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
Role of YAP/TAZ in mechanotransduction
Dupont, S., Morsut, L., Aragona, M., Enzo, E., Giulitti, S., Cordenonsi, M., Zanconato, F., Le Digabel, J., Forcato, M., Bicciato, S., et al. (2011) · Nature · doi:10.1038/nature10137 · Cited by 5,979
The NLRP3 Inflammasome: an overview of mechanisms of activation and regulation
Kelley, N., Jeltema, D., Duan, Y., & He, Y. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133328 · Cited by 3,539
Cell Movement Is Guided by the Rigidity of the Substrate
Lo, C.-M., Wang, H.-B., Dembo, M., & Wang, Y.-L. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76279-5 · Cited by 3,289
Piezo1 and Piezo2 Are Essential Components of Distinct Mechanically Activated Cation Channels
Coste, B., Mathur, J., Schmidt, M., Earley, T. J., Ranade, S., Petrus, M. J., Dubin, A. E., & Patapoutian, A. (2010) · Science · doi:10.1126/science.1193270 · Cited by 3,316
Flow-mediated endothelial mechanotransduction
Davies, P. F. (1995) · Physiological Reviews · doi:10.1152/physrev.1995.75.3.519 · Cited by 2,802
A 3D bioprinting system to produce human-scale tissue constructs with structural integrity
Kang, H.-W., Lee, S. J., Ko, I. K., Kengla, C., Yoo, J. J., & Atala, A. (2016) · Nature Biotechnology · doi:10.1038/nbt.3413 · Cited by 2,622
International Union of Pharmacology. XXV. Nomenclature and Classification of Adenosine Receptors
Fredholm, B. B., IJzerman, A. P., Jacobson, K. A., Klotz, K.-N., & Linden, J. (2001) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01511-4 · Cited by 2,585
Memristors with diffusive dynamics as synaptic emulators for neuromorphic computing
Wang, Z., Joshi, S., Savel’ev, S. E., Jiang, H., Midya, R., Lin, P., Hu, M., Ge, N., Strachan, J. P., Li, Z., et al. (2017) · Nature Materials · doi:10.1038/nmat4756 · Cited by 2,358
Effects of extracellular matrix viscoelasticity on cellular behaviour
Chaudhuri, O., Cooper-White, J., Janmey, P. A., Mooney, D. J., & Shenoy, V. B. (2020) · Nature · doi:10.1038/s41586-020-2612-2 · Cited by 2,224
Chiu, J.-J., & Chien, S. (2011) · Physiological Reviews · doi:10.1152/physrev.00047.2009 · Cited by 2,280
PLEIOTROPIC EFFECTS OF STATINS
Liao, J. K., & Laufs, U. (2005) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.45.120403.095748 · Cited by 1,994
Ros and ros-mediated cellular signaling
Zhang, J., Wang, X., Vikash, V., Ye, Q., Wu, D., Liu, Y., & Dong, W. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/4350965 · Cited by 1,980
Sarcopenia: Aging-Related Loss of Muscle Mass and Function
Larsson, L., Degens, H., Li, M., Salviati, L., Lee, Y. I., Thompson, W., Kirkland, J. L., & Sandri, M. (2019) · Physiological Reviews · doi:10.1152/physrev.00061.2017 · Cited by 1,797
Myotubes differentiate optimally on substrates with tissue-like stiffness
Engler, A. J., Griffin, M. A., Sen, S., Bönnemann, C. G., Sweeney, H. L., & Discher, D. E. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200405004 · Cited by 1,743
Signal transduction from the extracellular matrix.
