The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.
Suppression of autophagy in skeletal muscle uncovers the accumulation of ubiquitinated proteins and their potential role in muscle damage in Pompe disease.
Open accessAbstract
The role of autophagy, a catabolic lysosome-dependent pathway, has recently been recognized in a variety of disorders, including Pompe disease, the genetic deficiency of the glycogen-degrading lysosomal enzyme acid-alpha glucosidase. Accumulation of lysosomal glycogen, presumably transported from the cytoplasm by the autophagic pathway, occurs in multiple tissues, but pathology is most severe in skeletal and cardiac muscle. Skeletal muscle pathology also involves massive autophagic buildup in the core of myofibers. To determine if glycogen reaches the lysosome via autophagy and to ascertain whether autophagic buildup in Pompe disease is a consequence of induction of autophagy and/or reduced turnover due to defective fusion with lysosomes, we generated muscle-specific autophagy-deficient Pompe mice. We have demonstrated that autophagy is not required for glycogen transport to lysosomes in skeletal muscle. We have also found that Pompe disease involves induction of autophagy but manifests as a functional deficiency of autophagy because of impaired autophagosomal-lysosomal fusion. As a result, autophagic substrates, including potentially toxic aggregate-prone ubiquitinated proteins, accumulate in Pompe myofibers and may cause profound muscle damage.
Overview
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
Cites
Statistics
Verification
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Impaired autophagy is known to induce skeletal myofiber degeneration and muscle weakness (Masiero et al., 2009; Raben et al., 2008).”
From Proteasome dysfunction induces muscle growth defects and protein aggregation (2014) · cites this paper as Raben et al., 2008
Experimental — accuracy not yet measuredIn the citing paper
“Likewise, impairment of autophagy by muscle-specific ablation of ATG5 and ATG7 induces accumulation of abnormal mitochondria, induction of oxidative stress, apoptosis, muscle atrophy, weakness, several features of myopathy [230, 231].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [230]
In the citing paper
“Analogously, conditional Atg5 deletion in mouse skeletal muscle leads to accumulation of ubiquitin-positive inclusions and ultrastructural disorganization [478].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [478]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605
Self-citationAutophagy 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
Self-citationPankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Self-citationLevine, B., & Klionsky, D. J. (2004) · Developmental Cell · doi:10.1016/s1534-5807(04)00099-1 · Cited by 3,728
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
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500
Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H., & Johansen, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507002 · Cited by 3,276
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
The role of autophagy during the early neonatal starvation period
Kuma, A., Hatano, M., Matsui, M., Yamamoto, A., Nakaya, H., Yoshimori, T., Ohsumi, Y., Tokuhisa, T., & Mizushima, N. (2004) · Nature · doi:10.1038/nature03029 · Cited by 2,865
Self-citation
Research works printed but not linked: 2
- Kondomerkos, 2005, Histology and histopathology, 20, 689
- 2001, PNAS, 98, 14440, 10.1073/pnas.251541198 · DOI · Paper page
Cited by
Sorted by citations
Items 201–300 of 352
New insights into therapeutic options for Pompe disease
Richard, E., Douillard‐Guilloux, G., & Caillaud, C. (2011) · IUBMB Life · doi:10.1002/iub.529 · Cited by 24
Rescue of Advanced Pompe Disease in Mice with Hepatic Expression of Secretable Acid α-Glucosidase
Cagin, U., Puzzo, F., Gómez, M. J., Moya‐Nilges, M., Sellier, P., Abad, C., van Wittenberghe, L., Danièle, N., Guerchet, N., Gjata, B., et al. (2020) · Molecular Therapy · doi:10.1016/j.ymthe.2020.05.025 · Cited by 25
Age-related decline of chaperone-mediated autophagy in skeletal muscle leads to progressive myopathy
Santiago‐Fernández, O., Coletto, L., Tasset, I., Kaushik, S., Concepcion, A. R., Qaisar, R., Macho-González, A., Lindenau, K. L., Díaz, A., Khawaja, R. R., et al. (2025) · Nature Metabolism · doi:10.1038/s42255-025-01412-9 · Cited by 30
“72), Atg7 (ref.”
