Mechanical regulation of myofibroblast phenoconversion and collagen contraction
Abstract
Activated fibroblasts promote physiological wound repair following tissue injury. However, dysregulation of fibroblast activation contributes to the development of fibrosis by enhanced production and contraction of collagen-rich extracellular matrix. At the peak of their activities, fibroblasts undergo phenotypic conversion into highly contractile myofibroblasts by developing muscle-like features, including formation of contractile actin-myosin bundles. The phenotype and function of fibroblasts and myofibroblasts are mechanically regulated by matrix stiffness using a feedback control system that is integrated with the progress of tissue remodelling. The actomyosin contraction machinery and cell-matrix adhesion receptors are critical elements that are needed for mechanosensing by fibroblasts and the translation of mechanical signals into biological responses. Here, we focus on mechanical and chemical regulation of collagen contraction by fibroblasts and the involvement of these factors in their phenotypic conversion to myofibroblasts.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
During fibroblast-to-myofibroblast transition, complex mechanochemical signaling is activated involving profibrotic secreted factors TGFβ and Wnt and ECM-degrading enzymes and intracellular effectors required for stress fiber contractility.
“During fibroblast-to-myofibroblast transition, a complex mechanochemical signaling is activated involving profibrotic secreted factors such as TGFβ and Wnt and ECM-degrading enzymes and intracellular effectors required for stress fiber contractility [127,131].”
From Cellular and Molecular Mechanisms in the Pathogenesis of Classical, Vascular, and Hypermobile Ehlers‒Danlos Syndromes (2019) · cites this paper as [131]
Cites
Myofibroblasts and mechano-regulation of connective tissue remodelling
Tomasek, J. J., Gabbiani, G., Hinz, B., Chaponnier, C., & Brown, R. A. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm809 · Cited by 4,290 · see citing works
Self-citationTGF-β: the master regulator of fibrosis
Meng, X.-M., Nikolic-Paterson, D. J., & Lan, H. Y. (2016) · Nature Reviews Nephrology · doi:10.1038/nrneph.2016.48 · Cited by 3,528 · see citing works
Mechanotransduction Across the Cell Surface and Through the Cytoskeleton
Wang, N., Butler, J. P., & Ingber, D. E. (1993) · Science · doi:10.1126/science.7684161 · Cited by 3,007 · see citing works
Mechanotransduction and extracellular matrix homeostasis
Humphrey, J. D., Dufresne, E. R., & Schwartz, M. A. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3896 · Cited by 2,187 · see citing works
Hinz, B., Phan, S. H., Thannickal, V. J., Galli, A., Bochaton-Piallat, M.-L., & Gabbiani, G. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.070112 · Cited by 2,068 · see citing works
Self-citationNon-muscle myosin II takes centre stage in cell adhesion and migration
Vicente‐Manzanares, M., Ma, X., Adelstein, R. S., & Horwitz, A. R. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2786 · Cited by 2,041 · see citing works
Cell adhesion: integrating cytoskeletal dynamics and cellular tension
Parsons, J. T., Horwitz, A. R., & Schwartz, M. A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2957 · Cited by 1,991 · see citing works
ROCKs: multifunctional kinases in cell behaviour
Riento, K., & Ridley, A. J. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1128 · Cited by 1,941 · see citing works
Cardiac Fibrosis: The Fibroblast Awakens
Travers, J. G., Kamal, F. A., Robbins, J., Yutzey, K. E., & Blaxall, B. C. (2016) · Circulation Research · doi:10.1161/circresaha.115.306565 · Cited by 1,596 · see citing works
Stretching Single Talin Rod Molecules Activates Vinculin Binding
Hernández, A. E. D. R., Pérez‐Jiménez, R., Liu, R., Roca‐Cusachs, P., Fernández, J. M., & Sheetz, M. P. (2009) · Science · doi:10.1126/science.1162912 · Cited by 1,509 · see citing works
Presence of modified fibroblasts in granulation tissue and their possible role in wound contraction
Gabbiani, G., Ryan, G. B., & Majno, G. (1971) · Experientia · doi:10.1007/bf02147594 · Cited by 1,485 · see citing works
Calvo, F., Ege, N., Grande-Garcia, A., Hooper, S., Jenkins, R. P., Chaudhry, S. I., Harrington, K., Williamson, P., Moeendarbary, E., Charras, G., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2756 · Cited by 1,478 · see citing works
Common and unique mechanisms regulate fibrosis in various fibroproliferative diseases
Wynn, T. A. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31487 · Cited by 1,451 · see citing works
Alpha-Smooth Muscle Actin Expression Upregulates Fibroblast Contractile Activity
Hinz, B., Celetta, G., Tomasek, J. J., Gabbiani, G., & Chaponnier, C. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.9.2730 · Cited by 1,288 · see citing works
Self-citationBiernacka, A., Dobaczewski, M. P., & Frangogiannis, N. G. (2011) · Growth Factors · doi:10.3109/08977194.2011.595714 · Cited by 1,175 · see citing works
Desmoulière, A., Redard, M., Darby, I. A., & Gabbiani, G. (1995) · Europe PMC (PubMed Central) · Cited by 1,173 · see citing works
YAP/TAZ upstream signals and downstream responses
Totaro, A., Panciera, T., & Piccolo, S. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0142-z · Cited by 1,086 · see citing works
Integrin-mediated mechanotransduction
Sun, Z., Guo, S., & Fässler, R. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201609037 · Cited by 1,079 · see citing works
Type 2 immunity in tissue repair and fibrosis
Gieseck, R. L., Wilson, M. S., & Wynn, T. A. (2018) · Nature Reviews Immunology · doi:10.1038/nri.2017.90 · Cited by 1,055 · see citing works
Fibroblastic reticular cells in lymph nodes regulate the homeostasis of naive T cells
Link, A., Vogt, T. K., Favre, S., Britschgi, M. R., Acha‐Orbea, H., Hinz, B., Cyster, J. G., & Luther, S. A. (2007) · Nature Immunology · doi:10.1038/ni1513 · Cited by 934 · see citing works
Self-citationActin stress fibers – assembly, dynamics and biological roles
Tojkander, S., Gateva, G., & Lappalainen, P. (2012) · Journal of Cell Science · doi:10.1242/jcs.098087 · Cited by 900 · see citing works
Mechanosignaling through YAP and TAZ drives fibroblast activation and fibrosis
Liu, F., Lagares, D., Choi, K. M., Stopfer, L., Marinković, A., Vrbanac, V., Probst, C. K., Hiemer, S. E., Sisson, T. H., Horowitz, J. C., et al. (2015) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00300.2014 · Cited by 874 · see citing works
Mechanisms of Mechanotransduction
Orr, A. W., Helmke, B. P., Blackman, B. R., & Schwartz, M. A. (2006) · Developmental Cell · doi:10.1016/j.devcel.2005.12.006 · Cited by 809 · see citing works
The myofibroblast matrix: implications for tissue repair and fibrosis
Klingberg, F., Hinz, B., & White, E. S. (2013) · The Journal of Pathology · doi:10.1002/path.4104 · Cited by 776 · see citing works
Self-citationThe Role of Cancer-Associated Fibroblasts and Fibrosis in Liver Cancer
Affo, S., Yu, L.-X., & Schwabe, R. F. (2017) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-052016-100322 · Cited by 757 · see citing works
Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells
Zaidel-Bar, R., Ballestrem, C., Kam, Z., & Geiger, B. (2003) · Journal of Cell Science · doi:10.1242/jcs.00792 · Cited by 719 · see citing works
The myofibroblast: Paradigm for a mechanically active cell
Hinz, B. (2009) · Journal of Biomechanics · doi:10.1016/j.jbiomech.2009.09.020 · Cited by 695 · see citing works
Self-citationTotsukawa, G., Yamakita, Y., Yamashiro, S., Hartshorne, D. J., Sasaki, Y., & Matsumura, F. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.4.797 · Cited by 689 · see citing works
Forcing cells into shape: the mechanics of actomyosin contractility
Murrell, M. P., Oakes, P. W., Lenz, M., & Gardel, M. L. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4012 · Cited by 675 · see citing works
Nuclear Actin Regulates Dynamic Subcellular Localization and Activity of the SRF Cofactor MAL
Vartiainen, M., Guettler, S., Larijani, B., & Treisman, R. (2007) · Science · doi:10.1126/science.1141084 · Cited by 672 · see citing works
YAP regulates cell mechanics by controlling focal adhesion assembly
Nardone, G., Cruz, J. O. L., Vrbský, J., Martini, C., Přibyl, J., Skládal, P., Pešl, M., Caluori, G., Pagliari, S., Martino, F. D., et al. (2017) · Nature Communications · doi:10.1038/ncomms15321 · Cited by 669 · see citing works
Provenzano, P. P., Inman, D. R., Eliceiri, K. W., & Keely, P. J. (2009) · Oncogene · doi:10.1038/onc.2009.299 · Cited by 667 · see citing works
