vollaard, N. B. J., Gustafsson, T., Gallagher, I. J., Sundberg, C. J., Rankinen, T., Britton, S. L., Bouchard, C., Koch, L. G., & Timmons, J. A. (2011) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00634.2010 · Cited by 261 · see citing works

Stress-induced Skeletal Muscle Gadd45a Expression Reprograms Myonuclei and Causes Muscle Atrophy

Ebert, S. M., Dyle, M. C., Kunkel, S. D., Bullard, S. A., Bongers, K. S., Fox, D. K., Dierdorff, J. M., Foster, E. D., & Adams, C. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.374777 · Cited by 221 · see citing works

RUNX transcription factors: orchestrators of development

Mevel, R., Draper, J. E., Lie-a-Ling, M., Kouskoff, V., & Lacaud, G. (2019) · Development · doi:10.1242/dev.148296 · Cited by 211 · see citing works

Bone and muscle loss after spinal cord injury: organ interactions

Qin, W., Bauman, W. A., & Cardozo, C. P. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05806.x · Cited by 189 · see citing works

Autophagy and ALS: mechanistic insights and therapeutic implications

Chua, J. P., De Calbiac, H., Kabashi, E., & Barmada, S. J. (2022) · Autophagy · doi:10.1080/15548627.2021.1926656 · Cited by 189 · see citing works

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

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

Activation of autophagy in human skeletal muscle is dependent on exercise intensity and AMPK activation

Schwalm, C., Jamart, C., Benoit, N., Naslain, D., Prémont, C., Prévet, J., Thienen, R. V., Deldicque, L., & Francaux, M. (2015) · The FASEB Journal · doi:10.1096/fj.14-267187 · Cited by 174 · see citing works

Early Parenteral Nutrition Evokes a Phenotype of Autophagy Deficiency in Liver and Skeletal Muscle of Critically Ill Rabbits

Derde, S., Vanhorebeek, I., Güiza, F., Derese, I., Gunst, J., Fahrenkrog, B., Martinet, W., Vervenne, H. B. V. K., Ververs, E.-J., Larsson, L., et al. (2012) · Endocrinology · doi:10.1210/en.2011-2068 · Cited by 164 · see citing works

Autophagy in health and disease. 3. Involvement of autophagy in muscle atrophy

Sandri, M. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00531.2009 · Cited by 152 · see citing works

Cellular and molecular events controlling skeletal muscle mass in response to altered use

Favier, F. B., Benoit, H., & Freyssenet, D. G. (2008) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-007-0423-z · Cited by 149 · see citing works

Mechanisms of muscle growth and atrophy in mammals and Drosophila

Piccirillo, R., Demontis, F., Perrimon, N., & Goldberg, A. L. (2013) · Developmental Dynamics · doi:10.1002/dvdy.24036 · Cited by 145 · 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

The role of autophagy in sensitizing malignant glioma cells to radiation therapy

Zhuang, W., Qin, Z., & Liang, Z. (2009) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmp028 · Cited by 128 · see citing works

Gene profiling of skeletal muscle in an amyotrophic lateral sclerosis mouse model

de Aguilar, J. G., Niederhauser-Wiederkehr, C., Halter, B., de Tapia, M., Scala, F. D., Demougin, P., Dupuis, L., Primig, M., Meininger, V., & Loeffler, J. (2007) · Physiological Genomics · doi:10.1152/physiolgenomics.00017.2007 · Cited by 125 · see citing works

The beneficial role of proteolysis in skeletal muscle growth and stress adaptation

Bell, R. A. V., Al-Khalaf, M. H., & Megeney, L. A. (2016) · Skeletal Muscle · doi:10.1186/s13395-016-0086-6 · Cited by 117 · see citing works

Voluntary resistance wheel exercise from mid-life prevents sarcopenia and increases markers of mitochondrial function and autophagy in muscles of old male and female C57BL/6J mice

White, Z. R., Terrill, J. R., White, R. B., McMahon, C., Sheard, P., Grounds, M. D., & Shavlakadze, T. (2016) · Skeletal Muscle · doi:10.1186/s13395-016-0117-3 · Cited by 119 · see citing works

