The DOI matches its Crossref record; 83 of the 83 references it cites were found in a registry or an index.
Metastatic cancers promote cachexia through ZIP14 upregulation in skeletal muscle
Open accessAbstract
Patients with metastatic cancer experience a severe loss of skeletal muscle mass and function known as cachexia. Cachexia is associated with poor prognosis and accelerated death in patients with cancer, yet its underlying mechanisms remain poorly understood. Here, we identify the metal-ion transporter ZRT- and IRT-like protein 14 (ZIP14) as a critical mediator of cancer-induced cachexia. ZIP14 is upregulated in cachectic muscles of mice and in patients with metastatic cancer and can be induced by TNF-α and TGF-β cytokines. Strikingly, germline ablation or muscle-specific depletion of Zip14 markedly reduces muscle atrophy in metastatic cancer models. We find that ZIP14-mediated zinc uptake in muscle progenitor cells represses the expression of MyoD and Mef2c and blocks muscle-cell differentiation. Importantly, ZIP14-mediated zinc accumulation in differentiated muscle cells induces myosin heavy chain loss. These results highlight a previously unrecognized role for altered zinc homeostasis in metastatic cancer-induced muscle wasting and implicate ZIP14 as a therapeutic target for its treatment.
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?
In the citing paper
“Conversely, the increase of the metal-ion transporter ZRT- and IRT-like protein 14 (ZIP14), which controls the uptake of Zn ions, has been shown to promote muscle loss. ZIP14 is upregulated by TNF-α and TGF-β cytokines and ZIP14-dependent zinc accumulation induces myosin heavy chain loss, while muscle-specific deletion of ZIP14 prevents muscle loss in tumor-bearing mice30.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [30]
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
Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method
Livak, K. J., & Schmittgen, T. D. (2001) · Methods · doi:10.1006/meth.2001.1262 · Cited by 180,860
Subramanian, A., Tamayo, P., Mootha, V. K., Mukherjee, S., Ebert, B. L., Gillette, M. A., Paulovich, A., Pomeroy, S. L., Golub, T. R., Lander, E. S., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506580102 · Cited by 53,625
The Molecular Signatures Database Hallmark Gene Set Collection
Liberzon, A., Birger, C., Thorvaldsdóttir, H., Ghandi, M., Mesirov, J. P., & Tamayo, P. (2015) · Cell Systems · doi:10.1016/j.cels.2015.12.004 · Cited by 13,807
Mutation of the mouse klotho gene leads to a syndrome resembling ageing
Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837
Emerging Biological Principles of Metastasis
Lambert, A. W., Pattabiraman, D. R., & Weinberg, R. A. (2017) · Cell · doi:10.1016/j.cell.2016.11.037 · Cited by 3,191
Prognostic effect of weight loss prior tochemotherapy in cancer patients
DeWys, W. D., Begg, C. B., Lavin, P. T., Band, P. R., Bennett, J. M., Bertino, J. R., Cohen, M. H., Douglass, H. O., Engstrom, P. F., Ezdinli, E. Z., et al. (1980) · The American Journal of Medicine · doi:10.1016/s0149-2918(05)80001-3 · Cited by 2,350
Metastatic colonization by circulating tumour cells
Massagué, J., & Obenauf, A. C. (2016) · Nature · doi:10.1038/nature17038 · Cited by 2,062
Extracellular Vesicles in Cancer: Cell-to-Cell Mediators of Metastasis
Becker, A., Thakur, B. K., Weiss, J. M., Kim, H. S., Peinado, H., & Lyden, D. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.10.009 · Cited by 2,003
Baracos, V. E., Martin, L., Korc, M., Guttridge, D. C., & Fearon, K. C. H. (2018) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2017.105 · Cited by 1,738
Cancer cachexia: understanding the molecular basis
Argilés, J. M. A., Busquets, S., Stemmler, B., & López-Soriano, F. J. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3829 · Cited by 1,567
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 · cited 1×
“Interestingly, Mt1 and Mt2 are upregulated in muscle atrophic conditions, and their loss promotes muscle hypertrophy 48,50 .”
