The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Calcium's Role in Mechanotransduction during Muscle Development
Open accessAbstract
Mechanotransduction is a process where cells sense their surroundings and convert the physical forces in their environment into an appropriate response. Calcium plays a crucial role in the translation of such forces to biochemical signals that control various biological processes fundamental in muscle development. The mechanical stimulation of muscle cells may for example result from stretch, electric and magnetic stimulation, shear stress, and altered gravity exposure. The response, mainly involving changes in intracellular calcium concentration then leads to a cascade of events by the activation of downstream signaling pathways. The key calcium-dependent pathways described here include the nuclear factor of activated T cells (NFAT) and mitogen-activated protein kinase (MAPK) activation. The subsequent effects in cellular homeostasis consist of cytoskeletal remodeling, cell cycle progression, growth, differentiation, and apoptosis, all necessary for healthy muscle development, repair, and regeneration. A deregulation from the normal process due to disuse, trauma, or disease can result in a clinical condition such as muscle atrophy, which entails a significant loss of muscle mass. In order to develop therapies against such diseased states, we need to better understand the relevance of calcium signaling and the downstream responses to mechanical forces in skeletal muscle. The purpose of this review is to discuss in detail how diverse mechanical stimuli cause changes in calcium homeostasis by affecting membrane channels and the intracellular stores, which in turn regulate multiple pathways that impart these effects and control the fate of muscle tissue.
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.
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
The versatility and universality of calcium signalling
Berridge, M. J., Lipp, P., & Bootman, M. D. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35036035 · Cited by 5,701
Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L. (1991) · Cell · doi:10.1016/0092-8674(91)90124-h · Cited by 4,116
Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member
McPherron, A. C., Lawler, A. M., & Lee, S.-J. (1997) · Nature · doi:10.1038/387083a0 · Cited by 4,013
Role of cell shape in growth control
Folkman, J., & Moscona, A. (1978) · Nature · doi:10.1038/273345a0 · Cited by 2,422
Transcriptional regulation by calcium, calcineurin, and NFAT
Hogan, P. G., Chen, L., Nardone, J., & Rao, A. (2003) · Genes & Development · doi:10.1101/gad.1102703 · Cited by 1,991
Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
Schlaepfer, D. D., Hanks, S. K., Hunter, T., & Geer, P. V. D. (1994) · Nature · doi:10.1038/372786a0 · Cited by 1,595
Weaver, V. M., Petersen, O. W., Wang, F., Larabell, C. A., Briand, P., Damsky, C., & Bissell, M. J. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.137.1.231 · Cited by 1,483
Jaalouk, D. E., & Lammerding, J. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2597 · Cited by 1,396
Atrophy of the soleus muscle by hindlimb unweighting
Thomason, D. B., & Booth, F. W. (1990) · Journal of Applied Physiology · doi:10.1152/jappl.1990.68.1.1 · Cited by 631
Biochemical adaptation of human skeletal muscle to heavy resistance training and immobilization