Runx1 Directly Promotes Proliferation of Hair Follicle Stem Cells and Epithelial Tumor Formation in Mouse Skin

Hoi, C. S. L., Lee, S. E., Lu, S.-Y., McDermitt, D. J., Osorio, K. M., Piskun, C. M., Peters, R. M., Paus, R., & Tumbar, T. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01308-09 · Cited by 116 · see citing works

MIR106A-5p upregulation suppresses autophagy and accelerates malignant phenotype in nasopharyngeal carcinoma

Zhu, Q., Zhang, Q., Gu, M., Zhang, K., Xia, T., Zhang, S., Chen, W., Yin, H., Yao, H., Fan, Y., et al. (2020) · Autophagy · doi:10.1080/15548627.2020.1781368 · Cited by 115 · see citing works

To be or not to be, the level of autophagy is the question: Dual roles of autophagy in the survival response to starvation

Kang, C., & Avery, L. (2008) · Autophagy · doi:10.4161/auto.5154 · Cited by 124 · see citing works

Different autonomous myogenic cell populations revealed by ablation of Myf5-expressing cells during mouse embryogenesis

Gensch, N., Borchardt, T., Schneider, A., Riethmacher, D., & Braun, T. W. (2008) · Development · doi:10.1242/dev.019331 · Cited by 113 · see citing works

Runx1 modulates developmental, but not injury-driven, hair follicle stem cell activation

Osorio, K. M., Lee, S. E., McDermitt, D. J., Waghmare, S. K., Zhang, Y. V., Woo, H. N., & Tumbar, T. (2008) · Development · doi:10.1242/dev.012799 · Cited by 112 · see citing works

Dexamethasone-induced autophagy mediates muscle atrophy through mitochondrial clearance

Troncoso, R., Paredes, F., Parra, V., Gatica, D., Vásquez-Trincado, C., Quiroga, C., Bravo, R., López‐Crisosto, C., Rodriguez, A. E., Oyarzún, A. P., et al. (2014) · Cell Cycle · doi:10.4161/cc.29272 · Cited by 108 · see citing works

Of bears, frogs, meat, mice and men: complexity of factors affecting skeletal muscle mass and fat

Shavlakadze, T., & Grounds, M. D. (2006) · BioEssays · doi:10.1002/bies.20479 · Cited by 103 · see citing works

Failed reinnervation in aging skeletal muscle

Aare, S., Spendiff, S., Vuda, M., Elkrief, D., Pérez, A., Wu, Q., Mayaki, D., Hussain, S. N. A., Hettwer, S., & Hepple, R. T. (2016) · Skeletal Muscle · doi:10.1186/s13395-016-0101-y · Cited by 102 · see citing works

Mitochondrial and sarcoplasmic reticulum abnormalities in cancer cachexia: Altered energetic efficiency?

de Oliveira, C. C. F., Busquets, S., Toledo, M., Penna, F., Aylwin, M. P., Sirisi, S., Ventura‐Silva, A. P., Orpí, M., García, A., Sette, A., et al. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.11.009 · Cited by 101 · see citing works

RUNX1: an emerging therapeutic target for cardiovascular disease

Riddell, A., McBride, M., Braun, T., Nicklin, S., Cameron, E., Loughrey, C., & Martin, T. P. (2020) · Cardiovascular Research · doi:10.1093/cvr/cvaa034 · Cited by 91 · see citing works

S6 kinase inactivation impairs growth and translational target phosphorylation in muscle cells maintaining proper regulation of protein turnover

Mieulet, V., Roceri, M., Espeillac, C., Sotiropoulos, A., Ohanna, M., Oorschot, V., Klumperman, J., Sandri, M., & Pende, M. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00499.2006 · Cited by 99 · see citing works

Runx1 Transcription Factor Is Required for Myoblasts Proliferation during Muscle Regeneration

Umansky, K. B., Gruenbaum‐Cohen, Y., Tsoory, M., Feldmesser, E., Goldenberg, D., Brenner, O. J., & Groner, Y. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005457 · Cited by 88 · see citing works

Autophagy in Skeletal Muscle Homeostasis and in Muscular Dystrophies

Grumati, P., & Bonaldo, P. (2012) · Cells · doi:10.3390/cells1030325 · Cited by 87 · see citing works