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
IKKβ/NF-κB Activation Causes Severe Muscle Wasting in Mice
Cai, D., Frantz, J. D., Tawa, N. E., Melendez, P. A., Oh, B.-C., Lidov, H. G. W., Hasselgren, P.-O., Frontera, W. R., Lee, J., Glass, D. J., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.027 · Cited by 1,367
Cancer Cachexia: Mediators, Signaling, and Metabolic Pathways
Fearon, K. C. H., Glass, D. J., & Guttridge, D. C. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.06.011 · Cited by 1,244
Transition Metal Speciation in the Cell: Insights from the Chemistry of Metal Ion Receptors
Finney, L. A., & O'Halloran, T. V. (2003) · Science · doi:10.1126/science.1085049 · Cited by 1,100
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
A CXCL1 Paracrine Network Links Cancer Chemoresistance and Metastasis
Acharyya, S., Oskarsson, T., Vanharanta, S., Malladi, S., Kim, J., Morris, P. G., Manova-Todorova, K., Leversha, M., Hogg, N., Seshan, V. E., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.042 · Cited by 1,085
Self-citationThe tumour-induced systemic environment as a critical regulator of cancer progression and metastasis
McAllister, S. S., & Weinberg, R. A. (2014) · Nature Cell Biology · doi:10.1038/ncb3015 · Cited by 975
Understanding the mechanisms and treatment options in cancer cachexia
Fearon, K. C. H., Arends, J., & Baracos, V. E. (2012) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2012.209 · Cited by 952
NF-κB-Induced Loss of MyoD Messenger RNA: Possible Role in Muscle Decay and Cachexia
D, D. C. G., Mayo, M. W., Madrid, L. V., Wang, C., & Baldwin, A. S. (2000) · Science · doi:10.1126/science.289.5488.2363 · Cited by 922
TNF-α in promotion and progression of cancer
Balkwill, F. R. (2006) · Cancer and Metastasis Reviews · doi:10.1007/s10555-006-9005-3 · Cited by 919
Conditional mouse lung cancer models using adenoviral or lentiviral delivery of Cre recombinase
DuPage, M. J. P., Dooley, A. L., & Jacks, T. (2009) · Nature Protocols · doi:10.1038/nprot.2009.95 · Cited by 873
Mammalian Zinc Transporters: Nutritional and Physiologic Regulation
Lichten, L. A., & Cousins, R. J. (2009) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-033009-083312 · Cited by 749
The molecular regulation of myogenesis
Sabourin, L. A., & Rudnicki, M. A. (2000) · Clinical Genetics · doi:10.1034/j.1399-0004.2000.570103.x · Cited by 720
The E3 Ligase MuRF1 Degrades Myosin Heavy Chain Protein in Dexamethasone-Treated Skeletal Muscle
Clarke, B. A., Drujan, D., Willis, M. S., Murphy, L. O., Corpina, R. A., Burova, E., Rakhilin, S. V., Stitt, T. N., Patterson, C., Latres, E., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.09.009 · Cited by 683
WNT/TCF Signaling through LEF1 and HOXB9 Mediates Lung Adenocarcinoma Metastasis
Nguyen, D. X., Chiang, A. C., Zhang, X. H.-F., Kim, J. Y., Kris, M. G., Ladanyi, M., Gerald, W. L., & Massagué, J. (2009) · Journal of End-to-End-testing · doi:10.1016/j.cell.2009.04.030 · Cited by 627
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 610
Liuzzi, J. P., Lichten, L. A., Rivera, S., Blanchard, R. K., Aydemir, T. B., Knutson, M. D., Ganz, T., & Cousins, R. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502257102 · Cited by 594
Self-citationZinc is a novel intracellular second messenger
Yamasaki, S., Sakata-Sogawa, K., Hasegawa, A., Suzuki, T., Kabu, K., Sato, E., Kurosaki, T., Yamashita, S., Tokunaga, M., Nishida, K., et al. (2007) · Journal of Cell Biology · doi:10.1083/jcb.200702081 · Cited by 592
