Cited by 177Muscle Physiology and DisordersNeurogenetic and Muscular Disorders ResearchMeat and Animal Product Quality

The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.

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

Open access

Wang, Xiaoxia, Blagden, Chris, Fan, Jihua, Nowak, Scott J., Taniuchi, Ichiro, Littman, Dan R., Burden, Steven J.·2005·Genes & Development

DOI 10.1101/gad.1318305PMC PMC1176009

Open this paper in CoChat — free account Open PDF

Abstract

Disruptions in the use of skeletal muscle lead to muscle atrophy. After short periods of disuse, muscle atrophy is reversible, and even after prolonged periods of inactivity, myofiber degeneration is uncommon. The pathways that regulate atrophy, initiated either by peripheral nerve damage, immobilization, aging, catabolic steroids, or cancer cachexia, however, are poorly understood. Previously, we found that Runx1 (AML1), a DNA-binding protein that is homologous to Drosophila Runt and has critical roles in hematopoiesis and leukemogenesis, is poorly expressed in innervated muscle, but strongly induced in muscle shortly after denervation. To determine the function of Runx1 in skeletal muscle, we generated mice in which Runx1 was selectively inactivated in muscle. Here, we show that Runx1 is required to sustain muscle by preventing denervated myofibers from undergoing myofibrillar disorganization and autophagy, structural defects found in a variety of congenital myopathies. We find that only 29 genes, encoding ion channels, signaling molecules, and muscle structural proteins, depend upon Runx1 expression, suggesting that their misregulation causes the dramatic muscle wasting. These findings demonstrate an unexpected role for electrical activity in regulating muscle wasting, and indicate that muscle disuse induces compensatory mechanisms that limit myofiber atrophy. Moreover, these results suggest that reduced muscle activity could cause or contribute to congenital myopathies if Runx1 or its target genes were compromised.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1101/gad.1318305

Cites

43 of 43 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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
Calcium's Role in Mechanotransduction during Muscle Development
Damm, T. B., & Egli, M. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000356667 · Cited by 14,552
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
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
Autophagy as a Regulated Pathway of Cellular Degradation
Klionsky, D. J., & Emr, S. D. (2000) · Science · doi:10.1126/science.290.5497.1717 · Cited by 3,630
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
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
Autophagy in Health and Disease: A Double-Edged Sword
Shintani, T., & Klionsky, D. J. (2004) · Science · doi:10.1126/science.1099993 · Cited by 2,559
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
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

Show all 43 references

Research works printed but not linked: 1

1994, Mol. Cell. Biol., 14, 8051

Sorted by citations

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
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 1,159
Signaling in Muscle Atrophy and Hypertrophy
Sandri, M. (2008) · Physiology · doi:10.1152/physiol.00041.2007 · Cited by 866
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 823
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 546
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
Autophagy in skeletal muscle
Sandri, M. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.056 · Cited by 451
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 407
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
Dual roles of autophagy in the survival of Caenorhabditis elegans during starvation
Kang, C., You, Y.-J., & Avery, L. (2007) · Genes & Development · doi:10.1101/gad.1573107 · Cited by 294
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 194
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
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
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
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 194
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
“Conversely, genetic ablation of RUNX1 disinhibits autophagy and worsens atrophy [472].”
Background
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
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
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 169
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
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 156
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 147
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 150
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 130
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
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 124
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 125
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 120
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 114
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 115
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
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
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 113
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 104
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 106
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 104
RUNX1: an emerging therapeutic target for cardiovascular disease
Riddell, A., McBride, M., Braun, T. W., Nicklin, S. A., Cameron, E. R., Loughrey, C. M., & Martin, T. P. (2020) · Cardiovascular Research · doi:10.1093/cvr/cvaa034 · Cited by 101
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
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
Autophagy in Skeletal Muscle Homeostasis and in Muscular Dystrophies
Grumati, P., & Bonaldo, P. (2012) · Cells · doi:10.3390/cells1030325 · Cited by 96
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 87
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
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 85
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 79
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 72
RUNX1 and its understudied role in breast cancer
Janes, K. A. (2011) · Cell Cycle · doi:10.4161/cc.10.20.18029 · Cited by 70
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
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
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 67
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
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
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
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 62
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 62
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 58
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 60
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
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 56
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
Self-citation
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 54
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 60
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 54
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
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
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
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 44
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
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 43
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
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
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
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
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
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 35
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 36
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
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
Self-citation
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 44
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
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 37
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
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 33
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 30
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
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 32
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
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
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
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
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 29
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
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 24
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
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
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
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 23
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
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 18
Activation of Muscle Enhancers by MyoD and epigenetic modifiers
Blum, R. (2014) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24854 · Cited by 17
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

Authors: Wang, X., Blagden, C., Fan, J., Nowak, S. J., Taniuchi, I., Littman, D. R., & Burden, S. J.
Affiliations: Howard Hughes Medical Institute (US)
ORCID: Wang, Xiaoxia
Nowak, Scott J.
Taniuchi, Ichiro
Littman, Dan R.
Burden, Steven J.
Venue: Genes & Development
Publisher: Cold Spring Harbor Laboratory
Published: 2005-07-15
Volume: 19
Issue: 14
Pages: 1715-1722
ISSN: 0890-9369 (ISSN-L)
1549-5477
DOI: 10.1101/gad.1318305
PMC: PMC1176009
OpenAlex: W2099304566
Cited by: 177
References: 43
Citations by year: 2026: 7 · 2025: 7 · 2024: 9 · 2023: 6 · 2022: 13 · 2021: 9 · 2020: 11 · 2019: 4 · 2018: 3 · 2017: 4 · 2016: 9 · 2015: 14 · 2014: 14 · 2013: 8 · 2012: 17
Type: posted content
Language: en
Open access: bronze
doi.org
Locations: Genes & Development (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
HighWire Press Open Archive (submittedVersion)
Funders: Howard Hughes Medical Institute
National Institutes of Health
National Institute of Mental Health
National Institute of Neurological Disorders and Stroke (R01NS027963)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Health Sciences › Medicine › Genetics (clinical) › Neurogenetic and Muscular Disorders Research
Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Meat and Animal Product Quality
Keywords: RUNX1, skeletal muscle atrophy, denervation, myofibrillar disorganization, autophagy, myofiber degeneration, congenital myopathy, muscle electrical activity, compensatory mechanisms, ion channels, muscle structural proteins
MeSH terms: Forkhead Box Protein O1, Animals, Autophagy, DNA-Binding Proteins, Male, Mice, Mutant Strains, Mice, Transgenic, Models, Biological, Muscle Denervation, Muscular Atrophy, Myofibrils, Proto-Oncogene Proteins, Transcription Factors, Gene Expression, Muscle, Skeletal, Core Binding Factor Alpha 2 Subunit, Mice, Forkhead Transcription Factors

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

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks