The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
The Transcription Factor ATF4 Promotes Skeletal Myofiber Atrophy during Fasting
Open accessAbstract
Prolonged fasting alters skeletal muscle gene expression in a manner that promotes myofiber atrophy, but the underlying mechanisms are not fully understood. Here, we examined the potential role of activating transcription factor 4 (ATF4), a transcription factor with an evolutionarily ancient role in the cellular response to starvation. In mouse skeletal muscle, fasting increases the level of ATF4 mRNA. To determine whether increased ATF4 expression was required for myofiber atrophy, we reduced ATF4 expression with an inhibitory RNA targeting ATF4 and found that it reduced myofiber atrophy during fasting. Likewise, reducing the fasting level of ATF4 mRNA with a phosphorylation-resistant form of eukaryotic initiation factor 2alpha decreased myofiber atrophy. To determine whether ATF4 was sufficient to reduce myofiber size, we overexpressed ATF4 and found that it reduced myofiber size in the absence of fasting. In contrast, a transcriptionally inactive ATF4 construct did not reduce myofiber size, suggesting a requirement for ATF4-mediated transcriptional regulation. To begin to determine the mechanism of ATF4-mediated myofiber atrophy, we compared the effects of fasting and ATF4 overexpression on global skeletal muscle mRNA expression. Interestingly, expression of ATF4 increased a small subset of five fasting-responsive mRNAs, including four of the 15 mRNAs most highly induced by fasting. These five mRNAs encode proteins previously implicated in growth suppression (p21(Cip1/Waf1), GADD45alpha, and PW1/Peg3) or titin-based stress signaling [muscle LIM protein (MLP) and cardiac ankyrin repeat protein (CARP)]. Taken together, these data identify ATF4 as a novel mediator of skeletal myofiber atrophy during starvation.
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
“Importantly, the overexpression of ATF4 and GADD45 is sufficient to induce muscle loss [19, 20].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [19]
Citations
Cites
WAF1, a potential mediator of p53 tumor suppression
El-Deiry, W. S., Tokino, T., Velculescu, V. E., Levy, D. B., Parsons, R., Trent, J. M., Lin, D., Mercer, W. E., Kinzler, K. W., & Vogelstein, B. (1993) · Cell · doi:10.1016/0092-8674(93)90500-p · Cited by 8,321
The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases.
Wade Harper, J. (1993) · Cell · doi:10.1016/0092-8674(93)90499-g · Cited by 5,651
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
An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress
Harding, H. P., Zhang, Y., Zeng, H., Novoa, I., Lu, P. D., Calfon, M. A., Sadri, N., Yun, C., Popko, B., Paules, R. S., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,336
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
Bodine, S. C., Stitt, T. N., Gonzalez, M., Kline, W. O., Stover, G. L., Bauerlein, R., Zlotchenko, E., Scrimgeour, A., Lawrence, J. C., Glass, D. J., et al. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-1014 · Cited by 2,752
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
TRANSLATIONAL REGULATION OFGCN4AND THE GENERAL AMINO ACID CONTROL OF YEAST
Hinnebusch, A. G. (2005) · Annual Review of Microbiology · doi:10.1146/annurev.micro.59.031805.133833 · Cited by 1,297
Sandri, M., Lin, J., Handschin, C., Yang, W., Arany, Z. P., Lecker, S. H., Goldberg, A. L., & Spiegelman, B. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607795103 · Cited by 974
Signaling in Muscle Atrophy and Hypertrophy
Sandri, M. (2008) · Physiology · doi:10.1152/physiol.00041.2007 · Cited by 866
Cited by
Sorted by citations
Role of Inflammation in Muscle Homeostasis and Myogenesis
Costamagna, D., Costelli, P., Sampaolesi, M., & Penna, F. (2015) · Mediators of Inflammation · doi:10.1155/2015/805172 · Cited by 554
Kunkel, S. D., Suneja, M., Ebert, S. M., Bongers, K. S., Fox, D. K., Malmberg, S. E., Alipour, F., Shields, R. K., & Adams, C. M. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.020 · Cited by 345
“muscle, and the effects of spinal cord injury on human skeletal muscle were described previously (Adams et al., 2011; Ebert et al., 2010).”
Self-citationActivating transcription factor 4-dependent induction of FGF21 during amino acid deprivation
De Sousa-Coelho, A. L., Marrero, P. F., & Haro, D. (2012) · Biochemical Journal · doi:10.1042/bj20111748 · Cited by 246
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
Self-citationOPA1 deficiency promotes secretion of FGF21 from muscle that prevents obesity and insulin resistance
Pereira, R. O., Tadinada, S. M., Zasadny, F. M., Oliveira, K. J., Pires, K. M. P., Olvera, A., Jeffers, J., Souvenir, R., Mcglauflin, R., Seei, A., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201696179 · Cited by 211
Self-citationSignaling Pathways That Control Muscle Mass
Vainshtein, A., & Sandri, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134759 · Cited by 222
Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197
Recent progress toward understanding the molecular mechanisms that regulate skeletal muscle mass
Goodman, C. A., Mayhew, D. L., & Hornberger, T. A. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.07.013 · Cited by 183
Thbs1 induces lethal cardiac atrophy through PERK-ATF4 regulated autophagy
Vanhoutte, D., Schips, T. G., Vo, A., Grimes, K. M., Baldwin, T. A., Brody, M. J., Accornero, F., Sargent, M. A., & Molkentin, J. D. (2021) · Nature Communications · doi:10.1038/s41467-021-24215-4 · Cited by 176
Atherton, P. J., Greenhaff, P. L., Phillips, S. M., Bodine, S. C., Adams, C. M., & Lang, C. H. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00257.2016 · Cited by 180
Self-citationPaul, P. K., Bhatnagar, S., Mishra, V. K., Srivastava, S., Darnay, B. G., Choi, Y., & Kumar, A. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06351-11 · Cited by 157
Muscle-specific Drp1 overexpression impairs skeletal muscle growth via translational attenuation
Touvier, T., De Palma, C., Rigamonti, E., Scagliola, A., Incerti, E., Mazelin, L., Thomas, J.-L., D'Antonio, M., Politi, L., Schaeffer, L., et al. (2015) · Cell Death & Disease · doi:10.1038/cddis.2014.595 · Cited by 140
Bongers, K. S., Fox, D. K., Ebert, S. M., Kunkel, S. D., Dyle, M. C., Bullard, S. A., Dierdorff, J. M., & Adams, C. M. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00380.2013 · Cited by 150
Self-citationDyle, M. C., Ebert, S. M., Cook, D. P., Kunkel, S. D., Fox, D. K., Bongers, K. S., Bullard, S. A., Dierdorff, J. M., & Adams, C. M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.556241 · Cited by 138
Self-citationBohnert, K. R., Gallot, Y. S., Sato, S., Xiong, G., Hindi, S. M., & Kumar, A. (2016) · The FASEB Journal · doi:10.1096/fj.201600250rr · Cited by 127
Ebert, S. M., Dyle, M. C., Bullard, S. A., Dierdorff, J. M., Murry, D. J., Fox, D. K., Bongers, K. S., Lira, V. A., Meyerholz, D. K., Talley, J. J., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.681445 · Cited by 128
Self-citationLiu, J., Yang, J.-R., Chen, X.-M., Cai, G.-Y., Lin, L.-R., & He, Y.-N. (2015) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00096.2014 · Cited by 117
Fox, D. K., Ebert, S. M., Bongers, K. S., Dyle, M. C., Bullard, S. A., Dierdorff, J. M., Kunkel, S. D., & Adams, C. M. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00010.2014 · Cited by 125
