Cited by 178Autophagy in Disease and TherapyMuscle Physiology and DisordersMetabolism, Diabetes, and Cancer

The DOI matches its Crossref record; 73 of the 74 references it cites were found in a registry or an index.

Skeletal muscle autophagy: a new metabolic regulator

Open access

Neel, Brian A., Lin, Yuxi, Pessin, Jeffrey E.·2013·Trends in Endocrinology & Metabolism

DOI 10.1016/j.tem.2013.09.004PMC PMC3849822

Open this paper in CoChat — free account

Abstract

Autophagy classically functions as a physiological process to degrade cytoplasmic components, protein aggregates, and/or organelles, as a mechanism for nutrient breakdown, and as a regulator of cellular architecture. Proper autophagic flux is vital for both functional skeletal muscle, which controls the support and movement of the skeleton, and muscle metabolism. The role of autophagy as a metabolic regulator in muscle has been previously studied; however, the underlying molecular mechanisms that control autophagy in skeletal muscle have only recently begun to emerge. We review recent literature on the molecular pathways controlling skeletal muscle autophagy and discuss how they connect autophagy to metabolic regulation. We also focus on the implications these studies hold for understanding metabolic and muscle-wasting diseases.

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 · 10.1016/j.tem.2013.09.004

Cites

73 of 73 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.

1 retracted

RETRACTED: The Ubiquitin Ligase Mul1 Induces Mitophagy in Skeletal Muscle in Response to Muscle-Wasting Stimuli
Lokireddy, S., Wijesoma, I. W., Teng, S., Bonala, S., Gluckman, P. D., McFarlane, C., Sharma, M., & Kambadur, R. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.10.005 · Cited by 154
Retracted
AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227
Autophagy in the Pathogenesis of Disease
Levine, B., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2007.12.018 · Cited by 7,069
Autophagy fights disease through cellular self-digestion
Mizushima, N., Levine, B., Cuervo, A. M., & Klionsky, D. J. (2008) · Nature · doi:10.1038/nature06639 · Cited by 6,452
Autophagy regulates lipid metabolism
Singh, R., Kaushik, S., Wang, Y., Xiang, Y., Novak, I., Komatsu, M., Tanaka, K., Cuervo, A. M., & Czaja, M. J. (2009) · Nature · doi:10.1038/nature07976 · Cited by 3,975
Fiber Types in Mammalian Skeletal Muscles
Schiaffino, S., & Reggiani, C. (2011) · Physiological Reviews · doi:10.1152/physrev.00031.2010 · Cited by 3,022
The Beclin 1 network regulates autophagy and apoptosis
Kang, R., Zeh, H. J., Lotze, M. T., & Tang, D. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2010.191 · Cited by 2,485
In Vivo Analysis of Autophagy in Response to Nutrient Starvation Using Transgenic Mice Expressing a Fluorescent Autophagosome Marker
Mizushima, N., Yamamoto, A., Matsui, M., Yoshimori, T., & Ohsumi, Y. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-09-0704 · Cited by 2,105
mTOR regulation of autophagy
Jung, C. H., Ro, S.-H., Cao, J., Otto, N. M., & Kim, D.-H. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.017 · Cited by 2,090
Autophagy and Metabolism
Rabinowitz, J. D., & White, E. (2010) · Science · doi:10.1126/science.1193497 · Cited by 1,982