Picca, A., Triolo, M., Wohlgemuth, S. E., Martenson, M. S., Mankowski, R. T., Anton, S. D., Marzetti, E., Leeuwenburgh, C., & Hood, D. A. (2023) · Cells · doi:10.3390/cells12010183 · Cited by 23
The Role of Autophagy in Salivary Gland Homeostasis and Stress Responses
Morgan-Bathke, M. E., Lin, H. H., Ann, D. K., & Limesand, K. H. (2015) · Journal of Dental Research · doi:10.1177/0022034515590796 · Cited by 23
Shemesh, A., Wang, Y., Yang, Y., Yang, G., Johnson, D., Backer, J., Pessin, J. E., & Zong, H. (2014) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00212.2014 · Cited by 23
“Recent studies have observed that GAA knockout (KO) mice display marked accumulation of autophagic vesicles with altered macroautophagy function (8, 15, 18).”
BackgroundRegulation of Hspb7 by MEF2 and AP-1: implications for Hspb7 in muscle atrophy
Tobin, S. W., Yang, D., Girgis, J., Farahzad, A., Blais, A., & McDermott, J. C. (2016) · Journal of Cell Science · doi:10.1242/jcs.190009 · Cited by 24
“Atg7 then lipidates LC3B-I to form LC3B-II, which can form part of the autophagosome.”
BackgroundTaurine Rescues Cisplatin-Induced Muscle Atrophy in Vitro: A Morphological Study
Stacchiotti, A., Rovetta, F., Ferroni, M., Corsetti, G., Lavazza, A., Sberveglieri, G., & Aleo, M. F. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/840951 · Cited by 21
“amorphous and lamellar material resembled polyubiquitinated deposits described in muscles of autophagy-deficient Pompe mice [43].”
BackgroundMolecular mechanisms and potential interventions during aging-associated sarcopenia
Luo, X., Wang, J., Ju, Q., Li, T., & Bi, X. (2024) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2024.112020 · Cited by 23
Ucci, S., Renzini, A., Russi, V., Mangialardo, C., Cammarata, I., Cavioli, G., Santaguida, M. G., Virili, C., Centanni, M., Adamo, S., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225754 · Cited by 21
Kim, K. W., Cho, H., Khaliq, S. A., Son, K. H., & Yoon, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082862 · Cited by 21
“These findings support the requirement of autophagy in muscle function maintenance by clearing damaged proteins/organelles and ubiquitylated proteins, which are autophagic substrates [38].”
BackgroundNOVEL METHOD FOR DETECTION OF GLYCOGEN IN CELLS
Skurat, A. V., Segvich, D. M., DePaoli-Roach, A. A., & Roach, P. J. (2017) · Glycobiology · doi:10.1093/glycob/cwx005 · Cited by 21
“In Pompe disease, lysosomal glycogen disposal is defective due to mutation of the lysosomal α-glucosidase (acid maltase; GAA) resulting in massive accumulation of glycogen in the lysosomes, disrupting autophagic trafficking and lysosome function generally (Hirschhorn and Reuser 2000; Raben et al. 2008).”
Melatonin: A potential adjuvant therapy for septic myopathy
Liu, Y., Wang, D., Li, T., Xu, L., Li, Z., Bai, X., Tang, M., & Wang, Y.-C. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.114209 · Cited by 20
Autophagy and Cell Death of Purkinje Cells Overexpressing Doppel in Ngsk Prnp‐deficient Mice
Heitz, S., Grant, N., Leschiera, R., Haeberlé, A., Demais, V., Bombarde, G., & Bailly, Y. (2010) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00245.x · Cited by 25
Distinct roles of UVRAG and EGFR signaling in skeletal muscle homeostasis
Kim, M. J., Febbraro, D., Farkona, S., Gillmore, T., Son, J. E., Regeenes, R., Chang, H. H., Pollock‐Tahiri, E., Yang, J., Park, Y. J., et al. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101185 · Cited by 19
“For example, skeletal muscle-specific Atg5 deletion in mice shows loss of muscle mass with the accumulation of protein aggregates [34].”