Integrins and Extracellular Matrix in Mechanotransduction
Schwartz, M. A. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005066 · Cited by 662 · see citing works
Therapy for Fibrotic Diseases: Nearing the Starting Line
Friedman, S. L., Sheppard, D., Duffield, J. S., & Violette, S. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3004700 · Cited by 655 · see citing works
Specialized fibroblast differentiated states underlie scar formation in the infarcted mouse heart
Fu, X., Khalil, H., Kanisicak, O., Boyer, J. G., Vagnozzi, R. J., Maliken, B. D., Sargent, M. A., Prasad, V., Valiente-Alandi, I., Blaxall, B. C., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci98215 · Cited by 636 · see citing works
The extracellular matrix and transforming growth factor-β1: Tale of a strained relationship
Hinz, B. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.05.006 · Cited by 618 · see citing works
Self-citationExtracellular matrix as a driver of progressive fibrosis
Herrera, J., Henke, C. A., & Bitterman, P. B. (2018) · Journal of Clinical Investigation · doi:10.1172/jci93557 · Cited by 616 · see citing works
Thannickal, V. J., Lee, D. Y., White, E. S., Cui, Z., Larios, J. M., Chacon, R., Horowitz, J. C., Day, R. M., & Thomas, P. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208544200 · Cited by 606 · see citing works
Preparing the ground for tissue regeneration: from mechanism to therapy
Forbes, S. J., & Rosenthal, N. A. (2014) · Nature Medicine · doi:10.1038/nm.3653 · Cited by 585 · see citing works
Regeneration of fat cells from myofibroblasts during wound healing
Plikus, M. V., Guerrero-Juarez, C. F., Ito, M., Li, Y. R., Dedhia, P. H., Zheng, Y., Shao, M., Gay, D. L., Ramos, R., Hsi, T.-C., et al. (2017) · Science · doi:10.1126/science.aai8792 · Cited by 584 · see citing works
Pasapera, A. M., Schneider, I. C., Rericha, E. C., Schlaepfer, D. D., & Waterman, C. M. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200906012 · Cited by 573 · see citing works
Lampi, M. C., & Reinhart-King, C. A. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aao0475 · Cited by 551 · see citing works
Matrix stiffness-induced myofibroblast differentiation is mediated by intrinsic mechanotransduction
Huang, X., Yang, N., Fiore, V. F., Barker, T. H., Sun, Y., Morris, S. W., Ding, Q., Thannickal, V. J., & Zhou, Y. (2012) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2012-0050oc · Cited by 530 · see citing works
Fibroblasts in myocardial infarction: A role in inflammation and repair
Shinde, A. V., & Frangogiannis, N. G. (2013) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2013.11.015 · Cited by 516 · see citing works
Focal adhesion kinase links mechanical force to skin fibrosis via inflammatory signaling
Wong, V. W., Rustad, K. C., Akaishi, S., Sorkin, M., Glotzbach, J. P., Januszyk, M., Nelson, E. R., Levi, K., Paterno, J., Vial, I. N., et al. (2012) · Nature Medicine · doi:10.1038/nm.2574 · Cited by 515 · see citing works
The good and the bad collagens of fibrosis – Their role in signaling and organ function
Karsdal, M. A., Nielsen, S. H., Leeming, D. J., Langholm, L. L., Nielsen, M. J., Manon-Jensen, T., Siebuhr, A., Gudmann, N. S., Rønnow, S., Sand, J. M., et al. (2017) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2017.07.014 · Cited by 509 · see citing works
YAP/TAZ Are Mechanoregulators of TGF-β-Smad Signaling and Renal Fibrogenesis
Szeto, S. G., Narimatsu, M., Lu, M., He, X., Sidiqi, A. M., Tolosa, M. F., Chan, L., Freitas, K. D., Bialik, J. F., Majumder, S., et al. (2016) · Journal of the American Society of Nephrology · doi:10.1681/asn.2015050499 · Cited by 463 · see citing works
Self-citationZhou, Y., Huang, X., Hecker, L., Kurundkar, D., Kurundkar, A., Liu, H., Jin, T. H., Desai, L. P., Bernard, K. F., & Thannickal, V. J. (2013) · Journal of Clinical Investigation · doi:10.1172/jci66700 · Cited by 452 · see citing works
Role of YAP/TAZ in cell-matrix adhesion-mediated signalling and mechanotransduction
Dupont, S. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.10.034 · Cited by 449 · see citing works
Liver fibrosis: Direct antifibrotic agents and targeted therapies
Schuppan, D., Ashfaq–Khan, M., Yang, A. T., & Kim, Y. O. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.04.006 · Cited by 440 · see citing works
Extracellular matrix remodeling and cardiac fibrosis
Li, L., Zhao, Q., & Kong, W. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.01.013 · Cited by 428 · see citing works
Hinz, B. (2016) · Experimental Eye Research · doi:10.1016/j.exer.2015.07.009 · Cited by 424 · see citing works
Self-citationFocal 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 · see citing works
The big five in fibrosis: Macrophages, myofibroblasts, matrix, mechanics, and miscommunication
Pakshir, P., & Hinz, B. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.01.019 · Cited by 396 · see citing works
Self-citationSensing extracellular matrix: An update on discoidin domain receptor function
Vogel, W. F., Abdulhussein, R., & Ford, C. E. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.02.012 · Cited by 368 · see citing works
Small, E. M., Thatcher, J. E., Sutherland, L. B., Kinoshita, H., Gerard, R. D., Richardson, J. A., DiMaio, J. M., Sadek, H. A., Kuwahara, K., & Olson, E. N. (2010) · Circulation Research · doi:10.1161/circresaha.110.223172 · Cited by 368 · see citing works
Jun, J.-I., & Lau, L. F. (2018) · Journal of Clinical Investigation · doi:10.1172/jci93563 · Cited by 348 · see citing works
Extracellular rigidity sensing by talin isoform-specific mechanical linkages
Austen, K., Ringer, P., Mehlich, A., Chrostek‐Grashoff, A., Kluger, C., Klingner, C., Sabass, B., Zent, R., Rief, M., & Grashoff, C. (2015) · Nature Cell Biology · doi:10.1038/ncb3268 · Cited by 347 · see citing works
The precursor form of IL-1α is an intracrine proinflammatory activator of transcription
Werman, A., Werman-Venkert, R., White, R. M., Lee, J.-K., Werman, B., Krelin, Y., Voronov, E., Dinarello, C. A., & Apte, R. N. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308705101 · Cited by 346 · see citing works
Kapançi, Y., Assimacopoulos, A., Irlé, C., Zwahlen, A., & Gabbiani, G. (1974) · The Journal of Cell Biology · doi:10.1083/jcb.60.2.375 · Cited by 346 · see citing works
Signaling Networks that Regulate Cell MigrationPreprint
Devreotes, P. N., & Horwitz, A. R. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005959 · Cited by 345 · see citing works
Tschumperlin, D. J., Ligresti, G., Hilscher, M. B., & Shah, V. H. (2018) · Journal of Clinical Investigation · doi:10.1172/jci93561 · Cited by 343 · see citing works
Force activates smooth muscle α-actin promoter activity through the Rho signaling pathway
Zhao, X.-H., Laschinger, C. A., Arora, P. D., Szászi, K., Kapùs, A., & McCulloch, C. A. (2007) · Journal of Cell Science · doi:10.1242/jcs.001586 · Cited by 325 · see citing works
Self-citationJenkins, G. R. (2006) · Journal of Clinical Investigation · doi:10.1172/jci27183 · Cited by 314 · see citing works
Control of Mechanotransduction by Molecular Clutch Dynamics
Elósegui-Artola, A., Trepat, X., & Roca‐Cusachs, P. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.01.008 · Cited by 314 · see citing works
The α <sub>v</sub> β <sub>1</sub> 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 · see citing works
Diverse origins of the myofibroblast—implications for kidney fibrosis
Falke, L. L., Gholizadeh, S., Goldschmeding, R., Kok, R. J., & Nguyen, T. Q. (2015) · Nature Reviews Nephrology · doi:10.1038/nrneph.2014.246 · Cited by 297 · see citing works
Second harmonic imaging and scoring of collagen in fibrotic tissues
Strupler, M., Pena, A., Hernest, M., Tharaux, P., Martin, J. L., Beaurepaire, E., & Schanne‐Klein, M. (2007) · Optics Express · doi:10.1364/oe.15.004054 · Cited by 274 · see citing works
Shintani, Y., Fukumoto, Y., Chaika, N. V., Svoboda, R. A., Wheelock, M. J., & Johnson, K. R. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200708137 · Cited by 268 · see citing works
Kumar, A., Ouyang, M., van den Dries, K., McGhee, E. J., Tanaka, K., Anderson, M. D., Groisman, A., Goult, B. T., Anderson, K. I., & Schwartz, M. A. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201510012 · Cited by 256 · see citing works
Focal adhesion kinase modulates tension signaling to control actin and focal adhesion dynamics
Schöber, M., Raghavan, S., Nikolova, M., Polak, L., Pasolli, H. A., Beggs, H. E., Reichardt, L. F., & Fuchs, E. V. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200608010 · Cited by 253 · see citing works
The integrin–collagen connection – a glue for tissue repair?