Show all 74 references

Sorted by citations

A Narrative Review of Cancer-Related Fatigue (CRF) and Its Possible Pathogenesis
Yang, S., Chu, S., Gao, Y., Ai, Q., Liu, Y., Li, X., & Chen, N. (2019) · Cells · doi:10.3390/cells8070738 · Cited by 242
Cul3-KLHL20 Ubiquitin Ligase Governs the Turnover of ULK1 and VPS34 Complexes to Control Autophagy Termination
Liu, C.-C., Lin, Y.-C., Chen, Y.-H., Chen, C.-M., Pang, L.-Y., Chen, H.-A., Wu, P.-R., Lin, M.-Y., Jiang, S.-T., Tsai, T.-F., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2015.11.001 · Cited by 215
Self-citation
Rewiring of Glutamine Metabolism Is a Bioenergetic Adaptation of Human Cells with Mitochondrial DNA Mutations
Chen, Q., Kirk, K., Shurubor, Y. I., Zhao, D., Arreguin, A. J., Shahi, I., Valsecchi, F., Primiano, G., Calder, E. L., Carelli, V., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.03.002 · Cited by 210
Degeneration of Neuromuscular Junction in Age and Dystrophy
Rudolf, R., Khan, M. M., Labeit, S., & Deschenes, M. R. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00099 · Cited by 197
The ubiquitin proteasome system in atrophying skeletal muscle: roles and regulation
Bilodeau, P., Coyne, E. S., & Wing, S. S. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00125.2016 · Cited by 188
Energy metabolism in cachexia
Rohm, M., Zeigerer, A., Machado, J., & Herzig, S. (2019) · EMBO Reports · doi:10.15252/embr.201847258 · Cited by 168
Molecular mechanism of sarcopenia and cachexia: recent research advances
Sakuma, K., Aoi, W., & Yamaguchi, A. (2017) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-016-1933-3 · Cited by 160
Platelet-Rich Plasma Activates Proinflammatory Signaling Pathways and Induces Oxidative Stress in Tendon Fibroblasts
Hudgens, J. L., Sugg, K. B., Grekin, J. A., Gumucio, J. P., Bedi, A., & Mendias, C. L. (2016) · The American Journal of Sports Medicine · doi:10.1177/0363546516637176 · Cited by 141
Skeletal muscle-specific Prmt1 deletion causes muscle atrophy via deregulation of the PRMT6-FOXO3 axis
Choi, S., Jeong, H.-J., Kim, H., Choi, D., Cho, S.-C., Seong, J. K., Koo, S.-H., & Kang, J.-S. (2019) · Autophagy · doi:10.1080/15548627.2019.1569931 · Cited by 132
Current understanding of sarcopenia: possible candidates modulating muscle mass
Sakuma, K., Aoi, W., & Yamaguchi, A. (2014) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-014-1527-x · Cited by 133
Non-apoptotic cell death-based cancer therapy: Molecular mechanism, pharmacological modulators, and nanomedicine
Wang, X., Hua, P., He, C., & Chen, M. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.03.020 · Cited by 131
The Role of Autophagy in Skeletal Muscle Diseases
Xia, Q., Huang, X., Huang, J., Zheng, Y., March, M., Li, J., & Wei, Y. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.638983 · Cited by 137
Human Cachexia Induces Changes in Mitochondria, Autophagy and Apoptosis in the Skeletal Muscle
de Castro, G. S., Simoes, E., Lima, J. D. C. C., Ortiz‐Silva, M., Festuccia, W. T., Tokeshi, F., de Alcântara, P. S. M., Otoch, J. P., Coletti, D., & Seelaender, M. C. L. (2019) · Cancers · doi:10.3390/cancers11091264 · Cited by 118
The Effects of Calorie Restriction on Autophagy: Role on Aging Intervention
Chung, K. W., & Chung, H. Y. (2019) · Nutrients · doi:10.3390/nu11122923 · Cited by 125
The Essential Autophagy Gene ATG7 Modulates Organ Fibrosis via Regulation of Endothelial-to-Mesenchymal Transition
Singh, K. K., Lovren, F., Pan, Y., Quan, A., Ramadan, A., Matkar, P. N., Ehsan, M., Sandhu, P., Mantella, L. E., Gupta, N., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.604603 · Cited by 118
Copper (II) and/or arsenite-induced oxidative stress cascades apoptosis and autophagy in the skeletal muscles of chicken
Wang, Y., Zhao, H., Shao, Y., Liu, J., Li, J., Luo, L., & Xing, M. (2018) · Chemosphere · doi:10.1016/j.chemosphere.2018.05.013 · Cited by 111
Out of Control: The Role of the Ubiquitin Proteasome System in Skeletal Muscle during Inflammation
Haberecht-Müller, S., Krüger, E., & Fielitz, J. (2021) · Biomolecules · doi:10.3390/biom11091327 · Cited by 108
Autophagy induction in atrophic muscle cells requires ULK1 activation by TRIM32 through unanchored K63-linked polyubiquitin chains