MacDougall, J. D., Ward, G. R., Sale, D. G., & Sutton, J. R. (1977) · Journal of Applied Physiology · doi:10.1152/jappl.1977.43.4.700 · Cited by 312
Cited by
Items 101–200 of 347
Biswas, G., Adebanjo, O. A., Freedman, B. D., Anandatheerthavarada, H. K., Vijayasarathy, C., Zaidi, M., Kotlikoff, M., & Avadhani, N. G. (1999) · The EMBO Journal · doi:10.1093/emboj/18.3.522 · Cited by 369
LGR4 is a receptor for RANKL and negatively regulates osteoclast differentiation and bone resorption
Luo, J., Yang, Z., Ma, Y., Yue, Z., Lin, H., Qu, G., Huang, J., Dai, W., Li, C., Zheng, C., et al. (2016) · Nature Medicine · doi:10.1038/nm.4076 · Cited by 370
Human Pathophysiological Adaptations to the Space Environment
Demontis, G. C., Germani, M. M., Caiani, E. G., Barravecchia, I., Passino, C., & Angeloni, D. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00547 · Cited by 354
Ehrlich, J. S., Hansen, M. D. H., & Nelson, W. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00216-2 · Cited by 358
Liu, L., Zhang, Y., Chen, N., Shi, X., Tsang, B., & Yu, Y.-H. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30565 · Cited by 356
A Necessity for MAP Kinase Activation in Mammalian Spatial Learning
Selcher, J. C., Atkins, C. M., Trzaskos, J. M., Paylor, R., & Sweatt, J. D. (1999) · Learning & Memory · doi:10.1101/lm.6.5.478 · Cited by 341
Werner, M., Blanquer, S. B. G., Haimi, S. P., Korus, G., Dunlop, J. W. C., Duda, G. N., Grijpma, D. W., & Petersen, A. (2017) · Advanced Science · doi:10.1002/advs.201600347 · Cited by 345
Muscle as a “Mediator” of Systemic Metabolism
Baskin, K. K., Winders, B. R., & Olson, E. N. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2014.12.021 · Cited by 333
Nelson, C. M., & Bissell, M. J. (2005) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2005.05.001 · Cited by 332
Matheos, D. P., Kingsbury, T. J., Ahsan, U. S., & Cunningham, K. W. (1997) · Genes & Development · doi:10.1101/gad.11.24.3445 · Cited by 332
Human skeletal muscle possesses an epigenetic memory of hypertrophy
Seaborne, R. A., Strauss, J., Cocks, M., Shepherd, S., O’Brien, T. D., van Someren, K. A., Bell, P. G., Murgatroyd, C., Morton, J. P., Stewart, C. E., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-20287-3 · Cited by 334
α-Smooth Muscle Actin Is Crucial for Focal Adhesion Maturation in Myofibroblasts
Hinz, B., Dugina, V., Ballestrem, C., Wehrle-Haller, B., & Chaponnier, C. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-11-0729 · Cited by 322
YAP-mediated mechanotransduction tunes the macrophage inflammatory response
Meli, V. S., Atcha, H., Veerasubramanian, P. K., Nagalla, R. R., Luu, T. U., Chen, E. Y., Guerrero-Juarez, C. F., Yamaga, K., Pandori, W., Hsieh, J. Y., et al. (2020) · Science Advances · doi:10.1126/sciadv.abb8471 · Cited by 329
The α v β 1 integrin plays a critical in vivo role in tissue fibrosis
Reed, N. I., Jo, H., Chen, C., Tsujino, K., Arnold, T. D., DeGrado, W. F., & Sheppard, D. (2015) · Science Translational Medicine · doi:10.1126/scitranslmed.aaa5094 · Cited by 311
Alkner, B. A., & Tesch, P. A. (2004) · European Journal of Applied Physiology · doi:10.1007/s00421-004-1172-8 · Cited by 306
Dehkhoda, F., Lee, C. M. M., Medina, J., & Brooks, A. J. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00035 · Cited by 304
Skeletal muscle tissue engineering: methods to form skeletal myotubes and their applications