Cancer cachexia is regulated by selective targeting of skeletal muscle gene products
Acharyya, S., Ladner, K. J., Nelsen, L., Damrauer, J. S., Reiser, P. J., Swoap, S. J., & D, D. C. G. (2004) · Journal of Clinical Investigation · doi:10.1172/jci20174 · Cited by 541
Self-citationBreast cancer bone metastasis mediated by the Smad tumor suppressor pathway
Kang, Y., He, W., Tulley, S., Gupta, G. P., Serganova, I. S., Chen, C.-R., Manova-Todorova, K. O., Blasberg, R. G., Gerald, W. L., & Massagué, J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506517102 · Cited by 537
Intrinsic and extrinsic mechanisms regulating satellite cell function
Dumont, N. A., Wang, Y. X., & Rudnicki, M. A. (2015) · Development · doi:10.1242/dev.114223 · Cited by 491
Inhibition of Myogenic Differentiation in Proliferating Myoblasts by Cyclin D1-Dependent Kinase
Skapek, S. X., Rhee, J., Spicer, D. B., & Lassar, A. B. (1995) · Science · doi:10.1126/science.7863328 · Cited by 476
Cancer cachexia: Developing multimodal therapy for a multidimensional problem
Fearon, K. C. H. (2008) · European Journal of Cancer · doi:10.1016/j.ejca.2008.02.033 · Cited by 444
Inhibition of myogenic differentiation in proliferating myoblasts by cyclin D1-dependent kinase
(1995) · Trends in Genetics · doi:10.1016/0168-9525(95)90555-3 · Cited by 407
Gee, K. R., Zhou, Z., Qian, W., & Kennedy, R. T. (2002) · Journal of the American Chemical Society · doi:10.1021/ja011774y · Cited by 406
Loss of Lkb1 and Pten Leads to Lung Squamous Cell Carcinoma with Elevated PD-L1 Expression
Xu, C., Brainson, C. F., Koyama, S., Wu, H., Zhao, Y., Chen, Z., Herter-Sprie, G. S., Akbay, E. A., Tchaicha, J. H., Altabef, A. B., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.03.033 · Cited by 398
Excess TGF-β mediates muscle weakness associated with bone metastases in mice
Waning, D. L., Mohammad, K. S., Reiken, S. R., Xie, W., Andersson, D. C., John, S. K., Chiechi, A., Wright, L. E., Umanskaya, A., Niewolna, M., et al. (2015) · Nature Medicine · doi:10.1038/nm.3961 · Cited by 386
Mouse models of advanced spontaneous metastasis for experimental therapeutics
Francia, G., Cruz‐Muñoz, W., Man, S., Xu, P., & Kerbel, R. S. (2011) · Nature reviews. Cancer · doi:10.1038/nrc3001 · Cited by 380
Metalloproteomes: A Bioinformatic Approach
Andreini, C., Bertini, I., & Rosato, A. (2009) · Accounts of Chemical Research · doi:10.1021/ar900015x · Cited by 373
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
Jahchan, N. S., Dudley, J. T., Mazur, P. K., Flores, N. M., Yang, D., Palmerton, A., Zmoos, A., Vaka, D., Tran, K. Q. T., Zhou, M. J., et al. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0183 · Cited by 358
NF-κB–mediated Pax7 dysregulation in the muscle microenvironment promotes cancer cachexia
He, W. A., Berardi, E., Cardillo, V. M., Acharyya, S., Aulino, P., Thomas-Ahner, J., Wang, J., Bloomston, M., Muscarella, P., Nau, P., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci68523 · Cited by 357
Self-citationBonetto, A., Aydogdu, T., Kunzevitzky, N., Guttridge, D. C., Khuri, S., Koniaris, L. G., & Zimmers, T. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022538 · Cited by 348
Mechanisms of Muscle Degeneration, Regeneration, and Repair in the Muscular Dystrophies
Wallace, G. Q., & McNally, E. M. (2008) · Annual Review of Physiology · doi:10.1146/annurev.physiol.010908.163216 · Cited by 343
The Prognosis of Acute Respiratory Failure in Critically Ill Cancer Patients