Di Rienzo, M., Antonioli, M., Fusco, C., Liu, Y., Mari, M., Orhon, I., Refolo, G., Germani, F., Corazzari, M., Romagnoli, A., et al. (2019) · Science Advances · doi:10.1126/sciadv.aau8857 · Cited by 107
Regulation of Beclin 1 Protein Phosphorylation and Autophagy by Protein Phosphatase 2A (PP2A) and Death-associated Protein Kinase 3 (DAPK3)
Fujiwara, N., Usui, T., Ohama, T., & Sato, K. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.704908 · Cited by 105
Understanding of sarcopenia: from definition to therapeutic strategies
Kim, J. W., Kim, R., Choi, H., Lee, S., & Bae, G. (2021) · Archives of Pharmacal Research · doi:10.1007/s12272-021-01349-z · Cited by 103
Mitochondria: Inadvertent targets in chemotherapy-induced skeletal muscle toxicity and wasting?
Sorensen, J. C., Cheregi, B. D., Timpani, C. A., Nurgali, K., Hayes, A., & Rybalka, E. (2016) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-016-3045-3 · Cited by 96
Lysosomal Two-pore Channel Subtype 2 (TPC2) Regulates Skeletal Muscle Autophagic Signaling
Lin, P., Duann, P., Komazaki, S., Park, K. H., Li, H., Sun, M., Sermersheim, M., Gumpper, K., Parrington, J., Galione, A., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.608471 · Cited by 84
Role of AMPK in regulation of LC3 lipidation as a marker of autophagy in skeletal muscle
Fritzen, A. M., Frøsig, C., Jeppesen, J. F., Jensen, T. E., Lundsgaard, A., Serup, A. K., Schjerling, P., Proud, C. G., Richter, E. A., & Kiens, B. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.03.005 · Cited by 86
Disuse-associated loss of the protease Lonp1 in muscle impairs mitochondrial function and causes reduced skeletal muscle mass and strength
Xu, Z., Fu, T., Guo, Q., Zhou, D., Sun, W., Zhou, Z., Chen, X., Zhang, J., Liu, L., Xiao, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28557-5 · Cited by 82
Daily heat stress treatment rescues denervation‐activated mitochondrial clearance and atrophy in skeletal muscle
Tamura, Y., Kitaoka, Y., Matsunaga, Y., Hoshino, D., & Hatta, H. (2015) · The Journal of Physiology · doi:10.1113/jp270093 · Cited by 83
Sestrin 2 induces autophagy and attenuates insulin resistance by regulating AMPK signaling in C2C12 myotubes
Li, H., Liu, S., Yuan, H., Niu, Y., & Fu, L. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.03.023 · Cited by 78
Distribution of Dietary Protein Intake in Daily Meals Influences Skeletal Muscle Hypertrophy Via the Circadian Clock
Aoyama, S., Kim, H., Hirooka, R., Tanaka, M., Shimoda, T., Chijiki, H., Kojima, S., Sasaki, K., Takahashi, K., Makino, S., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2021.109336 · Cited by 77
β-Hydroxy-β-Methylbutyrate (HMB) Normalizes Dexamethasone-Induced Autophagy-Lysosomal Pathway in Skeletal Muscle
Girón, M. D., Vílchez, J. D., Shreeram, S., Salto, R., Manzano, M., Cabrera, E., Campos, N., Edens, N. K., Rueda, R., & López-Pedrosa, J. M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0117520 · Cited by 71
The Intriguing Regulators of Muscle Mass in Sarcopenia and Muscular Dystrophy
Sakuma, K., Aoi, W., & Yamaguchi, A. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00230 · Cited by 70
Skeletal Muscle Homeostasis in Duchenne Muscular Dystrophy: Modulating Autophagy as a Promising Therapeutic Strategy
Palma, C. D., Perrotta, C., Pellegrino, P., Clementi, E., & Cervia, D. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00188 · Cited by 66
Communication Between Autophagy and Insulin Action: At the Crux of Insulin Action-Insulin Resistance?
Frendo‐Cumbo, S., Tokarz, V. L., Bilan, P. J., Brumell, J. H., & Klip, A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.708431 · Cited by 66
Platinum-induced muscle wasting in cancer chemotherapy: Mechanisms and potential targets for therapeutic intervention
Moreira‐Pais, A., Ferreira, R. M., & da Costa, R. M. G. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.07.010 · Cited by 63
Dysregulated mitochondrial Ca2+ and ROS signaling in skeletal muscle of ALS mouse model
Zhou, J., Li, A., Li, X., & Yi, J. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.01.024 · Cited by 59