Juliano, R. L., & Haskill, S. (1993) · The Journal of cell biology · doi:10.1083/jcb.120.3.577 · Cited by 1,683
Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation
Balla, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00028.2012 · Cited by 1,638
The endoplasmic reticulum: structure, function and response to cellular signaling
Schwarz, D. S., & Blower, M. D. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2052-6 · Cited by 1,613
Three-dimensional in vitro cell culture models in drug discovery and drug repositioning
Langhans, S. A. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00006 · Cited by 1,522
Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels
Szabadkai, G., Bianchi, K., Várnai, P., De Stefani, D., Wieckowski, M. R., Cavagna, D., Nagy, A. I., Balla, T., & Rizzuto, R. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200608073 · Cited by 1,413
Rate of force development: physiological and methodological considerations
Maffiuletti, N. A., Aagaard, P., Blazevich, A. J., Folland, J., Tillin, N., & Duchateau, J. (2016) · European Journal of Applied Physiology · doi:10.1007/s00421-016-3346-6 · Cited by 1,424
Hormonal Responses and Adaptations to Resistance Exercise and Training
Kraemer, W. J., & Ratamess, N. A. (2005) · Sports Medicine · doi:10.2165/00007256-200535040-00004 · Cited by 1,389
Targeting integrin pathways: mechanisms and advances in therapy
Pang, X., He, X., Qiu, Z., Zhang, H., Xie, R., Liu, Z., Gu, Y., Zhao, N., Xiang, Q., & Cui, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01259-6 · Cited by 1,275
Biomechanics and biophysics of cancer cells☆
SURESH, S. (2007) · Acta Biomaterialia · doi:10.1016/j.actbio.2007.04.002 · Cited by 1,284
AMPK and PPARδ Agonists Are Exercise Mimetics
Narkar, V. A., Downes, M., Yu, R. T., Embler, E., Wang, Y.-X., Banayo, E., Mihaylova, M. M., Nelson, M. C., Zou, Y., Juguilon, H., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.051 · Cited by 1,222
A micropeptide encoded by a putative long noncoding RNA regulates muscle performance
Anderson, D. M., Anderson, K. M., Chang, C.-L., Makarewich, C. A., Nelson, B. R., McAnally, J. R., Kasaragod, P., Shelton, J. M., Liou, J., Bassel-Duby, R., et al. (2015) · Cell · doi:10.1016/j.cell.2015.01.009 · Cited by 1,216
Inositol Trisphosphate Receptor Ca2+Release Channels
Foskett, J. K., White, C., Cheung, K.-H., & Mak, D.-O. D. (2007) · Physiological Reviews · doi:10.1152/physrev.00035.2006 · Cited by 1,188
KRAS Mutation: From Undruggable to Druggable in Cancer
Huang, L., Guo, Z., Wang, F., & Fu, L. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00780-4 · Cited by 1,127
Regulation of mitochondrial biogenesis
Jornayvaz, F. R., & Shulman, G. I. (2010) · Essays in Biochemistry · doi:10.1042/bse0470069 · Cited by 1,119
Physical Principles of Nanoparticle Cellular Endocytosis
Zhang, S., Gao, H., & Bao, G. (2015) · ACS Nano · doi:10.1021/acsnano.5b03184 · Cited by 1,103
Harnessing nanotopography and integrin–matrix interactions to influence stem cell fate
Dalby, M. J., Gadegaard, N., & Oreffo, R. O. C. (2014) · Nature Materials · doi:10.1038/nmat3980 · Cited by 1,082
Endoplasmic reticulum stress signalling-from basic mechanisms to clinical applications
Almanza, A., Carlesso, A., Chintha, C., Creedican, S., Doultsinos, D., Leuzzi, B., Luís, A., McCarthy, N., Montibeller, L., More, S., et al. (2019) · The FEBS Journal · doi:10.1111/febs.14608 · Cited by 1,034
Sandri, M., Lin, J., Handschin, C., Yang, W., Arany, Z. P., Lecker, S. H., Goldberg, A. L., & Spiegelman, B. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607795103 · Cited by 974