Ostrovidov, S., Hosseini, V., Ahadian, S., Fujie, T., Parthiban, S. P., Ramalingam, M., Bae, H., Kaji, H., & Khademhosseini, A. (2014) · Tissue Engineering Part B: Reviews · doi:10.1089/ten.teb.2013.0534 · Cited by 302
Extracellular matrix-derived biomaterials in engineering cell function
Xing, H., Lee, H., Luo, L., & Kyriakides, T. R. (2020) · Biotechnology Advances · doi:10.1016/j.biotechadv.2019.107421 · Cited by 302
Beck, I. M. E., Vanden Berghe, W., Vermeulen, L., Yamamoto, K. R., Haegeman, G., & De Bosscher, K. (2009) · Endocrine Reviews · doi:10.1210/er.2009-0013 · Cited by 298
Wu, Z., Huang, X., Feng, Y., Handschin, C., Feng, Y., Gullicksen, P. S., Bare, O., Labow, M., Spiegelman, B., & Stevenson, S. C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606714103 · Cited by 291
HDAC4, a Human Histone Deacetylase Related to Yeast HDA1, Is a Transcriptional Corepressor
Wang, A. H., Bertos, N. R., Vezmar, M., Pelletier, N., Crosato, M., Heng, H. H., Th’ng, J., Han, J., & Yang, X.-J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.11.7816 · Cited by 294
Retinoic acid signaling and neuronal differentiation
Janesick, A., Wu, S. C., & Blumberg, B. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1815-9 · Cited by 295
Interlocking Transcriptional Feedback Loops Control White-Opaque Switching in Candida albicans
Zordan, R. E., Miller, M. G., Galgoczy, D. J., Tuch, B. B., & Johnson, A. D. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050256 · Cited by 292
The Physical and Biochemical Properties of the Extracellular Matrix Regulate Cell Fate
(2018) · Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2018.02.002 · Cited by 286
A Foxo/Notch pathway controls myogenic differentiation and fiber type specification
Kitamura, T., Kitamura, Y. I., Funahashi, Y., Shawber, C. J., Castrillon, D. H., Kollipara, R., DePinho, R. A., Kitajewski, J., & Accili, D. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32054 · Cited by 285
Muller, M. P., Jiang, T., Sun, C., Lihan, M., Pant, S., Mahinthichaichan, P., Trifan, A., & Tajkhorshid, E. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00608 · Cited by 282
Inflammation induced loss of skeletal muscle
Londhe, P., & Guttridge, D. C. (2015) · Bone · doi:10.1016/j.bone.2015.03.015 · Cited by 276
Davis, M. J., Earley, S., Li, Y.-S., & Chien, S. (2023) · Physiological Reviews · doi:10.1152/physrev.00053.2021 · Cited by 273
Scanningless and continuous 3D bioprinting of human tissues with decellularized extracellular matrix
Yu, C., Ma, X., Zhu, W., Wang, P., Miller, K. L., Stupin, J., Koroleva-Maharajh, A., Hairabedian, A., & Chen, S. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2018.12.009 · Cited by 272
Integrin αvβ3 is a coreceptor for human cytomegalovirus
Wang, X., Huang, D. Y., Huong, S.-M., & Huang, E.-S. (2005) · Nature Medicine · doi:10.1038/nm1236 · Cited by 268
Evidence-based Guidelines for Controlling pH in Mammalian Live-Cell Culture Systems
Michl, J., Park, K. C., & Swietach, P. (2019) · Communications Biology · doi:10.1038/s42003-019-0393-7 · Cited by 267
Mutations in CHMP2B in Lower Motor Neuron Predominant Amyotrophic Lateral Sclerosis (ALS)
Cox, L. E., Ferraiuolo, L., Goodall, E. F., Heath, P. R., Higginbottom, A., Mortiboys, H., Hollinger, H. C., Hartley, J. A., Brockington, A., Burness, C. E., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009872 · Cited by 262
Changes in satellite cells in human skeletal muscle after a single bout of high intensity exercise.