Crosstalk between autophagy and insulin resistance: evidence from different tissues
Sadeghi, A., Niknam, M., Momeni‐Moghaddam, M. A., Shabani, M., Aria, H., Bastin, A., Teimouri, M., Meshkani, R., & Akbari, H. (2023) · European journal of medical research · doi:10.1186/s40001-023-01424-9 · Cited by 72
Recent advances in pharmacological, hormonal, and nutritional intervention for sarcopenia
Sakuma, K., & Yamaguchi, A. (2017) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-017-2077-9 · Cited by 60
Suppressed autophagy flux in skeletal muscle of an amyotrophic lateral sclerosis mouse model during disease progression
Xiao, Y., Ma, C., Yi, J., Wu, S., Guo, L., Xu, X., Lin, P., Sun, J., & Zhou, J. (2015) · Physiological Reports · doi:10.14814/phy2.12271 · Cited by 57
The role of TGF-β signaling in muscle atrophy, sarcopenia and cancer cachexia
Lan, X., Deng, C., Wang, Q., Zhao, L., Jiao, B., & Xiang, Y. (2024) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2024.114513 · Cited by 61
Autophagy in Alcohol-Induced Multiorgan Injury: Mechanisms and Potential Therapeutic Targets
Li, Y., Wang, S., Ni, H., Huang, H., & Ding, W. (2014) · BioMed Research International · doi:10.1155/2014/498491 · Cited by 55
Resistance Exercise, Aging, Disuse, and Muscle Protein Metabolism
McKendry, J., Stokes, T., Mcleod, J. C., & Phillips, S. M. (2021) · Comprehensive physiology · doi:10.1002/cphy.c200029 · Cited by 78
IP3 receptor blockade restores autophagy and mitochondrial function in skeletal muscle fibers of dystrophic mice
Valladares-Ide, D., Utreras‐Mendoza, Y., Campos, C., Morales, C., Díaz‐Vegas, A., Contreras‐Ferrat, A. E., Westermeier, F., Jaimovich, E., Marchi, S., Pinton, P., et al. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.08.042 · Cited by 51
The Role of Lonp1 on Mitochondrial Functions during Cardiovascular and Muscular Diseases
Zanini, G., Selleri, V., Malerba, M., Solodka, K., Sinigaglia, G., Nasi, M., Mattioli, A. V., & Pinti, M. (2023) · Antioxidants · doi:10.3390/antiox12030598 · Cited by 50
Regulation of the Tumor-Suppressor BECLIN 1 by Distinct Ubiquitination Cascades
Boutouja, F., Brinkmeier, R., Mastalski, T., Magraoui, F. E., & Platta, H. W. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122541 · Cited by 50
The Importance of mTOR Trafficking for Human Skeletal Muscle Translational Control
Hodson, N. W., & Philp, A. (2018) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000173 · Cited by 50
Muscle dysfunction caused by loss ofMagel2in a mouse model of Prader-Willi and Schaaf-Yang syndromes
Kamaludin, A. A., Smolarchuk, C., Bischof, J. M., Eggert, R., Greer, J. J., Ren, J. T., Lee, J. J., Yokota, T., Berry, F. B., & Wevrick, R. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw225 · Cited by 45
Fucoxanthin rescues dexamethasone induced C2C12 myotubes atrophy
Zhiyin, L., Jinliang, C., Qiunan, C., Yunfei, Y., & Xiao, Q. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111590 · Cited by 48
Muscle LIM protein/CSRP3: a mechanosensor with a role in autophagy
Rashid, M. M., Runci, A., Polletta, L., Carnevale, I., Morgante, E., Foglio, E., Arcangeli, T., Sansone, L., Russo, M. A., & Tafani, M. (2015) · Cell Death Discovery · doi:10.1038/cddiscovery.2015.14 · Cited by 45
Insulin‐Like Growth Factor I Regulation and Its Actions in Skeletal Muscle
Vassilakos, G., & Barton, E. R. (2018) · Comprehensive physiology · doi:10.1002/cphy.c180010 · Cited by 48
ALS-associated mutation SOD1G93A leads to abnormal mitochondrial dynamics in osteocytes
Wang, H., Yi, J., Li, X., Xiao, Y., Dhakal, K. R., & Zhou, J. (2017) · Bone · doi:10.1016/j.bone.2017.10.010 · Cited by 43
The muscle to bone axis (and viceversa): An encrypted language affecting tissues and organs and yet to be codified?
Bosco, F., Musolino, V., Gliozzi, M., Nucera, S., Carresi, C., Zito, M. C., Scarano, F., Scicchitano, M., Reale, F., Ruga, S., et al. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105427 · Cited by 47
Absence of physiological Ca2+ transients is an initial trigger for mitochondrial dysfunction in skeletal muscle following denervation
Karam, C. N., Yi, J., Xiao, Y., Dhakal, K. R., Zhang, L., Li, X., Manno, C. D., Xu, J., Li, K., Cheng, H., et al. (2017) · Skeletal Muscle · doi:10.1186/s13395-017-0123-0 · Cited by 42