Molecular analyses provide insight into mechanisms underlying sarcopenia and myofibre denervation in old skeletal muscles of mice

Barns, M. E., Gondro, C., Tellam, R. L., Radley‐Crabb, H. G., Grounds, M. D., & Shavlakadze, T. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.04.025 · Cited by 84 · see citing works

AML1/RUNX1 Phosphorylation by Cyclin-Dependent Kinases Regulates the Degradation of AML1/RUNX1 by the Anaphase-Promoting Complex

Biggs, J. R., Peterson, L. F., Zhang, Y., Kraft, A. S., & Zhang, D. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00597-06 · Cited by 83 · see citing works

Identification of Genes that Elicit Disuse Muscle Atrophy via the Transcription Factors p50 and Bcl-3

Wu, C., Kandarian, S. C., & Jackman, R. W. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016171 · Cited by 82 · see citing works

Transcriptional activation of TFEB/ZKSCAN3 target genes underlies enhanced autophagy in spinobulbar muscular atrophy

Chua, J. P., Reddy, S., Merry, D. E., Adachi, H., Katsuno, M., Sobue, G., Robins, D. M., & Lieberman, A. P. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt527 · Cited by 77 · see citing works

Decoding the transcriptome of denervated muscle at single‐nucleus resolution

Lin, H., Ma, X., Sun, Y., Peng, H., Wang, Y., Thomas, S. S., & Hu, Z. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13023 · Cited by 69 · see citing works

RUNX1 and its understudied role in breast cancer

Janes, K. A. (2011) · Cell Cycle · doi:10.4161/cc.10.20.18029 · Cited by 70 · see citing works

Differential skeletal muscle gene expression after upper or lower motor neuron transection

Zeman, R. J., Zhao, J., Zhang, Y., Zhao, W., Wen, X., Wu, Y., Pan, J., Bauman, W. A., & Cardozo, C. P. (2009) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-009-0643-5 · Cited by 71 · see citing works

Neuron specific reduction in cuznsod is not sufficient to initiate a full sarcopenia phenotype

Sataranatarajan, K., Qaisar, R., Davis, C., Sakellariou, G. K., Vasilaki, A., Zhang, Y., Liu, Y., Bhaskaran, S., McArdle, A., Jackson, M., et al. (2015) · Redox Biology · doi:10.1016/j.redox.2015.04.005 · Cited by 67 · see citing works

Novel Approach to Meta-Analysis of Microarray Datasets Reveals Muscle Remodeling-related Drug Targets and Biomarkers in Duchenne Muscular Dystrophy

Kotelnikova, E. A., Shkrob, M., Pyatnitskiy, M. A., Ferlini, A., & Daraselia, N. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002365 · Cited by 66 · see citing works

The role of MyoD1 and histone modifications in the activation of muscle enhancers

Blum, R., & Dynlacht, B. D. (2013) · Epigenetics · doi:10.4161/epi.25441 · Cited by 63 · see citing works

Neurofibromin (Nf1) is required for skeletal muscle development

Kossler, N., Stricker, S., Rödelsperger, C., Robinson, P. N., Kim, J., Dietrich, C., Osswald, M., Kühnisch, J., Stevenson, D. A., Braun, T. W., et al. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr149 · Cited by 64 · see citing works

Multi-transcriptome analysis following an acute skeletal muscle growth stimulus yields tools for discerning global and MYC regulatory networks

Murach, K. A., Liu, Z., Jude, B., Figueiredo, V. C., Wen, Y., Khadgi, S., Lim, S., da Silva, F. M., Greene, N. P., Lanner, J. T., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102515 · Cited by 60 · see citing works

Age-related Differences in Dystrophin: Impact on Force Transfer Proteins, Membrane Integrity, and Neuromuscular Junction Stability

Hughes, D. C., Marcotte, G. R., Marshall, A. G., West, D. W. D., Baehr, L. M., Wallace, M. A., Saleh, P. M., Bodine, S. C., & Baar, K. (2016) · The Journals of Gerontology Series A · doi:10.1093/gerona/glw109 · Cited by 61 · see citing works

