The p97/VCP ATPase is critical in muscle atrophy and the accelerated degradation of muscle proteins

Identification of ubiquitin ligases required for skeletal muscle atrophy.

Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., et al. (2001) · Science · doi:10.1126/science.1065874 · Cited by 3,521 · see citing works

Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy.

Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2004) · Cell · doi:10.1016/s0092-8674(04)00400-3 · Cited by 3,012 · see citing works

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

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

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 · see citing works

Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression

Lecker, S. H., Jagoe, R. T., Gilbert, A., Gomes, M., Baracos, V., Bailey, J., Price, S. R., Mitch, W. E., & Goldberg, A. L. (2004) · The FASEB Journal · doi:10.1096/fj.03-0610com · Cited by 1,539 · see citing works

FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells.

Zhao, J., Brault, J. J., Schild, A., Cao, P., Sandri, M., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.004 · Cited by 1,489 · see citing works

Wasting as independent risk factor for mortality in chronic heart failure

Anker, S. D., Ponikowski, P. P., Varney, S. J., Chua, T. P., Clark, A. L., Webb-Peploe, K., Harrington, D., Kox, W. J., Poole-Wilson, P. A., & Coats, A. J. S. (1997) · The Lancet · doi:10.1016/s0140-6736(96)07015-8 · Cited by 1,399 · see citing works

Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein

Watts, G. D. J., Wymer, J., Kovach, M. J., Mehta, S. G., Mumm, S., Darvish, D., Pestronk, A., Whyte, M. P., & Kimonis, V. E. (2004) · Nature Genetics · doi:10.1038/ng1332 · Cited by 1,391 · see citing works

Exome Sequencing Reveals VCP Mutations as a Cause of Familial ALS

Johnson, J. O., Mandrioli, J., Benatar, M., Abramzon, Y., Van Deerlin, V. M., Trojanowski, J. Q., Gibbs, J. R., Brunetti, M., Gronka, S., Wuu, J., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.036 · Cited by 1,235 · see citing works

Mechanisms of Muscle Wasting — The Role of the Ubiquitin–Proteasome Pathway

Mitch, W. E., & Goldberg, A. L. (1996) · New England Journal of Medicine · doi:10.1056/nejm199612193352507 · Cited by 1,163 · see citing works

The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol

Ye, Y., Meyer, H. H., & Rapoport, T. A. (2001) · Nature · doi:10.1038/414652a · Cited by 1,099 · see citing works

Reversal of Cancer Cachexia and Muscle Wasting by ActRIIB Antagonism Leads to Prolonged Survival

Zhou, X., Wang, J. L., Lu, J., Song, Y., Kwak, K. S., Jiao, Q., Rosenfeld, R., Chen, Q., Boone, T. C., Simonet, W. S., et al. (2010) · Cell · doi:10.1016/j.cell.2010.07.011 · Cited by 941 · see citing works

IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1

Sacheck, J. M., Ohtsuka, A., McLary, S. C., & Goldberg, A. L. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00073.2004 · Cited by 606 · see citing works

Function of the p97–Ufd1–Npl4 complex in retrotranslocation from the ER to the cytosol

Ye, Y., Meyer, H. H., & Rapoport, T. A. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302169 · Cited by 598 · see citing works

Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases

Sacheck, J. M., Hyatt, J. K., Raffaello, A., Thomas Jagoe, R., Roy, R. R., Reggie Edgerton, V., Lecker, S. H., & Goldberg, A. L. (2007) · The FASEB Journal · doi:10.1096/fj.06-6604com · Cited by 585 · see citing works

During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation

Cohen, S., Brault, J. J., Gygi, S. P., Glass, D. J., Valenzuela, D. M., Gartner, C. A., Latres, E., & Goldberg, A. L. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200901052 · Cited by 584 · see citing works

A Series of Ubiquitin Binding Factors Connects CDC48/p97 to Substrate Multiubiquitylation and Proteasomal Targeting

Richly, H., Rapé, M., Braun, S. J., Rumpf, S., Hoege, C., & Jentsch, S. (2005) · Cell · doi:10.1016/j.cell.2004.11.013 · Cited by 523 · see citing works

Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease

Ju, J.-S., Fuentealba, R. A., Miller, S. E., Jackson, E., Piwnica-Worms, D., Baloh, R. H., & Weihl, C. C. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200908115 · Cited by 494 · see citing works

A complex of mammalian Ufd1 and Npl4 links the AAA‐ATPase, p97, to ubiquitin and nuclear transport pathways

Meyer, H. H., Shorter, J., Seemann, J., Pappin, D., & Warren, G. (2000) · The EMBO Journal · doi:10.1093/emboj/19.10.2181 · Cited by 446 · see citing works

Mobilization of Processed, Membrane-Tethered SPT23 Transcription Factor by CDC48UFD1/NPL4, a Ubiquitin-Selective Chaperone

Rapé, M., Hoppe, T., Gorr, I. H., Kalocay, M., Richly, H., & Jentsch, S. (2001) · Cell · doi:10.1016/s0092-8674(01)00595-5 · Cited by 438 · see citing works

Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin–proteasome degradation

Dai, R. M., & Li, C.-C. H. (2001) · Nature Cell Biology · doi:10.1038/35087056 · Cited by 437 · see citing works

VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD

Tresse, E., Salomons, F. A., Vesa, J., Bott, L. C., Kimonis, V., Yao, T.-P., Dantuma, N. P., & Taylor, J. P. (2010) · Autophagy · doi:10.4161/auto.6.2.11014 · Cited by 437 · see citing works

Importance of the ATP-Ubiquitin-Proteasome Pathway in the Degradation of Soluble and Myofibrillar Proteins in Rabbit Muscle Extracts

Solomon, V., & Goldberg, A. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.43.26690 · Cited by 432 · see citing works

COLD-SENSITIVE CELL-DIVISION-CYCLE MUTANTS OF YEAST: ISOLATION, PROPERTIES, AND PSEUDOREVERSION STUDIES

Moir, D., Stewart, S. E., Osmond, B. C., & Botstein, D. (1982) · Genetics · doi:10.1093/genetics/100.4.547 · Cited by 373 · see citing works

Signaling pathways perturbing muscle mass.