Materials as stem cell regulators
Murphy, W. L., McDevitt, T. C., & Engler, A. J. (2014) · Nature Materials · doi:10.1038/nmat3937 · Cited by 947
A family of microRNAs encoded by myosin genes governs myosin expression and muscle performance
van Rooij, E., Quiat, D., Johnson, B. A., Sutherland, L. B., Qi, X., Richardson, J. A., Kelm, R. J., & Olson, E. N. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.10.013 · Cited by 960
Ageing and neuronal vulnerability
Mattson, M. P., & Magnus, T. (2006) · Nature Reviews Neuroscience · doi:10.1038/nrn1886 · Cited by 957
Three-dimensional culture systems in cancer research: Focus on tumor spheroid model
Nath, S., & Devi, G. R. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.03.013 · Cited by 919
The Transcription Factor NFAT Promotes Exhaustion of Activated CD8 + T Cells
Martinez, G. J., Pereira, R. M., Äijö, T., Kim, E. Y., Marangoni, F., Pipkin, M. E., Togher, S., Heissmeyer, V., Zhang, Y. C., Crotty, S., et al. (2015) · Immunity · doi:10.1016/j.immuni.2015.01.006 · Cited by 857
Autoamplification of NFATc1 expression determines its essential role in bone homeostasis
Asagiri, M., Sato, K., Usami, T., Ochi, S., Nishina, H., Yoshida, H., Morita, I., Wagner, E. F., Mak, T. W., Serfling, E., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20051150 · Cited by 849
Seo, H., Chen, J., González-Avalos, E., Samaniego-Castruita, D., Das, A., Wang, Y. H., López-Moyado, I. F., Georges, R. O., Zhang, W., Onodera, A., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1905675116 · Cited by 808
Appreciating force and shape—the rise of mechanotransduction in cell biology
Iskratsch, T., Wolfenson, H., & Sheetz, M. P. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3903 · Cited by 798
G Protein–Coupled Receptor Rhodopsin
Palczewski, K. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142743 · Cited by 764
Glycogen synthase kinase-3 (GSK3): Inflammation, diseases, and therapeutics
Jope, R. S., Yuskaitis, C. J., & Beurel, E. (2007) · Neurochemical Research · doi:10.1007/s11064-006-9128-5 · Cited by 774
NAADP mobilizes calcium from acidic organelles through two-pore channels
Calcraft, P. J., Ruas, M., Pan, Z., Cheng, X., Arredouani, A., Hao, X., Tang, J., Rietdorf, K., Teboul, L., Chuang, K.-T., et al. (2009) · Nature · doi:10.1038/nature08030 · Cited by 760
Handschin, C., Rhee, J., Lin, J., Tarr, P. T., & Spiegelman, B. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1232352100 · Cited by 729
Yim, E. K. F., Pang, S. W., & Leong, K. W. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.02.031 · Cited by 735
Cell Wall and Secreted Proteins of Candida albicans: Identification, Function, and Expression
Chaffin, W. L., López-Ribot, J. L., Casanova, M., Gozalbo, D., & Martínez, J. P. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.1.130-180.1998 · Cited by 726
Rejuvenation of the muscle stem cell population restores strength to injured aged muscles
Cosgrove, B. D., Gilbert, P. M., Porpiglia, E., Mourkioti, F., Lee, S. P., Corbel, S. Y., Llewellyn, M. E., Delp, S. L., & Blau, H. M. (2014) · Nature Medicine · doi:10.1038/nm.3464 · Cited by 677
Function and therapeutic value of astrocytes in neurological diseases
Lee, H.-G., Wheeler, M. A., & Quintana, F. J. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00390-x · Cited by 662
MicroRNA-206 Delays ALS Progression and Promotes Regeneration of Neuromuscular Synapses in Mice
