Targeting extracellular matrix stiffness to attenuate disease: from molecular mechanisms to clinical trials
Abstract
Tissues stiffen during aging and during the pathological progression of cancer, fibrosis, and cardiovascular disease. Extracellular matrix stiffness is emerging as a prominent mechanical cue that precedes disease and drives its progression by altering cellular behaviors. Targeting extracellular matrix mechanics, by preventing or reversing tissue stiffening or interrupting the cellular response, is a therapeutic approach with clinical potential. Major drivers of changes to the mechanical properties of the extracellular matrix include phenotypically converted myofibroblasts, transforming growth factor β (TGFβ), and matrix cross-linking. Potential pharmacological interventions to overcome extracellular matrix stiffening are emerging clinically. Aside from targeting stiffening directly, alternative approaches to mitigate the effects of increased matrix stiffness aim to identify and inhibit the downstream cellular response to matrix stiffness. Therapeutic interventions that target tissue stiffening are discussed in the context of their limitations, preclinical drug development efforts, and clinical trials.
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MRG-201 is a synthetic miRNA mimic of miR-29 designed to reduce the expression of collagen and other scar formation related proteins.
“MRG-201 is a synthetic miRNA mimic of miR-29 designed to reduce the expression of collagen and other scar formation related proteins.[238, 241]”
From RNA delivery biomaterials for the treatment of genetic and rare diseases (2019) · cites this paper as [241]
Cites
Tissue Cells Feel and Respond to the Stiffness of Their Substrate
Discher, D. E., Janmey, P., & Wang, Y.-L. (2005) · Science · doi:10.1126/science.1116995 · Cited by 6,382 · see citing works
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 · see citing works
The Nuclear Factor NF- B Pathway in InflammationPreprint
Lawrence, T. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a001651 · Cited by 4,926 · see citing works
Remodelling the extracellular matrix in development and disease
Bonnans, C., Chou, J., & Werb, Z. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3904 · Cited by 4,367 · see citing works
The biology and function of fibroblasts in cancer
Kalluri, R. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.73 · Cited by 4,366 · see citing works
The extracellular matrix at a glance
Frantz, C., Stewart, K. M., & Weaver, V. M. (2010) · Journal of Cell Science · doi:10.1242/jcs.023820 · Cited by 4,334 · see citing works
Tensional homeostasis and the malignant phenotype
Paszek, M. J., Zahir, N., Johnson, K. R., Lakins, J. N., Rozenberg, G. I., Gefen, A., Reinhart-King, C. A., Margulies, S. S., Dembo, M., Boettiger, D., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.08.010 · Cited by 3,941 · see citing works
Self-citationÖzdemir, B. C., Pentcheva-Hoang, T., Carstens, J. L., Zheng, X., Wu, C.-C., Simpson, T. R., Laklai, H., Sugimoto, H., Kahlert, C., Novitskiy, S. V., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.04.005 · Cited by 2,681 · see citing works
Effects of substrate stiffness on cell morphology, cytoskeletal structure, and adhesion
Yeung, T., Georges, P. C., Flanagan, L. A., Marg, B., Ortiz, M., Funaki, M., Zahir, N., Ming, W., Weaver, V., & Janmey, P. A. (2005) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20041 · Cited by 2,325 · 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
The extracellular matrix modulates the hallmarks of cancer
Pickup, M. W., Mouw, J. K., & Weaver, V. M. (2014) · EMBO Reports · doi:10.15252/embr.201439246 · Cited by 2,014 · see citing works
Nuclear Lamin-A Scales with Tissue Stiffness and Enhances Matrix-Directed Differentiation
Swift, J., Ivanovska, I. L., Buxboim, A., Harada, T., Dingal, P. C. D. P., Pinter, J., Pajerowski, J. D., Spinler, K. R., Shin, J., Tewari, M., et al. (2013) · Science · doi:10.1126/science.1240104 · Cited by 1,998 · see citing works
Yu, Q., & Stamenkovic, I. (2000) · PubMed · Cited by 1,952 · see citing works
Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus
Wang, N., Tytell, J. D., & Ingber, D. E. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2594 · Cited by 1,768 · see citing works
Yu, Q., & Stamenkovic, I. (2000) · Genes & Development · doi:10.1101/gad.14.2.163 · Cited by 1,754 · see citing works
Aragona, M., Panciera, T., Manfrin, A., Giulitti, S., Michielin, F., Elvassore, N., Dupont, S., & Piccolo, S. (2013) · Cell · doi:10.1016/j.cell.2013.07.042 · Cited by 1,651 · see citing works
Pegaptanib, a targeted anti-VEGF aptamer for ocular vascular disease
Ng, E. W. M., Shima, D. T., Calias, P., Cunningham, E. T., Guyer, D. R., & Adamis, A. P. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd1955 · Cited by 1,591 · see citing works
Integrin signalling during tumour progression
Guo, W., & Giancotti, F. G. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1490 · Cited by 1,473 · see citing works
Targeting the TGFβ signalling pathway in disease
Akhurst, R. J., & Hata, A. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3810 · Cited by 1,466 · see citing works
Liu-Chittenden, Y., Huang, B., Shim, J. S., Chen, Q., Lee, S.-J., Anders, R. A., Liu, J. O., & Pan, D. (2012) · Genes & Development · doi:10.1101/gad.192856.112 · Cited by 1,452 · see citing works
FAK in cancer: mechanistic findings and clinical applications