Zeltz, C., & Gullberg, D. (2016) · Journal of Cell Science · doi:10.1242/jcs.180992 · Cited by 245 · see citing works
Horowitz, J. C., Rogers, D. S., Sharma, V., Vittal, R., White, E. S., Cui, Z., & Thannickal, V. J. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.10.001 · Cited by 241 · see citing works
Extracellular matrix: The driving force of mammalian diseases
Iozzo, R. V., & Gubbiotti, M. A. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.03.023 · Cited by 236 · see citing works
Sodek, J. (1977) · Archives of Oral Biology · doi:10.1016/0003-9969(77)90095-4 · Cited by 233 · see citing works
Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution
von der Ecken, J., Heissler, S. M., Pathan-Chhatbar, S., Manstein, D. J., & Raunser, S. (2016) · Nature · doi:10.1038/nature18295 · Cited by 228 · see citing works
Hinz, B., Gabbiani, G., & Chaponnier, C. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200201049 · Cited by 226 · see citing works
Self-citationβ- and γ-cytoplasmic actins display distinct distribution and functional diversity
Dugina, V. B., Zwaenepoel, I., Gabbiani, G., Clément, S., & Chaponnier, C. (2009) · Journal of Cell Science · doi:10.1242/jcs.041970 · Cited by 225 · see citing works
The origin of fibrogenic myofibroblasts in fibrotic liver
Kisseleva, T. (2017) · Hepatology · doi:10.1002/hep.28948 · Cited by 224 · see citing works
Prestress in the extracellular matrix sensitizes latent TGF-β1 for activation
Klingberg, F., Chow, M. L., Koehler, A., Boo, S., Buscemi, L., Quinn, T. M., Costell, M., Alman, B. A., Genot, E. M., & Hinz, B. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201402006 · Cited by 222 · see citing works
Self-citationMartin, K., Pritchett, J. P., Llewellyn, J., Mullan, A. F., Athwal, V. S., Dobie, R., Harvey, E., Zeef, L. A. H., Farrow, S. N., Streuli, C. H., et al. (2016) · Nature Communications · doi:10.1038/ncomms12502 · Cited by 220 · see citing works
Lysophosphatidic acid as a lipid mediator with multiple biological actions
Aikawa, S., Hashimoto, T., Kano, K., & Aoki, J. (2014) · The Journal of Biochemistry · doi:10.1093/jb/mvu077 · Cited by 215 · see citing works
Stretch-induced Activation of Transforming Growth Factor-β1 in Pulmonary Fibrosis
Froese, A. R., Shimbori, C., Bellaye, P.-S., Inman, M., Obex, S., Fatima, S., Jenkins, G., Gauldie, J., Ask, K., & Kolb, M. (2016) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201508-1638oc · Cited by 214 · see citing works
Xu, M. Y., Porte, J., Knox, A. J., Weinreb, P. H., Maher, T. M., Violette, S. M., McAnulty, R. J., Sheppard, D., & Jenkins, G. R. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.080160 · Cited by 212 · see citing works
Expression of α-Smooth Muscle Actin Determines the Fate of Mesenchymal Stromal Cells
Talele, N. P., Fradette, J., Davies, J. E., Kapùs, A., & Hinz, B. (2015) · Stem Cell Reports · doi:10.1016/j.stemcr.2015.05.004 · Cited by 210 · see citing works
Self-citationVinculin controls talin engagement with the actomyosin machinery
Atherton, P., Stutchbury, B., Wang, D.-Y., Jethwa, D., Tsang, R., Meiler-Rodriguez, E., Wang, P., Bate, N., Zent, R., Barsukov, I., et al. (2015) · Nature Communications · doi:10.1038/ncomms10038 · Cited by 210 · see citing works
Integrin-mediated regulation of TGFβ in fibrosis
Henderson, N. C., & Sheppard, D. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.10.005 · Cited by 209 · see citing works
Discoidin domain receptors in disease
Borza, C. M., & Pozzi, A. (2013) · Matrix Biology · doi:10.1016/j.matbio.2013.12.002 · Cited by 205 · see citing works
Johnson, L. A., Rodansky, E. S., Haak, A. J., Larsen, S. D., Neubig, R. R., & Higgins, P. (2013) · Inflammatory Bowel Diseases · doi:10.1097/01.mib.0000437615.98881.31 · Cited by 198 · see citing works
Tension, contraction and tissue morphogenesis
Heer, N. C., & Martin, A. C. (2017) · Development · doi:10.1242/dev.151282 · Cited by 195 · see citing works
Therapeutic approaches to control tissue repair and fibrosis: Extracellular matrix as a game changer
Walraven, M., & Hinz, B. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.02.020 · Cited by 194 · see citing works
Self-citationFarndale, R. W., Lisman, T., Bihan, D. G., Hamaia, S. W., Smerling, C., Pugh, N., Konitsiotis, A. D., Leitinger, B., de Groot, P. G., Jarvis, G. E., et al. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360241 · Cited by 193 · see citing works
Distinct focal adhesion protein modules control different aspects of mechanotransduction
Stutchbury, B., Atherton, P., Tsang, R., Wang, D., & Ballestrem, C. (2017) · Journal of Cell Science · doi:10.1242/jcs.195362 · Cited by 190 · see citing works
Long-range self-organization of cytoskeletal myosin II filament stacks
Hu, S., Dasbiswas, K., Guo, Z., Tee, Y.-H., Thiagarajan, V., Hersen, P., Chew, T., Safran, S. A., Zaidel‐Bar, R., & Bershadsky, A. D. (2017) · Nature Cell Biology · doi:10.1038/ncb3466 · Cited by 183 · see citing works
Jiang, D., Correa‐Gallegos, D., Christ, S., Stefańska, A., Liu, J., Ramesh, P., Rajendran, V., Santis, M. M. D., Wagner, D. E., & Rinkevich, Y. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0073-8 · Cited by 182 · see citing works
α11β1 Integrin Recognizes the GFOGER Sequence in Interstitial Collagens
Zhang, W., Käpylä, J., Puranen, J. S., Knight, C. G., Tiger, C., Pentikäinen, O. T., Johnson, M. S., Farndale, R. W., Heino, J., & Gullberg, D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210313200 · Cited by 180 · see citing works
Matrix Stiffness: the Conductor of Organ Fibrosis
Santos, A., & Lagares, D. (2018) · Current Rheumatology Reports · doi:10.1007/s11926-018-0710-z · Cited by 179 · see citing works
The inner workings of stress fibers − from contractile machinery to focal adhesions and back
Livne, A., & Geiger, B. (2016) · Journal of Cell Science · doi:10.1242/jcs.180927 · Cited by 178 · see citing works
The collagen receptor subfamily of the integrins
White, D. J., Puranen, S., Johnson, M. S., & Heino, J. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2003.08.016 · Cited by 176 · see citing works
Shephard, P., Martin, G. E. M., Smola, S., Brunner, G., Krieg, T. M., & Smola, H. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63764-9 · Cited by 176 · see citing works
Architecture shapes contractility in actomyosin networks
Koenderink, G. H., & Paluch, E. K. (2018) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2018.01.015 · Cited by 175 · see citing works
Asano, Y., Ihn, H., Yamane, K., Jinnin, M., & Tamaki, K. (2006) · The American Journal of Pathology · doi:10.2353/ajpath.2006.041306 · Cited by 175 · see citing works
Expression of integrin β1 by fibroblasts is required for tissue repair in vivo
Liu, S., Shiwen, X., Blumbach, K., Eastwood, M., Denton, C. P., Eckes, B., Krieg, T., Abraham, D., & Leask, A. (2010) · Journal of Cell Science · doi:10.1242/jcs.070672 · Cited by 172 · see citing works
Molecular and tissue alterations of collagens in fibrosis
Ricard‐Blum, S., Baffet, G., & Théret, N. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.02.004 · Cited by 170 · see citing works
Klingberg, F., Chau, G., Walraven, M., Boo, S., Koehler, A., Chow, M. L., Olsen, A. L., Im, M., Lodyga, M., Wells, R. G., et al. (2018) · Journal of Cell Science · doi:10.1242/jcs.201293 · Cited by 169 · see citing works
Self-citationTropomyosin Isoforms Specify Functionally Distinct Actin Filament Populations In Vitro
Gateva, G., Kremneva, E., Reindl, T., Kotila, T., Kogan, K., Gressin, L., Gunning, P. W., Manstein, D. J., Michelot, A., & Lappalainen, P. (2017) · Current Biology · doi:10.1016/j.cub.2017.01.018 · Cited by 168 · see citing works
The perivascular origin of pathological fibroblasts
Di Carlo, S. E., & Peduto, L. (2018) · Journal of Clinical Investigation · doi:10.1172/jci93558 · Cited by 164 · see citing works
Sisson, T. H., Ajayi, I. O., Subbotina, N., Dodi, A. E., Rodansky, E. S., Chibucos, L. N., Kim, K. K., Keshamouni, V. G., White, E. S., Zhou, Y., et al. (2015) · American Journal Of Pathology · doi:10.1016/j.ajpath.2014.12.005 · Cited by 160 · see citing works
CCN2 is required for bleomycin‐induced skin fibrosis in mice
Liu, S., Shiwen, X., Abraham, D., & Leask, A. (2010) · Arthritis & Rheumatism · doi:10.1002/art.30074 · Cited by 156 · see citing works
Chen, H., Qu, J., Huang, X., Kurundkar, A., Zhu, L., Yang, N., Venado, A. E., Ding, Q., Liu, G., Antony, V. B., et al. (2016) · Nature Communications · doi:10.1038/ncomms12564 · Cited by 153 · see citing works
Xu, H., Bihan, D. G., Chang, F., Huang, P. H., Farndale, R. W., & Leitinger, B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052209 · Cited by 150 · see citing works
Tojkander, S., Gateva, G., Husain, A., Krishnan, R., & Lappalainen, P. (2015) · eLife · doi:10.7554/elife.06126 · Cited by 149 · see citing works
Mechanisms of Lung Fibrosis Resolution
Glasser, S. W., Hagood, J. S., Wong, S. S., Taype, C. A., Madala, S. K., & Hardie, W. D. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2016.01.018 · Cited by 148 · see citing works
Speight, P., Kofler, M., Szászi, K., & Kapus, A. (2016) · Nature Communications · doi:10.1038/ncomms11642 · Cited by 144 · see citing works