Self-citationAmino acid sensing in skeletal muscle
Moro, T., Ebert, S. M., Adams, C. M., & Rasmussen, B. B. (2016) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2016.06.010 · Cited by 104
Self-citationThe Interplay between Mitochondrial Morphology and Myomitokines in Aging Sarcopenia
Romanello, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010091 · Cited by 101
TWEAK and TRAF6 regulate skeletal muscle atrophy
Kumar, A., Bhatnagar, S., & Paul, P. K. (2012) · Current opinion in clinical nutrition and metabolic care · doi:10.1097/mco.0b013e328351c3fc · Cited by 103
Inhibition of the Fission Machinery Mitigates OPA1 Impairment in Adult Skeletal Muscles
Romanello, V., Scalabrin, M., Albiero, M., Blaauw, B., Scorrano, L., & Sandri, M. (2019) · Cells · doi:10.3390/cells8060597 · Cited by 91
Buraschi, S., Neill, T., & Iozzo, R. V. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.10.005 · Cited by 92
Neurodegeneration: Keeping ATF4 on a Tight Leash
Pitale, P. M., Gorbatyuk, O. S., & Gorbatyuk, M. S. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00410 · Cited by 87
Skeletal Muscle Atrophy: Discovery of Mechanisms and Potential Therapies
Ebert, S. M., Al-Zougbi, A., Bodine, S. C., & Adams, C. M. (2019) · Physiology · doi:10.1152/physiol.00003.2019 · Cited by 80
Decorin is an autophagy-inducible proteoglycan and is required for proper in vivo autophagy
Gubbiotti, M. A., Neill, T., Frey, H., Schaefer, L., & Iozzo, R. V. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.09.001 · Cited by 81
MYTHO is a novel regulator of skeletal muscle autophagy and integrity
Leduc‐Gaudet, J., Franco‐Romero, A., Cefis, M., Moamer, A., Broering, F. E., Milan, G., Sartori, R., Chaffer, T. J., Dulac, M., Marcangeli, V., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36817-1 · Cited by 75
Seaborne, R. A. E., Hughes, D. C., Turner, D. C., Owens, D. J., Baehr, L. M., Gorski, P. P., Semenova, E. A., Borisov, O., Larin, A. K., Popov, D. V., et al. (2019) · The Journal of Physiology · doi:10.1113/jp278073 · Cited by 72
ATF 4 activity: a common feature shared by many kinds of slow‐aging mice
Li, W., Li, X., & Miller, R. A. (2014) · Aging Cell · doi:10.1111/acel.12264 · Cited by 74
PERK regulates skeletal muscle mass and contractile function in adult mice
Gallot, Y. S., Bohnert, K. R., Straughn, A. R., Xiong, G., Hindi, S. M., & Kumar, A. (2019) · The FASEB Journal · doi:10.1096/fj.201800683rr · Cited by 67
Endoplasmic reticulum stress and unfolded protein response: Roles in skeletal muscle atrophy
Ji, Y., Jiang, Q., Chen, B., Chen, X., Li, A., Shen, D., Shen, Y., Liu, H., Qian, X., Yao, X., et al. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.116799 · Cited by 69
Decorin-inducible Peg3 Evokes Beclin 1-mediated Autophagy and Thrombospondin 1-mediated Angiostasis
Torres, A., Gubbiotti, M. A., & Iozzo, R. V. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.753632 · Cited by 63
Ebert, S. M., Bullard, S. A., Basisty, N., Marcotte, G. R., Skopec, Z. P., Dierdorff, J. M., Al‐Zougbi, A., Tomcheck, K. C., DeLau, A. D., Rathmacher, J. A., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012095 · Cited by 65