Azoulay, É., Thiéry, G., Chevret, S., Moreau, D., Darmon, M., Bergeron, A., Yang, K., Meignin, V., Ciroldi, M., Gall, J. L., et al. (2004) · Medicine · doi:10.1097/01.md.0000145370.63676.fb · Cited by 327
Acharyya, S., Butchbach, M. E. R., Sahenk, Z., Wang, H., Saji, M., Carathers, M., Ringel, M. D., Skipworth, R. J. E., Fearon, K. C. H., Hollingsworth, M. A., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.10.004 · Cited by 323
Self-citationTissue‐specific regulation of zinc metabolism and metallothionein genes by interleukin 1
Cousins, R. J., & Leinart, A. S. (1988) · The FASEB Journal · doi:10.1096/fasebj.2.13.2458983 · Cited by 312
Health Evaluation of Experimental Laboratory Mice
Burkholder, T. H., Foltz, C. J., Karlsson, E. M., Linton, C. G., & Smith, J. M. (2012) · Current Protocols in Mouse Biology · doi:10.1002/9780470942390.mo110217 · Cited by 307
Physiologic implications of metal-ion transport by ZIP14 and ZIP8
Jenkitkasemwong, S., Wang, C., Mackenzie, B., & Knutson, M. D. (2012) · BioMetals · doi:10.1007/s10534-012-9526-x · Cited by 251
Self-citationJenkitkasemwong, S., Wang, C.-Y., Coffey, R., Zhang, W., Chan, A., Biel, T., Kim, J.-S., Hojyo, S., Fukada, T., & Knutson, M. D. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.002 · Cited by 245
Self-citationRequirement of MEF2A, C, and D for skeletal muscle regeneration
Liu, N., Nelson, B. R., Bezprozvannaya, S., Shelton, J. M., Richardson, J. A., Bassel‐Duby, R., & Olson, E. N. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401732111 · Cited by 227
Cancer Causes Cardiac Atrophy and Autophagy in a Sexually Dimorphic Manner
Cosper, P. F., & Leinwand, L. A. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-3145 · Cited by 215
Dalal, B. I., Keown, P. A., & Greenberg, A. H. (1993) · PubMed Central · Cited by 208
Muscle Wasting and Impaired Myogenesis in Tumor Bearing Mice Are Prevented by ERK Inhibition
Penna, F., Costamagna, D., Fanzani, A., Bonelli, G., Baccino, F. M., & Costelli, P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013604 · Cited by 191
Hojyo, S., Fukada, T., Shimoda, S., Ohashi, W., Bin, B.-H., Koseki, H., & Hirano, T. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018059 · Cited by 176
Self-citationThe Biology of Bone MetastasisPreprint
Esposito, M., Guise, T. A., & Kang, Y. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a031252 · Cited by 174
Polge, C., Heng, A.-É., Jarzaguet, M., Ventadour, S., Claustre, A., Combaret, L., Béchet, D., Matondo, M., Uttenweiler‐Joseph, S., Monsarrat, B., et al. (2011) · The FASEB Journal · doi:10.1096/fj.11-180968 · Cited by 157
Kwon, M.-C., & Berns, A. J. M. (2013) · Molecular Oncology · doi:10.1016/j.molonc.2013.02.010 · Cited by 150
The Multiple Faces of the Metal Transporter ZIP14 (SLC39A14)
Aydemir, T. B., & Cousins, R. J. (2018) · Journal of Nutrition · doi:10.1093/jn/nxx041 · Cited by 148
Protein breakdown in cancer cachexia
Sandri, M. (2016) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2015.11.002 · Cited by 134
Talmadge, J. E., & Fidler, I. J. (1982) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/69.4.975 · Cited by 134
Serum and tissue trace elements in colorectal cancer
Gupta, S., Shukla, V. K., Vaidya, M. P., Roy, S. K., & Gupta, S. (1993) · Journal of Surgical Oncology · doi:10.1002/jso.2930520311 · Cited by 129
Isolation, Culture, and Transplantation of Muscle Satellite Cells
Motohashi, N., Asakura, Y., & Asakura, A. (2014) · Journal of Visualized Experiments · doi:10.3791/50846 · Cited by 115