BackgroundChallenges in diagnosis and treatment of late-onset Pompe disease
Desnuelle, C., & Salviati, L. (2011) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32834a1e00 · Cited by 19
Protective effect of caspase inhibition on compression‐induced muscle damage
Teng, B. T., Tam, E. W., Benzie, I. F. F., & Siu, P. M. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2011.209619 · Cited by 20
“Muscle-specific Atg5 and Atg7 knockout mice have been demonstrated to result in considerable muscle atrophy, decrease in force production and induction of morphological features of myopathy including the presence of protein aggregates and abnormal mitochondria (Raben et al. 2008; Masiero et al. 2009; Masiero & Sandri,…”
BackgroundSkeletal muscle-specific Sidt2 knockout in mice induced muscular dystrophy-like phenotype
Liu, H., Jiang, W., Chen, X., Chang, G., Zhao, L., Li, X., & Zhang, H. (2018) · Metabolism · doi:10.1016/j.metabol.2018.05.004 · Cited by 19
Indices of Defective Autophagy in Whole Muscle and Lysosome Enriched Fractions From Aged D2-mdx Mice
Krishna, S., Spaulding, H. R., Quindry, T. S., Hudson, M. B., Quindry, J. C., & Selsby, J. T. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.691245 · Cited by 18
Xia, F., Liu, P., & Li, M. (2020) · Medicinal Research Reviews · doi:10.1002/med.21772 · Cited by 18
Zhong, J., Gou, Y., Zhao, P., Dong, X., Guo, M., Li, A., Hao, A., Luu, H. H., He, T., Reid, R. R., et al. (2023) · Pediatric Discovery · doi:10.1002/pdi3.3 · Cited by 17
“99,100 Activation of autophagy is critical for energy utilization and clearance of intracellular lipid, which can preferentially hydrolyze intrahepatic lipid droplets to promote mitochondrial fatty acids β ‐oxidation.”
Inhibition of autophagy rescues muscle atrophy in a LGMDD2 Drosophila model
Blázquez‐Bernal, Á., Fernández‐Costa, J. M., Bargiela, A., & Artero, R. D. (2021) · The FASEB Journal · doi:10.1096/fj.202100539rr · Cited by 17
Novel therapeutic approaches for inclusion body myositis
Lloyd, T. E. (2010) · Current Opinion in Rheumatology · doi:10.1097/bor.0b013e32833f0f4a · Cited by 17
TRIM32 and Malin in Neurological and Neuromuscular Rare Diseases
Kumarasinghe, L., Xiong, L., García-Gimeno, M. A., Lazzari, E., Sanz, P., & Meroni, G. (2021) · Cells · doi:10.3390/cells10040820 · Cited by 16
“As some studies indicate that dysfunctional autophagy can abolish cell differentiation and cause muscle atrophy in mouse models, TRIM32 involvement in autophagy regulation awaits further elucidation, in particular in the context of LGMDR8 [90–92].”
Cell type-selective targeted delivery of a recombinant lysosomal enzyme for enzyme therapies
Baik, A. D., Calafati, P., Zhang, X., Aaron, N. A., Mehra, A., Møller-Tank, S., Miloscio, L., Praggastis, M., Giovannone, N., Pan, C., et al. (2021) · Molecular Therapy · doi:10.1016/j.ymthe.2021.08.020 · Cited by 20
Tajima, Y., Saito, S., Ohno, K., Tsukimura, T., Tsujino, S., & Sakuraba, H. (2011) · Journal of Human Genetics · doi:10.1038/jhg.2011.36 · Cited by 15
Low survival rate and muscle fiber-dependent aging effects in the McArdle disease mouse model
Real‐Martínez, A., Brull, A., Huerta, J., Tarrasó, G., Lucía, A., Martín, M. A., Arenas, J., Andreu, A. L., Nogales‐Gadea, G., Vissing, J., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-41414-8 · Cited by 15
Farah, B. L., Madden, L. R., Li, S., Nance, S. A., Bird, A., Bursac, N., Yen, P. M., Young, S. P., & Koeberl, D. D. (2014) · The FASEB Journal · doi:10.1096/fj.13-244202 · Cited by 14
Shen, S., Li, Y., Li, L., Bai, Y., & Liu, H. (2017) · Analytica Chimica Acta · doi:10.1016/j.aca.2017.11.005 · Cited by 13
Canfora, I., Tarantino, N., & Pierno, S. (2022) · Cells · doi:10.3390/cells11162566 · Cited by 16
“Another example was observed in mice with muscle-specific removal of Atg5, a component of the autophagic mechanism [40].”