Glass, D. J. (2010) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/mco.0b013e32833862df · Cited by 359 · see citing works

Patterns of gene expression in atrophying skeletal muscles: response to food deprivation

Jagoe, R. T., Lecker, S. H., Gomes, M., & Goldberg, A. L. (2002) · The FASEB Journal · doi:10.1096/fj.02-0312com · Cited by 344 · see citing works

Reversible inhibitor of p97, DBeQ, impairs both ubiquitin-dependent and autophagic protein clearance pathways

Chou, T., Brown, S. J., Minond, D., Nordin, B. E., Li, K., Jones, A. C., Chase, P. S., Porubsky, P. R., Stoltz, B. M., Schoenen, F. J., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1015312108 · Cited by 323 · see citing works

Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles.

Tawa, N. E., Odessey, R., & Goldberg, A. L. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119513 · Cited by 322 · see citing works

Involvement of Valosin-containing Protein, an ATPase Co-purified with IκBα and 26 S Proteasome, in Ubiquitin-Proteasome-mediated Degradation of IκBα

Dai, R., Chen, E., Longo, D. L., Gorbea, C. M., & Li, C.-C. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3562 · Cited by 315 · see citing works

UBXD7 Binds Multiple Ubiquitin Ligases and Implicates p97 in HIF1α Turnover

Alexandru, G., Graumann, J., Smith, G. T., Kolawa, N. J., Fang, R., & Deshaies, R. J. (2008) · Cell · doi:10.1016/j.cell.2008.06.048 · Cited by 305 · see citing works

Downstream of Akt: FoxO3 and mTOR in the regulation of autophagy in skeletal muscle

Mammucari, C., Schiaffino, S., & Sandri, M. (2008) · Autophagy · doi:10.4161/auto.5905 · Cited by 295 · see citing works

Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy

Medina, R., Wing, S. S., & Goldberg, A. L. (1995) · Biochemical Journal · doi:10.1042/bj3070631 · Cited by 294 · see citing works

Rad23 Promotes the Targeting of Proteolytic Substrates to the Proteasome

Chen, L., & Madura, K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4902-4913.2002 · Cited by 291 · see citing works

An abundant and ubiquitous homo‐oligomeric ring‐shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF.

Peters, J. M., Walsh, M. J., & Franke, W. W. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb08300.x · Cited by 282 · see citing works

Cdc48 (p97): a ‘molecular gearbox’ in the ubiquitin pathway?

Jentsch, S., & Rumpf, S. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.11.005 · Cited by 280 · see citing works

Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin

Ramadan, K., Bruderer, R., Spiga, F. M., Popp, O., Baur, T., Gotta, M., & Meyer, H. H. (2007) · Nature · doi:10.1038/nature06388 · Cited by 261 · see citing works

RNA interference of valosin-containing protein (VCP/p97) reveals multiple cellular roles linked to ubiquitin/proteasome-dependent proteolysis

Wójcik, C., Yano, M., & Demartino, G. (2003) · Journal of Cell Science · doi:10.1242/jcs.00841 · Cited by 251 · see citing works

The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover

Xu, S., Peng, G., Wang, Y., Fang, S., & Karbowski, M. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-09-0748 · Cited by 243 · see citing works

VCP disease associated with myopathy, Paget disease of bone and frontotemporal dementia: Review of a unique disorder

Kimonis, V. E., Fulchiero, E. C., Vesa, J., & Watts, G. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.09.003 · Cited by 227 · see citing works

Muscle Wasting in Aged, Sarcopenic Rats Is Associated with Enhanced Activity of the Ubiquitin Proteasome Pathway

Altun, M., Besche, H. C., Overkleeft, H. S., Piccirillo, R., Edelmann, M. J., Kessler, B. M., Goldberg, A. L., & Ulfhake, B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.129718 · Cited by 226 · see citing works

Diverse functions with a common regulator: Ubiquitin takes command of an AAA ATPase

Ye, Y. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.01.005 · Cited by 213 · see citing works

AAA ATPase p97/Valosin-containing Protein Interacts with gp78, a Ubiquitin Ligase for Endoplasmic Reticulum-associated Degradation

Zhong, X., Shen, Y., Ballar, P., Apostolou, A., Agami, R., & Fang, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409034200 · Cited by 209 · see citing works

Trim32 is a Ubiquitin Ligase Mutated in Limb Girdle Muscular Dystrophy Type 2H that Binds to Skeletal Muscle Myosin and Ubiquitinates Actin

Kudryashova, E., Kudryashov, D. S., Kramerova, I. A., & Spencer, M. J. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.09.068 · Cited by 207 · see citing works

ATP binds to proteasomal ATPases in pairs with distinct functional effects implying an ordered reaction cycle