Cancer-Induced Reprogramming of Host Glucose Metabolism: “Vicious Cycle” Supporting Cancer Progression
Schwartsburd, P. M. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00218 · Cited by 45
Effects of steroid treatment on growth, nutrient partitioning, and expression of genes related to growth and nutrient metabolism in adult triploid rainbow trout (Oncorhynchus mykiss)
Cleveland, B. M., & Weber, G. M. (2016) · Domestic Animal Endocrinology · doi:10.1016/j.domaniend.2016.01.001 · Cited by 40
The emergence of protein arginine methyltransferases in skeletal muscle and metabolic disease
vanLieshout, T. L., & Ljubicic, V. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00251.2019 · Cited by 40
Apobec2 deficiency causes mitochondrial defects and mitophagy in skeletal muscle
Sato, Y., Ohtsubo, H., Nihei, N., Kaneko, T., Sato, Y., Adachi, S.-I., Kondo, S., Nakamura, M., Mizunoya, W., Iida, H., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201700493r · Cited by 39
Physiological and Pathological Mitochondrial Clearance Is Related to Pectoralis Major Muscle Pathogenesis in Broilers With Wooden Breast Syndrome
Hosotani, M., Kawasaki, T., Hasegawa, Y., Wakasa, Y., Hoshino, M., Takahashi, N., Ueda, H. H., Takaya, T., Iwasaki, T., & Watanabe, T. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00579 · Cited by 42
The Current Landscape of Pharmacotherapies for Sarcopenia
Bahat, G., & Özkök, S. (2024) · Drugs & Aging · doi:10.1007/s40266-023-01093-7 · Cited by 41
Regulation of protein degradation pathways by amino acids and insulin in skeletal muscle of neonatal pigs
Suryawan, A., & Davis, T. A. (2014) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/2049-1891-5-8 · Cited by 38
The Autophagy Regulatory Molecule CSRP3 Interacts with LC3 and Protects Against Muscular Dystrophy
Cui, C., Han, S., Tang, S., He, H., Shen, X., Zhao, J., Chen, Y., Wei, Y., Wang, Y., Zhu, Q. C., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030749 · Cited by 37
How autophagy can restore proteostasis defects in multiple diseases?
Joshi, V., Upadhyay, A., Prajapati, V. K., & Mishra, A. (2020) · Medicinal Research Reviews · doi:10.1002/med.21662 · Cited by 40
Pharmacological inhibition of myostatin protects against skeletal muscle atrophy and weakness after anterior cruciate ligament tear
Wolfe, C. N., Gumucio, J. P., Grekin, J. A., Khouri, R. K., Russell, A. J., Bedi, A., & Mendias, C. L. (2017) · Journal of Orthopaedic Research® · doi:10.1002/jor.23537 · Cited by 36
Mechanical Signaling in the Pathophysiology of Critical Illness Myopathy
Corpeño, R., & Larsson, L. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00023 · Cited by 37
Endothelial Senescence and Chronic Fatigue Syndrome, a COVID-19 Based Hypothesis
Sfera, A., Osorio, C. P., del Campo, C. M. Z.-M., Pereida, S., Maurer, S., Maldonado, J. C., & Kozlakidis, Z. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.673217 · Cited by 34
Exercise Reduces the Resumption of Tumor Growth and Proteolytic Pathways in the Skeletal Muscle of Mice Following Chemotherapy
de Lima, E. A., Teixeira, A. A. D. S., Biondo, L. A., Diniz, T. A., Silveira, L. S., Coletti, D., Busquets, S., & Neto, J. C. R. (2020) · Cancers · doi:10.3390/cancers12113466 · Cited by 32
Angiotensin-(1-7) Prevents Lipopolysaccharide-Induced Autophagy via the Mas Receptor in Skeletal Muscle
Rivera, J. C. A., Ábrigo, J., Tacchi, F., Simón, F., Brandan, E., Santos, R. A. S., Bäder, M., Chiong, M., & Cabello‐Verrugio, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249344 · Cited by 32
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
Fasting Drives Nrf2-Related Antioxidant Response in Skeletal Muscle
Lettieri‐Barbato, D., Minopoli, G., Caggiano, R., Izzo, R., Santillo, M., Aquilano, K., & Faraonio, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207780 · Cited by 29
Phosphate stimulates myotube atrophy through autophagy activation: evidence of hyperphosphatemia contributing to skeletal muscle wasting in chronic kidney disease
Zhang, Y., Yang, M. G., Bao, J., Gu, L., Yu, H., & Yuan, W. (2018) · BMC Nephrology · doi:10.1186/s12882-018-0836-2 · Cited by 30