Crameri, R. M., Langberg, H., Magnusson, P., Jensen, C. H., Schrøder, H. D., Olesen, J. L., Suetta, C., Teisner, B., & Kjaer, M. (2004) · The Journal of Physiology · doi:10.1113/jphysiol.2004.061846 · Cited by 262
Single-nucleus RNA-seq and FISH identify coordinated transcriptional activity in mammalian myofibers
Dos Santos, M., Backer, S., Saintpierre, B., Izac, B., Andrieu, M., Letourneur, F., Relaix, F., Sotiropoulos, A., & Maire, P. (2020) · Nature Communications · doi:10.1038/s41467-020-18789-8 · Cited by 259
The shear stress of it all: the cell membrane and mechanochemical transduction
White, C. R., & Frangos, J. A. (2007) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2007.2128 · Cited by 255
Understanding phosphoinositides: rare, dynamic, and essential membrane phospholipids
Dickson, E. J., & Hille, B. (2019) · Biochemical Journal · doi:10.1042/bcj20180022 · Cited by 254
Merry, T. L., & Ristow, M. (2016) · The Journal of Physiology · doi:10.1113/jp271957 · Cited by 246
Van De Water, L., Varney, S., & Tomasek, J. J. (2013) · Advances in Wound Care · doi:10.1089/wound.2012.0393 · Cited by 251
Talin as a mechanosensitive signaling hub
Goult, B. T., Yan, J., & Schwartz, M. A. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201808061 · Cited by 250
Biophysics of tumor microenvironment and cancer metastasis – a mini review
Emon, B., Bauer, J., Jain, Y., Jung, B., & Saif, T. (2018) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2018.07.003 · Cited by 245
Skeletal Muscle Wasting and Renewal: A Pivotal Role of Myokine IL-6
Belizário, J. E., Fontes-Oliveira, C. C., Borges, J. P., Kashiabara, J. A., & Vannier, E. (2016) · SpringerPlus · doi:10.1186/s40064-016-2197-2 · Cited by 244
CRISPR-mediated Genome Editing Restores Dystrophin Expression and Function in mdx Mice
Xu, L., Park, K. H., Zhao, L., Xu, J., El Refaey, M., Gao, Y., Zhu, H., Ma, J., & Han, R. (2016) · Molecular Therapy · doi:10.1038/mt.2015.192 · Cited by 244
Ishijima, M., Rittling, S. R., Yamashita, T., Tsuji, K., Kurosawa, H., Nifuji, A., Denhardt, D. T., & Noda, M. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.3.399 · Cited by 240
How microglia sense and regulate neuronal activity
Umpierre, A. D., & Wu, L. (2021) · Glia · doi:10.1002/glia.23961 · Cited by 237
Skeletal changes during and after spaceflight
Vico, L., & Hargens, A. (2018) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2018.37 · Cited by 236
Acetylcholine receptor-aggregating activity of agrin isoforms and mapping of the active site.
Gesemann, M., Denzer, A. J., & Ruegg, M. A. (1995) · The Journal of cell biology · doi:10.1083/jcb.128.4.625 · Cited by 236
The sarcomeric Z-disc: a nodal point in signalling and disease
Frank, D., Kuhn, C., Katus, H. A., & Frey, N. (2006) · Journal of Molecular Medicine · doi:10.1007/s00109-005-0033-1 · Cited by 235
The Role of Oxidative Stress in Skeletal Muscle Myogenesis and Muscle Disease
Lian, D., Chen, M.-M., Wu, H., Deng, S., & Hu, X. (2022) · Antioxidants · doi:10.3390/antiox11040755 · Cited by 232
Wu, X., Jiang, Y., Rommelfanger, N. J., Yang, F., Zhou, Q., Yin, R., Liu, J., Cai, S., Ren, W., Shin, A., et al. (2022) · Nature Biomedical Engineering · doi:10.1038/s41551-022-00862-w · Cited by 222