Sulzmaier, F. J., Jean, C., & Schlaepfer, D. D. (2014) · Nature Reviews Cancer · doi:10.1038/nrc3792 · Cited by 1,381 · see citing works
Myofibroblast contraction activates latent TGF-β1 from the extracellular matrix
Wipff, P.-J., Rifkin, D. B., Meister, J.-J., & Hinz, B. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704042 · Cited by 1,346 · see citing works
NF-κB in the liver—linking injury, fibrosis and hepatocellular carcinoma
Luedde, T., & Schwabe, R. F. (2011) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2010.213 · Cited by 1,345 · see citing works
Edwards, D. R., Murphy, G., Reynolds, J. J., Whitham, S. E., Docherty, A. J., Angel, P., & Heath, J. K. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02449.x · Cited by 1,221 · see citing works
Biernacka, A., Dobaczewski, M. P., & Frangogiannis, N. G. (2011) · Growth Factors · doi:10.3109/08977194.2011.595714 · Cited by 1,175 · see citing works
Targeting RAS–ERK signalling in cancer: promises and challenges
Samatar, A. A., & Poulikakos, P. I. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4281 · Cited by 1,163 · see citing works
Aortic Stiffness, Blood Pressure Progression, and Incident Hypertension
Kaess, B. M., Rong, J., Larson, M. G., Hamburg, N. M., Vita, J. A., Levy, D. A., Benjamin, E. J., Vasan, R. S., & Mitchell, G. F. (2012) · JAMA · doi:10.1001/2012.jama.10503 · Cited by 1,086 · see citing works
Is NF-κB a good target for cancer therapy? Hopes and pitfalls
Baud, V., & Karin, M. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2781 · Cited by 1,059 · see citing works
Stupp, R., Hegi, M. E., Gorlia, T., Erridge, S. C., Perry, J., Hong, Y.-K., Aldape, K. D., Lhermitte, B., Pietsch, T., Grujicic, D., et al. (2014) · The Lancet Oncology · doi:10.1016/s1470-2045(14)70379-1 · Cited by 1,052 · see citing works
The MAPK cascades: Signaling components, nuclear roles and mechanisms of nuclear translocation
Plotnikov, A. N., Zehorai, E., Procaccia, S., & Seger, R. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.12.012 · Cited by 990 · see citing works
Dynamic molecular processes mediate cellular mechanotransduction
Hoffman, B. D., Grashoff, C., & Schwartz, M. A. (2011) · Nature · doi:10.1038/nature10316 · Cited by 956 · see citing works
Wei, S. C., Fattet, L., Tsai, J. H., Guo, Y., Pai, V. H., Majeski, H. E., Chen, A. C., Sah, R. L., Taylor, S. S., Engler, A. J., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3157 · Cited by 934 · see citing works
Regulating Rho GTPases and their regulators
Hodge, R. G., & Ridley, A. J. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.67 · Cited by 903 · see citing works
Connective-tissue growth factor (CTGF) modulates cell signalling by BMP and TGF-β
Abreu, J. G., Ketpura, N. I., Reversade, B., & Robertis, E. M. D. (2002) · Nature Cell Biology · doi:10.1038/ncb826 · Cited by 901 · 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
Is there new hope for therapeutic matrix metalloproteinase inhibition?
Vandenbroucke, R. E., & Libert, C. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4390 · Cited by 840 · see citing works
Metabolic control of YAP and TAZ by the mevalonate pathway
Sorrentino, G., Ruggeri, N., Specchia, V., Cordenonsi, M., Mano, M., Dupont, S., Manfrin, A., Ingallina, E., Sommaggio, R., Piazza, S., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb2936 · Cited by 779 · 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
Integrins and cancer: regulators of cancer stemness, metastasis, and drug resistance
Seguin, L., Desgrosellier, J. S., Weis, S. M., & Cheresh, D. A. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.12.006 · Cited by 685 · 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
Tissue Stiffness Dictates Development, Homeostasis, and Disease Progression
Handorf, A. M., Zhou, Y., Halanski, M. A., & Li, W. (2015) · Organogenesis · doi:10.1080/15476278.2015.1019687 · Cited by 647 · see citing works
Rac and Rho GTPases in cancer cell motility control
Parri, M., & Chiarugi, P. (2010) · Cell Communication and Signaling · doi:10.1186/1478-811x-8-23 · Cited by 641 · see citing works
A Peptide Mimicking VGLL4 Function Acts as a YAP Antagonist Therapy against Gastric Cancer
Jiao, S., Wang, H., Shi, Z., Dong, A., Zhang, W., Song, X., He, F., Wang, Y., Zhang, Z., Wang, W., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.01.010 · Cited by 605 · see citing works
Evolving therapies for liver fibrosis
Schuppan, D., & Kim, Y. O. (2013) · Journal of Clinical Investigation · doi:10.1172/jci66028 · Cited by 596 · see citing works
Pleiotropic effects of statin therapy: molecular mechanisms and clinical results
Wang, C., Liu, P., & Liao, J. K. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2007.11.004 · Cited by 593 · see citing works
The rationale for targeting the LOX family in cancer
Barker, H. E., Cox, T. R., & Erler, J. T. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3319 · Cited by 592 · see citing works
Increased stiffness of the rat liver precedes matrix deposition: implications for fibrosis
Georges, P. C., Hui, J.-J., Gombos, Z., McCormick, M. E., Wang, A. Y., Uemura, M., Mick, R., Janmey, P. A., Furth, E. E., & Wells, R. G. (2007) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00032.2007 · Cited by 577 · see citing works
Lipson, K. E., Wong, C., Teng, Y., & Spong, S. M. (2012) · Fibrogenesis & Tissue Repair · doi:10.1186/1755-1536-5-s1-s24 · Cited by 576 · see citing works
Recent trends in cardiovascular mortality in the United States and public health goals.