Velasquez, L. S., Sutherland, L. B., Liu, Z., Grinnell, F., Kamm, K. E., Schneider, J. W., Olson, E. N., & Small, E. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1316764110 · Cited by 142 · see citing works
YAP1 Is a Driver of Myofibroblast Differentiation in Normal and Diseased Fibroblasts
Piersma, B., de Rond, S., Werker, P. M. N., Boo, S., Hinz, B., van Beuge, M. M., & Bank, R. A. (2015) · The American Journal of Pathology · doi:10.1016/j.ajpath.2015.08.011 · Cited by 135 · see citing works
Self-citationDiscoidin Domain Receptor 1 Null Mice Are Protected against Hypertension-Induced Renal Disease
Flamant, M., Placier, S., Rodenas, A., Curat, C. A., Vogel, W. F., Chatziantoniou, C., & Dussaule, J. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006060677 · Cited by 128 · see citing works
Luchsinger, L. L., Patenaude, C. A., Smith, B. D., & Layne, M. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.276931 · Cited by 127 · see citing works
Mechanical Stress Is Required for High-Level Expression of Connective Tissue Growth Factor
Schild, C., & Trüeb, B. (2002) · Experimental Cell Research · doi:10.1006/excr.2001.5458 · Cited by 126 · see citing works
Vittal, R., Horowitz, J. C., Moore, B. B., Zhang, H., Martínez, F. J., Toews, G. B., Standiford, T. J., & Thannickal, V. J. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)62260-2 · Cited by 126 · see citing works
Crider, B. J., Risinger, G. M., Haaksma, C. J., Howard, E. W., & Tomasek, J. J. (2011) · Journal of Investigative Dermatology · doi:10.1038/jid.2011.219 · Cited by 124 · see citing works
Regulation of myofibroblast activities: Calcium pulls some strings behind the scene
Castella, L. F., Gabbiani, G., McCulloch, C. A., & Hinz, B. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.04.033 · Cited by 123 · see citing works
Self-citationGuerrot, D., Kerroch, M., Placier, S., Vandermeersch, S., Avillach, C., Mael-Ainin, M., Chatziantoniou, C., & Dussaule, J. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.03.023 · Cited by 122 · see citing works
Sabra, H., Brunner, M., Mandati, V., Wehrle‐Haller, B., Lallemand, D., Ribba, A., Chevalier, G., Guardiola, P., Block, M. R., & Bouvard, D. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.808063 · Cited by 121 · see citing works
Knipe, R. S., Probst, C. K., Lagares, D., Franklin, A., Spinney, J. J., Brazee, P. L., Grasberger, P. E., Zhang, L., Black, K. E., Sakai, N., et al. (2017) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2017-0075oc · Cited by 121 · see citing works
Disruption of Interleukin-1 Signaling Improves the Quality of Wound Healing
Thomay, A. A., Daley, J. M., Sabo, E., Worth, P. J., Shelton, L. J., Harty, M. W., Reichner, J. S., & Albina, J. E. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.080765 · Cited by 119 · see citing works
Actomyosin contractility and collective migration: may the force be with you
Pandya, P., Orgaz, J. L., & Sanz‐Moreno, V. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.06.006 · Cited by 115 · see citing works
A biomechanical perspective on stress fiber structure and function
Kassianidou, E., & Kumar, S. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.04.006 · Cited by 114 · see citing works
Tissue-resident mesenchymal stromal cells: Implications for tissue-specific antifibrotic therapies
Lemos, D. R., & Duffield, J. S. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aan5174 · Cited by 113 · see citing works
Mapping of DDR1 Distribution and Oligomerization on the Cell Surface by FRET Microscopy
Mihai, C., Chotani, M. A., Elton, T. S., & Agarwal, G. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.10.067 · Cited by 112 · see citing works
Myosin II in mechanotransduction: master and commander of cell migration, morphogenesis, and cancer
Aguilar-Cuenca, R., Juanes-García, A., & Vicente‐Manzanares, M. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1439-5 · Cited by 109 · see citing works
LTBPs in biology and medicine: LTBP diseases
Rifkin, D. B., Rifkin, W. J., & Zilberberg, L. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.11.014 · Cited by 109 · see citing works
Structural basis of the collagen‐binding mode of discoidin domain receptor 2
Ichikawa, O., Osawa, M., Nishida, N., Goshima, N., Nomura, N., & Shimada, I. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601833 · Cited by 109 · see citing works
The collagen receptor DDR1 regulates cell spreading and motility by associating with myosin IIA
Huang, Y., Arora, P. D., McCulloch, C. A., & Vogel, W. F. (2009) · Journal of Cell Science · doi:10.1242/jcs.046219 · Cited by 108 · see citing works
Self-citationMatrix-fibrinogen enhances wound closure by increasing both cell proliferation and migration
Rybarczyk, B. J., Lawrence, S. O., & Simpson‐Haidaris, P. J. (2003) · Blood · doi:10.1182/blood-2003-03-0822 · Cited by 106 · see citing works
Discoidin Domain Receptor 1 Mediates Myosin-Dependent Collagen Contraction
Coelho, N. M., Arora, P. D., van Putten, S., Boo, S., Petrovic, P., Lin, A. X., Hinz, B., & McCulloch, C. A. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.01.061 · Cited by 105 · see citing works
Self-citationUnbekandt, M., & Olson, M. F. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1133-6 · Cited by 103 · see citing works
Miranda, M. Z., Bialik, J. F., Speight, P., Dan, Q., Yeung, T., Szászi, K., Pedersen, S. F., & Kapus, A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.780502 · Cited by 103 · see citing works
Mediated nuclear import and export of TAZ and the underlying molecular requirements
Kofler, M., Speight, P., Little, D., Ciano‐Oliveira, C. D., Szászi, K., & Kapùs, A. (2018) · Nature Communications · doi:10.1038/s41467-018-07450-0 · Cited by 102 · see citing works
Muscle-specific stress fibers give rise to sarcomeres in cardiomyocytes
Fenix, A. M., Neininger, A. C., Taneja, N., Hyde, K., Visetsouk, M. R., Garde, R. J., Liu, B., Nixon, B. R., Manalo, A. E., Becker, J. R., et al. (2018) · eLife · doi:10.7554/elife.42144 · Cited by 101 · see citing works
Pathology of collagen degradation. A review.
Pérez-Tamayo, R. (1978) · PubMed Central · Cited by 97 · see citing works
Vesey, D. A., Cheung, C. W. Y., Cuttle, L., Endre, Z. H., Gobe, G. C., & Johnson, D. W. (2002) · PubMed · doi:10.1067/mlc.2002.128468 · Cited by 97 · see citing works
The molecular clutch model for mechanotransduction evolves
Swaminathan, V., & Waterman, C. M. (2016) · Nature Cell Biology · doi:10.1038/ncb3350 · Cited by 96 · see citing works
Mechanosensing in cell–matrix adhesions – Converting tension into chemical signals
Hytönen, V. P., & Wehrle‐Haller, B. (2015) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.10.027 · Cited by 96 · see citing works
A Role of Myocardin Related Transcription Factor-A (MRTF-A) in Scleroderma Related Fibrosis
Shiwen, X., Stratton, R. J., Nikitorowicz-Buniak, J., Abdi, B. A., Ponticos, M., Denton, C. P., Abraham, D., Takahashi, A., Suki, B., Layne, M. D., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126015 · Cited by 95 · see citing works
Shedding of Discoidin Domain Receptor 1 by Membrane-type Matrix Metalloproteinases
Fu, H.-L., Sohail, A., Valiathan, R. R., Wasinski, B. D., Kumarasiri, M., Mahasenan, K. V., Bernardo, M. M., Tokmina‐Roszyk, D., Fields, G. B., Mobashery, S., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.409599 · Cited by 94 · see citing works
TGF-β-induced differentiation into myofibroblasts involves specific regulation of two MKL1 isoforms
Scharenberg, M. A., Pippenger, B. E., Sack, R., Zingg, D., Ferralli, J., Schenk, S., Martín, I., & Chiquet‐Ehrismann, R. (2014) · Journal of Cell Science · doi:10.1242/jcs.142075 · Cited by 93 · see citing works
Shea, B. S., & Tager, A. M. (2012) · Proceedings of the American Thoracic Society · doi:10.1513/pats.201201-005aw · Cited by 92 · see citing works
Matrix mechanics and regulation of the fibroblast phenotype
Hinz, B. (2013) · Periodontology 2000 · doi:10.1111/prd.12030 · Cited by 91 · see citing works
Self-citationDiscoidin domain receptor 1 (DDR1) kinase as target for structure-based drug discovery
Kothiwale, S., Borza, C. M., Lowe, E. W., Pozzi, A., & Meiler, J. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.09.025 · Cited by 91 · see citing works
Penke, L. R. K., Huang, S. K., White, E. S., & Peters-Golden, M. L. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.558130 · Cited by 86 · see citing works
Schulz, J.-N., Plomann, M., Sengle, G., Gullberg, D., Krieg, T. M., & Eckes, B. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.01.025 · Cited by 86 · see citing works
Matrix-driven Myosin II Mediates the Pro-fibrotic Fibroblast Phenotype
Southern, B. D., Grove, L. M., Rahaman, S. O., Abraham, S., Scheraga, R. G., Niese, K. A., Sun, H., Herzog, E. L., Liu, F., Tschumperlin, D. J., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.712380 · Cited by 85 · see citing works
Makino, K., Makino, T., Stawski, L., Lipson, K. E., Leask, A., & Trojanowska, M. E. (2017) · Arthritis Research & Therapy · doi:10.1186/s13075-017-1356-3 · Cited by 84 · see citing works
In the beginning there were soft collagen-cell gels: towards better 3D connective tissue models?