Smith, D. M., Fraga, H., Reis, C. R. S., Kafri, G., & Goldberg, A. (2011) · Cell · doi:10.1016/j.cell.2011.02.005 · Cited by 202 · see citing works

Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation

Weihl, C. C., Dalal, S. R., Pestronk, A., & Hanson, P. I. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi426 · Cited by 195 · see citing works

Recent advances in p97/VCP/Cdc48 cellular functions

Yamanaka, K., Sasagawa, Y., & Ogura, T. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.07.001 · Cited by 191 · see citing works

Valosin-containing Protein (p97) Is a Regulator of Endoplasmic Reticulum Stress and of the Degradation of N-End Rule and Ubiquitin-Fusion Degradation Pathway Substrates in Mammalian Cells

Wójcik, C., Rowicka, M., Kudlicki, A. S., Nowis, D., McConnell, E. J., Kujawa, M., & Demartino, G. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-05-0432 · Cited by 189 · see citing works

Heat shock and oxygen radicals stimulate ubiquitin-dependent degradation mainly of newly synthesized proteins

Medicherla, B., & Goldberg, A. L. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200803022 · Cited by 175 · see citing works

Pathological consequences of VCP mutations on human striated muscle

Hubbers, C. U., Clemen, C. S., Kesper, K., Boddrich, A., Hofmann, A., Kamarainen, O., Tolksdorf, K., Stumpf, M., Reichelt, J., Roth, U., et al. (2007) · Brain · doi:10.1093/brain/awl238 · Cited by 170 · see citing works

Coordinate activation of autophagy and the proteasome pathway by FoxO transcription factor

Zhao, J., Brault, J. J., Schild, A., & Goldberg, A. L. (2008) · Autophagy · doi:10.4161/auto.5633 · Cited by 164 · see citing works

Functional ATPase Activity of p97/Valosin-containing Protein (VCP) Is Required for the Quality Control of Endoplasmic Reticulum in Neuronally Differentiated Mammalian PC12 Cells

Kobayashi, T., Tanaka, K., Inoue, K., & Kakizuka, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207783200 · Cited by 148 · see citing works

The ubiquitin-selective chaperone CDC-48/p97 links myosin assembly to human myopathy

Janiesch, P. C., Kim, J., Mouysset, J., Barikbin, R., Lochmüller, H., Cassata, G., Krause, S., & Hoppe, T. (2007) · Nature Cell Biology · doi:10.1038/ncb1554 · Cited by 143 · see citing works

Cdc48/p97 and Shp1/p47 regulate autophagosome biogenesis in concert with ubiquitin-like Atg8

Krick, R., Bremer, S., Welter, E., Schlotterhose, P., Mühe, Y., Eskelinen, E., & Thumm, M. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201002075 · Cited by 139 · see citing works

Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities

Wang, Q., Song, C., & Li, C.-C. H. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02840-1 · Cited by 137 · see citing works

Targeted deletion of p97 (VCP/CDC48) in mouse results in early embryonic lethality

Müller, J. M. M., Deinhardt, K., Rosewell, I., Warren, G., & Shima, D. T. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.12.206 · Cited by 133 · see citing works

Comparison of turnover of several myofibrillar proteins and critical evaluation of double isotope method.

Zak, R., Martı́n, A., Prior, G., & Rabinowitz, M. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40409-1 · Cited by 129 · see citing works

Recent advances in the biology and therapy of muscle wasting

Glass, D. J., & Roubenoff, R. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05809.x · Cited by 127 · see citing works

A Conserved Unfoldase Activity for the p97 AAA-ATPase in Proteasomal Degradation

Beskow, A., Grimberg, K. B., Bott, L. C., Salomons, F. A., Dantuma, N. P., & Young, P. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.09.050 · Cited by 115 · see citing works

Human Fas-Associated Factor 1, Interacting with Ubiquitinated Proteins and Valosin-Containing Protein, Is Involved in the Ubiquitin-Proteasome Pathway

Song, E. J., Yim, S.-H., Kim, E., Kim, N.-S., & Lee, K. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.6.2511-2524.2005 · Cited by 115 · see citing works

Elevated Expression of Valosin-Containing Protein (p97) Is Associated with Poor Prognosis of Prostate Cancer

Tsujimoto, Y., Tomita, Y., Hoshida, Y., Kono, T., Oka, T., Yamamoto, S., Nonomura, N., Okuyama, Ä., & Aozasa, K. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-03-0191 · Cited by 114 · see citing works

Hereditary Inclusion Body Myopathy-Linked p97/VCP Mutations in the NH2 Domain and the D1 Ring Modulate p97/VCP ATPase Activity and D2 Ring Conformation

Halawani, D., LeBlanc, A. C., Rouiller, I., Michnick, S. W., Servant, M. J., & Latterich, M. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00252-09 · Cited by 111 · see citing works

Imbalances in p97 co‐factor interactions in human proteinopathy

Fernández‐Sáiz, V., & Buchberger, A. (2010) · EMBO Reports · doi:10.1038/embor.2010.49 · Cited by 108 · see citing works

SVIP is a novel VCP/p97-interacting protein whose expression causes cell vacuolation

Nagahama, M., Suzuki, M., Hamada, Y., Hatsuzawa, K., Tani, K., Yamamoto, A., & Tagaya, M. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.02-07-0115 · Cited by 95 · see citing works

Unc45b Forms a Cytosolic Complex with Hsp90 and Targets the Unfolded Myosin Motor Domain