Roberts, M. D., McCarthy, J. J., Hornberger, T. A., Phillips, S. M., Mackey, A. L., Nader, G. A., Boppart, M. D., Kavazis, A. N., Reidy, P. T., Ogasawara, R., et al. (2023) · Physiological Reviews · doi:10.1152/physrev.00039.2022 · Cited by 214
Mitochondria-associated apoptotic signalling in denervated rat skeletal muscle
Siu, P. M., & Alway, S. E. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2004.081083 · Cited by 216
Vereker, E., O'Donnell, E., & Lynch, M. A. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-18-06811.2000 · Cited by 214
The Arf GTPase-activating protein ASAP1 regulates the actin cytoskeleton
Randazzo, P. A., Andrade, J., Miura, K., Brown, M. T., Long, Y.-Q., Stauffer, S., Roller, P., & Cooper, J. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.070552297 · Cited by 210
Zinovkin, R. A., & Zamyatnin, A. A. (2019) · Current Molecular Pharmacology · doi:10.2174/1874467212666181127151059 · Cited by 209
Time-Dependent Reversal of Long-Term Potentiation by an Integrin Antagonist
Stäubli, U., Chun, D., & Lynch, G. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-09-03460.1998 · Cited by 205
Li, H., Wu, G., Ware, D., Davis, K. R., & Yang, Z. (1998) · Plant Physiology · doi:10.1104/pp.118.2.407 · Cited by 194
Rac and Cdc42 GTPases control hematopoietic stem cell shape, adhesion, migration, and mobilization
Yang, F.-C., Atkinson, S. J., Gu, Y., Borneo, J. B., Roberts, A. W., Zheng, Y., Pennington, J., & Williams, D. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.101546898 · Cited by 201
Kolczynska, K., Loza-Valdes, A., Hawro, I., & Sumara, G. (2020) · Lipids in Health and Disease · doi:10.1186/s12944-020-01286-8 · Cited by 199
Hashimoto, A., Okada, H., Jiang, A., Kurosaki, M., Greenberg, S., Clark, E. A., & Kurosaki, T. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.7.1287 · Cited by 199
Thirupathi, A., & de Souza, C. T. (2017) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-017-0576-y · Cited by 198
The Involvement of Mg2+ in Regulation of Cellular and Mitochondrial Functions
Pilchova, I., Klacanova, K., Tatarkova, Z., Kaplan, P., & Racay, P. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/6797460 · Cited by 198
Insights into TREM2 biology by network analysis of human brain gene expression data
Forabosco, P., Ramasamy, A., Trabzuni, D., Walker, R., Smith, C., Bras, J., Levine, A. P., Hardy, J., Pocock, J. M., Guerreiro, R., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.05.001 · Cited by 180
Neurovascular Dysfunction in Vascular Dementia, Alzheimer's and Atherosclerosis
Shabir, O., Berwick, J., & Francis, S. E. (2018) · BMC Neuroscience · doi:10.1186/s12868-018-0465-5 · Cited by 191
Magnetic field effects in biology from the perspective of the radical pair mechanism
Zadeh-Haghighi, H., & Simon, C. (2022) · Journal of The Royal Society Interface · doi:10.1098/rsif.2022.0325 · Cited by 197
Di Benedetto, G., Burgaletto, C., Bellanca, C. M., Munafò, A., Bernardini, R., & Cantarella, G. (2022) · Cells · doi:10.3390/cells11172728 · Cited by 189
Interplay of space radiation and microgravity in DNA damage and DNA damage response