Sidney, S., Quesenberry, C. P., Jaffe, M. G., Sorel, M., Nguyen-Huynh, M. N., Kushi, L. H., Go, A. S., & Rana, J. S. (2016) · JAMA Cardiology · doi:10.1001/jamacardio.2016.1326 · Cited by 569 · see citing works
Cell-ECM traction force modulates endogenous tension at cell–cell contacts
Maruthamuthu, V., Sabass, B., Schwarz, U. S., & Gardel, M. L. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011123108 · Cited by 520 · see citing works
Morris, J. C., Tan, A. R., Olencki, T. E., Shapiro, G. I., Dezube, B. J., Reiss, M., Hsu, F. J., Berzofsky, J. A., & Lawrence, D. P. (2014) · PLoS ONE · doi:10.1371/journal.pone.0090353 · Cited by 487 · see citing works
Arora, P. D., Narani, N., & McCulloch, C. A. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65334-5 · Cited by 465 · see citing works
Gene Expression Profiles Distinguish Idiopathic Pulmonary Fibrosis from Hypersensitivity Pneumonitis
Selman, M., Pardo, A., Barrera, L., Estrada, A., Watson, S. R., Wilson, K., Aziz, N. A., Kaminski, N., & Zlotnik, A. (2005) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200504-644oc · Cited by 455 · see citing works
3D collagen alignment limits protrusions to enhance breast cancer cell persistence
Riching, K. M., Cox, B. L., Salick, M. R., Pehlke, C., Riching, A. S., Ponik, S. M., Bass, B. R., Crone, W. C., Jiang, Y., Weaver, A. M., et al. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.10.035 · Cited by 446 · see citing works
Age-related vascular stiffening: causes and consequences
Kohn, J. C., Lampi, M. C., & Reinhart-King, C. A. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00112 · Cited by 440 · see citing works
Self-citationFAK signaling in human cancer as a target for therapeutics
Lee, B. Y., Timpson, P., Horvath, L. G., & Daly, R. J. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.10.001 · Cited by 431 · see citing works
Schiller, H. B., Hermann, M.-R., Polleux, J., Vignaud, T., Zanivan, S. R., Friedel, C. C., Sun, Z., Raducanu, A., Gottschalk, K., Théry, M., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2747 · Cited by 430 · see citing works
Matrix stiffening promotes a tumor vasculature phenotype
Bordeleau, F., Mason, B. N., Lollis, E. M., Mazzola, M. C., Zanotelli, M. R., Somasegar, S., Califano, J. P., Montague, C. R., LaValley, D. J., Huynh, J., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1613855114 · Cited by 419 · see citing works
Self-citationThe Hippo pathway effector YAP controls mouse hepatic stellate cell activation
Mannaerts, I., Leite, S. B., Verhulst, S., Claerhout, S., Eysackers, N., Thoen, L. F. R., Hoorens, A., Reynaert, H., Halder, G., & van Grunsven, L. A. (2015) · Journal of Hepatology · doi:10.1016/j.jhep.2015.04.011 · Cited by 410 · see citing works
Age-Related Intimal Stiffening Enhances Endothelial Permeability and Leukocyte Transmigration
Huynh, J., Nishimura, N., Rana, K., Peloquin, J. M., Califano, J. P., Montague, C. R., King, M. R., Schaffer, C. B., & Reinhart‐King, C. A. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002761 · Cited by 403 · see citing works
Self-citationCellular Traction Stresses Increase with Increasing Metastatic Potential
Kraning-Rush, C. M., Califano, J. P., & Reinhart‐King, C. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032572 · Cited by 393 · see citing works
Self-citationDoes This Patient Have Breast Cancer?
Barton, M. B., Harris, R., & Fletcher, S. W. (1999) · JAMA · doi:10.1001/jama.282.13.1270 · Cited by 371 · see citing works
The Rho GEFs LARG and GEF-H1 regulate the mechanical response to force on integrins
Guilluy, C., Swaminathan, V., García‐Mata, R., O’Brien, E. T., Superfine, R., & Burridge, K. (2011) · Nature Cell Biology · doi:10.1038/ncb2254 · Cited by 369 · see citing works
Verdine, G. L., & Walensky, L. D. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-2184 · Cited by 362 · see citing works
Uribarri, J., Peppa, Μ., Cai, W., Goldberg, T., Lu, M. M., He, C., & Vlassara, H. (2003) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000051593.41395.b9 · Cited by 331 · see citing works
Arterial Stiffening Precedes Systolic Hypertension in Diet-Induced Obesity
Weisbrod, R. M., Shiang, T., Al Sayah, L., Fry, J. L., Bajpai, S., Reinhart-King, C. A., Lob, H. E., Santhanam, L., Mitchell, G., Cohen, R. A., et al. (2013) · Hypertension · doi:10.1161/hypertensionaha.113.01744 · Cited by 317 · see citing works
Self-citationThe 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
Targeting Nuclear Factor-Kappa B to Overcome Resistance to Chemotherapy
Godwin, P., Baird, A., Heavey, S., Barr, M. P., O'Byrne, K. J., & Gately, K. A. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00120 · Cited by 302 · see citing works
MMPs as therapeutic targets—Still a viable option?