Self-citationIdentification of the MuRF1 Skeletal Muscle Ubiquitylome Through Quantitative Proteomics
Baehr, L. M., Hughes, D. C., Lynch, S. A., Haver, D. V., Maia, T. M., Marshall, A. G., Radoshevich, L., Impens, F., Waddell, D. S., & Bodine, S. C. (2021) · Function · doi:10.1093/function/zqab029 · Cited by 63
Miyake, M., Nomura, A., Ogura, A., Takehana, K., Kitahara, Y., Takahara, K., Tsugawa, K., Miyamoto, C., Miura, N., Sato, R., et al. (2015) · The FASEB Journal · doi:10.1096/fj.15-275990 · Cited by 62
Bongers, K. S., Fox, D. K., Kunkel, S. D., Stebounova, L. V., Murry, D. J., Pufall, M. A., Ebert, S. M., Dyle, M. C., Bullard, S. A., Dierdorff, J. M., et al. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00472.2014 · Cited by 64
Self-citationOyabu, M., Takigawa, K., Mizutani, S., Hatazawa, Y., Fujita, M., Ohira, Y., Sugimoto, T., Suzuki, O., Tsuchiya, K., Suganami, T., et al. (2022) · The FASEB Journal · doi:10.1096/fj.202101385rr · Cited by 63
Furlow, J. D., Watson, M. L., Waddell, D. S., Neff, E. S., Baehr, L. M., Ross, A. P., & Bodine, S. C. (2013) · Physiological Genomics · doi:10.1152/physiolgenomics.00022.2013 · Cited by 62
ER Stress and Unfolded Protein Response in Cancer Cachexia
Roy, A., & Kumar, A. (2019) · Cancers · doi:10.3390/cancers11121929 · Cited by 55
Implications of glucocorticoid therapy in idiopathic inflammatory myopathies
Hanaoka, B. Y., Peterson, C. A., Horbinski, C., & Crofford, L. J. (2012) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2012.85 · Cited by 57
Confounding Roles of ER Stress and the Unfolded Protein Response in Skeletal Muscle Atrophy
Gallot, Y. S., & Bohnert, K. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052567 · Cited by 61
Biology of Activating Transcription Factor 4 (ATF4) and Its Role in Skeletal Muscle Atrophy
Ebert, S. M., Rasmussen, B. B., Judge, A. R., Judge, S. M., Larsson, L., Wek, R. C., Anthony, T. G., Marcotte, G. R., Miller, M. J., Yorek, M. A., et al. (2021) · Journal of Nutrition · doi:10.1093/jn/nxab440 · Cited by 64
Self-citationGadd45a Protein Promotes Skeletal Muscle Atrophy by Forming a Complex with the Protein Kinase MEKK4
Bullard, S. A., Seo, S., Schilling, B., Dyle, M. C., Dierdorff, J. M., Ebert, S. M., DeLau, A. D., Gibson, B. W., & Adams, C. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.740308 · Cited by 56
Self-citationThbs1 regulates skeletal muscle mass in a TGFβ-Smad2/3-ATF4-dependent manner
Vanhoutte, D., Schips, T. G., Minerath, R. A., Huo, J., Kavuri, N. S. S., Prasad, V., Lin, S.-C., Bround, M. J., Sargent, M. A., Adams, C. M., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114149 · Cited by 48
Self-citationMechanisms of protein balance in skeletal muscle
Anthony, T. G. (2016) · Domestic Animal Endocrinology · doi:10.1016/j.domaniend.2016.02.012 · Cited by 59
Woodworth‐Hobbs, M. E., Perry, B. D., Rahnert, J. A., Hudson, M. B., Zheng, B., & Price, S. R. (2017) · Physiological Reports · doi:10.14814/phy2.13530 · Cited by 50
Korponay, T. C., Balnis, J., Vincent, C. E., Singer, D. V., Chopra, A., Adam, A. P., Ginnan, R. G., Singer, H. A., & Jaitovich, A. (2019) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2019-0061oc · Cited by 47