Williams, A. H., Valdez, G., Moresi, V., Qi, X., McAnally, J., Elliott, J. L., Bassel-Duby, R., Sanes, J. R., & Olson, E. N. (2009) · Science · doi:10.1126/science.1181046 · Cited by 673
Khoshnoodi, J., Pedchenko, V., & Hudson, B. G. (2008) · Microscopy Research and Technique · doi:10.1002/jemt.20564 · Cited by 668
Effects of Aging on Muscle Fibre Type and Size
Deschenes, M. R. (2004) · Sports Medicine · doi:10.2165/00007256-200434120-00002 · Cited by 671
Integrins and Extracellular Matrix in Mechanotransduction
Schwartz, M. A. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005066 · Cited by 662
From space to Earth: Advances in human physiology from 20 years of bed rest studies (1986–2006)
Pavy-Le Traon, A., Heer, M., Narici, M. V., Rittweger, J., & Vernikos, J. (2007) · European Journal of Applied Physiology · doi:10.1007/s00421-007-0474-z · Cited by 658
Mechanically Activated Ion Channels
Ranade, S. S., Syeda, R., & Patapoutian, A. (2015) · Neuron · doi:10.1016/j.neuron.2015.08.032 · Cited by 652
Nanopattern-induced changes in morphology and motility of smooth muscle cells
Yim, E. K. F., Reano, R. M., Pang, S. W., Yee, A. F., Chen, C. S., & Leong, K. W. (2005) · Biomaterials · doi:10.1016/j.biomaterials.2005.01.058 · Cited by 628
Structure–function of the multifunctional Ca2+/calmodulin-dependent protein kinase II
HUDMON, A., & SCHULMAN, H. (2002) · Biochemical Journal · doi:10.1042/bj20020228 · Cited by 615
Miller, B. F., Olesen, J. L., Hansen, M., Døssing, S., Crameri, R. M., Welling, R. J., Langberg, H., Flyvbjerg, A., Kjaer, M., Babraj, J. A., et al. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2005.093690 · Cited by 610
Sarcopenia from mechanism to diagnosis and treatment in liver disease
Dasarathy, S., & Merli, M. (2016) · Journal of Hepatology · doi:10.1016/j.jhep.2016.07.040 · Cited by 608
Spacek, J., & Harris, K. M. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-01-00190.1997 · Cited by 599
Mimitou, E. P., Lareau, C. A., Chen, K. Y., Zorzetto-Fernandes, A. L., Hao, Y., Takeshima, Y., Luo, W., Huang, T.-S., Yeung, B. Z., Papalexi, E., et al. (2021) · Nature Biotechnology · doi:10.1038/s41587-021-00927-2 · Cited by 529
Regulation of NFATc1 in Osteoclast Differentiation
Kim, J. H., & Kim, N. (2014) · Journal of Bone Metabolism · doi:10.11005/jbm.2014.21.4.233 · Cited by 570
Gonzalez-Cadavid, N. F., Taylor, W. E., Yarasheski, K., Sinha-Hikim, I., Ma, K., Ezzat, S., Shen, R., Lalani, R., Asa, S., Mamita, M., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.25.14938 · Cited by 571
Bottinelli, R., Canepari, M., Pellegrino, M. A., & Reggiani, C. (1996) · The Journal of Physiology · doi:10.1113/jphysiol.1996.sp021617 · Cited by 565
Ca2+ buffering and action potential-evoked Ca2+ signaling in dendrites of pyramidal neurons
Helmchen, F., Imoto, K., & Sakmann, B. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79653-4 · Cited by 559
Apoptosis of adherent cells by recruitment of caspase-8 to unligated integrins
Stupack, D. G., Puente, X. S., Boutsaboualoy, S., Storgard, C. M., & Cheresh, D. A. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200106070 · Cited by 554
Baker, B. M., Trappmann, B., Wang, W. Y., Sakar, M. S., Kim, I. L., Shenoy, V. B., Burdick, J. A., & Chen, C. S. (2015) · Nature Materials · doi:10.1038/nmat4444 · Cited by 556
Pulsatile Stimulation Determines Timing and Specificity of NF-κB-Dependent Transcription
Ashall, L., Horton, C. A., Nelson, D. E., Paszek, P., Harper, C. V., Sillitoe, K., Ryan, S., Spiller, D. G., Unitt, J. F., Broomhead, D. S., et al. (2009) · Science · doi:10.1126/science.1164860 · Cited by 543