Srikakulam, R., Liu, L., & Winkelmann, D. A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002137 · Cited by 89 · see citing works

Enhanced ATPase activities as a primary defect of mutant valosin‐containing proteins that cause inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia

Manno, A., Noguchi, M., Fukushi, J., Motohashi, Y., & Kakizuka, A. (2010) · Genes to Cells · doi:10.1111/j.1365-2443.2010.01428.x · Cited by 88 · see citing works

Role of p97 AAA-ATPase in the Retrotranslocation of the Cholera Toxin A1 Chain, a Non-ubiquitinated Substrate

Kothe, M., Ye, Y., Wagner, J. S., Luca, H. E. D., Kern, E., Rapoport, T. A., & Lencer, W. I. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503138200 · Cited by 86 · see citing works

Physical and Functional Interaction between Dorfin and Valosin-containing Protein That Are Colocalized in Ubiquitylated Inclusions in Neurodegenerative Disorders

Ishigaki, S., Hishikawa, N., Niwa, J.-I., Iemura, S.-I., Natsume, T., Hori, S., Kakizuka, A., Tanaka, K., & Sobue, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406683200 · Cited by 76 · see citing works

New ATPase regulators—p97 goes to the PUB

Madsen, L., Seeger, M., Semple, C. A. M., & Hartmann‐Petersen, R. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.05.017 · Cited by 72 · see citing works

Expression Level of Valosin-Containing Protein (p97) Is Associated with Prognosis of Esophageal Carcinoma

Yamamoto, S., Tomita, Y., Hoshida, Y., Iizuka, N., Kidogami, S., Miyata, H., Takiguchi, S., Fujiwara, Y., Yasuda, T., Yano, M., et al. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-0723-03 · Cited by 71 · see citing works

The reversible depolymerization of actin by potassium iodide

Szent‐Györgyi, A. G. (1951) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(51)90188-9 · Cited by 65 · see citing works

Protein quality control gets muscle into shape

Kim, J., Löwe, T., & Hoppe, T. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.03.007 · Cited by 65 · see citing works

2-Anilino-4-aryl-1,3-thiazole inhibitors of valosin-containing protein (VCP or p97)

Bursavich, M. G., Parker, D. P., Willardsen, J. A., Gao, Z., Davis, T., Ostanin, K., Robinson, R., Peterson, A., Cimbora, D. M., Zhu, J.-F., et al. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.01.058 · Cited by 62 · see citing works

Valosin-containing protein and the pathogenesis of frontotemporal dementia associated with inclusion body myopathy

Guinto, J. B., Ritson, G. P., Taylor, J. P., & Forman, M. S. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0224-7 · Cited by 59 · see citing works

An investigation of the cause of death from cancer

Houten, L., & Reilley, A. A. (1980) · Journal of Surgical Oncology · doi:10.1002/jso.2930130205 · Cited by 41 · see citing works

p97 homologs from Caenorhabditis elegans, CDC‐48.1 and CDC‐48.2, suppress the aggregate formation of huntingtin exon1 containing expanded polyQ repeat

Nishikori, S., Yamanaka, K., Sakurai, T., Esaki, M., & Ogura, T. (2008) · Genes to Cells · doi:10.1111/j.1365-2443.2008.01214.x · Cited by 34 · see citing works

Effect of Sera from Fed and Fasted Pigs on Proliferation and Protein Turnover in Cultured Myogenic Cells

White, M. E., Allen, C. E., & Dayton, W. R. (1988) · Journal of Animal Science · doi:10.2527/jas1988.66134x · Cited by 25 · see citing works

Liver Cytochrome P450 3A Endoplasmic Reticulum-associated Degradation

Acharya, P., Liao, M., Engel, J. C., & Correia, M. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.186981 · Cited by 22 · see citing works

Mechanisms regulating skeletal muscle growth and atrophy

Schiaffino, S., Dyar, K. A., Ciciliot, S., Blaauw, B., & Sandri, M. (2013) · The FEBS Journal · doi:10.1111/febs.12253 · Cited by 1,492 · see citing works

Muscle wasting in disease: molecular mechanisms and promising therapies

Cohen, S., Nathan, J. A., & Goldberg, A. L. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4467 · Cited by 1,089 · see citing works

Mechanisms of muscle atrophy and hypertrophy: implications in health and disease

Sartori, R., Romanello, V., & Sandri, M. (2021) · Nature Communications · doi:10.1038/s41467-020-20123-1 · Cited by 940 · see citing works

Protein breakdown in muscle wasting: Role of autophagy-lysosome and ubiquitin-proteasome

Sandri, M. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.04.023 · Cited by 689 · see citing works

Proteotoxic crisis, the ubiquitin-proteasome system, and cancer therapy

Deshaies, R. J. (2014) · BMC Biology · doi:10.1186/s12915-014-0094-0 · Cited by 334 · see citing works

Myostatin/activin pathway antagonism: molecular basis and therapeutic potential

Han, H. Q., Zhou, X., Mitch, W. E., & Goldberg, A. L. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.05.019 · Cited by 314 · see citing works

Mutant Copper-Zinc Superoxide Dismutase (SOD1) Induces Protein Secretion Pathway Alterations and Exosome Release in Astrocytes

Basso, M., Pozzi, S., Tortarolo, M., Fiordaliso, F., Bisighini, C., Pasetto, L., Spaltro, G., Lidonnici, D., Gensano, F., Battaglia, E., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.425066 · Cited by 274 · see citing works