Regulation of MyoD function in the dividing myoblast
Wei, Q., & Paterson, B. M. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02120-2 · Cited by 113
Ohly, P., Dohle, C., Abel, J., Seißler, J., & Gleichmann, H. (2000) · Diabetologia · doi:10.1007/s001250050009 · Cited by 111
Diaphragm and ventilatory dysfunction during cancer cachexia
Roberts, B. M., Ahn, B., Smuder, A. J., Al‐Rajhi, M., Gill, L., Beharry, A. W., Powers, S. K., Fuller, D. D., Ferreira, L. F., & Judge, A. R. (2013) · The FASEB Journal · doi:10.1096/fj.12-222844 · Cited by 111
Global secretome analysis identifies novel mediators of bone metastasis
Blanco, M. A., LeRoy, G., Khan, Z., Alečković, M., Zee, B. M., Garcia, B. A., & Kang, Y. (2012) · Cell Research · doi:10.1038/cr.2012.89 · Cited by 93
Schmitt, T. L., Martignoni, M. E., Bachmann, J., Fechtner, K., Friess, H., Kinscherf, R., & Hildebrandt, W. (2007) · Journal of Molecular Medicine · doi:10.1007/s00109-007-0177-2 · Cited by 85
Experimental cancer cachexia: Evolving strategies for getting closer to the human scenario
Penna, F., Busquets, S., & Argilés, J. M. A. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.09.002 · Cited by 72
Impaired regeneration: A role for the muscle microenvironment in cancer cachexia
Talbert, E. E., & Guttridge, D. C. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.09.009 · Cited by 71
Blockade of Metallothioneins 1 and 2 Increases Skeletal Muscle Mass and Strength
Summermatter, S., Bouzan, A., Pierrel, E., Melly, S., Stauffer, D., Gutzwiller, S., Nolin, E., Dornelas, C., Fryer, C., Leighton-Davies, J., et al. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00305-16 · Cited by 66
Iguchi, H., Onuma, E., Sato, K., Sato, K., & Ogata, E. (2001) · International Journal of Cancer · doi:10.1002/ijc.1425 · Cited by 64
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
Eley, H. L., Skipworth, R. J. E., Deans, D. A. C., Fearon, K. C. H., & Tisdale, M. J. (2007) · British Journal of Cancer · doi:10.1038/sj.bjc.6604150 · Cited by 50
Myosin heavy chain is not selectively decreased in murine cancer cachexia
Cosper, P. F., & Leinwand, L. A. (2011) · International Journal of Cancer · doi:10.1002/ijc.26298 · Cited by 43
Cardiac and skeletal muscles show molecularly distinct responses to cancer cachexia
Shum, A. M. Y., Fung, D. C. Y., Corley, S., McGill, M. C., Bentley, N. L., Tan, T. C., Wilkins, M. R., & Polly, P. (2015) · Physiological Genomics · doi:10.1152/physiolgenomics.00128.2014 · Cited by 38
Excessive intracellular zinc accumulation in cardiac and skeletal muscles of dystrophic hamsters
Crawford, A. J., & Bhattacharya, S. K. (1987) · Experimental Neurology · doi:10.1016/0014-4886(87)90137-3 · Cited by 37
Systemic zinc redistribution and dyshomeostasis in cancer cachexia
Siren, P. M. A., & Siren, M. J. (2010) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1007/s13539-010-0009-z · Cited by 32
Buclez, P.-O., Leite, G. D. F., Relizani, K., Beley, C., García, L., & Benchaouir, R. (2016) · Molecular Therapy — Methods & Clinical Development · doi:10.1038/mtm.2016.35 · Cited by 26
Isolation, Culture, Functional Assays, and Immunofluorescence of Myofiber-Associated Satellite Cells
Vogler, T. O., Gadek, K. E., Cadwallader, A. B., Elston, T. L., & Olwin, B. B. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3810-0_11 · Cited by 18
The role of zinc in the anti-tumour and anti-cachectic activity of D-myo-inositol 1,2,6-triphosphate