Fingleton, B. (2007) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2007.06.006 · Cited by 280 · see citing works
Raghu, G., Brown, K. K., Collard, H. R., Cottin, V., Gibson, K. F., Kaner, R. J., Lederer, D. J., Martinez, F. J., Noble, P. W., Song, J. W., et al. (2017) · The Lancet Respiratory Medicine · doi:10.1016/s2213-2600(16)30421-0 · Cited by 278 · see citing works
Hinz, B. (2005) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2005.09.004 · Cited by 272 · see citing works
Emerging roles of ADAM and ADAMTS metalloproteinases in cancer
Rocks, N., Paulissen, G., Hour, M. E., Quesada, F., Crahay, C., Gueders, M. M., Foidart, J. M., Noël, A., & Cataldo, D. D. (2007) · Biochimie · doi:10.1016/j.biochi.2007.08.008 · Cited by 266 · see citing works
Vennin, C., Chin, V. T., Warren, S. C., Lucas, M. C., Herrmann, D., Magenau, A., Mélénec, P., Walters, S. N., del Monte‐Nieto, G., Conway, J. R. W., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aai8504 · Cited by 264 · see citing works
Monnier, V. M., Mustata, G. T., Biemel, K. M., Reihl, O., LEDERER, M. O., ZHENYU, D., & Sell, D. R. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1333.061 · Cited by 245 · see citing works
Chan, N., Willis, A. D., Kornhauser, N., Ward, M. M., Lee, S. B., Nackos, E., Seo, B. R., Chuang, E., Cigler, T., Moore, A. L., et al. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-16-1326 · Cited by 233 · see citing works
Rational Design of Small Molecule Inhibitors Targeting RhoA Subfamily Rho GTPases
Shang, X., Marchioni, F., Sipes, N. S., Evelyn, C. R., Jerabek‐Willemsen, M., Duhr, S., Seibel, W. L., Wortman, M. D., & Zheng, Y. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.05.009 · Cited by 226 · 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
Liu, S. B., Ikenaga, N., Peng, Z., Sverdlov, D. Y., Greenstein, A., Smith, V., Schuppan, D., & Popov, Y. (2016) · The FASEB Journal · doi:10.1096/fj.14-268425 · Cited by 224 · see citing works
Engagement of αvβ3 Integrin Regulates Proliferation and Apoptosis of Hepatic Stellate Cells
Zhou, X., Murphy, F. R., Gehdu, N., Zhang, J., Iredale, J. P., & Benyon, R. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311668200 · Cited by 219 · see citing works
DeFilippis, R. A., Chang, H., Dumont, N., Rabban, J. T., Chen, Y.-Y., Fontenay, G. V., Berman, H. K., Gauthier, M. L., Zhao, J., Hu, D., et al. (2012) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0107 · Cited by 212 · 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
Phase 1 Study of Anti-CTGF Monoclonal Antibody in Patients with Diabetes and Microalbuminuria
Adler, S. G., Schwartz, S. L., Williams, M. E., Arauz-Pacheco, C., Bolton, W. K., Lee, T. T., Li, D., Neff, T. B., Urquilla, P. R., & Sewell, K. L. (2010) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.09321209 · 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
Benson, A. B., Wainberg, Z. A., Hecht, J. R., Михайлович, В. Д., Dong, H., Bendell, J. C., & Kudrik, F. J. (2017) · The Oncologist · doi:10.1634/theoncologist.2017-0024 · Cited by 198 · see citing works
Targeting FAK in human cancer: from finding to first clinical trials
Golubovskaya, V. (2014) · Frontiers in bioscience · doi:10.2741/4236 · Cited by 197 · see citing works
Cellular mechanosensing: Getting to the nucleus of it all
Fedorchak, G. R., Kaminski, A., & Lammerding, J. (2014) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2014.06.009 · Cited by 191 · see citing works
Kothapalli, D., Liu, S., Bae, Y., Monslow, J., Xu, T., Hawthorne, E. A., Byfield, F. J., Castagnino, P. A., Rao, S. J., Rader, D. J., et al. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.09.018 · Cited by 186 · see citing works
Drug targeting to myofibroblasts: Implications for fibrosis and cancer
Yazdani, S., Bansal, R., & Prakash, J. (2017) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2017.07.010 · Cited by 186 · see citing works
Balza, E., Borsi, L., Allemanni, G., & Zardi, L. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80580-5 · Cited by 181 · see citing works
Raghu, G., Scholand, M. B., de Andrade, J. A., LANCASTER, L. H., Mageto, Y. N., Goldin, J. G., Brown, K. K., Flaherty, K. R., Wencel, M. L., Wanger, J. S., et al. (2016) · European Respiratory Journal · doi:10.1183/13993003.01030-2015 · Cited by 176 · see citing works
Ins and Outs of Kinase DFG Motifs
Treiber, D. K., & Shah, N. P. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.06.001 · Cited by 174 · see citing works
Lysyl Oxidase, a Targetable Secreted Molecule Involved in Cancer Metastasis
Cox, T. R., Gartland, A., & Erler, J. T. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-2306 · Cited by 174 · see citing works
Fibrosis: recent advances in myofibroblast biology and new therapeutic perspectives