Molecular basis of physiological heart growth: fundamental concepts and new players
Maillet, M., van Berlo, J. H., & Molkentin, J. D. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3495 · Cited by 536
A role for Rho in Ras transformation
Qiu, R. G., Chen, J., McCormick, F., & Symons, M. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.25.11781 · Cited by 533
Cox, C. D., Bae, C., Ziegler, L., Hartley, S., Nikolova-Krstevski, V., Rohde, P. R., Ng, C.-A., Sachs, F., Gottlieb, P. A., & Martinac, B. (2016) · Nature Communications · doi:10.1038/ncomms10366 · Cited by 528
Neuronal calcium sensor proteins: generating diversity in neuronal Ca2+ signalling
Burgoyne, R. D. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2093 · Cited by 527
Guidelines for the use of flow cytometry and cell sorting in immunological studies (third edition)
Cossarizza, A., Chang, H., Radbruch, A., Abrignani, S., Addo, R., Akdis, M., Andrä, I., Andreata, F., Annunziato, F., Arranz, E., et al. (2021) · European Journal of Immunology · doi:10.1002/eji.202170126 · Cited by 531
Case, L. B., & Waterman, C. M. (2015) · Nature Cell Biology · doi:10.1038/ncb3191 · Cited by 520
Skeletal Muscle Fiber Type: Influence on Contractile and Metabolic Properties
Zierath, J. R., & Hawley, J. A. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020348 · Cited by 518
Impairment of an endothelial NAD(+)-H2S signaling network is a reversible cause of vascular aging
Das, A., Huang, G. X., Bonkowski, M. S., Longchamp, A., Li, C., Schultz, M. B., Kim, L.-J., Osborne, B., Joshi, S., Lu, Y., et al. (2018) · Cell · doi:10.1016/j.cell.2018.02.008 · Cited by 496
Sex-Based Differences in Skeletal Muscle Kinetics and Fiber-Type Composition
Haizlip, K. M., Harrison, B. C., & Leinwand, L. A. (2015) · Physiology · doi:10.1152/physiol.00024.2014 · Cited by 521
Matrix metalloproteinase-9 is required for hippocampal late-phase long-term potentiation and memory
Nagy, V., Bozdagi, O., Matynia, A., Balcerzyk, M., Okulski, P., Dzwonek, J., Costa, R. M., Silva, A. J., Kaczmarek, L., & Huntley, G. W. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4359-05.2006 · Cited by 499
Ilić, D., Almeida, E. A. C., Schlaepfer, D. D., Dazin, P., Aizawa, S., & Damsky, C. H. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.2.547 · Cited by 495
Animal models for muscular dystrophy show different patterns of sarcolemmal disruption
Straub, V., Rafael, J. A., Chamberlain, J. S., & Campbell, K. P. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.2.375 · Cited by 488
Integrin Dynamics and Matrix Assembly
Pankov, R., Cukierman, E., Katz, B.-Z., Matsumoto, K., Lin, D. C., Lin, S., Hahn, C., & Yamada, K. M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.5.1075 · Cited by 482
Renal Autoregulation in Health and Disease
Carlström, M., Wilcox, C. S., & Arendshorst, W. J. (2015) · Physiological Reviews · doi:10.1152/physrev.00042.2012 · Cited by 485
Elusive roles for reactive astrocytes in neurodegenerative diseases
Ben Haim, L., Carrillo-de Sauvage, M.-A., Ceyzériat, K., & Escartin, C. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00278 · Cited by 453
Preserving Healthy Muscle during Weight Loss
Cava, E., Yeat, N. C., & Mittendorfer, B. (2017) · Advances in Nutrition · doi:10.3945/an.116.014506 · Cited by 452
Stathopoulos, A. M., & Cyert, M. S. (1997) · Genes & Development · doi:10.1101/gad.11.24.3432 · Cited by 442
Mitochondrial quality control and muscle mass maintenance.