Moreno-Villanueva, M., Wong, M., Lu, T., Zhang, Y., & Wu, H. (2017) · npj Microgravity · doi:10.1038/s41526-017-0019-7 · Cited by 181
Influence of aging on the in vivo properties of human patellar tendon
Carroll, C. C., Dickinson, J. M., Haus, J. M., Lee, G. A., Hollon, C. J., Aagaard, P., Magnusson, S. P., & Trappe, T. A. (2008) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00059.2008 · Cited by 186
Latent virus reactivation in astronauts on the international space station
Mehta, S. K., Laudenslager, M. L., Stowe, R. P., Crucian, B. E., Feiveson, A. H., Sams, C. F., & Pierson, D. L. (2017) · npj Microgravity · doi:10.1038/s41526-017-0015-y · Cited by 188
Calcium signaling in vertebrate embryonic patterning and morphogenesis
Slusarski, D. C., & Pelegri, F. (2007) · Developmental Biology · doi:10.1016/j.ydbio.2007.04.043 · Cited by 178
Runx1 prevents wasting, myofibrillar disorganization, and autophagy of skeletal muscle
Wang, X., Blagden, C., Fan, J., Nowak, S. J., Taniuchi, I., Littman, D. R., & Burden, S. J. (2005) · Genes & Development · doi:10.1101/gad.1318305 · Cited by 177
Choi, D., Park, E., Jung, E., Cha, B., Lee, S., Yu, J., Kim, P. M., Lee, S., Hong, Y. J., Koh, C. J., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.125068 · Cited by 176
Cells move when ions and water flow
Schwab, A., Nechyporuk-Zloy, V., Fabian, A., & Stock, C. (2006) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-006-0138-6 · Cited by 176
Understanding the extracellular forces that determine cell fate and maintenance
Kumar, A., Placone, J. K., & Engler, A. J. (2017) · Development · doi:10.1242/dev.158469 · Cited by 175
Cai, B., Kasikara, C., Doran, A. C., Ramakrishnan, R., Birge, R. B., & Tabas, I. (2018) · Science Signaling · doi:10.1126/scisignal.aar3721 · Cited by 175
Ihalainen, T. O., Aires, L., Herzog, F. A., Schwartlander, R., Moeller, J., & Vogel, V. (2015) · Nature Materials · doi:10.1038/nmat4389 · Cited by 172
VDAC1 at the crossroads of cell metabolism, apoptosis and cell stress
Shoshan-Barmatz, V., N. Maldonado, E., & Krelin, Y. (2017) · Cell Stress · doi:10.15698/cst2017.10.104 · Cited by 170
Park, H.-S., Lee, S. C., Cardenas, M. E., & Heitman, J. (2019) · Cell Host & Microbe · doi:10.1016/j.chom.2019.08.004 · Cited by 168
Landrein, B., Kiss, A., Sassi, M., Chauvet, A., Das, P., Cortizo, M., Laufs, P., Takeda, S., Aida, M., Traas, J., et al. (2015) · eLife · doi:10.7554/elife.07811 · Cited by 167
López-Camarillo, C., Aréchaga Ocampo, E., López Casamichana, M., Pérez-Plasencia, C., Álvarez-Sánchez, E., & Marchat, L. A. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms13010142 · Cited by 165
Sarcopenia and Cognitive Decline in Older Adults: Targeting the Muscle–Brain Axis
Arosio, B., Calvani, R., Ferri, E., Coelho-Junior, H. J., Carandina, A., Campanelli, F., Ghiglieri, V., Marzetti, E., & Picca, A. (2023) · Nutrients · doi:10.3390/nu15081853 · Cited by 165
Pogozelski, A. R., Geng, T., Li, P., Yin, X., Lira, V. A., Zhang, M., Chi, J.-T., & Yan, Z. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007934 · Cited by 164
Sudhakar, A. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24813 · Cited by 162
RetractedCytoskeletal signaling: is memory encoded in microtubule lattices by CaMKII phosphorylation?