Brown, R. A. (2013) · Experimental Cell Research · doi:10.1016/j.yexcr.2013.07.001 · Cited by 83 · see citing works
Cellular Signaling by Collagen-Binding Integrins
Heino, J. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-94-017-9153-3_10 · Cited by 83 · see citing works
Colonic pericryptal fibroblasts
Sappino, A. P., Dietrich, P. Y., Skalli, O., Widgren, S., & Gabbiani, G. (1989) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/bf00718649 · Cited by 83 · see citing works
Olaso, E., Lin, H., Wang, L., & Friedman, S. L. (2011) · Fibrogenesis & Tissue Repair · doi:10.1186/1755-1536-4-5 · Cited by 82 · see citing works
Chaponnier, C., Goethals, M., Janmey, P. A., Gabbiani, F., Gabbiani, G., & Vandekerckhove, J. S. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.130.4.887 · Cited by 81 · see citing works
Mesenchymal stromal cells and liver fibrosis: a complicated relationship
Haldar, D., Henderson, N. C., Hirschfield, G. M., & Newsome, P. N. (2016) · The FASEB Journal · doi:10.1096/fj.201600433r · Cited by 81 · see citing works
Sakai, N., Chun, J. J. M., Duffield, J. S., Lagares, D., Wada, T., Luster, A. D., & Tager, A. M. (2016) · Kidney International · doi:10.1016/j.kint.2016.09.030 · Cited by 81 · see citing works
Zhao, H., Bian, H., Bu, X., Zhang, S., Zhang, P., Yu, J., Lai, X., Li, D., Zhu, C., Yao, L., et al. (2016) · Molecular Therapy · doi:10.1038/mt.2016.109 · Cited by 80 · see citing works
Juskaite, V., Corcoran, D., & Leitinger, B. (2017) · eLife · doi:10.7554/elife.25716 · Cited by 78 · see citing works
Cytokinesis requires localized β-actin filament production by an actin isoform specific nucleator
Chen, A., Arora, P. D., McCulloch, C. A., & Wilde, A. (2017) · Nature Communications · doi:10.1038/s41467-017-01231-x · Cited by 78 · see citing works
Self-citationContribution of collagen adhesion receptors to tissue fibrosis
Coelho, N. M., & McCulloch, C. A. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2440-8 · Cited by 72 · see citing works
Self-citationA novel mechanism of TGFβ‐induced actin reorganization mediated by Smad proteins and Rho GTPases
Vardouli, L., Vasilaki, E., Papadimitriou, E., Kardassis, D., & Stournaras, C. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06549.x · Cited by 71 · see citing works
MacGillivray, M. K., Cruz, T. F., & McCulloch, C. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003186200 · Cited by 67 · see citing works
Self-citationLatella, G., & Rieder, F. (2017) · Current Opinion in Gastroenterology · doi:10.1097/mog.0000000000000363 · Cited by 67 · see citing works
Sonin, D. L., Wakatsuki, T., Routhu, K. V., Harmann, L. M., Petersen, M., Meyer, J., & Strande, J. L. (2013) · Journal of Cardiovascular Pharmacology and Therapeutics · doi:10.1177/1074248413485434 · Cited by 66 · see citing works
Actomyosin stress fiber mechanosensing in 2D and 3D
Lee, S., & Kumar, S. (2016) · F1000Research · doi:10.12688/f1000research.8800.1 · Cited by 66 · see citing works
Interactions between the discoidin domain receptor 1 and β1 integrin regulate attachment to collagen
Staudinger, L. A., Spano, S. J., Lee, W., Coelho, N. M., Rajshankar, D., Bendeck, M. P., Moriarty, T. J., & McCulloch, C. A. (2013) · Biology Open · doi:10.1242/bio.20135090 · Cited by 64 · see citing works
Self-citationCalcium Homeostasis and Ionic Mechanisms in Pulmonary Fibroblasts
Janssen, L. J., Mukherjee, S., & Ask, K. (2015) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2014-0269tr · Cited by 63 · see citing works
Mammalian nonmuscle myosin II comes in three flavors
Shutova, M. S., & Svitkina, T. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.03.103 · Cited by 62 · see citing works
O’Connor, J. W., Riley, P. N., Nalluri, S. M., Ashar, P. K., & Gomez, E. W. (2014) · Journal of Cellular Physiology · doi:10.1002/jcp.24895 · Cited by 61 · see citing works
Shitomi, Y., Thøgersen, I. B., Ito, N., Leitinger, B., Enghild, J. J., & Itoh, Y. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-10-1463 · Cited by 60 · see citing works
Lin, C., Borensztajn, K., & Spek, C. A. (2017) · Journal of Thrombosis and Haemostasis · doi:10.1111/jth.13623 · Cited by 59 · see citing works
Myosin II isoform co-assembly and differential regulation in mammalian systems
Beach, J. R., & Hammer, J. A. (2015) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.01.012 · Cited by 58 · see citing works
Lo, Y. Y. C., Luo, L., McCulloch, C. A., & Cruz, T. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.12.7059 · Cited by 58 · see citing works
Self-citationVarney, S. D., Betts, C. B., Zheng, R., Wu, L., Hinz, B., Zhou, J., & Water, L. V. D. (2016) · Journal of Cell Science · doi:10.1242/jcs.170589 · Cited by 58 · see citing works
Self-citationMechanical signaling through the discoidin domain receptor 1 plays a central role in tissue fibrosis
Coelho, N. M., & McCulloch, C. A. (2018) · Cell Adhesion & Migration · doi:10.1080/19336918.2018.1448353 · Cited by 56 · see citing works
Self-citationOh, R. S., Haak, A. J., Smith, K. M. J., Ligresti, G., Choi, K. M., Xie, T., Wang, S., Walters, P., Thompson, M. A., Freeman, M., et al. (2018) · Journal of Cell Science · doi:10.1242/jcs.209932 · Cited by 55 · see citing works
Speight, P., Nakano, H., Kelley, T. J., Hinz, B., & Kapùs, A. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-04-0220 · Cited by 54 · see citing works
Self-citationMechanical stability of talin rod controls cell migration and substrate sensing
Rahikainen, R., von Essen, M., Schaefer, M., Qi, L., Azizi, L., Kelly, C., Ihalainen, T. O., Wehrle‐Haller, B., Bastmeyer, M., Huang, C., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-03335-2 · Cited by 54 · see citing works
Htwe, S. S., Cha, B. H., Yue, K., Khademhosseini, A., Knox, A. J., & Ghaemmaghami, A. M. (2017) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2016-0306oc · Cited by 54 · see citing works
Ungefroren, H., Gieseler, F., Kaufmann, R., Settmacher, U., Lehnert, H., & Rauch, B. H. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19061568 · Cited by 54 · see citing works
Turner, N. A. (2013) · Vascular Pharmacology · doi:10.1016/j.vph.2013.06.002 · Cited by 53 · see citing works
Tomasek, J. J., Haaksma, C. J., Schwartz, R. J., & Howard, E. W. (2012) · Wound Repair and Regeneration · doi:10.1111/wrr.12001 · Cited by 50 · see citing works
The Role of Discoidin Domain Receptor 1 in Inflammation, Fibrosis and Renal Disease
Dorison, A., Dussaule, J., & Chatziantoniou, C. (2017) · The Nephron journals/Nephron journals · doi:10.1159/000479119 · Cited by 49 · see citing works
Smooth muscle actin isoforms: A tug of war between contraction and compliance
Arnoldi, R., Hiltbrunner, A., Dugina, V. B., Tille, J., & Chaponnier, C. (2013) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2013.06.002 · Cited by 48 · see citing works
Clément, S., Hinz, B., Dugina, V. B., Gabbiani, G., & Chaponnier, C. (2005) · Journal of Cell Science · doi:10.1242/jcs.01732 · Cited by 46 · see citing works
Self-citationBhadriraju, K., Chung, K., Spurlin, T. A., Haynes, R. J., Elliott, J. T., & Plant, A. L. (2009) · Biomaterials · doi:10.1016/j.biomaterials.2009.08.036 · Cited by 45 · see citing works
Integrins and extracellular matrix in mechanotransduction
Ramage, L. (2011) · Cell Health and Cytoskeleton · doi:10.2147/chc.s21829 · Cited by 44 · see citing works
Prunotto, M., Bruschi, M., Gunning, P. W., Gabbiani, G., Weibel, F., Ghiggeri, G. M., Petretto, A., Scaloni, A., Bonello, T., Schevzov, G., et al. (2015) · Cytoskeleton · doi:10.1002/cm.21230 · Cited by 43 · see citing works
Regulation of adipose oestrogen output by mechanical stress
Ghosh, S., Ashcraft, K. A., Jahid, M. J., April, C., Ghajar, C. M., Ruan, J., Wang, H., Foster, M., Hughes, D. C., Ramírez, A. G., et al. (2013) · Nature Communications · doi:10.1038/ncomms2794 · Cited by 42 · see citing works
Song, S., Shackel, N. A., Wang, X. M., Ajami, K., McCaughan, G. W., & Gorrell, M. D. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.11.068 · Cited by 40 · see citing works
Does Breathing Amplify Fibrosis?
Hinz, B., & Suki, B. (2016) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201601-0149ed · Cited by 39 · see citing works
Self-citationYamashiro, S., Gokhin, D. S., Sui, Z., Bergeron, S. E., Rubenstein, P. A., & Fowler, V. M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.555128 · Cited by 39 · see citing works
Riquelme‐Guzmán, C., Contreras, O., & Brandan, E. (2017) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00013.2017 · Cited by 37 · see citing works
Loss of γ-cytoplasmic actin triggers myofibroblast transition of human epithelial cells
Lechuga, S., Baranwal, S., Li, C., Naydenov, N. G., Kuemmerle, J. F., Dugina, V. B., Chaponnier, C., & Ivanov, A. I. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-03-0815 · Cited by 37 · see citing works
Kanangat, S., Postlethwaite, A. E., Higgins, G. C., & Hasty, K. A. (2006) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700097 · Cited by 36 · see citing works
Flagged first, then by citations
2 of the 211 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Transforming growth factor–β in tissue fibrosis
Frangogiannis, N. G. (2019) · The Journal of Experimental Medicine · doi:10.1084/jem.20190103 · Cited by 1,310 · see citing works
Fibroblast and myofibroblast activation in normal tissue repair and fibrosis
Younesi, F. S., Miller, A. E., Barker, T. H., Rossi, F. M. V., & Hinz, B. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00716-0 · Cited by 711 · see citing works
“anti-fibrotic therapies to break this loop, which has evolved multiple redundancies to promote rapid healing of injured tissues at the expense of functionality 72 .”
InfluentialSelf-citationEvasion of apoptosis by myofibroblasts: a hallmark of fibrotic diseases
Hinz, B., & Lagares, D. (2019) · Nature Reviews Rheumatology · doi:10.1038/s41584-019-0324-5 · Cited by 616 · see citing works
Self-citationRole of fibroblasts in wound healing and tissue remodeling on Earth and in space
Cialdai, F., Risaliti, C., & Monici, M. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.958381 · Cited by 373 · see citing works
Pakshir, P., Noskovicova, N., Lodyga, M., Son, D. O., Schuster, R., Goodwin, A., Karvonen, H., & Hinz, B. (2020) · Journal of Cell Science · doi:10.1242/jcs.227900 · Cited by 293 · see citing works
“…recent strategies tackle different components of the TGF-β1 activation machinery, which provide cell- and context-specificity (Akhurst, 2017; de Gramont et al., 2017; Friedman et al., 2013; Ganesh and Massague, 2018; Hinz, 2016c; Huynh et al., 2019; Lodyga and Hinz, 2019; Varga and Pasche, 2009).”
BackgroundSelf-citationThe Role of Myofibroblasts in Physiological and Pathological Tissue Repair
Schuster, R., Younesi, F., Ezzo, M., & Hinz, B. (2023) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041231 · Cited by 232 · see citing works
Self-citationPlatelet-rich plasma accelerates skin wound healing by promoting re-epithelialization
Xu, P., Wu, Y., Zhou, L., Yang, Z., Zhang, X., Hu, X., Yang, J., Wang, M., Wang, B., Luo, G., et al. (2020) · Burns & Trauma · doi:10.1093/burnst/tkaa028 · Cited by 206 · see citing works
“In the middle and late stages, the differentiation of fibroblasts into myofibroblasts gradually increased with the formation of granulation tissue, which will drive the effective contraction of the wound margin [51, 52].”
BackgroundImplant Fibrosis and the Underappreciated Role of Myofibroblasts in the Foreign Body Reaction
Noskovicova, N., Hinz, B., & Pakshir, P. (2021) · Cells · doi:10.3390/cells10071794 · Cited by 184 · see citing works
Self-citationThe inflammatory speech of fibroblasts
Schuster, R., Rockel, J. S., Kapoor, M., & Hinz, B. (2021) · Immunological Reviews · doi:10.1111/imr.12971 · Cited by 174 · see citing works
Self-citationNoskovičová, N., Schuster, R., van Putten, S., Ezzo, M., Koehler, A., Boo, S., Coelho, N. M., Griggs, D. W., Ruminski, P., McCulloch, C. A., et al. (2021) · Nature Biomedical Engineering · doi:10.1038/s41551-021-00722-z · Cited by 173 · see citing works
Self-citationYu, Z., Xu, C., Song, B., Zhang, S., Chen, C., Li, C., & Zhang, S. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04554-0 · Cited by 170 · see citing works
“Some α-SMA-negative myofibroblasts can also contribute to tissue fibrosis by producing stress fibers made up of β-actin [26].”