BackgroundParkin deficiency exacerbates fasting-induced skeletal muscle wasting in mice
Peker, N., Sharma, M., & Kambadur, R. (2022) · npj Parkinson s Disease · doi:10.1038/s41531-022-00419-3 · Cited by 13
To be or not to be cell autonomous? Autophagy says both
Fenouille, N., Nascimbeni, A. C., Botti, J., Dupont, N., Morel, É., & Codogno, P. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170025 · Cited by 15
Autophagy thwarts muscle disease
Tolkovsky, A. M. (2010) · Nature Medicine · doi:10.1038/nm1110-1188 · Cited by 12
ATG14 and RB1CC1 play essential roles in maintaining muscle homeostasis
Li, D., Vogel, P., Li-Harms, X., Wang, B., & Kundu, M. (2021) · Autophagy · doi:10.1080/15548627.2021.1911549 · Cited by 13
“For example, skeletal muscles of all the genetic models (atg14-cKO, rb1cc1-cKO, ulk1 ulk2-cDKO, atg5-cKO and atg7-cKO mice) [6,7] showed the typical SQSTM ubiquitin deposits associated with impaired autophagy; however, targeting Atg14 expression in the heart resulted in more rapid and prominent accumulation of mitocho…”
BackgroundSanchez, A. M. J., Candau, R. B., Raibon, A., & Bernardi, H. (2015) · InTech eBooks · doi:10.5772/60698 · Cited by 13
“Similar muscle alterations have been obtained in muscle-specific Atg5-/- mice [87], confirming the necessity to have regular autophagic flux in the cells, even during atrophy.”
BackgroundEffects of atorvastatin on autophagy in skeletal muscles of diabetic rats
Yang, B., Sun, J. L., Yuan, Y., & Sun, Z. (2017) · Journal of Diabetes Investigation · doi:10.1111/jdi.12789 · Cited by 11
Schaaf, G., Canibano‐Fraile, R., van Gestel, T. J. M., van der Ploeg, A. T., & Pijnappel, W. W. M. P. (2019) · Annals of Translational Medicine · doi:10.21037/atm.2019.04.48 · Cited by 14
Poyatos‐García, J., Blázquez‐Bernal, Á., Selva‐Gimenez, M., Bargiela, A., Espinosa-Espinosa, J., Vázquez‐Manrique, R. P., Bigot, A., Artero, R. D., & Vilchez, J. J. (2023) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2023.01.004 · Cited by 10
Kan, S., Huang, J. Y., Harb, J. F., Rha, A. K., Dalton, N. D., Christensen, C. L., Chan, Y., Davis‐Turak, J., Neumann, J. C., & Wang, R. (2022) · Scientific Reports · doi:10.1038/s41598-022-25914-8 · Cited by 11
“Excessive autophagic buildup is well-documented in PD patients and in PD mice[17, 18] and may be a potential mechanism of pathogenesis.”
BackgroundAutophagy and Exercise: Current Insights and Future Research Directions
Botella, J., Shaw, C. S., & Bishop, D. J. (2023) · International Journal of Sports Medicine · doi:10.1055/a-2153-9258 · Cited by 12
“These differences in autophagy flux appear important from a functional perspective as glycolytic muscle is more susceptible than oxidative muscle to structural and functional alterations with deficient au - tophagy [31, 32].”
BackgroundAtg5flox-Derived Autophagy-Deficient Model of Pompe Disease: Does It Tell the Whole Story?
Lim, J., Zare, H., Puertollano, R., & Raben, N. (2017) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2017.08.002 · Cited by 11
“Accumulation of autophagic substrates and the absence of LC3-II in muscle from either line indicated the efficient suppression of autophagy.(3,5) Of note, in the absence of the disruptive autophagic buildup, ERT cleared lysosomal glycogen in muscle very efficiently in both strains.”
BackgroundInfluentialSelf-citationRega, L. R., Leo, E. D., Nieri, D., & Luciani, A. (2022) · Cells · doi:10.3390/cells11030326 · Cited by 10
“Pompe α-Glucosidase Glycogen Yes Yes ?? Yes [72,73,87,88] Defects in soluble non−enzymatic lysosomal proteins Niemann-Pick disease type C2 NPC2 Cholesterol and sphingolipids Yes Yes ?? Yes [78,79]”
BackgroundYu, X., Ma, J., Lin, F. W., Zhao, W., Fu, X., & Zhao, Z. J. (2012) · BMC Cell Biology · doi:10.1186/1471-2121-13-28 · Cited by 10
“For example, both Atg5 and Atg7 mice show muscle loss accompanied by accumulation of protein aggregates and abnormal membranous structures in the muscle cells [23,24].”