Ma, W., Cai, Y. M., Shen, Y., Chen, X., Zhang, L., Ji, Y., Chen, Z., Zhu, J., Yang, X., & Sun, H. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.663384 · Cited by 46
Role of ATF4 in skeletal muscle atrophy
Adams, C. M., Ebert, S. M., & Dyle, M. C. (2017) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000362 · Cited by 46
Self-citationImplications of mitochondrial fusion and fission in skeletal muscle mass and health
Romanello, V., & Sandri, M. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.02.011 · Cited by 46
Kny, M., & Fielitz, J. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.878755 · Cited by 48
Inoue, Y., Kawachi, S., Ohkubo, T., Nagasaka, M., Ito, S., Fukuura, K., Itoh, Y., Ohoka, N., Morishita, D., & Hayashi, H. (2017) · FEBS Letters · doi:10.1002/1873-3468.12869 · Cited by 44
ATF4 selectively regulates heat nociception and contributes to kinesin-mediated TRPM3 trafficking
Xie, M.-X., Cao, X., Zeng, W., Lai, R.-C., Guo, L., Wang, J., Xiao, Y.-B., Zhang, X., Chen, D., Liu, X., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21731-1 · Cited by 38
Perry, B. D., Rahnert, J. A., Xie, Y., Zheng, B., Woodworth‐Hobbs, M. E., & Price, S. R. (2018) · PLoS ONE · doi:10.1371/journal.pone.0191313 · Cited by 42
The transcription regulator ATF4 is a mediator of skeletal muscle aging
Miller, M. J., Marcotte, G. R., Basisty, N., Wehrfritz, C., Ryan, Z. C., Strub, M. D., McKeen, A. T., Stern, J. I., Nath, K. A., Rasmussen, B. B., et al. (2023) · GeroScience · doi:10.1007/s11357-023-00772-y · Cited by 40
Self-citationTinkum, K. L., White, L. S., Marpegán, L., Herzog, E. D., Piwnica-Worms, D. R., & Piwnica-Worms, H. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.494328 · Cited by 34
Fibrogenic Potential of PW1/Peg3 Expressing Cardiac Stem Cells
Yaniz‐Galende, E., Roux, M., Nadaud, S., Mougenot, N., Bouvet, M., Claude, O., Lebreton, G., Blanc, C., Pinet, F., Atassi, F., et al. (2017) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2017.06.010 · Cited by 33
Doerr, V., Montalvo, R. N., Kwon, O. S., Talbert, E. E., Hain, B. A., Houston, F. E., & Smuder, A. J. (2020) · Antioxidants · doi:10.3390/antiox9030263 · Cited by 35
Wischnewski, S., Thäwel, T., Ikenaga, C., Kocharyan, A., Lerma-Martin, C., Zulji, A., Rausch, H.-W., Brenner, D., Thomas, L., Kutza, M., et al. (2024) · Nature Aging · doi:10.1038/s43587-024-00645-9 · Cited by 34
Marco, G. D., Gherardi, G., Mario, A. D., Piazza, I., Baraldo, M., Mattarei, A., Blaauw, B., Rizzuto, R., Stefani, D. D., & Mammucari, C. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-06426-x · Cited by 31
Pasteuning-Vuhman, S., der Meulen, J. W. B.-V., van Putten, M., Overzier, M., ten Dijke, P., Kiełbasa, S. M., Arindrarto, W., Wolterbeek, R., Lezhnina, K. V., Ozerov, I. V., et al. (2016) · The FASEB Journal · doi:10.1096/fj.201600675r · Cited by 31
Cui, Q., Yang, H., Gu, Y., Zong, C., Chen, X., Lin, Y., Sun, H., Shen, Y., & Zhu, J. (2020) · Annals of Translational Medicine · doi:10.21037/atm-20-7400 · Cited by 30
Roberson, P. A., Mobley, C. B., Romero, M. A., Haun, C. T., Osburn, S. C., Mumford, P. W., Vann, C. G., Greer, R. A., Ferrando, A. A., & Roberts, M. D. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2020.628405 · Cited by 28