Hinz, B., & Gabbiani, G. (2010) · F1000 Biology Reports · doi:10.3410/b2-78 · Cited by 172 · see citing works
MicroRNAs in fibrosis: opportunities and challenges
O’Reilly, S. (2016) · Arthritis Research & Therapy · doi:10.1186/s13075-016-0929-x · Cited by 165 · see citing works
Increased expression of ADAM family members in human breast cancer and breast cancer cell lines
Lendeckel, U., Kohl, J., Arndt, M., Carl‐McGrath, S., Donat, H., & Röcken, C. (2004) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-004-0619-y · Cited by 163 · see citing works
Cal, S., & López-Otı́n, C. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.01.013 · Cited by 160 · see citing works
Kohan, M., Muro, A. F., White, E. S., & Berkman, N. (2010) · The FASEB Journal · doi:10.1096/fj.10-154435 · Cited by 160 · see citing works
Sampson, N., Kozieł, R., Zenzmaier, C., Bubendorf, L., Plas, E., Jansen‐Dürr, P., & Berger, P. (2011) · Molecular Endocrinology · doi:10.1210/me.2010-0340 · Cited by 158 · see citing works
Small-molecule inhibitors targeting G-protein–coupled Rho guanine nucleotide exchange factors
Shang, X., Marchioni, F., Evelyn, C. R., Sipes, N. S., Zhou, X., Seibel, W. L., Wortman, M. D., & Zheng, Y. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1212324110 · Cited by 158 · see citing works
Rho-kinase inhibitors as therapeutics: from pan inhibition to isoform selectivity
Hahmann, C., & Schroeter, T. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0189-x · Cited by 153 · see citing works
Rho Kinases in Cardiovascular Physiology and Pathophysiology
Shi, J., & Wei, L. (2013) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0b013e3182a3718f · Cited by 153 · see citing works
Isaacson, K. J., Jensen, M. M., Subrahmanyam, N. B., & Ghandehari, H. (2017) · Journal of Controlled Release · doi:10.1016/j.jconrel.2017.01.034 · Cited by 149 · see citing works
Santhanam, L., Tuday, E. C., Webb, A. K., Dowzicky, P. M., Kim, J. H., Oh, Y. J., Sikka, G., Kuo, M. M., Halushka, M. K., Macgregor, A. M., et al. (2010) · Circulation Research · doi:10.1161/circresaha.109.215228 · Cited by 141 · see citing works
Hecht, J. R., Benson, A. B., Михайлович, В. Д., Yang, Y., Bendell, J. C., & Verma, U. N. (2017) · The Oncologist · doi:10.1634/theoncologist.2016-0479 · Cited by 135 · see citing works
Couppé, C., Svensson, R. B., Grosset, J.-F., Kovanen, V., Nielsen, R. H., Olsen, M. R., Larsen, J. O., Praet, S., Skovgaard, D. C., Hansen, M., et al. (2014) · AGE · doi:10.1007/s11357-014-9665-9 · Cited by 131 · see citing works
Extracellular Matrix Stiffness Regulates Osteogenic Differentiation through MAPK Activation
Hwang, J.-H., Byun, M. R., Kim, A. R., Kim, K. M., Cho, H. J., Lee, Y. H., Kim, J.-W., Jeong, M. G., Hwang, E. S., & Hong, J. H. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135519 · Cited by 130 · see citing works
Spotlight on ixazomib: potential in the treatment of multiple myeloma
Azab, A. K., Muz, B., Ghazarian, R., Ou, M., Luderer, M. J., & Kusdono, H. D. (2016) · Drug Design Development and Therapy · doi:10.2147/dddt.s93602 · Cited by 130 · see citing works
Overexpression of MMP9 in macrophages attenuates pulmonary fibrosis induced by bleomycin
Cabrera, S., Gaxiola, M., Arreola, J. L., Ramı́rez, R., Jara, P., D'Armiento, J. M., Richards, T. J., Selman, M., & Pardo, A. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.06.022 · Cited by 128 · see citing works
Jia, D., Liu, Z., Deng, N., Tan, T. Z., Huang, R. Y., Taylor‐Harding, B., Cheon, D., Lawrenson, K., Wiedemeyer, W. R., Walts, A. E., et al. (2016) · Cancer Letters · doi:10.1016/j.canlet.2016.09.001 · Cited by 128 · see citing works
Bertrand, A., Ziaei, S., Ehret, C., Duchemin, H., Mamchaoui, K., Bigot, A., Mayer, M., Quijano-Roy, S., Desguerre, I., Lainé, J., et al. (2014) · Journal of Cell Science · doi:10.1242/jcs.144907 · Cited by 127 · see citing works
Novel prospects of statins as therapeutic agents in cancer
Pisanti, S., Picardi, P., Ciaglia, E., D’Alessandro, A., & Bifulco, M. (2014) · Pharmacological Research · doi:10.1016/j.phrs.2014.06.013 · Cited by 126 · 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
Sero, J., Sailem, H., Ardy, R. C., Almuttaqi, H., Zhang, T., & Bakal, C. (2015) · Molecular Systems Biology · doi:10.15252/msb.20145644 · Cited by 123 · see citing works
Yao, Q., Cao, S., Li, C., Mengesha, A., Kong, B., & Wei, M. (2010) · International Journal of Cancer · doi:10.1002/ijc.25506 · Cited by 120 · see citing works
An emerging treatment option for glaucoma: Rho kinase inhibitors
Chang, R. T., & Wang, S. K. (2014) · Clinical ophthalmology · doi:10.2147/opth.s41000 · Cited by 118 · see citing works
Nintedanib: First Global Approval
McCormack, P. L. (2014) · Drugs · doi:10.1007/s40265-014-0335-0 · Cited by 115 · see citing works
Rho kinase proteins--pleiotropic modulators of cell survival and apoptosis.