Mechanisms Modulating Skeletal Muscle Phenotype

Blaauw, B., Schiaffino, S., & Reggiani, C. (2013) · Comprehensive physiology · doi:10.1002/cphy.c130009 · Cited by 278 · see citing works

Signaling Pathways That Control Muscle Mass

Vainshtein, A., & Sandri, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134759 · Cited by 214 · see citing works

The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass

Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works

The ubiquitin-proteasome system and autophagy: Coordinated and independent activities

Cohen‐Kaplan, V., Livneh, I., Avni, N., Cohen-Rosenzweig, C., & Ciechanover, A. J. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.07.019 · Cited by 196 · see citing works

Mechanisms of skeletal muscle aging: insights from <i>Drosophila</i> and mammalian models

Demontis, F., Piccirillo, R., Goldberg, A. L., & Perrimon, N. (2013) · Disease Models &amp; Mechanisms · doi:10.1242/dmm.012559 · Cited by 238 · see citing works

Mechanisms of muscle growth and atrophy in mammals and Drosophila

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

New roles for desmin in the maintenance of muscle homeostasis

Agnetti, G., Herrmann, H. O., & Cohen, S. (2021) · FEBS Journal · doi:10.1111/febs.15864 · Cited by 125 · see citing works

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 · see citing works

Trim32 reduces PI3K–Akt–FoxO signaling in muscle atrophy by promoting plakoglobin–PI3K dissociation

Cohen, S., Lee, D., Zhai, B., Gygi, S. P., & Goldberg, A. L. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201304167 · Cited by 103 · see citing works

Proteasome stress in skeletal muscle mounts a long-range protective response that delays retinal and brain aging

Rai, M., Coleman, Z., Curley, M., Nityanandam, A., Platt, A., Robles‐Murguia, M., Jiao, J., Finkelstein, D., Wang, Y., Xu, B., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.03.005 · Cited by 96 · see citing works

VCP-dependent muscle degeneration is linked to defects in a dynamic tubular lysosomal network in vivo

Johnson, A. E., Shu, H., Hauswirth, A. G., Tong, A., & Davis, G. W. (2015) · eLife · doi:10.7554/elife.07366 · Cited by 83 · see citing works

Control of proteasomal proteolysis by mTOR

Zhao, J., Garcia, G. A., & Goldberg, A. L. (2016) · Nature · doi:10.1038/nature16472 · Cited by 79 · see citing works

Inhibitors of the ATPase p97/VCP: From basic research to clinical applications

Kilgas, S., & Ramadan, K. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2022.12.007 · Cited by 78 · see citing works

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 73 · see citing works

VCP maintains lysosomal homeostasis and TFEB activity in differentiated skeletal muscle

Arhzaouy, K., Papadopoulos, C., Schulze, N., Pittman, S., Meyer, H., & Weihl, C. (2019) · Autophagy · doi:10.1080/15548627.2019.1569933 · Cited by 67 · see citing works

Musclin, A Myokine Induced by Aerobic Exercise, Retards Muscle Atrophy During Cancer Cachexia in Mice

Re Cecconi, A. D., Forti, M., Chiappa, M., Zhu, Z., Zingman, L. V., Cervo, L., Beltrame, L., Marchini, S., & Piccirillo, R. (2019) · Cancers · doi:10.3390/cancers11101541 · Cited by 66 · see citing works

Cellular and molecular features of neurogenic skeletal muscle atrophy

Ehmsen, J. T., & Höke, A. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113379 · Cited by 63 · see citing works

Identification 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 62 · see citing works

Myofibril breakdown during atrophy is a delayed response requiring the transcription factor PAX4 and desmin depolymerization

Volodin, A., Kosti, I., Goldberg, A. L., & Cohen, S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1612988114 · Cited by 62 · see citing works

ZFAND5/ZNF216 is an activator of the 26S proteasome that stimulates overall protein degradation

Lee, D., Takayama, S., & Goldberg, A. L. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1809934115 · Cited by 58 · see citing works

Localization of planarian β-CATENIN-1 reveals multiple roles during anterior-posterior regeneration and organogenesis

Sureda-Gómez, M., Martín-Durán, J. M., & Adell, T. (2016) · Development · doi:10.1242/dev.135152 · Cited by 57 · see citing works

Skeletal Muscle-Specific Methyltransferase METTL21C Trimethylates p97 and Regulates Autophagy-Associated Protein Breakdown

Wiederstein, J. L., Nolte, H., Günther, S., Piller, T., Baraldo, M., Kostin, S., Bloch, W., Schindler, N., Sandri, M., Blaauw, B., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.03.136 · Cited by 52 · see citing works

Docosahexaenoic Acid, a Potential Treatment for Sarcopenia, Modulates the Ubiquitin–Proteasome and the Autophagy–Lysosome Systems

Lee, J. H., Jeon, J. H., & Lee, M. J. (2020) · Nutrients · doi:10.3390/nu12092597 · Cited by 56 · see citing works

Selective Autophagy by Close Encounters of the Ubiquitin Kind

Vainshtein, A., & Grumati, P. (2020) · Cells · doi:10.3390/cells9112349 · Cited by 54 · see citing works

TRAF6 Inhibition Rescues Dexamethasone-Induced Muscle Atrophy

Sun, H., Gong, Y., Qiu, J., Chen, Y., Ding, F., & Zhao, Q. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150611126 · Cited by 52 · see citing works

Create and preserve: Proteostasis in development and aging is governed by Cdc48/p97/VCP