Filamin C regulates skeletal muscle atrophy by stabilizing dishevelled-2 to inhibit autophagy and mitophagy
Han, S., Cui, C., Zhao, X., Zhang, Y., Zhang, Y. L., Zhao, J., Shen, X., He, H., Wang, J., Ma, M., et al. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.11.022 · Cited by 29
Widespread modulation of gene expression by copy number variation in skeletal muscle
Geistlinger, L., da Silva, V. H., César, A. S. M., Tizioto, P. C., Waldron, L., Zimmer, R., Regitano, L. C. D. A., & Coutinho, L. L. (2018) · Scientific Reports · doi:10.1038/s41598-018-19782-4 · Cited by 30
Perturbation of PI3K/Akt signaling affected autophagy modulation in dystrophin-deficient myoblasts
Yazid, M. D., & Chen, H.-C. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00785-0 · Cited by 27
A Collagen Hydrolysate Containing Tripeptides Ameliorates Sarcopenia in Middle-Aged Mice
Kim, J. E., Kwon, E., & Han, Y. (2022) · Molecules · doi:10.3390/molecules27092718 · Cited by 27
An integrative correlation of myopathology, phenotype and genotype in late onset Pompe disease
Kulessa, M., Weyer-Menkhoff, I., Viergutz, L., Kornblum, C., Claeys, K. G., Schneider, I., Plöckinger, U., Young, P., Boentert, M., Vielhaber, S., et al. (2019) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12580 · Cited by 25
Effects of crowding on the three main proteolytic mechanisms of skeletal muscle in rainbow trout (Oncorhynchus mykiss)
Valenzuela, C., Ponce, C., Zuloaga, R., González, P., Avendaño-Herrera, R. E., Valdés, J. A., & Molina, A. (2020) · BMC Veterinary Research · doi:10.1186/s12917-020-02518-w · Cited by 25
Fighting obesity: When muscle meets fat
Yang, X., Bi, P., & Kuang, S. (2014) · Adipocyte · doi:10.4161/21623945.2014.964075 · Cited by 25
Autophagy induction in the skeletal myogenic differentiation of human tonsil-derived mesenchymal stem cells
Park, S., Choi, Y., Jung, N., Kim, J., Oh, S., Yu, Y., Ahn, J., Jo, I., Choi, B., & Jung, S. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.2898 · Cited by 25
New Molecular Targets and Lifestyle Interventions to Delay Aging Sarcopenia
Sanchis-Gomar, F., Pareja-Galeano, H., Mayero, S., Perez-Quilis, C., & Lucia, A. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00156 · Cited by 24
Unacylated ghrelin restores insulin and autophagic signaling in skeletal muscle of diabetic mice
Tam, B. T., Pei, X. M., Yung, B. Y., Yip, S. P., Chan, L., Wong, S. C. C., & Siu, P. M. (2015) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-015-1721-5 · Cited by 24
Age, gender and side-stratified grip strength norms and related socio-demographic factors for 20–80 years Iranian healthy population: Comparison with consolidated and international norms
Rostamzadeh, S., Saremi, M., & Bradtmiller, B. (2020) · International Journal of Industrial Ergonomics · doi:10.1016/j.ergon.2020.103003 · Cited by 22
Longitudinal assessment of metal concentrations and copper isotope ratios in the G93A SOD1 mouse model of amyotrophic lateral sclerosis
Enge, T. G., Ecroyd, H. W., Jolley, D. F., Yerbury, J. J., & Dosseto, A. (2016) · Metallomics · doi:10.1039/c6mt00270f · Cited by 22
Effects of Heat Stress Treatment on Age-dependent Unfolded Protein Response in Different Types of Skeletal Muscle
Tamura, Y., Matsunaga, Y., Kitaoka, Y., & Hatta, H. (2016) · The Journals of Gerontology Series A · doi:10.1093/gerona/glw063 · Cited by 21
Acute Heat Exposure Alters Autophagy Signaling in C2C12 Myotubes
Summers, C. M., & Valentine, R. J. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2019.01521 · Cited by 19
Dysregulated Autophagy and Mitophagy in a Mouse Model of Duchenne Muscular Dystrophy Remain Unchanged Following Heme Oxygenase-1 Knockout
Mucha, O., Kaziród, K., Podkalicka, P., Rusin, K., Dulak, J., & Łoboda, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010470 · Cited by 20
Lactate-induced autophagy activation: unraveling the therapeutic impact of high-intensity interval training on insulin resistance in type 2 diabetic rats
Pirani, H., Soltany, A., Rezaei, M. H., Fard, A. K., Nikooie, R., Khoramipoor, K., Chamari, K., & Khoramipour, K. (2024) · Scientific Reports · doi:10.1038/s41598-023-50589-0 · Cited by 20