Craddock, T. J. A., Tuszynski, J. A., & Hameroff, S. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002421 · Cited by 160
Genetically enhancing mitochondrial antioxidant activity improves muscle function in aging
Umanskaya, A., Santulli, G., Xie, W., Andersson, D. C., Reiken, S. R., & Marks, A. R. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1412754111 · Cited by 157
Whitman, S. A., Wacker, M. J., Richmond, S. R., & Godard, M. P. (2005) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-005-1473-8 · Cited by 156
Positioning and usefulness of biomarkers in inflammatory bowel disease
Sakurai, T., & Saruta, M. (2023) · Digestion · doi:10.1159/000527846 · Cited by 156
Huh, M. S., Parker, M. H., Scimè, A., Parks, R., & Rudnicki, M. A. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200403004 · Cited by 156
The Role of Extracellular Regulated Kinases I/II in Late-Phase Long-Term Potentiation
Rosenblum, K., Futter, M., Voss, K., Erent, M., Skehel, P. A., French, P., Obosi, L., Jones, M. W., & Bliss, T. V. P. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-13-05432.2002 · Cited by 155
Glycosphingolipids and Neuroinflammation in Parkinson’s Disease
Belarbi, K., Cuvelier, E., Bonte, M.-A., Desplanque, M., Gressier, B., Devos, D., & Chartier-Harlin, M.-C. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00408-1 · Cited by 155
Modulation of Microglial Process Convergence Toward Neuronal Dendrites by Extracellular Calcium
Eyo, U. B., Gu, N., De, S., Dong, H., Richardson, J. R., & Wu, L.-J. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.3279-14.2015 · Cited by 154
Agostini, D., Donati Zeppa, S., Lucertini, F., Annibalini, G., Gervasi, M., Ferri Marini, C., Piccoli, G., Stocchi, V., Barbieri, E., & Sestili, P. (2018) · Nutrients · doi:10.3390/nu10081103 · Cited by 151
Apoptosis in skeletal muscle and its relevance to atrophy
Dupont-Versteegden, E. E. (2006) · World Journal of Gastroenterology · doi:10.3748/wjg.v12.i46.7463 · Cited by 150
Molecular determinants of Ca 2+ /calmodulin-dependent regulation of Ca v 2.1 channels
Lee, A., Zhou, H., Scheuer, T., & Catterall, W. A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2237000100 · Cited by 150
BDNF is a mediator of glycolytic fiber-type specification in mouse skeletal muscle
Delezie, J., Weihrauch, M., Maier, G., Tejero, R., Ham, D. J., Gill, J. F., Karrer-Cardel, B., Rüegg, M. A., Tabares, L., & Handschin, C. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1900544116 · Cited by 141
YAP-Mediated Mechanotransduction in Skeletal Muscle
Fischer, M., Rikeit, P., Knaus, P., & Coirault, C. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00041 · Cited by 145
Giangregorio, L., & Blimkie, C. J. (2002) · Sports Medicine · doi:10.2165/00007256-200232070-00005 · Cited by 135
Starring or supporting role? Satellite cells and skeletal muscle fiber size regulation
Murach, K. A., Fry, C. S., Kirby, T. J., Jackson, J. R., Lee, J. D., White, S. H., Dupont-Versteegden, E. E., McCarthy, J. J., & Peterson, C. A. (2018) · Physiology · doi:10.1152/physiol.00019.2017 · Cited by 137
Drug development for alzheimer’s disease: Microglia induced neuroinflammation as a target
Dong, Y., Li, X., Cheng, J., & Hou, L. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030558 · Cited by 136
RHO GTPases: from new partners to complex immune syndromes
El Masri, R., & Delon, J. (2021) · Nature Reviews Immunology · doi:10.1038/s41577-021-00500-7 · Cited by 131
Biophysical regulation of macrophages in health and disease
Meli, V. S., Veerasubramanian, P. K., Atcha, H., Reitz, Z., Downing, T. L., & Liu, W. F. (2019) · Journal of Leukocyte Biology · doi:10.1002/jlb.mr0318-126r · Cited by 133
Metadata
- Authors
- Benavides Damm, T., & Egli, M.
- Venue
- Cellular Physiology and Biochemistry
- Publisher
- S. Karger AG
- Published
- 2014
- Volume
- 33
- Issue
- 2
- Pages
- 249-272
- ISSN
- 1015-8987 (ISSN-L)
- 1421-9778
- OpenAlex
- W2036145275
- Cited by
- 14,502
- References
- 12
- FWCI
- 363.21
- Type
- journal article
- Language
- en
- Open access
- gold
- Licence
- creativecommons.org/licenses/by-nc/3.0/ (vor)
- creativecommons.org/licenses/by-nc/3.0/ (tdm)
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