BackgroundForesto, C. S., Paula-Gomes, S., Silveira, W. A., Graça, F. A., Kettelhut, Í. D. C., Gonçalves, D. A. P., & Mattiello‐Sverzut, A. C. (2016) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00687.2015 · Cited by 10
“In addition, unlike Beclin-1 haploinsufficiency mice, Atg7 or Atg5 homozygous knockout mice, which display an impairment in autophagy, showed an exacerbation of the muscle loss during denervation and fasting (29) and the myopathic phenotype in a mouse model of Pompe disease (40).”
BackgroundResultLiang, Q., Vlaar, E. C., Pijnenburg, J. M., Rijkers, E., Demmers, J., Vulto, A. G., van der Ploeg, A. T., van Til, N. P., & Pijnappel, W. W. M. P. (2023) · Journal of Proteomics · doi:10.1016/j.jprot.2023.105037 · Cited by 9
Wu, Q., Huang, Q., Xu, Z., Hou, C., & Wang, C. (2025) · Journal of Inflammation Research · doi:10.2147/jir.s554850 · Cited by 10
Dyrk1b promotes autophagy during skeletal muscle differentiation by upregulating 4e-bp1
Bhat, N., Narayanan, A., Fathzadeh, M., Shah, K., Dianatpour, M., Ziki, M. D. A., & Mani, A. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.110186 · Cited by 9
Metabolic Dysfunction in Motor Neuron Disease: Shedding Light through the Lens of Autophagy
Silva, S. D., Turner, B. J., & Perera, N. D. (2022) · Metabolites · doi:10.3390/metabo12070574 · Cited by 7
Autophagic flux is impaired in the brain tissue of Tay-Sachs disease mouse model
Sengül, T., Can, M., Ateş, N., & Seyrantepe, V. (2023) · PLoS ONE · doi:10.1371/journal.pone.0280650 · Cited by 8
“cultured fibroblasts of Fabry patients [32], mucolipidosis type II, III [33] and type IV (MLIV) fibroblasts [34], muscle fibers of Pompe disease [35], and brain of Gaucher disease mice model [36].”
BackgroundCellular mechanisms of acute rhabdomyolysis in inherited metabolic diseases
de Calbiac, H., Imbard, A., & de Lonlay, P. (2024) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12781 · Cited by 9
“328 – 331 Autophagy deficiency has been linked to skeletal muscle damage and mass loss, myopathy and decreased muscle performance 332 – 335 and its modulation is a key therapeutic strategy for improving muscle performance.”
Wang, Y., Bai, L., Li, S., Wen, Y., Liu, Q., Li, R., & Liu, Y. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02216-6 · Cited by 7
Molecular Mechanisms Controlling Skeletal Muscle Mass
Sakuma, K., & Yamaguchi, A. (2015) · InTech eBooks · doi:10.5772/60876 · Cited by 8
Pastores, G. M. (2010) · Advances in neurobiology · doi:10.1007/978-1-4419-7104-3_23 · Cited by 7
“A disturbance of autophagy has also been found in the mouse model of Pompe disease; which interestingly has been linked to a deficiency in the trafficking/processing of recombinant enzyme along the endocytic pathway (Raben et al., 2008).”
BackgroundFrom Acid Alpha-Glucosidase Deficiency to Autophagy: Understanding the Bases of POMPE Disease
Sánchez-Porras, V., Guevara, J., & Echeverri-Peña, O. Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512481 · Cited by 6
“(2008) described an accumulation of non-phosphorylated p62 in GAA-KO mice [46], and Sato et al.”
BackgroundTherapeutic targeting of GDF11 in muscle atrophy: Insights and strategies
Wang, C., Liu, X., Hu, X., Wu, T., & Duan, R. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.135321 · Cited by 6
pathways during ultra-endurance running Modulation of autophagy and ubiquitin-proteasome
Féasson, L., Jamart, C., Francaux, M., Millet, G. Y., Deldicque, L., & Frère, D. (2012) · Cited by 6
Nakanishi, T., Tokunaga, T., Ishida, T., Kobayashi, I., Katahama, Y., Yano, A., Erickson, L., & Kawahara, S. (2018) · Asian-Australasian Journal of Animal Sciences · doi:10.5713/ajas.18.0370 · Cited by 6
“Previous studies in rodents have shown that both excessive activity of autophagy and autophagy inhibition are detrimental to maintaining muscle homeostasis, and both contribute to the progression of muscle atrophy [10,23].”