Street, C. A., & Bryan, B. A. (2011) · PubMed · Cited by 114 · see citing works
Haage, A., & Schneider, I. C. (2014) · The FASEB Journal · doi:10.1096/fj.13-245613 · Cited by 110 · see citing works
Watts, K., Sampson, E. M., Schultz, G. S., & Spiteri, M. A. (2005) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2004-0127oc · Cited by 109 · see citing works
Lietha, D., & Eck, M. J. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003800 · Cited by 108 · see citing works
Combination therapies in oncology
Webster, R. M. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.3 · Cited by 106 · see citing works
Golubovskaya, V., Figel, S. A., Ho, B. T., Johnson, C. P., Yemma, M., Huang, G., Zheng, M., Nyberg, C., Magis, A. T., Ostrov, D. A., et al. (2012) · Carcinogenesis · doi:10.1093/carcin/bgs120 · Cited by 103 · see citing works
Gradually softening hydrogels for modeling hepatic stellate cell behavior during fibrosis regression
Caliari, S. R., Perepelyuk, M., Soulas, E. M., Lee, G. Y., Wells, R. G., & Burdick, J. A. (2016) · Integrative Biology · doi:10.1039/c6ib00027d · Cited by 99 · see citing works
Bordeleau, F., Califano, J. P., Abril, Y. L. N., Mason, B. N., LaValley, D. J., Shin, S. J., Weiss, R. S., & Reinhart‐King, C. A. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1505421112 · Cited by 97 · see citing works
Self-citationSeppen, J., van der Rijt, R., Looije, N., van Til, N. P., Lamers, W. H., & Elferink, R. P. J. O. (2003) · Molecular Therapy · doi:10.1016/s1525-0016(03)00234-x · Cited by 96 · see citing works
Alternative splicing as a biomarker and potential target for drug discovery
Le, K.-Q., Prabhakar, B. S., Hong, W.-J., & Li, L.-C. (2015) · Acta Pharmacologica Sinica · doi:10.1038/aps.2015.43 · Cited by 95 · see citing works
RPEL Proteins Are the Molecular Targets for CCG-1423, an Inhibitor of Rho Signaling
Hayashi, K., Watanabe, B., Nakagawa, Y., Minami, S., & Morita, T. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089016 · Cited by 95 · see citing works
Mone, M. D., Koehne, C., Rediske, J. J., Hughes, T. E., & Valencia, J. (2004) · Diabetologia · doi:10.1007/s00125-004-1392-9 · Cited by 94 · see citing works
Bourd, K., Bonnier, D., Leyme, A., Mari, B. P., Tufféry, P., Samson, M., Ezan, F., Baffet, G., & Théret, N. (2010) · Hepatology · doi:10.1002/hep.24598 · 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
TGFβ stimulated re-epithelialisation is regulated by CTGF and Ras/MEK/ERK signalling
Secker, G. A., Shortt, A. J., Sampson, E. M., Schwarz, Q., Schultz, G. S., & Daniels, J. T. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.09.001 · Cited by 90 · see citing works
Antibody-targeted myofibroblast apoptosis reduces fibrosis during sustained liver injury
Douglass, A., Wallace, K., Parr, R., Park, J., Durward, E., Broadbent, I. D., Barelle, C. J., Porter, A. J., & Wright, M. C. (2008) · Journal of Hepatology · doi:10.1016/j.jhep.2008.01.032 · Cited by 88 · see citing works
New therapeutics for the prevention and reduction of scarring
Occleston, N. L., O’Kane, S., Goldspink, N., & Ferguson, M. W. J. (2008) · Drug Discovery Today · doi:10.1016/j.drudis.2008.08.009 · Cited by 87 · see citing works
Studies on beta‐aminopropionitrile in patients with scleroderma
Keiser, H. R., & Sjoerdsma, A. (1967) · Clinical Pharmacology & Therapeutics · doi:10.1002/cpt196784593 · Cited by 80 · see citing works
Substrate stiffness regulates temporary NF-κB activation via actomyosin contractions
Ishihara, S., Yasuda, M., Harada, I., Mizutani, T., Kawabata, K., & Haga, H. (2013) · Experimental Cell Research · doi:10.1016/j.yexcr.2013.09.018 · Cited by 76 · see citing works
Bai, F., Morcos, F., Cheng, R. R., Jiang, H., & Onuchic, J. N. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1615932113 · Cited by 76 · see citing works
Mimura, Y., Ihn, H., Jinnin, M., Asano, Y., Yamane, K., & Tamaki, K. (2005) · Journal of Investigative Dermatology · doi:10.1111/j.0022-202x.2005.23701.x · Cited by 70 · see citing works
The treatment of idiopathic pulmonary fibrosis
Woodcock, H. V., & Maher, T. M. (2014) · F1000Prime Reports · doi:10.12703/p6-16 · Cited by 63 · see citing works
Targeting the PDGF Signaling Pathway in the Treatment of Non-Malignant Diseases
Heldin, C. (2013) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-013-9484-2 · Cited by 61 · see citing works
Olsen, K. C., Epa, A. P., Kulkarni, A. A., Kottmann, R. M., McCarthy, C. E., Johnson, G. V. W., Thatcher, T. H., Phipps, R. P., & Sime, P. J. (2013) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2013-0092oc · Cited by 58 · 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
Simvastatin Ameliorates Matrix Stiffness-Mediated Endothelial Monolayer Disruption
Lampi, M. C., Faber, C. J., Huynh, J., Bordeleau, F., Zanotelli, M. R., & Reinhart‐King, C. A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0147033 · Cited by 48 · see citing works
Self-citationTransglutaminase inhibitors: a patent review
Keillor, J. W., & Apperley, K. Y.-P. (2015) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2016.1115836 · Cited by 46 · see citing works
Pirfenidone Initiates a New Era in the Treatment of Idiopathic Pulmonary Fibrosis
Selvaggio, A. S., & Noble, P. W. (2015) · Annual Review of Medicine · doi:10.1146/annurev-med-120214-013614 · Cited by 45 · see citing works
Transglutaminase-2: evolution from pedestrian protein to a promising therapeutic target