Romanello, V., & Sandri, M. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2015.00422 · Cited by 434
Oxytocin and Vasopressin Agonists and Antagonists as Research Tools and Potential Therapeutics
Manning, M., Misicka, A., Olma, A., Bankowski, K., Stoev, S., Chini, B., Durroux, T., Mouillac, B., Corbani, M., & Guillon, G. (2012) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2012.02303.x · Cited by 423
New fundamental resistance exercise determinants of molecular and cellular muscle adaptations
Toigo, M., & Boutellier, U. (2006) · European Journal of Applied Physiology · doi:10.1007/s00421-006-0238-1 · Cited by 437
Requirements for both Rac1 and Cdc42 in membrane ruffling and phagocytosis in leukocytes
Cox, D., Chang, P., Zhang, Q., Reddy, P. G., Bokoch, G. M., & Greenberg, S. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.9.1487 · Cited by 436
Czubryt, M. P., McAnally, J., Fishman, G. I., & Olson, E. N. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0337639100 · Cited by 418
Exercise Attenuates the Major Hallmarks of Aging
Garatachea, N., Pareja-Galeano, H., Sanchis-Gomar, F., Santos-Lozano, A., Fiuza-Luces, C., Morán, M., Emanuele, E., Joyner, M. J., & Lucia, A. (2015) · Rejuvenation Research · doi:10.1089/rej.2014.1623 · Cited by 413
Glover, E. I., Phillips, S. M., Oates, B. R., Tang, J. E., Tarnopolsky, M. A., Selby, A., Smith, K., & Rennie, M. J. (2008) · The Journal of Physiology · doi:10.1113/jphysiol.2008.160333 · Cited by 414
Focal adhesions, stress fibers and mechanical tension
Burridge, K., & Guilluy, C. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.10.029 · Cited by 409
Pallafacchina, G., Calabria, E., Serrano, A. L., Kalhovde, J. M., & Schiaffino, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142166599 · Cited by 402
Bengtsson, N. E., Hall, J. K., Odom, G. L., Phelps, M. P., Andrus, C. R., Hawkins, R. D., Hauschka, S. D., Chamberlain, J. R., & Chamberlain, J. S. (2017) · Nature Communications · doi:10.1038/ncomms14454 · Cited by 387
Different Neuronal Activity Patterns Induce Different Gene Expression Programs
Tyssowski, K. M., DeStefino, N. R., Cho, J.-H., Dunn, C. J., Poston, R. G., Carty, C. E., Jones, R. D., Chang, S. M., Romeo, P., Wurzelmann, M. K., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.04.001 · Cited by 390
Palacios, D., Mozzetta, C., Consalvi, S., Caretti, G., Saccone, V., Proserpio, V., Marquez, V. E., Valente, S., Mai, A., Forcales, S. V., et al. (2010) · Cell Stem Cell · doi:10.1016/j.stem.2010.08.013 · Cited by 392
Glucose or diabetes activates p38 mitogen-activated protein kinase via different pathways
Igarashi, M., Wakasaki, H., Takahara, N., Ishii, H., Jiang, Z.-Y., Yamauchi, T., Kuboki, K., Meier, M., Rhodes, C. J., & King, G. L. (1999) · Journal of Clinical Investigation · doi:10.1172/jci3326 · Cited by 386
Dementia in Down syndrome: unique insights for Alzheimer disease research
Lott, I. T., & Head, E. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-018-0132-6 · Cited by 383
The impact of extended bed rest on the musculoskeletal system in the critical care environment
Parry, S. M., & Puthucheary, Z. A. (2015) · Extreme Physiology & Medicine · doi:10.1186/s13728-015-0036-7 · Cited by 383
Chakrabarti, R., Ji, W.-K., Stan, R. V., de Juan Sanz, J., Ryan, T. A., & Higgs, H. N. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201709111 · Cited by 349
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.