Franz, A., Ackermann, L., & Hoppe, T. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.03.031 · Cited by 49 · see citing works

Valosin-containing protein (VCP)–Adaptor Interactions are Exceptionally Dynamic and Subject to Differential Modulation by a VCP Inhibitor

Xue, L., Blythe, E. E., Freiberger, E. C., Mamrosh, J. L., Hebert, A. S., Reitsma, J. M., Hess, S. Y., Coon, J. J., & Deshaies, R. J. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m116.061036 · Cited by 50 · see citing works

Histone Deacetylase 6 Is a FoxO Transcription Factor-dependent Effector in Skeletal Muscle Atrophy

Ratti, F., Ramond, F., Moncollin, V., Simonet, T., Milan, G., Méjat, A., Thomas, J.-L., Streichenberger, N., Gilquin, B., Matthias, P., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.600916 · Cited by 47 · see citing works

Dual roles of mTORC1-dependent activation of the ubiquitin-proteasome system in muscle proteostasis

Kaiser, M. S., Milan, G., Ham, D. J., Lin, S., Oliveri, F., Chojnowska, K., Tintignac, L. A. J., Mittal, N., Zimmerli, C. E., Glass, D. J., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-04097-y · Cited by 46 · see citing works

Role of calpains in promoting desmin filaments depolymerization and muscle atrophy

Cohen, S. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118788 · Cited by 44 · see citing works

Nutraceuticals and Exercise against Muscle Wasting during Cancer Cachexia

Aquila, G., Cecconi, A. D. R., Brault, J., Corli, O., & Piccirillo, R. (2020) · Cells · doi:10.3390/cells9122536 · Cited by 41 · see citing works

Small Molecular Weight Soybean Protein-Derived Peptides Nutriment Attenuates Rat Burn Injury-Induced Muscle Atrophy by Modulation of Ubiquitin-Proteasome System and Autophagy Signaling Pathway

Zhao, F., Yu, Y., Liu, W., Zhang, J., Liu, X., Liu, L., & Yin, H. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b05387 · Cited by 41 · see citing works

A unique IBMPFD-related P97/VCP mutation with differential binding pattern and subcellular localization

Erzurumlu, Y., Köse, F. A., Gözen, O., Gözüaçık, D., Toth, E. A., & Ballar, P. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.01.006 · Cited by 41 · see citing works

A critical discussion on the relationship between E3 ubiquitin ligases, protein degradation, and skeletal muscle wasting: it’s not that simple

Hughes, D. C., Goodman, C. A., Baehr, L. M., Gregorevic, P., & Bodine, S. C. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00457.2023 · Cited by 42 · see citing works

Mechanisms Modulating Skeletal Muscle Phenotype

Blaauw, B., Schiaffino, S., & Reggiani, C. (2013) · Comprehensive physiology · doi:10.1002/j.2040-4603.2013.tb00534.x · Cited by 38 · see citing works

Activation of the SDF1/CXCR4 pathway retards muscle atrophy during cancer cachexia

Martinelli, G. B., Olivari, D., Cecconi, A. D. R., Talamini, L., Ottoboni, L., Lecker, S. H., Stretch, C., Baracos, V. E., Bathe, O. F., Resovi, A., et al. (2016) · Oncogene · doi:10.1038/onc.2016.153 · Cited by 38 · see citing works

Effect of denervation on the regulation of mitochondrial transcription factor A expression in skeletal muscle

Tryon, L. D., Crilly, M. J., & Hood, D. A. (2015) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00266.2014 · Cited by 32 · see citing works

Inadequate fine-tuning of protein synthesis and failure of amino acid homeostasis following inhibition of the ATPase VCP/p97

Parzych, K., Chinn, T. M., Chen, Z., Loaiza, S., Porsch, F., Valbuena, G. N., Kleijnen, M. F., Karadimitris, A., Gentleman, E., Keun, H. C., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.373 · Cited by 31 · see citing works

UBE2L3, a Partner of MuRF1/TRIM63, Is Involved in the Degradation of Myofibrillar Actin and Myosin

Peris-Moreno, D., Malige, M., Claustre, A., Armani, A., Coudy‐Gandilhon, C., Deval, C., Béchet, D., Fafournoux, P., Sandri, M., Combaret, L., et al. (2021) · Cells · doi:10.3390/cells10081974 · Cited by 27 · see citing works

UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins

Hellerschmied, D., Roessler, M., Lehner, A., Gazda, L., Stejskal, K., Imre, R., Mechtler, K., Dammermann, A., & Clausen, T. (2018) · Nature Communications · doi:10.1038/s41467-018-02924-7 · Cited by 25 · see citing works

Bidirectional substrate shuttling between the 26S proteasome and the Cdc48 ATPase promotes protein degradation

Li, H., Ji, Z., Paulo, J. A., Gygi, S. P., & Rapoport, T. A. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.01.029 · Cited by 23 · see citing works

Group I Paks support muscle regeneration and counteract cancer‐associated muscle atrophy

Perpetuini, A. C., Cecconi, A. D. R., Chiappa, M., Martinelli, G. B., Fuoco, C., Desiderio, G., Castagnoli, L., Gargioli, C., Piccirillo, R., & Cesareni, G. (2018) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12303 · Cited by 23 · see citing works

MicroRNA deep sequencing in two adult stem cell populations identifies miR-501 as a novel regulator of myosin heavy chain during muscle regeneration

Mizbani, A., Luca, E., Rushing, E. J., & Krützfeldt, J. (2016) · Development · doi:10.1242/dev.136051 · Cited by 22 · see citing works