BackgroundAutophagy selectively clears ER in TNF-α-induced muscle atrophy
Dueren, U. K., Wei, A. A. J., Gressler, A. E., Rapp, S., Popp, O., Kerridge, R., Buonomo, V., Grumati, P., Mertins, P., Selbach, M., et al. (2026) · Autophagy Reports · doi:10.1080/27694127.2026.2649064 · Cited by 5
“Additional knockout models targeting Atg5, mTOR, ULK2, VPS15, and AMPK further emphasize the finely tuned regulation required for autophagy to remain beneficial [69–73].”
Sui, Z., Wang, X., Zhang, X., Zhou, H., Liu, C., Mai, K., & He, G. (2023) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2023.109068 · Cited by 5
Autophagy in striated muscle diseases
Bailin, P. L., Zhang, L., Zhang, L., & Han, R. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.1000067 · Cited by 5
“The fusion of autophagosome-lysosome is suppressed while autophagy initiation is induced in GAA mutant mouse model (92).”
BackgroundCooke, D., & Ables, G. P. (2023) · Scientific Reports · doi:10.1038/s41598-023-47676-7 · Cited by 5
“Autophagy is essential for muscle mass preservation 21,22 and its activation is a potential mechanism through which SAAR may enhance health span 6,7,23 .”
BackgroundAutophagic vacuolar myopathy: Danon disease and related myopathies
Sugie, K. (2021) · Neurology and Clinical Neuroscience · doi:10.1111/ncn3.12554 · Cited by 5
Historical Overview of Autophagy
Dunn, W. A., Schröder, L., & Aris, J. P. (2013) · Springer eBooks · doi:10.1007/978-1-4614-6561-4_1 · Cited by 5
Cellular mechanisms promoting cachexia and how they are opposed by sirtuins
Samant, S. A., Pillai, V. B., & Gupta, M. P. (2018) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2018-0479 · Cited by 5
“Muscle-specific deletion of the autophagy genes Atg7 or Atg5 result in profound myofiber degeneration (Masiero et al. 2009; Raben et al. 2008) underscoring the essential role played by autophagy in maintaining muscle homeostasis.”
BackgroundAutophagy as a therapeutic linchpin in metabolic diseases and obesity-associated diabetes
Vakili, O., Klionsky, D. J., Reiter, R. J., Ren, J., Deshpande, A., Ahn, K. S., Cho, W., Hushmandi, K., & Kumar, A. P. (2026) · Autophagy · doi:10.1080/15548627.2026.2636096 · Cited by 7
“Glycophagosomes appear in Drosophila and mice [38,39], but genetic evidence suggests non-canonical, ATG5-independent mechanisms in muscle [40].”
The Epiphyseal Growth Plate: The Engine That Drives Bone Elongation
Srinivas, V., & Shapiro, I. M. (2011) · Springer eBooks · doi:10.1007/978-1-4419-1795-9_80 · Cited by 4
Influence of skeletal muscle heterogeneity on autophagic signaling and response
Rahman, F. A., & Quadrilatero, J. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2562429 · Cited by 4
Zrelski, M. M., Eckhard, M., Fichtinger, P., Hösele, S., Sombke, A., Mill, L., Kustermann, M., Schmidt, W. M., Norwood, F., Schlötzer-Schrehardt, U. M., et al. (2025) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.70001 · Cited by 3
Altering Autophagy: Mouse Models of Human Disease
Hale, A. N., Ledbetter, D., Gawriluk, T. R., & Rucker, E. B. (2013) · InTech eBooks · doi:10.5772/55258 · Cited by 5
“These data indicated that the disruption of functional autophagy and accumulation of toxic ubiquitin-positive structures promoted muscular myopathy [55].”
BackgroundOsteosarcopenia as a Lipotoxic Disease
Saedi, A. A., Goodman, C. A., Myers, D. E., Hayes, A., & Duque, G. (2019) · Springer eBooks · doi:10.1007/978-3-030-25890-0_6 · Cited by 4
Aguilar-González, A., González-Correa, J. E., Barriocanal‐Casado, E., Ramos-Hernández, I., Lerma-Juárez, M. A., Greco, S., Rodríguez‐Sevilla, J. J., Molina-Estévez, F. J., Montalvo-Romeral, V., Ronzitti, G., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116298 · Cited by 4
Acheson, J., Joanisse, S., Sale, C., & Hodson, N. W. (2024) · Bioscience Reports · doi:10.1042/bsr20240137 · Cited by 4
“ATG5-KO also induces glycolytic myofiber atrophy, which is associated with autophagy protein build-up and impaired lysosome morphology within the intermyofibrillar space [183].”