BackgroundMultipotent stromal cells: One name, multiple identities
Soliman, H., Theret, M., Scott, W., Hill, L., Underhill, T. M., Hinz, B., & Rossi, F. M. V. (2021) · Cell Stem Cell · doi:10.1016/j.stem.2021.09.001 · Cited by 147 · see citing works
Self-citationKeloid disorder: Fibroblast differentiation and gene expression profile in fibrotic skin diseases
Macarak, E. J., Wermuth, P. J., Rosenbloom, J., & Uitto, J. (2020) · Experimental Dermatology · doi:10.1111/exd.14243 · Cited by 142 · see citing works
Condorelli, A. G., Dellambra, E., Logli, E., Zambruno, G., & Castiglia, D. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225707 · Cited by 130 · see citing works
“Following wound re-epithelialization, myofibroblasts are physiologically cleared through cell death via apoptosis or de-activated and converted in a different cell lineage [40].”
BackgroundPassive myocardial mechanical properties: meaning, measurement, models
Emig, R., Zgierski-Johnston, C., Timmermann, V., Taberner, A., Nash, M., Kohl, P., & Peyronnet, R. (2021) · Biophysical Reviews · doi:10.1007/s12551-021-00838-1 · Cited by 115 · see citing works
“…of Engineering, University of Freiburg, Freiburg, Germany Extracellular stiffness affects all cardiac cell types The stiffness of the extracellular environment influences a host of cellular processes, including direction of cell migration, cell division and differentiation (Hinz et al. 2019, Fig.”
BackgroundEmig, R., Knodt, W., Krussig, M. J., Zgierski-Johnston, C. M., Gorka, O., Groß, O., Kohl, P. K., Ravens, U., & Peyronnet, R. (2021) · Cells · doi:10.3390/cells10030663 · Cited by 100 · see citing works
“The mechanical properties of the extracellular matrix (ECM) in particular, act as a driver for a number of cell functions including differentiation, motility, myofibroblast phenoconversion, and collagen production [1].”
BackgroundChiarelli, N., Ritelli, M., Zoppi, N., & Colombi, M. (2019) · Genes · doi:10.3390/genes10080609 · Cited by 82 · see citing works
“During fibroblast-to-myofibroblast transition, a complex mechanochemical signaling is activated involving profibrotic secreted factors such as TGFβ and Wnt and ECM-degrading enzymes and intracellular effectors required for stress fiber contractility [127,131].”
BackgroundHealing the diabetic wound: Unlocking the secrets of genes and pathways
Kamal, R., Awasthi, A., Pundir, M., & Thakur, S. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176645 · Cited by 78 · see citing works
Cellular and Molecular Mechanisms of Wound Repair: From Biology to Therapeutic Innovation
Jin, C., Jin, Y., Ding, Z., Nuch, K. S., Han, M., Shim, J., Chien, P. N., & Heo, C. Y. (2025) · Cells · doi:10.3390/cells14231850 · Cited by 76 · see citing works
“…integrin-and DNA damage response (DDR)-mediated activation of FAK–YAP/TAZ pathways, they sense matrix stiffness, while interacting with type 2 immune signaling, such as interleukin-33 (IL-33), interleukin-4 (IL-4), and interleukin-13 (IL-13) to shape the inflammatory-to-repair transition [74–77].”
Diversity of Fibroblasts and Their Roles in Wound HealingPreprint
Jiang, D., Guo, R., Machens, H., & Rinkevich, Y. (2022) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041222 · Cited by 76 · see citing works
Collagen Fibril Density Modulates Macrophage Activation and Cellular Functions during Tissue Repair
Sapudom, J., Mohamed, W. K. E. A., Garcia‐Sabaté, A., Alatoom, A., Karaman, S., Mahtani, N., & Teo, J. C. M. (2020) · Bioengineering · doi:10.3390/bioengineering7020033 · Cited by 72 · see citing works
“It suggests that a dense fibrillar matrix might act as a negative feedback for myofibroblasts to prevent an excessive production of matrix proteins and remodeling in physiological conditions [74].”
BackgroundCondorelli, A. G., Hachem, M. E., Zambruno, G., Nyström, A., Candi, E., & Castiglia, D. (2021) · Journal of Biomedical Science · doi:10.1186/s12929-021-00732-8 · Cited by 71 · see citing works
“α-SMA, α-smooth muscle actin) and secretion of ECM matricellular proteins [70, 71].”
BackgroundEpithelial–Mesenchymal Transition Mechanisms in Chronic Airway Diseases: A Common Process to Target?
Mottais, A., Riberi, L., Falco, A., Soccal, S., Gohy, S. T., & Rose, V. D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512412 · Cited by 72 · see citing works
Myofibroblast Markers and Microscopy Detection Methods in Cell Culture and Histology
Younesi, F. S., Son, D. O., de Firmino, J. B., & Hinz, B. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1382-5_3 · Cited by 67 · see citing works
Self-citationZinc sulfide nanoparticles improve skin regeneration
Han, B., FANG, W. H., Zhao, S., Yang, Z., & Hoang, B. X. (2020) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2020.102263 · Cited by 60 · see citing works
Astrocyte responses to experimental glaucoma in mouse optic nerve head
Quillen, S. E., Schaub, J. A., Quigley, H. A., Pease, M. E., Korneva, A., & Kimball, E. (2020) · PLoS ONE · doi:10.1371/journal.pone.0238104 · Cited by 57 · see citing works
Arif, S., Attiogbe, E., & Moulin, V. J. (2021) · Wound Repair and Regeneration · doi:10.1111/wrr.12919 · Cited by 55 · see citing works
“A review of what is known about this functionality has been recently published by Hinz et al.(4)”
BackgroundInfluentialEnzymatic cross-linking of collagens in organ fibrosis – resolution and assessment
Pehrsson, M., Mortensen, J. H., Manon‐Jensen, T., Bay‐Jensen, A., Karsdal, M. A., & Davies, M. J. (2021) · Expert Review of Molecular Diagnostics · doi:10.1080/14737159.2021.1962711 · Cited by 55 · see citing works
Cellular crosstalk in fibrosis: Insights into macrophage and fibroblast dynamics
Froom, Z. S. C. S., Callaghan, N. I., & Huyer, L. D. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110203 · Cited by 58 · see citing works
Type III Collagen Regulates Matrix Architecture and Mechanosensing during Wound Healing
Stewart, D. C., Brisson, B. K., Yen, W. K., Liu, Y., Wang, C., Ruthel, G. T., Gullberg, D., Mauck, R. L., Maden, M., Lin Han, B., et al. (2024) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2024.08.013 · Cited by 55 · see citing works
Cardiac Fibroblast to Myofibroblast Phenotype Conversion—An Unexploited Therapeutic Target
Czubryt, M. P. (2019) · Journal of Cardiovascular Development and Disease · doi:10.3390/jcdd6030028 · Cited by 49 · see citing works
“However, it is cell contractility and the production of stress fibers that truly defines the “myo”fibroblast phenotype, as not all cells that secrete increased ECM levels are necessarily myofibroblasts, although increased ECM production appears to be a general hallmark of these cells for the most part [40].”
BackgroundChen, Z., Ezzo, M., Zondag, B., Rakhshani, F., Ma, Y., Hinz, B., & Kumacheva, E. (2023) · Advanced Materials · doi:10.1002/adma.202305964 · Cited by 48 · see citing works
Self-citationEremichev, R. Y., Kulebyakina, M., Alexandrushkina, N. A., Nimiritsky, P., Basalova, N. A., Grigorieva, O., Egiazaryan, M., Dyikanov, D. T., Va, T., & Макаревич, П. И. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.616893 · Cited by 41 · see citing works
“In SCs, mentioned molecular targets comprise a system necessary for mechanosensing, mediating resistance to mechanical forces and subsequent transformation into myofibroblasts (Hinz et al., 2019).”
BackgroundInfluentialVerteporfin inhibits the persistent fibrotic phenotype of lesional scleroderma dermal fibroblasts
Shiwen, X., Racanelli, M., Ali, A., Simon, A., Quesnel, K., Stratton, R. J., & Leask, A. (2021) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-020-00596-x · Cited by 41 · see citing works
Integrin Regulation of CAF Differentiation and Function
DiPersio, C. M., & Water, L. V. D. (2019) · Cancers · doi:10.3390/cancers11050715 · Cited by 38 · see citing works
“As discussed below, roles for specific integrin-ECM interactions in controlling myofibroblast differentiation and ECM rigidity are clear [42,43].”
BackgroundNADPH oxidase 4 is dispensable for skin myofibroblast differentiation and wound healing
Siedlar, A. M., Seredenina, T. S., Faivre, A., Cambet, Y., Stasia, M. J., André‐Lévigne, D., Bochaton‐Piallat, M., Pittet-Cuenod, B. M., de Seigneux, S., Krause, K., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102609 · Cited by 36 · see citing works
Novel approaches to target fibroblast mechanotransduction in fibroproliferative diseases
Ezzo, M., & Hinz, B. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108528 · Cited by 38 · see citing works
Self-citationFibrosis in burns: an overview of mechanisms and therapies
Faour, S., Farahat, M., Aijaz, A., & Jeschke, M. G. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00254.2023 · Cited by 37 · see citing works
Tissue transglutaminase in fibrosis — more than an extracellular matrix cross-linker
Benn, M. C., Weber, W., Klotzsch, E., Viola Vogel, B., & Pot, S. A. (2019) · Current Opinion in Biomedical Engineering · doi:10.1016/j.cobme.2019.06.003 · Cited by 36 · see citing works
Yang, J., Liu, X., Wang, W., Chen, Y., Liu, J., Zhang, Z., Wu, C., Jiang, X., Liang, Y., & Zhang, J. (2022) · Bioelectrochemistry · doi:10.1016/j.bioelechem.2022.108247 · Cited by 35 · see citing works
A story of fibers and stress: Matrix‐embedded signals for fibroblast activation in the skin
Sawant, M., Hinz, B., Schönborn, K., Zeinert, I., Eckes, B., Krieg, T., & Schuster, R. (2021) · Wound Repair and Regeneration · doi:10.1111/wrr.12950 · Cited by 34 · see citing works
“lattices do not experience the strains required to activate into mature myofibroblast phenotypes.(118,122) A comprehensive comparison of human dermal fibroblasts grown in retracting versus strained collagen”
BackgroundInfluentialSelf-citationAhuja, S., & Zaheer, S. (2023) · Cell Biology International · doi:10.1002/cbin.12097 · Cited by 32 · see citing works
“In addition, these cells also express more structural collagen and synthesize cytokines, growth factors, and matrix proteins (Carthy, 2018; Hinz et al., 2019; Klingberg et al., 2013).”