Advance in topical biomaterials and mechanisms for the intervention of pressure injury
Pan, Y., Yang, D., Zhou, M., Liu, Y., Pan, J., Wu, Y., Huang, L., & Li, H. (2023) · iScience · doi:10.1016/j.isci.2023.106956 · Cited by 19
Poor Bone Quality in Patients With Amyotrophic Lateral Sclerosis
Caplliure-Llopis, J., Escrivá, D., Benlloch, M., de la Rubia Ortí, J. E., Estrela, J. M., & Barrios, C. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.599216 · Cited by 19
The melanocortin receptor type 3 agonist d -Trp(8)-γMSH decreases inflammation and muscle wasting in arthritic rats
Gómez-SanMiguel, A. B., Martı́n, A. I., Nieto‐Bona, M. P., Fernández‐Galaz, C., Villanúa, M. Á., & López‐Calderón, A. (2015) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12036 · Cited by 18
Differences in the expression of genes involved in skeletal muscle proteolysis between broiler and layer chicks during food deprivation
Saneyasu, T., Kimura, S., Inui, M., Yoshimoto, Y., Honda, K., & Kamisoyama, H. (2015) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2015.04.007 · Cited by 20
Protein homeostasis in LGMDR9 (LGMD2I) – The role of ubiquitin–proteasome and autophagy–lysosomal system
Franekova, V., Storjord, H. I., Leivseth, G., & Nilssen, Ø. (2020) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12684 · Cited by 18
How Do Skeletal Muscles Die? An Overview
Carmeli, E., Aizenbud, D., & Rom, O. (2015) · Advances in experimental medicine and biology · doi:10.1007/5584_2015_140 · Cited by 17
Ligand-induced rapid skeletal muscle atrophy in HSA-Fv2E-PERK transgenic mice
Miyake, M., Kuroda, M., Kiyonari, H., Takehana, K., Hisanaga, S., Morimoto, M., Zhang, J., Oyadomari, M., Sakaue, H., & Oyadomari, S. (2017) · PLoS ONE · doi:10.1371/journal.pone.0179955 · Cited by 17
Cancer-associated muscle weakness - From triggers to molecular mechanisms
Shorter, E., Engman, V., & Lanner, J. T. (2024) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2024.101260 · Cited by 22
Activation of macroautophagy and chaperone-mediated autophagy in human skeletal muscle by high-intensity exercise in normoxia and hypoxia and after recovery with or without post-exercise ischemia
Martinez‐Canton, M., Galván-Álvarez, V., Gallego-Selles, Á., Gelabert‐Rebato, M., García-Gonzalez, E., González, J. J., Martín-Rincón, M., & Calbet, J. A. L. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.07.012 · Cited by 17
Plectin regulates Wnt signaling mediated-skeletal muscle development by interacting with Dishevelled-2 and antagonizing autophagy
Yin, H., Han, S., Cui, C., Wang, Y., Li, D., & Zhu, Q. (2021) · Gene · doi:10.1016/j.gene.2021.145562 · Cited by 16
O-GlcNAcylation: The Underestimated Emerging Regulators of Skeletal Muscle Physiology
Liu, Y., Hu, Y., Fan, W.-X., Quan, X., Xu, B., & Li, S. (2022) · Cells · doi:10.3390/cells11111789 · Cited by 15
A muscle-centric view of time-restricted feeding for older adults
Lees, M. J., Hodson, N. W., & Moore, D. R. (2021) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000789 · Cited by 15
Sarcopenia; functional concerns, molecular mechanisms involved, and seafood as a nutritional intervention – review article
Jayawardena, T. U., Kim, S., & Jeon, Y. (2021) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2021.1969889 · Cited by 15
Muscle-Bone Crosstalk in Amyotrophic Lateral Sclerosis
Zhou, J., Yi, J., & Bonewald, L. (2015) · Current Osteoporosis Reports · doi:10.1007/s11914-015-0281-0 · Cited by 15
Temporal analysis of skeletal muscle remodeling post hindlimb ischemia reveals intricate autophagy regulation
Scalabrin, M., Engman, V., MacCannell, A. D. V., Critchlow, A. J., Roberts, L. D., Yuldasheva, N. Y., & Bowen, T. S. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00174.2022 · Cited by 12
Kinetic modeling of leucine-mediated signaling and protein metabolism in human skeletal muscle
McColl, T. J., & Clarke, D. C. (2023) · iScience · doi:10.1016/j.isci.2023.108634 · Cited by 12
Serum sestrins: potential predictive molecule in human sarcopenia
Rajan, S. P., Anwar, M., Jain, B., Khan, M. A., Dey, S., & Dey, A. B. (2020) · Aging Clinical and Experimental Research · doi:10.1007/s40520-020-01642-9 · Cited by 14