Glycophagy: molecular mechanisms, regulatory signals, and disease associations
Chen, L., Jiang, J., Meiqing, L., & Chen, L. (2026) · Autophagy Reports · doi:10.1080/27694127.2025.2595375 · Cited by 4
“…encoding lysosomal GAA, which leads to the deficiency of GAA, blocking the degradation steps of glycogen by lysosomes during the process of autophagy (rather than the fusion disorder of autophagosomes and lysosomes), ultimately resulting in abnormal accumulation of glycogen in lysosomes [99–102] .”
Role of mitochondrial dysfunction in muscle wasting in cancer cachexia: a narrative review
Su, X., Wang, S., Qu, Y., Wang, Y., Tian, Z., Chao, X., Li, Z., & Ma, D. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-07906-8 · Cited by 7
Lithium treatment rescues dysfunctional autophagy in the cell models of Tay-Sachs disease
Basırlı, H., Can, M., Sengül, T., & Seyrantepe, V. (2024) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2024.108140 · Cited by 3
Autophagy signaling in hypertrophied muscles of diabetic and control rats
Scervino, M. V. M., Fortes, M. A. S., Vitzel, K. F., de Souza, D. R., Murata, G. M., Santana, G. O., da Silva, E. B., Levada‐Pires, A. C., Kuwabara, W. M. T., Alba‐Loureiro, T. C., et al. (2023) · FEBS Open Bio · doi:10.1002/2211-5463.13677 · Cited by 3
The role of autophagy in skeletal muscle homeostasis
Ogata, T. (2012) · The Journal of Physical Fitness and Sports Medicine · doi:10.7600/jpfsm.1.159 · Cited by 3
Baik, A. D., Calafati, P., Aaron, N. A., Mehra, A., Møller-Tank, S., Miloscio, L., Wang, L., Praggastis, M., Birnbaum, M. S., Pan, C., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.04.22.051672 · Cited by 3
Lemmer, I. L., Haas, D. T., Rivera, F., Kotschi, S., Matta, L., Willemsen, N., Jethwa, C., Guerra, J., Gómez, A. M., Toksöz, I., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.20.537611 · Cited by 4
“When autophagy is suppressed, such as in Pompe disease, this is associated with ubiquitylated protein inclusion bodies and markers of muscle damage 33 .”
Yeo, D. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-88361-3_8 · Cited by 4
Ribeiro, D. N., de Assis, A. P., Pinto, A. P., Ropelle, E. R., Pauli, J., de Freitas, E. C., & da Silva, A. S. R. (2025) · Advanced Exercise and Health Science · doi:10.1016/j.aehs.2025.08.005 · Cited by 2
Divino, I. A., da Vieira‐da‐Silva, A. L., Esteca, M. V., Tonon, R. P., da Cruz, F. O. G., Braga, R. R., Ropelle, E. R., Gandra, P. G., & Baptista, I. L. (2025) · Acta Physiologica · doi:10.1111/apha.70082 · Cited by 2
“It is known that inhibition of autophagy leads to muscle atrophy and that MURF-1 is increased in skeletal muscle in rodent models with deficiency in autophagic flux, such as Atg7 − / − and Atg5 − / − mice [45].”
Skeletal Muscle Homeostasis and Aging in Drosophila
Puppa, M., & Demontis, F. (2015) · Healthy ageing and longevity · doi:10.1007/978-3-319-18326-8_5 · Cited by 2
Freij, K. W., Cleveland, B. M., & Biga, P. R. (2024) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2024.101193 · Cited by 2
Cox, T. M. (2017) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0002270.pub2 · Cited by 2
Quezada, E. R., Blanco, N., Llanos, P., Criollo, A., Chiong, M., & Buvinic, S. (2026) · Cell Death Discovery · doi:10.1038/s41420-026-02982-7 · Cited by 2
“The proposal has been approved by the IACUC of the Universidad de Chile (N° 21446 – ODO – UCH-e2).”