Cefis, M., Dargegen, M., Marcangeli, V., Taherkhani, S., Dulac, M., Leduc‐Gaudet, J., Mayaki, D., Hussain, S. N. A., & Gouspillou, G. (2024) · Acta Physiologica · doi:10.1111/apha.14119 · Cited by 30
GADD45A is a mediator of mitochondrial loss, atrophy, and weakness in skeletal muscle
Marcotte, G. R., Miller, M. J., Kunz, H., Ryan, Z. C., Strub, M. D., Vanderboom, P. M., Heppelmann, C. J. H., Chau, S., Ruff, Z. D. V., Kilroe, S. P., et al. (2023) · JCI Insight · doi:10.1172/jci.insight.171772 · Cited by 26
Self-citationAn investigation of p53 in skeletal muscle aging
Ebert, S. M., Dierdorff, J. M., Meyerholz, D. K., Bullard, S. A., Al‐Zougbi, A., DeLau, A. D., Tomcheck, K. C., Skopec, Z. P., Marcotte, G. R., Bodine, S. C., et al. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00363.2019 · Cited by 27
Self-citationChen, W., Lv, Y. T., Zhang, H. X., Ruan, D., Wang, S., & Lin, Y. C. (2013) · Poultry Science · doi:10.3382/ps.2013-03099 · Cited by 27
Hughes, D. C., Marcotte, G. R., Baehr, L. M., West, D. W. D., Marshall, A. G., Ebert, S. M., Davidyan, A., Adams, C. M., Bodine, S. C., & Baar, K. (2018) · The Journal of Physiology · doi:10.1113/jp275833 · Cited by 27
Self-citationMemme, J. M., Sanfrancesco, V. C., & Hood, D. A. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00080.2023 · Cited by 25
Proteins regulating cap-dependent translation are downregulated during total knee arthroplasty
Ratchford, S. M., Bailey, A. N., Senesac, H. A., Hocker, A. D., Smolkowski, K., Lantz, B. A., Jewett, B. A., Gilbert, J. S., & Dreyer, H. C. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00601.2011 · Cited by 25
Frataxin deficiency lowers lean mass and triggers the integrated stress response in skeletal muscle
Vásquez-Trincado, C., Dunn, J., Han, J. I., Hymms, B., Tamaroff, J. G., Patel, M., Nguyen, S., Dedio, A., Wade, K., Enigwe, C., et al. (2022) · JCI Insight · doi:10.1172/jci.insight.155201 · Cited by 23
Wang, H., Wilson, G. J., Zhou, D., Lezmi, S., Chen, X., Layman, D. K., & Pan, Y. (2015) · British Journal Of Nutrition · doi:10.1017/s0007114515002172 · Cited by 21
Örd, T., Örd, D., & Örd, T. (2018) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2018.01.014 · Cited by 20
Use of mRNA expression signatures to discover small molecule inhibitors of skeletal muscle atrophy
Adams, C. M., Ebert, S. M., & Dyle, M. C. (2015) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000159 · Cited by 21
Self-citationBrown, D., Ryan, K., Daniel, Z. C. T. R., Mareko, M. H. D., Talbot, R., Moreton, J., Giles, T. C., Emes, R. D., Hodgman, C. T., Parr, T., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-34315-9 · Cited by 21
Emerging molecular mediators and targets for age-related skeletal muscle atrophy
Brown, L. A., Guzman, S. D., & Brooks, S. V. (2020) · Translational research · doi:10.1016/j.trsl.2020.03.001 · Cited by 22
Clark, K. A., & Kadrmas, J. L. (2013) · Cytoskeleton · doi:10.1002/cm.21106 · Cited by 19
Ruff, Z. D. V., Miller, M. J., Moro, T., Reidy, P. T., Ebert, S. M., Volpi, E., Adams, C. M., & Rasmussen, B. B. (2025) · GeroScience · doi:10.1007/s11357-025-01564-2 · Cited by 21
Self-citationHuman DBR1 deficiency impairs stress granule–dependent PKR antiviral immunity
Ru, S., Tang, S., Xu, H., Yin, J., Guo, Y., Song, L., Jin, Z., Lee, D., Chan, Y.-H., Chen, X., et al. (2024) · The Journal of Experimental Medicine · doi:10.1084/jem.20240010 · Cited by 18
Emerging mechanisms and therapeutics in inflammatory muscle diseases
Wischnewski, S., Rausch, H.-W., Ikenaga, C., Leipe, J., Lloyd, T. E., & Schirmer, L. (2025) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2025.01.005 · Cited by 19
Elliott, R. M., de Roos, B., Duthie, S. J., Bouwman, F. G., Rubio‐Aliaga, I., Crosley, L. K., Mayer, C., Polley, A. C. J., Heim, C., Coort, S. L., et al. (2014) · Genes & Nutrition · doi:10.1007/s12263-014-0432-4 · Cited by 18
Kelahmetoglu, Y., Jannig, P. R., Červenka, I., Koch, L. G., Britton, S. L., Zhou, J., Wang, H., Robinson, M. M., Nair, K. S., & Ruas, J. L. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.591476 · Cited by 18
Metabolic signatures of muscle mass loss in an elderly Taiwanese population
Lo, C.-J., Ko, Y., Chang, S., Tang, H.-Y., Huang, C.-Y., Huang, Y., Ho, H., Lin, C., & Cheng, M. (2020) · Aging · doi:10.18632/aging.202209 · Cited by 17
Regulatory Roles of GADD45α in Skeletal Muscle and Adipocyte
You, W., Xu, Z., & Shan, T. (2019) · Current Protein and Peptide Science · doi:10.2174/1389203720666190624143503 · Cited by 16
CORP: Gene delivery into murine skeletal muscle using in vivo electroporation
Hughes, D. C., Hardee, J. P., Waddell, D. S., & Goodman, C. A. (2022) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00088.2022 · Cited by 17
Chen, W., Tangara, M., Xu, J., & Peng, J. (2012) · Experimental Physiology · doi:10.1113/expphysiol.2011.01083.x · Cited by 16
ATF4 Is a Fundamental Regulator of Nutrient Sensing and Protein Turnover
Rasmussen, B. B., & Adams, C. M. (2020) · Journal of Nutrition · doi:10.1093/jn/nxaa067 · Cited by 13
Self-citationRossetti, M. L., Tomko, R. J., & Gordon, B. S. (2020) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-020-03963-9 · Cited by 13
Dominant-negative p53-overexpression in skeletal muscle induces cell death and fiber atrophy in rats
Langer, H. T., Mossakowski, A. A., Sule, R. O., Gomes, A. V., & Baar, K. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05160-6 · Cited by 13
Pharmacology of manipulating lean body mass
Sepulveda, P. V., Bush, E. D., & Baar, K. (2014) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.12320 · Cited by 12
Copola, A. G. L., dos Santos, Í. G. D., Coutinho, L. L., Del‐Bem, L., Campos-Júnior, P. H. A., Mamede, I., Nogueira, J. M., Costa, A. C., Silva, G. A. B., & Jorge, É. C. (2022) · BMC Genomics · doi:10.1186/s12864-022-08396-w · Cited by 9
Human myofiber‐enriched aging‐induced lncRNA FRAIL1 promotes loss of skeletal muscle function
Miller, M. J., Gries, K. J., Marcotte, G. R., Ryan, Z., Strub, M. D., Kunz, H., Arendt, B. K., Dasari, S., Ebert, S. M., Adams, C. M., et al. (2024) · Aging Cell · doi:10.1111/acel.14097 · Cited by 8
Self-citationCai, C., Zhang, L., Liu, X., Li, J., Ma, Y., Jiang, R., Li, Z., Li, G., Tian, Y., Kang, X., et al. (2023) · Poultry Science · doi:10.1016/j.psj.2023.102682 · Cited by 9
ATF4 inhibits TRPV4 function and controls itch perception in rodents and nonhuman primates
Xie, M.-X., Rao, J.-H., Tian, X.-Y., Liu, J., Li, X., Chen, Z., Cao, Y., Chen, A.-N., Shu, H., & Zhang, X. (2024) · Pain · doi:10.1097/j.pain.0000000000003189 · Cited by 8
Pasteuning-Vuhman, S., Putker, K., Winter, C. T.-D., der Meulen, J. D., Vliet, L. V., Overzier, M., Plomp, J., Aartsma-Rus, A., & van Putten, M. V. (2018) · PLoS ONE · doi:10.1371/journal.pone.0197388 · Cited by 9
Zumbaugh, M. D., Yen, C., Bodmer, J. S., Shi, H., & Gerrard, D. E. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.682052 · Cited by 9
Colorectal Cancer Chemotherapy Drug Bevacizumab May Induce Muscle Atrophy Through CDKN1A and TIMP4
Xu, Q., Li, J., Wu, Y., Zhou, W., & Xu, Z. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.897495 · Cited by 8
Myotube Protein Content Associates with Intracellular L-Glutamine Levels
de Vasconcelos, D. A. A., Giesbertz, P., Murata, G. M., de Souza, D. R., Fiamoncini, J., Duque-Guimaraes, D. E., Leandro, C. G., Hirabara, S. M., Daniel, H., Curi, R., et al. (2019) · Cellular Physiology and Biochemistry · doi:10.33594/000000130 · Cited by 8
Sprint and Strength Training Modulates Autophagy and Proteostasis in Aging Sprinters
Hentilä, J., Hulmi, J. J., Laakkonen, E. K., Ahtiainen, J. P., Suominen, H., & Korhonen, M. T. (2020) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000002340 · Cited by 8
Zolfaghari, M., Faramarzi, M., Hedayati, M., & Ghaffari, M. (2022) · Journal of Food Biochemistry · doi:10.1111/jfbc.14202 · Cited by 7
Metadata
- Authors
- Ebert, S. M., Monteys, A. M., Fox, D. K., Bongers, K. S., Shields, B. E., Malmberg, S. E., Davidson, B. L., Suneja, M., & Adams, C. M.
- Affiliations
- University of Iowa (US)
- Iowa City VA Medical Center (US)
- Corresponding author
- Suneja, Manish
- Adams, Christopher M.
- ORCID
- Venue
- Molecular Endocrinology
- Publisher
- The Endocrine Society
- Published
- 2010-04
- Volume
- 24
- Issue
- 4
- Pages
- 790-799
- ISSN
- 0888-8809 (ISSN-L)
- 1944-9917
- PMC
- PMC2852358
- OpenAlex
- W1965629756
- Cited by
- 130
- References
- 53
- Citations by year
- 2026: 3 · 2025: 8 · 2024: 10 · 2023: 5 · 2022: 13 · 2021: 8 · 2020: 13 · 2019: 8 · 2018: 8 · 2017: 9 · 2016: 8 · 2015: 12 · 2014: 6 · 2013: 6 · 2012: 8
- FWCI
- 2.34
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular Endocrinology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Veterans Affairs (I01 BX000976)
- National Institute of General Medical Sciences (T32GM073610, T32GM007337)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR059115)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Keywords
- ATF4, muscle fiber atrophy, skeletal muscle, fasting, starvation response, eIF2α phosphorylation, transcriptional regulation, muscle gene expression, p21, GADD45A, muscle LIM protein, cardiac ankyrin repeat protein, growth inhibition
- MeSH terms
- Animals, Fasting, Male, Mice, Inbred C57BL, Muscular Atrophy, RNA, Messenger, Polymerase Chain Reaction, Muscle, Skeletal, Oligonucleotide Array Sequence Analysis, Mice, Activating Transcription Factor 4
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