Authors: Neel, B. A., Lin, Y., & Pessin, J. E.
Affiliations: Albert Einstein College of Medicine (US)
Columbia University (US)
Corresponding author: Pessin, Jeffrey E.
ORCID: Neel, Brian A.
Pessin, Jeffrey E.
Venue: Trends in Endocrinology & Metabolism
Publisher: Elsevier BV
Published: 2013-12
Volume: 24
Issue: 12
Pages: 635-643
ISSN: 1043-2760 (ISSN-L)
DOI: 10.1016/j.tem.2013.09.004
PMC: PMC3849822
OpenAlex: W2054835522
Cited by: 178
References: 74
Citations by year: 2026: 9 · 2025: 8 · 2024: 12 · 2023: 7 · 2022: 16 · 2021: 24 · 2020: 20 · 2019: 14 · 2018: 13 · 2017: 16 · 2016: 14 · 2015: 12 · 2014: 13
FWCI: 1.54
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Trends in Endocrinology and Metabolism (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Institute on Aging (AG23475, T32AG023475)
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK033823, R37DK033823, DK033823, P60DK020541)
National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR-064420, R01AR064420)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords: autophagic flux, muscle metabolism, metabolic regulation
MeSH terms: Animals, Autophagy, Humans, Signal Transduction, Muscle, Skeletal

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

Skeletal muscle autophagy: a new metabolic regulator

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