Russell, S. T., Siren, P. M. A., Siren, M. J., & Tisdale, M. J. (2010) · British Journal of Cancer · doi:10.1038/sj.bjc.6605562 · Cited by 13
Larsson, S., Karlberg, I. H., Selin, E., Daneryd, P., & Peterson, H.-I. (1987) · PubMed · Cited by 7
Cited by
Sorted by citations
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
Chen, B., Yu, P., Chan, W. N., Xie, F., Zhang, Y., Liang, L., Leung, K. T., Lo, K. W., Yu, J., Tse, G. M. K., et al. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01679-y · Cited by 420
Tumour extracellular vesicles and particles induce liver metabolic dysfunction
Wang, G., Li, J., Bojmar, L., Chen, H., Li, Z., Tobias, G. C., Hu, M., Homan, E. A., Lucotti, S., Zhao, F., et al. (2023) · Nature · doi:10.1038/s41586-023-06114-4 · Cited by 280
Self-citationCachexia: A systemic consequence of progressive, unresolved disease
Ferrer, M., Anthony, T. G., Ayres, J. S., Biffi, G., Brown, J. C., Caan, B. J., Feliciano, E. M. C., Coll, A. P., Dunne, R. F., Goncalves, M. D., et al. (2023) · Cell · doi:10.1016/j.cell.2023.03.028 · Cited by 282
Cancer Cachexia: More Than Skeletal Muscle Wasting
Schmidt, S. F., Rohm, M., Herzig, S., & Díaz, M. B. (2018) · Trends in cancer · doi:10.1016/j.trecan.2018.10.001 · Cited by 229
Metadata
- Authors
- Wang, G., Biswas, A. K., Ma, W., Kandpal, M., Coker, C., Grandgenett, P. M., Hollingsworth, M. A., Jain, R., Tanji, K., Lόpez-Pintado, S., Borczuk, A., Hebert, D., Jenkitkasemwong, S., Hojyo, S., Davuluri, R. V., Knutson, M. D., Fukada, T., & Acharyya, S.
- Affiliations
- Columbia University (US)
- Northwestern University (US)
- Fred and Pamela Buffett Cancer Center (US)
- Icahn School of Medicine at Mount Sinai (US)
- NewYork–Presbyterian Hospital (US)
- Weill Cornell Medicine (US)
- Columbia University Irving Medical Center (US)
- University of Florida (US)
- German Rheumatism Research Centre (DE)
- Tokushima Bunri University (JP)
- Corresponding author
- Acharyya, Swarnali
- ORCID
- Venue
- Nature Medicine
- Published
- 2018-06
- Volume
- 24
- Issue
- 6
- Pages
- 770-781
- ISSN
- 1078-8956 (ISSN-L)
- 1546-170X
- PMC
- PMC6015555
- OpenAlex
- W2805831922
- Cited by
- 188
- References
- 83
- Citations by year
- 2026: 17 · 2025: 29 · 2024: 21 · 2023: 22 · 2022: 30 · 2021: 22 · 2020: 23 · 2019: 19 · 2018: 5
- FWCI
- 6.19
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Nature Medicine (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Japan Society for the Promotion of Science (17H04011)
- National Cancer Institute (P50CA127297, R00CA172697, U01CA210240, P30CA013696, R50CA211462)
- National Institute of Diabetes and Digestive and Kidney Diseases (R56DK080706, R01DK080706)
- U.S. National Library of Medicine (R01LM011297)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology (medical) › Nutrition and Health in Aging
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Keywords
- cancer cachexia, metastatic cancer, ZIP14, zinc homeostasis, skeletal muscle atrophy, muscle atrophy, zinc uptake, muscle progenitor cells, MyoD, MEF2C, myosin heavy chain, TNF-α, TGF-beta, therapeutic target
- MeSH terms
- Animals, Cachexia, Cell Differentiation, Cell Line, Disease Models, Animal, Humans, Mice, Inbred C57BL, Neoplasm Metastasis, Neoplasms, Tumor Necrosis Factor-alpha, Zinc, Up-Regulation, Cytokines, Transforming Growth Factor beta, Muscle, Skeletal, Myosin Heavy Chains, Cation Transport Proteins
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