Gene expression and muscle fiber function in a porcine ICU model

Banduseela, V. C., Ochala, J., Chen, Y., Göransson, H., Norman, H. S., Radell, P. J., Eriksson, L. I., Hoffman, E. P., & Larsson, L. (2009) · Physiological Genomics · doi:10.1152/physiolgenomics.00026.2009 · Cited by 60 · see citing works

Resistance Training Enhances Skeletal Muscle Innervation Without Modifying the Number of Satellite Cells or their Myofiber Association in Obese Older Adults

Messi, M. L., Li, T., Wang, Z.-M., Marsh, A. P., Nicklas, B. J., & Delbono, O. (2015) · The Journals of Gerontology Series A · doi:10.1093/gerona/glv176 · Cited by 60 · see citing works

Cathepsin B Contributes to Autophagy-related 7 (Atg7)-induced Nod-like Receptor 3 (NLRP3)-dependent Proinflammatory Response and Aggravates Lipotoxicity in Rat Insulinoma Cell Line

Li, S., Du, L., Zhang, L., Hu, Y., Xia, W., Wu, J., Zhu, J., Chen, L., Zhu, F., Li, C., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.494286 · Cited by 58 · see citing works

RUNX transcription factors: association with pediatric asthma and modulated by maternal smoking

Haley, K. J., Lasky-Su, J., Manoli, S. E., Smith, L. A., Shahsafaei, A., Weiss, S. T., & Tantisira, K. (2011) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00348.2010 · Cited by 58 · see citing works

Effects of aging and Parkinson’s disease on motor unit remodeling: influence of resistance exercise training

Kelly, N. A., Hammond, K. G., Bickel, C. S., Windham, S. T., Tuggle, S. C., & Bamman, M. M. (2017) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00563.2017 · Cited by 57 · see citing works

MACF1 links Rapsyn to microtubule- and actin-binding proteins to maintain neuromuscular synapses

Oury, J., Liu, Y., Töpf, A., Todorovic, S., Hoedt, E., Preethish‐Kumar, V., Neubert, T. A., Lin, W., Lochmüller, H., & Burden, S. J. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201810023 · Cited by 57 · see citing works

CHIP functions an E3 ubiquitin ligase of Runx1

Shang, Y., Zhao, X., Xu, X., Xin, H., Li, X., Zhai, Y., He, D., Jia, B., Chen, W., & Chang, Z. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.06.043 · Cited by 53 · see citing works

Genome-wide mapping of Sox6 binding sites in skeletal muscle reveals both direct and indirect regulation of muscle terminal differentiation by Sox6

An, C.-I., Dong, Y., & Hagiwara, N. (2011) · BMC Developmental Biology · doi:10.1186/1471-213x-11-59 · Cited by 56 · see citing works

Combined EGFR and Autophagy Modulation Impairs Cell Migration and Enhances Radiosensitivity in Human Glioblastoma Cells

Palumbo, S., Tini, P., Toscano, M., Allavena, G., Angeletti, F., Manai, F., Miracco, C., Comincini, S., & Pirtoli, L. (2014) · Journal of Cellular Physiology · doi:10.1002/jcp.24640 · Cited by 52 · see citing works

Transcriptional repression of the RUNX3/AML2 gene by the t(8;21) and inv(16) fusion proteins in acute myeloid leukemia

Cheng, C. K., Li, L., Cheng, S. H., Lau, K., Chan, N. P. H., Wong, R. S. M., Shing, M. M. K., Li, C. K., & Ng, M. H. L. (2008) · Blood · doi:10.1182/blood-2008-02-137083 · Cited by 51 · see citing works

Functional interplay between p63 and p53 controls RUNX1 function in the transition from proliferation to differentiation in human keratinocytes

Masse, I., Barbollat‐Boutrand, L., Molina, M. J., Berthier‐Vergnes, O., Joly‐Tonetti, N., Martin, M. T., de Fromentel, C. C., Kanitakis, J., & Lamartine, J. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.62 · Cited by 47 · see citing works

Rel A/p65 is required for cytokine-induced myotube atrophy

Yamaki, T., Wu, C., Gustin, M., Lim, J. K., Jackman, R. W., & Kandarian, S. C. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00111.2012 · Cited by 46 · see citing works