Micro-computed tomography for non-invasive evaluation of muscle atrophy in mouse models of disease

Pasetto, L., Olivari, D., Nardo, G., Trolese, M. C., Bendotti, C., Piccirillo, R., & Bonetto, V. (2018) · PLoS ONE · doi:10.1371/journal.pone.0198089 · Cited by 20 · see citing works

The 2022 On-site Padua Days on Muscle and Mobility Medicine hosts the University of Florida Institute of Myology and the Wellstone Center, March 30 - April 3, 2022 at the University of Padua and Thermae of Euganean Hills, Padua, Italy: The collection of abstracts

Sweeney, H. L., Masiero, S., & Carraro, U. (2022) · European Journal of Translational Myology · doi:10.4081/ejtm.2022.10440 · Cited by 19 · see citing works

Breakdown of Filamentous Myofibrils by the UPS–Step by Step

Aweida, D., & Cohen, S. (2021) · Biomolecules · doi:10.3390/biom11010110 · Cited by 19 · see citing works

Early postmortem muscle proteome and metabolome of beef longissimus thoracis muscle classified by pH at 6 hours postmortem

Schulte, M. D., Hochmuth, K. G., Steadham, E. M., Lonergan, S. M., Hansen, S. L., & Huff-Lonergan, E. J. (2022) · Journal of Proteomics · doi:10.1016/j.jprot.2022.104756 · Cited by 17 · see citing works

Cardiac-Restricted Expression of VCP/TER94 RNAi or Disease Alleles Perturbs Drosophila Heart Structure and Impairs Function

Viswanathan, M., Blice‐Baum, A. C., Sang, T., & Cammarato, A. (2016) · Journal of Cardiovascular Development and Disease · doi:10.3390/jcdd3020019 · Cited by 17 · see citing works

Aberrant signaling and senescence associated protein degradation

Ferbeyre, G. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.06.016 · Cited by 16 · see citing works

The p97‐Nploc4 ATPase complex plays a role in muscle atrophy during cancer and amyotrophic lateral sclerosis

Cecconi, A. D. R., Barone, M., Gaspari, S., Tortarolo, M., Bendotti, C., Porcu, L., Terribile, G., & Piccirillo, R. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13011 · Cited by 14 · see citing works

The AAA‐ATPase ATAD1 and its partners promote degradation of desmin intermediate filaments in muscle

Aweida, D., & Cohen, S. (2022) · EMBO Reports · doi:10.15252/embr.202255175 · Cited by 12 · see citing works

USP3 : Key deubiquitylation enzyme in human diseases

Zhang, H., Liu, W., Wu, Y., & Chen, C. (2024) · Cancer Science · doi:10.1111/cas.16178 · Cited by 15 · see citing works

Chaperoning myosin assembly in muscle formation and aging

Pokrzywa, W., & Hoppe, T. (2013) · Worm · doi:10.4161/worm.25644 · Cited by 15 · see citing works

Down‐regulation of the mitochondrial i‐AAA protease Yme1L induces muscle atrophy via FoxO3a and myostatin activation

Lee, Y. J., Kim, G. H., Park, S. I., & Lim, J. H. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14799 · Cited by 15 · see citing works

Phosphorylation Modifications Regulating Cardiac Protein Quality Control Mechanisms

Mishra, S., Dunkerly-Eyring, B. L., Keceli, G., & Ranek, M. J. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.593585 · Cited by 14 · see citing works

VCP/p97 controls signals of the ERK1/2 pathway transmitted via the Shoc2 scaffolding complex: novel insights into IBMPFD pathology

Jang, H., Jang, E. R., Wilson, P. G., Anderson, D., & Galperin, E. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-03-0144 · Cited by 11 · see citing works

Betaine attenuates age-related suppression in autophagy via Mettl21c/p97/VCP axis to delay muscle loss

Chen, S., Chen, J., Wang, C., He, T., Yang, Z., Huang, W., Luo, X., & Zhu, H. (2023) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2023.109555 · Cited by 12 · see citing works

Losing pieces without disintegrating: Contractile protein loss during muscle atrophy

Schiaffino, S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1700190114 · Cited by 12 · see citing works

Proteasome gene expression is controlled by coordinated functions of multiple transcription factors

Gilda, J. E., Nahar, A., Kasiviswanathan, D., Tropp, N., Gilinski, T., Lahav, T., Alexandrovich, D., Mandel-Gutfreund, Y., Park, S., & Shemer, S. (2024) · Journal of Cell Biology · doi:10.1083/jcb.202402046 · Cited by 6 · see citing works

Blocking Cancer Growth with Less POMP or Proteasomes

Goldberg, A. L., Zhao, J., & Collins, G. A. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.005 · Cited by 8 · see citing works

Valosin-containing protein VCP/p97 is essential for the intracellular development of Leishmania and its survival under heat stress

Aguiar, B. G. A., Padmanabhan, P. K., Dumas, C., & Papadopoulou, B. (2018) · Cellular Microbiology · doi:10.1111/cmi.12867 · Cited by 8 · see citing works

Post-meeting report of the 2022 On-site Padua Days on Muscle and Mobility Medicine, March 30 - April 3, 2022, Padua, Italy

Carraro, U., Bittmann, F. N., Ivanova, E. P., Jónsson, H., Kern, H., Leeuwenburgh, C., Mayr, W., Scalabrin, M., Schaefer, L. V., Smeriglio, P., et al. (2022) · European Journal of Translational Myology · doi:10.4081/ejtm.2022.10521 · Cited by 7 · see citing works