Agnihotri, N., & Mehta, K. (2016) · Amino Acids · doi:10.1007/s00726-016-2320-2 · Cited by 44 · see citing works
Nenna, A., Spadaccio, C., Lusini, M., Ulianich, L., Chello, M., & Nappi, F. (2016) · Recent Advances in Cardiovascular Drug Discovery (Formerly Recent Patents on Cardiovascular Drug Discovery) · doi:10.2174/1574890110666151104120039 · Cited by 43 · see citing works
Friedman, S., Levy, R., Garrett, W. M., Doval, D., Bondarde, S. A., Sahoo, T., Lokanatha, D., Julka, P. K., Shenoy, K., Nagarkar, R. V., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.sabcs-09-5056 · Cited by 40 · see citing works
3-[2-(Aminomethyl)-5-[(pyridin-4-yl)carbamoyl]phenyl] benzoates as soft ROCK inhibitors
Boland, S., Defert, O., Alen, J., Bourin, A., Castermans, K., Kindt, N., Boumans, N., Panitti, L., de Velde, S. V., Stalmans, I., et al. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.09.040 · Cited by 31 · see citing works
CCR 20th Anniversary Commentary: In the Beginning, There Was PS-341
Teicher, B. A., & Anderson, K. C. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2549 · Cited by 28 · see citing works
Clostridial C3 Toxins Target Monocytes/Macrophages and Modulate Their Functions
Barth, H., Fischer, S., Möglich, A., & Förtsch, C. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00339 · Cited by 27 · see citing works
Daneshpour, N., Griffin, M., Collighan, R. J., & Perrie, Y. (2010) · Journal of drug targeting · doi:10.3109/1061186x.2010.531731 · Cited by 25 · see citing works
Targeting cancer cells using aptamers: cell-SELEX approach and recent advancements
Barman, J. (2015) · RSC Advances · doi:10.1039/c4ra12407c · Cited by 23 · see citing works
A new role for Rab GTPases during early mitotic stages
Das, S., Hehnly, H., & Doxsey, S. (2014) · Small GTPases · doi:10.4161/sgtp.29565 · Cited by 23 · see citing works
Rho GEFs and GAPs: Emerging integrators of extracellular matrix signaling
Kutys, M. L., & Yamada, K. M. (2015) · Small GTPases · doi:10.4161/21541248.2014.989792 · Cited by 19 · see citing works
Maeda, S., Matsui, T., Ojima, A., Suematsu, M., Kaseda, K., Higashimoto, Y., Yamakawa, R., & Yamagishi, S. (2015) · Ophthalmic Research · doi:10.1159/000440768 · Cited by 18 · see citing works
Karna, P., Cao, Z., Oprea, G. M., Cohen, C., Harris, W. B., Waller, E. K., O'Regan, R. M., Wc, W., & Yang, L. P. H. (2009) · Cancer Research · doi:10.1158/0008-5472.sabcs-5056 · Cited by 1 · see citing works
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Therapeutic Targeting of the Tumor Microenvironment
Bejarano, L., Jordão, M. J. C., & Joyce, J. A. (2021) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-1808 · Cited by 1,672 · see citing works
The stiffness of living tissues and its implications for tissue engineering
Guimarães, C. F., Gasperini, L., Marques, A. P., & Reis, R. L. (2020) · Nature Reviews Materials · doi:10.1038/s41578-019-0169-1 · Cited by 1,515 · see citing works
Extracellular matrix and its therapeutic potential for cancer treatment
Huang, J., Zhang, L., Wan, D., Zhou, L., Zheng, S., Lin, S., & Qiao, Y. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00544-0 · Cited by 962 · see citing works
Extracellular matrix-based materials for regenerative medicine
Hussey, G. S., Dziki, J. L., & Badylak, S. F. (2018) · Nature Reviews Materials · doi:10.1038/s41578-018-0023-x · Cited by 844 · see citing works
TGF-β in Hepatic Stellate Cell Activation and Liver Fibrogenesis—Updated 2019
Dewidar, B., Meyer, C., Dooley, S., & Meindl-Beinker, A. N. (2019) · Cells · doi:10.3390/cells8111419 · Cited by 837 · see citing works
Cold and hot tumors: from molecular mechanisms to targeted therapy
Wu, B., Zhang, B., Li, B., Wu, H., & Jiang, M. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01979-x · Cited by 751 · see citing works
Cellular mechanotransduction in health and diseases: from molecular mechanism to therapeutic targets
Di, X., Gao, X., Peng, L., Ai, J., Jin, X., Qi, S., Li, H., Wang, K., & Luo, D. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01501-9 · Cited by 660 · see citing works
Evasion 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
The extracellular matrix and the immune system: A mutually dependent relationship
Sutherland, T. E., Dyer, D. P., & Allen, J. E. (2023) · Science · doi:10.1126/science.abp8964 · Cited by 519 · see citing works
Cellular and molecular mechanisms of kidney fibrosis
Djudjaj, S., & Boor, P. (2018) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2018.06.002 · Cited by 478 · see citing works
Tumor initiation and early tumorigenesis: molecular mechanisms and interventional targets
Zhang, S., Xiao, X., Yi, Y., Wang, X., Zhu, L., Shen, Y., Lin, D., & Wu, C. H. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01848-7 · Cited by 440 · see citing works
Engineered materials for organoid systems
Kratochvil, M. J., Seymour, A. J., Li, T. L., Pașca, S. P., Kuo, C. J., & Heilshorn, S. C. (2019) · Nature Reviews Materials · doi:10.1038/s41578-019-0129-9 · Cited by 413 · see citing works
Janmey, P. A., Fletcher, D. A., & Reinhart‐King, C. A. (2019) · Physiological Reviews · doi:10.1152/physrev.00013.2019 · Cited by 411 · see citing works
Self-citationBachmann, M., Kukkurainen, S., Hytönen, V. P., & Wehrle‐Haller, B. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2018 · Cited by 400 · see citing works
Sleeboom, J. J. F., van Tienderen, G. S., Schenke‐Layland, K., van der Laan, L. J. W., Khalil, A., & Verstegen, M. M. A. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.adg3840 · Cited by 391 · see citing works