Transcriptomic and Proteomic of Gastrocnemius Muscle in Peripheral Artery Disease

Ferrucci, L., Candia, J., Ubaida‐Mohien, C., Lyashkov, A. E., Banskota, N., Leeuwenburgh, C., Wohlgemuth, S. E., Guralnik, J. M., Kaileh, M., Zhang, D., et al. (2023) · Circulation Research · doi:10.1161/circresaha.122.322325 · Cited by 45 · see citing works

Stretching and electrical stimulation reduce the accumulation of MyoD, myostatin and atrogin-1 in denervated rat skeletal muscle

Russo, T. L., Peviani, S. M., Durigan, J. L. Q., Gigo‐Benato, D., Delfino, G. B., & Salvini, T. F. (2010) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-010-9203-z · Cited by 45 · see citing works

Self-Eating for Muscle Fitness: Autophagy in the Control of Energy Metabolism

Sebastián, D., & Antonio Zorzano, A. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.06.030 · Cited by 42 · see citing works

Transcriptional landscape of myogenesis from human pluripotent stem cells reveals a key role of TWIST1 in maintenance of skeletal muscle progenitors

Choi, I. Y., Lim, H., Cho, H. J., Oh, Y., Chou, B.-K., Bai, H., Cheng, L., Kim, Y. J., Hyun, S., Kim, H., et al. (2020) · eLife · doi:10.7554/elife.46981 · Cited by 41 · see citing works

miR-206 integrates multiple components of differentiation pathways to control the transition from growth to differentiation in rhabdomyosarcoma cells

MacQuarrie, K. L., Yao, Z., Young, J. M., Cao, Y., & Tapscott, S. J. (2012) · Skeletal Muscle · doi:10.1186/2044-5040-2-7 · Cited by 41 · see citing works

Systems analysis of transcriptional data provides insights into muscle's biological response to botulinum toxin

Mukund, K., Mathewson, M. A., Minamoto, V. B., Ward, S. R., Subramaniam, S., & Lieber, R. L. (2014) · Muscle & Nerve · doi:10.1002/mus.24211 · Cited by 38 · see citing works

Association and expression quantitative trait loci (eQTL) analysis of porcine AMBP, GC and PPP1R3B genes with meat quality traits

Çınar, M. U., Kayan, A., Uddin, M. J., Jonas, E., Tesfaye, D., Phatsara, C., Ponsuksili, S., Wimmers, K., Tholen, E., Looft, C., et al. (2011) · Molecular Biology Reports · doi:10.1007/s11033-011-1274-4 · Cited by 38 · see citing works

Skeletal muscle atrophy after sciatic nerve damage: Mechanistic insights

Yadav, A., & Dabur, R. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176506 · Cited by 38 · see citing works

Mechanisms underlying the sparing of masticatory versus limb muscle function in an experimental critical illness model

Aare, S., Ochala, J., Norman, H. S., Radell, P. J., Eriksson, L. I., Göransson, H., Chen, Y., Hoffman, E. P., & Larsson, L. (2011) · Physiological Genomics · doi:10.1152/physiolgenomics.00116.2011 · Cited by 36 · see citing works

Activation of autophagy by globular adiponectin is required for muscle differentiation

Gamberi, T., Modesti, A., Magherini, F., D’Souza, D. M., Hawke, T. J., & Fiaschi, T. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.01.016 · Cited by 35 · see citing works

categoryCompare, an analytical tool based on feature annotations

Flight, R. M., Harrison, B. J., Mohammad, F., Bunge, M. B., Moon, L. D. F., Petruska, J. C., & Rouchka, E. C. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00098 · Cited by 33 · see citing works

Emodin Induces Growth Arrest and Death of Human Vascular Smooth Muscle Cells Through Reactive Oxygen Species and p53

Wang, X., Zou, Y., Sun, A., Xu, D.-L., Niu, Y., Wang, S., Wang, K., & Ge, J. (2007) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0b013e318033dfb3 · Cited by 34 · see citing works

The 24-hour molecular landscape after exercise in humans reveals MYC is sufficient for muscle growth