BackgroundSui, J., Pragnère, S., & Kurniawan, N. A. (2025) · Biomaterials Science · doi:10.1039/d5bm00210a · Cited by 32 · see citing works
Chen, Y., Zhang, X., Liu, Z., Yang, J., Chen, C., Wang, J., Yang, Z., He, L., Xu, P., Hu, X., et al. (2021) · Burns & Trauma · doi:10.1093/burnst/tkab004 · Cited by 30 · see citing works
“To our knowledge, moderated collagen coordinates the interaction of growth factors, cytokines and chemokines, which affects cell behavior as a consequence of their binding to specific cell surface receptors or ECM proteins([34,35]).”
BackgroundLiu, Z., Cao, Y., Liu, G., Yin, S., Ma, J., Liu, J., Zhang, M., & Wang, Y. (2019) · Experimental Cell Research · doi:10.1016/j.yexcr.2019.111504 · Cited by 30 · see citing works
Fang, C., Zeng, Z., Ni, B., Wen, X., Fang, Z., Zou, J., & Zhang, G. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1681875 · Cited by 29 · see citing works
“This ECM stiffening further promotes TGF-β1 release and biomechanical activation of myofibroblasts, forming a vicious positive feedback loop that drives fibrosis progression (Hinz et al., 2019; Hinz, 2009).”
Squecco, R., Chellini, F., Idrizaj, E., Tani, A., Garella, R., Pancani, S., Pavan, P., Bambi, F., Zecchi‐Orlandini, S., & Sassoli, C. (2020) · Cells · doi:10.3390/cells9051199 · Cited by 29 · see citing works
“Obviously, the in vitro experimentation eliminates many paracrine/juxtacrine mechanisms, possibly regulating in situ intercellular interactions and cell functionality as well as the mechanical forces exerted by the surrounding microenvironment, including ECM stiffness, affecting cell behavior [16,18,109].”
BackgroundInfluentialAndo, R., Sakai, A., Iida, T., Kataoka, K., Mizutani, Y., & Enomoto, A. (2022) · Cancers · doi:10.3390/cancers14143315 · Cited by 29 · see citing works
“expression is downregulated by a soft substrate, but the detailed mechanisms by which Col1α1 expression is regulated in rCAFs are not well known [35,60].”
BackgroundThe Human Dermis as a Target of Nanoparticles for Treating Skin Conditions
Salazar, J., Carmona, T., Zacconi, F. C. M., Venegas-Yazigi, D. A., Cabello‐Verrugio, C., Choi, W. I., & Vilos, C. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics15010010 · Cited by 29 · see citing works
Pakshir, P., Younesi, F. S., Wootton, K.-A., Battiston, K. G., Whitton, G., Ilagan, B., Louka, D., Statham, M., Mackey, G., Daley, A. B., et al. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2022.121586 · Cited by 28 · see citing works
Self-citationChang, K., Zhang, X., Lin, S., Lin, S., Lin, Y., Akhrymuk, I. V., Lin, S., & Lin, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011152 · Cited by 27 · see citing works
Hamilton, D. W., Walker, J. T., Tinney, D., Grynyshyn, M., El‐Warrak, A. O., Truscott, E. A., & Flynn, L. E. (2021) · Wound Repair and Regeneration · doi:10.1111/wrr.12981 · Cited by 26 · see citing works
Dynamic and static biomechanical traits of cardiac fibrosis
Liu, H., Fan, P., Jin, F., Huang, G., Guo, X., & Xu, F. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.1042030 · Cited by 27 · see citing works
“developing muscle-like features, including formation of contractile actin-myosin bundles (Hinz et al., 2019).”
BackgroundThe role of immunosuppressive myofibroblasts in the aging process and age-related diseases
Salminen, A. (2023) · Journal of Molecular Medicine · doi:10.1007/s00109-023-02360-1 · Cited by 26 · see citing works
“Subsequently, the initiation of the fibrogenic process increases the stiffness of the matrix, thus enhancing myofibroblast differentiation and fibrotic activity [144, 145].”
Myofibroblast Gene Expression Profile after Tooth Extraction in the Rabbit
Marconcini, S., Denaro, M., Cosola, S., Gabriele, M., Toti, P., Mijiritsky, E., Proietti, A., Basolo, F., Giammarinaro, E., & Covani, U. (2019) · Materials · doi:10.3390/ma12223697 · Cited by 24 · see citing works
“Myofibroblasts, like smooth muscle cells and fibroblasts, develop contractile force upon phosphorylation of myosin light chains, which allows the myosin head to interact with actin filaments [12].”
BackgroundDas, S. J., Wishart, T. F. L., Jandeleit-Dahm, K. A. M., & Lovicu, F. J. (2020) · Experimental Eye Research · doi:10.1016/j.exer.2020.107918 · Cited by 24 · see citing works
Kim, S., Lee, H., Kim, J. A., & Park, T. H. (2022) · Biomaterials Advances · doi:10.1016/j.bioadv.2022.212780 · Cited by 24 · see citing works
Li, Z., & Bratlie, K. M. (2021) · Materials Science and Engineering C · doi:10.1016/j.msec.2021.111915 · Cited by 25 · see citing works
Animal and Human Models of Tissue Repair and Fibrosis: An Introduction
Lagares, D., & Hinz, B. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1382-5_20 · Cited by 23 · see citing works
Self-citationKindlin-2 Mediates Mechanical Activation of Cardiac Myofibroblasts
Godbout, E., Son, D. O., Hume, S., Boo, S., Sarrazy, V., Clément, S., Kapùs, A., Wehrle‐Haller, B., Bruckner‐Tuderman, L., Has, C., et al. (2020) · Cells · doi:10.3390/cells9122702 · Cited by 23 · see citing works
“Two main factors control myofibroblast activation: transforming growth factor beta (TGF-β1) and mechanical stress [47,48].”
BackgroundSelf-citationWang, Y., Zhang, Y., Lu, B., Xi, J., Ocansey, D. K. W., Mao, F., Hao, D., & Yan, Y. (2023) · Stem Cells International · doi:10.1155/2023/2828981 · Cited by 23 · see citing works
“TGF-β could induce the transformation of fibroblast phenotype to myofibroblast phenotype, and the process of induction is also the process of tissue fibrosis [22].”
BackgroundLeask, A. (2021) · Wound Repair and Regeneration · doi:10.1111/wrr.12889 · Cited by 22 · see citing works
“fibrotic lesions occurs due to a constitutively activated, feed-forward mechanotransductive (pro-adhesive/contractile) signaling loop.(21)”
BackgroundFocusing on the Native Matrix Proteins in Calcific Aortic Valve Stenosis
Anousakis‐Vlachochristou, N., Athanasiadou, D., Carneiro, K. M. M., & Toutouzas, K. P. (2023) · JACC Basic to Translational Science · doi:10.1016/j.jacbts.2023.01.009 · Cited by 23 · see citing works
Cell-Laden 3D Hydrogels of Type I Collagen Incorporating Bacterial Nanocellulose Fibers
Malandain, N., Sanz-Fraile, H., Farré, R., Otero, J., Roig, A., & Laromaine, A. (2023) · ACS Applied Bio Materials · doi:10.1021/acsabm.3c00126 · Cited by 22 · see citing works
50 Years of Myofibroblasts: How the Myofibroblast Concept Evolved
Gabbiani, G. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1382-5_1 · Cited by 23 · see citing works
Atiba, A. S., Abdo, W. S., Ali, E. K., Abd-Elsalam, M. M., Amer, M. E., Monsef, A. S. A., Taha, R. S., Antar, S. A., & Mahmoud, A. M. (2022) · Biomarkers · doi:10.1080/1354750x.2022.2085800 · Cited by 21 · see citing works
“Additionally, wound healing is mediated by cellular forces generated in the contractile elements of fibroblasts and myofibroblasts (Bainbridge 2013, Hinz et al. 2019).”
BackgroundDing, N., Fu, X., Gui, Q., Wu, M., Niu, Z., Du, A., Liu, J., Wu, H., Wang, Y., Yue, X., et al. (2023) · Advanced Healthcare Materials · doi:10.1002/adhm.202303192 · Cited by 21 · see citing works
A Rodent Model of Hypertrophic Scarring: Splinting of Rat Wounds
Son, D. O., & Hinz, B. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1382-5_27 · Cited by 20 · see citing works
Self-citationSchussler, O., Chachques, J. C., Alifano, M., & Lecarpentier, Y. (2021) · Journal of Cardiovascular Translational Research · doi:10.1007/s12265-021-10154-4 · Cited by 21 · see citing works
Sassoli, C., Nistri, S., Chellini, F., & Bani, D. (2021) · Current Molecular Medicine · doi:10.2174/1566524021666210309113650 · Cited by 20 · see citing works
Matera, D. L., Lee, A. T., Hiraki, H. L., & Baker, B. M. (2021) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-021-00698-5 · Cited by 21 · see citing works
Therapeutic downregulation of neuronal PAS domain 2 (Npas2) promotes surgical skin wound healing
Shibuya, Y., Hokugo, A., Okawa, H., Kondo, T., Khalil, D., Wang, L., Roca, Y., Clements, A., Sasaki, H., Berry, E., et al. (2022) · eLife · doi:10.7554/elife.71074 · Cited by 19 · see citing works
“It is widely known that myofibroblasts that secrete excessive collagen into the ECM are involved in the pathogenesis of hypertrophic scars (1, 9).”