Deletion of muscle Igf1 exacerbates disuse atrophy weakness in mice

Spradlin, R. A., Vassilakos, G., Matheny, M. K., Jones, N. C., Goldman, J., Lei, H., & Barton, E. R. (2021) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00090.2021 · Cited by 7 · see citing works

Mitochondrial Maintenance in Skeletal MusclePreprint

de Smalen, L. M., & Handschin, C. (2024) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041514 · Cited by 7 · see citing works

Functional phosphatome requirement for protein homeostasis, networked mitochondria, and sarcomere structure in C. elegans muscle

Lehmann, S., Bass, J. J., Barratt, T. F., Ali, M., & Szewczyk, N. J. (2017) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12196 · Cited by 5 · see citing works

Perturbation of multiprotein complexes in skeletal muscle induces protective proteases in the CNS that degrade pathogenic proteins

Rai, M., Baddeley, H. J. E., Chuang, C.-L., Platt, A., Curley, M., Finkelstein, D., & Demontis, F. (2025) · npj Aging · doi:10.1038/s41514-025-00288-z · Cited by 5 · see citing works

The protein segregase VCP/p97 promotes host antifungal defense via regulation of SYK activation

Shao, Z., Wang, L., Cao, L., Chen, T., Jia, X., Sun, W., Gao, C., & Xiao, H. Q. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012674 · Cited by 4 · see citing works

Sunitinib-mediated inhibition of STAT3 in skeletal muscle and spinal cord does not affect the disease in a mouse model of ALS

Tortarolo, M., Cecconi, A. D. R., Camporeale, L., Margotta, C., Nardo, G., Pasetto, L., Bonetto, V., Galbiati, M., Crippa, V., Poletti, A., et al. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106576 · Cited by 4 · see citing works

Integration of proteomic and genetic approaches to assess developmental muscle atrophy

Brooks, D. S., Vishal, K., Bawa, S., Alder, A., & Geisbrecht, E. R. (2021) · Journal of Experimental Biology · doi:10.1242/jeb.242698 · Cited by 3 · see citing works

The RU486-dependent activation of the GeneSwitch system in adult muscles leads to severe adverse effects in Drosophila

Zappia, M. P., Damschroder, D., Westacott, A., Wessells, R. J., & Frolov, M. V. (2024) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkae039 · Cited by 2 · see citing works

Important Factors in the Formation and Clearance of Protein Aggregation

(2013) · Journal of Developing Drugs · doi:10.4172/2329-6631.1000e136 · Cited by 2 · see citing works

Signaling Pathways That Promote Muscle Catabolism in Cachexia

Gilda, J. E., & Cohen, S. (2022) · Springer eBooks · doi:10.1007/978-3-031-09518-4_5 · Cited by 2 · see citing works

Dysregulation of the ubiquitin–proteasome system in aging skeletal muscle

Song, G., Lee, B.-Y., & Baek, K. (2026) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2026.119504 · Cited by 1 · see citing works

Analysis of proteasome stress in different cell types defines a conserved transcriptional response signature and its modulation with aging

Rai, M., Wang, Y., Stephan, A., Nityanandam, A., & Demontis, F. (2026) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkag245 · Cited by 1 · see citing works

Metabolic and proteomic pathways in muscle involved in beef tenderness development

Schulte, M. D. (2022) · doi:10.31274/td-20240329-502 · Cited by 1 · see citing works

Lysine methylation signaling in skeletal muscle biology: from myogenesis to clinical insights

Cordeiro-Spinetti, E., & Rothbart, S. B. (2023) · Biochemical Journal · doi:10.1042/bcj20230223

Characterization of the Cytosolic Translocation of the CYP3A2 Protein with Ubiquitination in Male and Female Rats

Honda, M., Fujimori, H., & Aiba, T. (2026) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b25-00571

Biological Accessibility and Analytical Recovery in Myofibrillar Protein Loss During Skeletal Muscle Atrophy

Ngo, T. H. P., & Lee, W. (2026) · Biomolecules · doi:10.3390/biom16101398

p97’s roles in muscle atrophy, mitochondrial membrane protein turnover, and the effects of p97 inhibition

McDonald, D. (2012) · Microreviews in Cell and Molecular Biology

The p97‐Nploc4 ATPase complex plays a role in muscle atrophy during cancer and amyotrophic lateral sclerosis

Cecconi, A. D. R., Barone, M., Gaspari, S., Tortarolo, M., Bendotti, C., Porcu, L., Terribile, G., & Piccirillo, R. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13011 · Cited by 14 · see citing works

Myofibril breakdown during atrophy is a delayed response requiring the transcription factor PAX4 and desmin depolymerization

Volodin, A., Kosti, I., Goldberg, A. L., & Cohen, S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1612988114 · Cited by 62 · see citing works

Ret finger protein mediates Pax7-induced ubiquitination of MyoD in skeletal muscle atrophy

Joung, H., Eom, G. H., Choe, N., Lee, H. M., Ko, J., Kwon, D., Nam, Y. S., Min, H.-K., Shin, S., Kook, J., et al. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.07.006 · Cited by 17 · see citing works

Importance of the ATP-Ubiquitin-Proteasome Pathway in the Degradation of Soluble and Myofibrillar Proteins in Rabbit Muscle Extracts

Solomon, V., & Goldberg, A. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.43.26690 · Cited by 432 · see citing works