Edman, S., Jones, R. G., Jannig, P. R., Fernandez‐Gonzalo, R., Norrbom, J., Thomas, N. T., Khadgi, S., Koopmans, P. J., da Silva, F. M., Chambers, T. L., et al. (2024) · EMBO Reports · doi:10.1038/s44319-024-00299-z · Cited by 32 · see citing works

Distinct MUNC lncRNA structural domains regulate transcription of different promyogenic factors

Przanowska, R. K., Weidmann, C. A., Saha, S., Cichewicz, M. A., Jensen, K. N., Przanowski, P., Irving, P. S., Janes, K. A., Guertin, M. J., Weeks, K. M., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110361 · Cited by 32 · see citing works

Deconvoluting the ontogeny of hematopoietic stem cells

Samokhvalov, I. M. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1364-7 · Cited by 31 · see citing works

The impact of postexercise essential amino acid ingestion on the ubiquitin proteasome and autophagosomal-lysosomal systems in skeletal muscle of older men

Dickinson, J. M., Reidy, P. T., Gundermann, D. M., Borack, M. S., Walker, D. K., D’Lugos, A. C., Volpi, E., & Rasmussen, B. B. (2016) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00632.2016 · Cited by 30 · see citing works

The Order of Exercise during Concurrent Training for Rehabilitation Does Not Alter Acute Genetic Expression, Mitochondrial Enzyme Activity or Improvements in Muscle Function

MacNeil, L., Glover, E. I., Bergstra, T. G., Safdar, A., & Tarnopolsky, M. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0109189 · Cited by 30 · see citing works

The effect of mild traumatic brain injury on peripheral nervous system pathology in wild-type mice and the G93A mutant mouse model of motor neuron disease

Evans, T. M., Jaramillo, C. A., Sataranatarajan, K., Watts, L. T., Sabia, M., Qi, W., & Remmen, H. V. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.04.041 · Cited by 29 · see citing works

Transcriptional networks regulating the costamere, sarcomere, and other cytoskeletal structures in striated muscle

Estrella, N. L., & Naya, F. J. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1512-0 · Cited by 29 · see citing works

Muscle-Derived Extracellular Signal-Regulated Kinases 1 and 2 Are Required for the Maintenance of Adult Myofibers and Their Neuromuscular Junctions

Seaberg, B. L., Henslee, G., Wang, S., Paez-Colasante, X., Landreth, G. E., & Rimer, M. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.01071-14 · Cited by 29 · see citing works

Muscle Wasting and Early Mobilization in Acute Respiratory Distress Syndrome

Walsh, C. J., Batt, J. A. E., Herridge, M. S., & dos Santos, C. C. (2014) · Clinics in Chest Medicine · doi:10.1016/j.ccm.2014.08.016 · Cited by 28 · see citing works

Changes of Gene Expression Patterns of Muscle Pathophysiology-Related Transcription Factors During Denervated Muscle Atrophy

Yang, X., Li, M., Ji, Y., Lin, Y., Xu, L., Gu, X., Sun, H., Wang, W., Shen, Y., Liu, H., et al. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.923190 · Cited by 28 · see citing works

HOXA5 plays tissue-specific roles in the developing respiratory system

Landry‐Truchon, K., Houde, N., Boucherat, O., Joncas, F., Dasen, J. S., Philippidou, P., Mansfield, J. H., & Jeannotte, L. (2017) · Development · doi:10.1242/dev.152686 · Cited by 28 · see citing works

Genetic architecture of gene expression in ovine skeletal muscle

Kogelman, L. J. A., Byrne, K. A., Vuocolo, T., Watson‐Haigh, N. S., Kadarmideen, H. N., Kijas, J., Oddy, V. H., Gardner, G. E., Gondro, C., & Tellam, R. L. (2011) · BMC Genomics · doi:10.1186/1471-2164-12-607 · Cited by 25 · see citing works

The TOR Pathway at the Neuromuscular Junction: More Than a Metabolic Player?