Identification of alterations of immunometabolism associated with Pompe disease
Verdera, H. C., Gargaro, M., Cagin, U., Manni, G., Scalisi, G., Veron, P., Barcelos, E. C. S., Pieroni, B., Mencarelli, G., Ricciuti, D., et al. (2026) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-026-06135-y · Cited by 1
Shacka, J. J. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814350457_0014 · Cited by 1
The Autophagy-Dependent Signaling in Skeletal Muscle
Sakuma, K., Aizawa, M., Wakabayashi, H., & Yamaguchi, A. (2017) · Springer eBooks · doi:10.1007/978-981-10-3292-9_4 · Cited by 1
Markby, G. R., & Sakamoto, K. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822003-0.00019-x · Cited by 1
Monika, M., Gupta, S. K., Dua, A., & Mittal, A. (2024) · Journal of Applied Biology & Biotechnology · doi:10.7324/jabb.2024.176603 · Cited by 1
Autophagy markers expression pattern in developing liver of the yotari (dab1 -/-) mice and humans
Maras, E. D., Kelam, N., Racetin, A., Haque, E., Dražić, M., Vukojević, K., Katsuyama, Y., Saraga‐Babić, M., & Filipović, N. (2024) · Acta Histochemica · doi:10.1016/j.acthis.2024.152224 · Cited by 1
Поздняя форма болезни Помпе: диагностические и терапевтические подходы
Desnuelle (2015) · DOAJ (DOAJ: Directory of Open Access Journals) · doi:10.17650/2222-8721-2012-0-3-20-32 · Cited by 1
Nonmitochondrial Metabolic Cardioskeletal Myopathies
El‐Gharbawy, A., & Vockley, J. E. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-800040-3.00014-5 · Cited by 1
Molecular Mechanisms, Therapeutic Targets and Pharmacological Interventions: An Update
Kwatra, M., Ahmed, S., Panda, S. R., Naidu, V. G. M., & Gupta, N. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.95996 · Cited by 1
Autophagy in Mammalian Development and Differentiation
(2021) · Frontiers research topics · doi:10.3389/978-2-88971-339-4 · Cited by 1
Choi, R. S. (2010) · Eukaryon · Cited by 1
Examining Autophagy and Mitophagy as Inducible Mechanisms of Cellular Remodelling
Bloemberg, D. (2017) · UWSpace (University of Waterloo) · Cited by 1
Nfe2l1-mediated proteasome function controls muscle energy metabolism in obesityPreprint
Bartelt, A., Lemmer, I. L., Willemsen, N., Kotschi, S., Toksöz, I., Gjika, E., Khani, S., Haas, D. T., Krahmer, N., Rohm, M., et al. (2023) · Research Square · doi:10.21203/rs.3.rs-2874236/v1 · Cited by 1
THE ZEBRAFISH AS A MODEL TO ELUCIDATE HUMAN DISEASES AND DEVELOPMENT
Lee, S. L. C. (2011) · Figshare · Cited by 1
Metadata
- Authors
- Raben, N., Hill, V., Shea, L., Takikita, S., Baum, R., Mizushima, N., Ralston, E., & Plotz, P.
- Affiliations
- National Institutes of Health (US)
- Tokyo Medical and Dental University (JP)
- Corresponding author
- Raben, N.
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2008-09-04
- Volume
- 17
- Issue
- 24
- Pages
- 3897-3908
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- PMC
- PMC2638578
- OpenAlex
- W2136000647
- Cited by
- 352
- References
- 61
- Citations by year
- 2026: 14 · 2025: 10 · 2024: 15 · 2023: 19 · 2022: 21 · 2021: 21 · 2020: 16 · 2019: 18 · 2018: 17 · 2017: 23 · 2016: 18 · 2015: 26 · 2014: 25 · 2013: 21 · 2012: 33
- FWCI
- 12.22
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Human Molecular Genetics (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- York University
- Institut National de la Santé et de la Recherche Médicale
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke
- National Institute of Arthritis and Musculoskeletal and Skin Diseases
- Topics
- Health Sciences › Medicine › Genetics (clinical) › Lysosomal Storage Disorders Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Glycogen Storage Diseases and Myoclonus
- Keywords
- Pompe disease, autophagy, skeletal muscle, acid alpha-glucosidase deficiency, lysosomal glycogen accumulation, ubiquitinated proteins, protein aggregation, muscle damage
- MeSH terms
- alpha-Glucosidases, Animals, Autophagy, Female, Glycogen Storage Disease Type II, Male, Mice, Transgenic, Muscular Diseases, Proteins, Mice, Knockout, Muscle, Skeletal, Mice, Ubiquitination
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