BackgroundInfluentialZhao, J., Yang, S., Xu, Y., Qin, S., Bie, F., Chen, L., Zhou, F., Xie, J., Liu, X., Shu, B., et al. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.04.014 · Cited by 19 · see citing works
Li, C., Peng, Z., Zhou, Y., Su, Y., Bu, P., Meng, X., Li, B., & Xu, Y. (2021) · Bone and Joint Research · doi:10.1302/2046-3758.109.bjr-2020-0421.r2 · Cited by 18 · see citing works
Grigorieva, O., Basalova, N. A., Vigovskiy, M. A., Arbatskiy, M. S., Dyachkova, U., Kulebyakina, M., Kulebyakin, K. Y., Tyurin‐Kuzmin, P. A., Kalinina, N., & Efimenko, A. Y. (2023) · Biomedicines · doi:10.3390/biomedicines11030840 · Cited by 18 · see citing works
“When cultivating MSCs on dECM derived from dermal fibroblasts with the addition of TGFβ-1 for 96 h (F), the number of cells including αSMA in the stress fibers increased in culture, which represents a classic attribute of myofibroblast differentiation (Figure 2A).”
BackgroundInfluentialGenetic Deletion of Polo-Like Kinase 2 Induces a Pro-Fibrotic Pulmonary Phenotype
Kant, T. A., Newe, M., Winter, L., Hoffmann, M., Kämmerer, S., Klapproth, E., Künzel, K., Kühnel, M., Neubert, L., El‐Armouche, A., et al. (2021) · Cells · doi:10.3390/cells10030617 · Cited by 18 · see citing works
“, non-physiological surface rigidity of culture dishes [30,31].”
BackgroundMechanosensing model of fibroblast cells adhered on a substrate with varying stiffness and thickness
Yang, W., Luo, M., Gao, Y., Feng, X., & Chen, J. (2022) · Journal of the Mechanics and Physics of Solids · doi:10.1016/j.jmps.2022.105137 · Cited by 18 · see citing works
Chellini, F., Tani, A., Zecchi‐Orlandini, S., Giannelli, M., & Sassoli, C. (2020) · Applied Sciences · doi:10.3390/app10217878 · Cited by 17 · see citing works
Molecular signaling in biomaterial-induced foreign body response: current perspectives
Rahaman, S. G., Khan, M. I., Sankaran, K. R., & Rahaman, S. O. (2025) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00595.2025 · Cited by 17 · see citing works
Role of integrins in the development of fibrosis in the trabecular meshwork
Faralli, J. A., Filla, M. S., & Peters, D. M. P. (2023) · Frontiers in Ophthalmology · doi:10.3389/fopht.2023.1274797 · Cited by 15 · see citing works
The regenerative journey: exploring stem cell roles from injury detection to tissue repair
Sharifi, M. A., Yasin, N. F., Kamarul, T., & Sharifi, A. M. (2025) · Stem Cell Research & Therapy · doi:10.1186/s13287-025-04609-7 · Cited by 14 · see citing works
“The contraction of these fibers generates tension within the ECM, drawing the wound margins inward and promoting faster closure [41].”
Mendoza, F. A., & Jiménez, S. A. (2021) · Rheumatology · doi:10.1093/rheumatology/keab762 · Cited by 14 · see citing works
Zhang, L., Yan, H., Tai, Y., Xue, Y., Wei, Y., Wang, K., Zhao, Q., Wang, S., Kong, D., & Midgley, A. C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041575 · Cited by 14 · see citing works
“However, the synthesis and deposition of fibrillar collagen I in progressive fibrosis appears to take over the role of the predominant source of ECM mechanical stress and becomes the principal driver of the myofibroblast phenotype [62].”
BackgroundSapao, P., Roberson, E. D. O., Shi, B., Assassi, S., Skaug, B. A., Lee, F., Naba, A., White, B. E. P., Córdova-Fletes, C., Tsou, P., et al. (2022) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2022.08.052 · Cited by 14 · see citing works
Angelini, A., Trial, J., Saltzman, A. B., Malovannaya, A., & Cieslik, K. A. (2023) · iScience · doi:10.1016/j.isci.2023.107283 · Cited by 13 · see citing works
Garvin, A. M., & Katwa, L. C. (2023) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00224.2023 · Cited by 13 · see citing works
Biophysical perspectives to understanding cancer-associated fibroblasts
Devarasou, S., Kang, M., & Shin, J. H. (2024) · APL Bioengineering · doi:10.1063/5.0199024 · Cited by 12 · see citing works
Repurposing mesalazine against cardiac fibrosis in vitro
Hoffmann, M., Kant, T. A., Emig, R., Rausch, J. S. E., Newe, M., Schubert, M., Künzel, K., Winter, L., Klapproth, E., Peyronnet, R., et al. (2020) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-020-01998-9 · Cited by 13 · see citing works
“When fibroblasts are activated, the cytoskeleton is remodeled, which contributes to a number of cell functions (Hinz et al. 2001; Hinz et al. 2019).”
BackgroundGonzález‐Pérez, M., Camasão, D. B., Mantovani, D., Alonso, M., & Rodríguez‐Cabello, J. C. (2021) · Biomaterials Science · doi:10.1039/d0bm02197k · Cited by 13 · see citing works
Nucleocytoplasmic Shuttling of the Mechanosensitive Transcription Factors MRTF and YAP/TAZ
Kofler, M., & Kapùs, A. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1382-5_15 · Cited by 12 · see citing works
Sbrana, F., Chellini, F., Tani, A., Parigi, M., Garella, R., Palmieri, F., Zecchi‐Orlandini, S., Squecco, R., & Sassoli, C. (2024) · Microscopy Research and Technique · doi:10.1002/jemt.24648 · Cited by 11 · see citing works
“In particular, the filamentous structures are referable to (Hinz et al., 2019; Pakshir et al., 2020).”
Schoberleitner, I., Lackner, M., Coraça-Huber, D. C., Augustin, A., Imsirovic, A., Sigl, S., & Wolfram, D. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252111675 · Cited by 11 · see citing works
“The contractile activity of myofibroblasts, driven by sustained TGF-β signaling [40,79], contributes significantly to capsule contraction and rigidity [23,29,86].”
BackgroundEngineered microenvironment for the study of myofibroblast mechanobiology
Xu, Y. D., Koya, R. C., Ask, K., & Zhao, R. (2021) · Wound Repair and Regeneration · doi:10.1111/wrr.12955 · Cited by 12 · see citing works
“Myofibroblasts are mechanosensitive cells that have been shown to contribute to aberrant wound healing through generating high contraction forces and secreting abundant ECM proteins.(1,2) A variety of”
BackgroundEffect of Extracellular Matrix Stiffness on Candesartan Efficacy in Anti-Fibrosis and Antioxidation
Zhu, T., Song, J., Gao, B., Zhang, J., Li, Y., Ye, Z., Zhao, Y., Guo, X., Xu, F., & Li, F. (2023) · Antioxidants · doi:10.3390/antiox12030679 · Cited by 10 · see citing works
“Upon tissue injury, CFs exposed to high strain or ECM stiffness undergo differentiation int myofibroblasts, in which α-SMA is the most used myofibroblast biomarker and represents th activation degree of CFs [34].”
BackgroundWei, S., Chen, P., Tsai, M., Hsu, T., Hsieh, C., Fan, H., Chen, T., Xie, R., Chen, G., & Chen, Y. (2024) · Advanced Healthcare Materials · doi:10.1002/adhm.202303320 · Cited by 10 · see citing works
Tenascins and osteopontin in biological response in cornea
Sumioka, T., Matsumoto, K., Reinach, P. S., & Saika, S. (2023) · The Ocular Surface · doi:10.1016/j.jtos.2023.05.005 · Cited by 10 · see citing works
Yisireyili, M., Wubulikasimu, W., Aili, A., Li, Y., Aziguli, A., Aipire, A., Maimaitiaili, A., Zhang, W., Cao, Z., Abulajiang, M., et al. (2019) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2019.7669 · Cited by 10 · see citing works
A review and empirical findings of fasciae and muscle interactions in low back pain
van Amstel, R. N., Weide, G., Wesselink, E. O., Noten, K., Jacobs, K., Pool‐Goudzwaard, A., & Jaspers, R. T. (2025) · Frontiers in Physiology · doi:10.3389/fphys.2025.1604459 · Cited by 10 · see citing works
“Fibroblasts and myofibroblasts are responsive to mechanical stimuli, particularly through a feedback control system via the extracellular matrix (Hinz et al., 2019).”
InfluentialThe prevalence of Dupuytren’s disease in patients with diabetes mellitus
Ganesan, S., Tantone, R. P., Komatsu, D. E., & Hurst, L. C. (2023) · Communications Medicine · doi:10.1038/s43856-023-00332-7 · Cited by 9 · see citing works
Condorelli, A. G., Nobili, R., Muglia, A., Scarpelli, G., Marzuolo, E., Stefanis, C. D., Rota, R., Diociaiuti, A., Alaggio, R., Castiglia, D., et al. (2024) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2023.10.045 · Cited by 8 · see citing works
- Authors
- Hinz, B., McCulloch, C. A., & Coelho, N. M.
- Affiliations
- University of Toronto (CA)
- Corresponding author
- Coelho, Nuno M.
- Venue
- Experimental Cell Research
- Publisher
- Elsevier BV
- Published
- 2019-06
- Volume
- 379
- Issue
- 1
- Pages
- 119-128
- ISSN
- 0014-4827 (ISSN-L)
- OpenAlex
- W2934133090
- Semantic Scholar
- 6f2d57f6aad8ed5a88713504974535d1eb19f620
- Cited by
- 182
- References
- 211
- Citations by year
- 2026: 23 · 2025: 19 · 2024: 28 · 2023: 27 · 2022: 20 · 2021: 38 · 2020: 14 · 2019: 13
- FWCI
- 2.47
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Experimental Cell Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research CIHR (#375597)
- Canada Foundation for Innovation and Ontario Research Fund (#36050)
- E-Rare Joint Transnational Program ‘Development of Innovative Therapeutic Approaches for Rare Diseases’ (# ERL-138395)
- CMC is supported by a CIHR Operating grant (MOP416228)
- Canada Research Chair in Matrix Dynamics
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Health Sciences › Medicine › Rehabilitation › Wound Healing and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Keywords
- collagen contraction, fibroblast activation, extracellular matrix stiffness, mechanotransduction, actomyosin contractility, fibrosis, tissue remodeling, wound healing
- MeSH terms
- Animals, Collagen, Extracellular Matrix, Fibrosis, Humans, Phenotype, Wound Healing, Myofibroblasts
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