Castets, P., Ham, D. J., & Rüegg, M. A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00162 · Cited by 24 · see citing works

Cancer Cachexia Induces Preferential Skeletal Muscle Myosin Loss When Combined With Denervation

Yamada, T., Ashida, Y., Tatebayashi, D., Abe, M., & Himori, K. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00445 · Cited by 22 · see citing works

A chromatin immunoprecipitation screen in mouse keratinocytes reveals Runx1 as a direct transcriptional target of ΔNp63

Ortt, K., Raveh, E., Gat, U., & Sinha, S. (2008) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21700 · Cited by 22 · see citing works

The Core Binding Factor CBF Negatively Regulates Skeletal Muscle Terminal Differentiation

Philipot, O., Joliot, V., Aït-Mohamed, O., Pellentz-Lemattre, C., Robin, P., Fritsch, L., & Ait‐Si‐Ali, S. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009425 · Cited by 21 · see citing works

ICU-acquired weakness

dos Santos, C. C., & Batt, J. A. E. (2012) · Current Opinion in Critical Care · doi:10.1097/mcc.0b013e328357cb5e · Cited by 20 · see citing works

Silencing of IGF2BP1 restrains ox‐LDL‐induced lipid accumulation and inflammation by reducing RUNX1 expression and promoting autophagy in macrophages

Liu, M., Tao, G., Cao, Y., Hu, Y., & Zhang, Z. (2022) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.22994 · Cited by 20 · see citing works

RNA Expression Analysis of Passive Transfer Myasthenia Supports Extraocular Muscle as a Unique Immunological Environment

Zhou, Y., Kaminski, H. J., Gong, B., Cheng, G., Feuerman, J. M., & Kusner, L. L. (2014) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.14-14422 · Cited by 20 · see citing works

Gene profiling of embryonic skeletal muscle lacking type I ryanodine receptor Ca2+ release channel

Filipova, D., Walter, A. M., Gaspar, J. A., Brunn, A., Linde, N. F., Ardestani, M. A., Deckert, M., Hescheler, J., Pfitzer, G., Sachinidis, A., et al. (2016) · Scientific Reports · doi:10.1038/srep20050 · Cited by 20 · see citing works

The roles of Runx1 in skeletal development and osteoarthritis: A concise review

Liu, Y., Huang, C., Bai, M., Pi, C., Zhang, D., & Xie, J. (2022) · Heliyon · doi:10.1016/j.heliyon.2022.e12656 · Cited by 17 · see citing works

Activation of Muscle Enhancers by MyoD and epigenetic modifiers

Blum, R. (2014) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24854 · Cited by 17 · see citing works

Effects of low-level laser therapy after nerve reconstruction in rat denervated soleus muscle adaptation

Silva‐Couto, M. A., Gigo‐Benato, D., Tim, C. R., Parizotto, N. A., Salvini, T. F., & Russo, T. L. (2012) · Brazilian Journal of Physical Therapy · doi:10.1590/s1413-35552012005000035 · Cited by 17 · see citing works

Runx1 Limits Atrophy

(2005) · Science s STKE · doi:10.1126/stke.2942005tw272

Runx1 Transcription Factor Is Required for Myoblasts Proliferation during Muscle Regeneration

Umansky, K. B., Gruenbaum‐Cohen, Y., Tsoory, M., Feldmesser, E., Goldenberg, D., Brenner, O. J., & Groner, Y. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005457 · Cited by 88 · see citing works

TWEAK/Fn14 system is a critical regulator of denervation‐induced skeletal muscle atrophy

Kumar, A., Bhatnagar, S., Mittal, A., & Glass, D. J. (2010) · The FASEB Journal · doi:10.1096/fasebj.24.1_supplement.801.30

Gaining insight into the role of FoxO1 in the progression of disuse-induced skeletal muscle atrophy

Vilchinskaya, N. A., Altaeva, E. G., & Lomonosova, Y. N. (2022) · Advances in Biological Regulation · doi:10.1016/j.jbior.2022.100903 · Cited by 30 · see citing works

RUNX1 promotes denervation-induced muscle atrophy by activating the JUNB/NF-κB pathway and driving M1 macrophage polarization

Hu, W., Huang, Y., Yin, W., Huang, Y., & Wu, J. (2025) · Open Life Sciences · doi:10.1515/biol-2025-1157