Harrison, S. A., Abdelmalek, M. F., Caldwell, S., Shiffman, M. L., Diehl, A. M., Ghalib, R., Lawitz, E. J., Rockey, D. C., Schall, R. A., Jia, C., et al. (2018) · Gastroenterology · doi:10.1053/j.gastro.2018.07.006 · Cited by 384 · see citing works
Targeting lysyl oxidase (LOX) overcomes chemotherapy resistance in triple negative breast cancer
Saatci, Ö., Kaymak, A., Raza, U., Ersan, P. G., Akbulut, Ö., Banister, C. E., Sikirzhytski, V., Tokat, Ü. M., Aykut, G., Ansari, S. A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16199-4 · Cited by 373 · see citing works
Nicolás‐Boluda, A., Vaquero, J., Vimeux, L., Guilbert, T., Ghamry-Barrin, S., Kantari‐Mimoun, C., Ponzo, M., Renault, G., Deptuła, P., Pogoda, K., et al. (2021) · eLife · doi:10.7554/elife.58688 · Cited by 371 · see citing works
Shen, Y., Wang, X., Lu, J., Salfenmoser, M., Wirsik, N. M., Schleußner, N., Imle, A., Valls, A. F., Radhakrishnan, P., Liang, J., et al. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.05.005 · Cited by 337 · see citing works
Mechanisms and impact of altered tumour mechanics
Mohammadi, H., & Sahai, E. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0131-2 · Cited by 336 · see citing works
Targeting the tumor stroma for cancer therapy
Xu, M., Zhang, T., Xia, R., Wei, Y., & Wei, X. (2022) · Molecular Cancer · doi:10.1186/s12943-022-01670-1 · Cited by 322 · see citing works
Mechanoregulation of YAP and TAZ in Cellular Homeostasis and Disease Progression
Cai, X., Wang, K.-C., & Meng, Z. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.673599 · Cited by 311 · see citing works
Maller, O., Drain, A. P., Barrett, A. S., Borgquist, S., Ruffell, B., Zakharevich, I., Pham, T. T. M., Gruosso, T., Kuasne, H., Lakins, J. N., et al. (2020) · Nature Materials · doi:10.1038/s41563-020-00849-5 · Cited by 295 · see citing works
Amargant, F., Manuel, S. L., Tu, Q., Parkes, W. S., Rivas, F., Zhou, L. T., Rowley, J. E., Villanueva, C. E., Hornick, J. E., Shekhawat, G. S., et al. (2020) · Aging Cell · doi:10.1111/acel.13259 · Cited by 280 · see citing works
Multifaceted Design and Emerging Applications of Tissue Adhesives
Ma, Z., Bao, G., & Li, J. (2021) · Advanced Materials · doi:10.1002/adma.202007663 · Cited by 271 · see citing works
Myofibroblasts: Function, Formation, and Scope of Molecular Therapies for Skin Fibrosis
Tai, Y., Woods, E. L., Dally, J., Kong, D., Steadman, R., Moseley, R., & Midgley, A. C. (2021) · Biomolecules · doi:10.3390/biom11081095 · Cited by 244 · see citing works
Zhang, D., Wang, G., Yu, X., Wei, T., Farbiak, L., Johnson, L. T., Taylor, A. M., Xu, J., Hong, Y., Zhu, H., et al. (2022) · Nature Nanotechnology · doi:10.1038/s41565-022-01122-3 · Cited by 243 · see citing works
Mechanical communication in fibrosis progression
Long, Y., Niu, Y., Liang, K., & Du, Y. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2021.10.002 · Cited by 233 · see citing works
The 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
The Extracellular Matrix: Its Composition, Function, Remodeling, and Role in Tumorigenesis
Dzobo, K., & Dandara, C. (2023) · Biomimetics · doi:10.3390/biomimetics8020146 · Cited by 209 · see citing works
Muir, A. J., Levy, C., Janssen, H. L. A., Montano‐Loza, A. J., Shiffman, M. L., Caldwell, S., Luketic, V., Ding, D., Jia, C., McColgan, B. J., et al. (2019) · Hepatology · doi:10.1002/hep.30237 · Cited by 195 · see citing works
Mechanical regulation of myofibroblast phenoconversion and collagen contraction
Hinz, B., McCulloch, C. A., & Coelho, N. M. (2019) · Experimental Cell Research · doi:10.1016/j.yexcr.2019.03.027 · Cited by 182 · see citing works
The 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
Glaviano, A., Lau, H., Carter, L. M., Lee, E. H. C., Lam, H. Y., Okina, E., Tan, D. J. J., Tan, W., Ang, H. L., Carbone, D., et al. (2025) · Journal of Hematology & Oncology · doi:10.1186/s13045-024-01634-6 · Cited by 162 · see citing works
Mechanical Aspects of Angiogenesis
Kretschmer, M., Rüdiger, D., & Zahler, S. (2021) · Cancers · doi:10.3390/cancers13194987 · Cited by 151 · see citing works
Hu, Q., Zhu, Y., Mei, J., Liu, Y. L., & Zhou, G. (2025) · Journal of Hematology & Oncology · doi:10.1186/s13045-025-01717-y · Cited by 151 · see citing works
Lin, P. K., & Davis, G. E. (2023) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.123.318237 · Cited by 145 · see citing works
Li, S., Li, C. R., Zhang, Y., He, X., Chen, X., Zeng, X., Liu, F., Chen, Y., & Chen, J. (2019) · Theranostics · doi:10.7150/thno.35665 · Cited by 143 · see citing works
Zhang, M., Yang, D., Dong, C., Huang, H., Feng, G., Chen, Q., Zheng, Y., Tang, H., Chen, Y., & Jing, X. (2022) · ACS Nano · doi:10.1021/acsnano.2c04630 · Cited by 143 · see citing works
Mechano-therapeutics: Targeting Mechanical Signaling in Fibrosis and Tumor Stroma
Tschumperlin, D. J., & Lagares, D. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107575 · Cited by 142 · see citing works
Methods of Delivering Mechanical Stimuli to Organ-on-a-Chip
Kaarj, K., & Yoon, J. (2019) · Micromachines · doi:10.3390/mi10100700 · Cited by 140 · see citing works
Regulation of cellular senescence by extracellular matrix during chronic fibrotic diseases
Blokland, K. E. C., Pouwels, S. D., Schuliga, M. J., Knight, D. A., & Burgess, J. K. (2020) · Clinical Science · doi:10.1042/cs20190893 · Cited by 129 · see citing works
Xin, Y., Li, K., Huang, M. L., Liang, C., Siemann, D. W., Wu, L., Tan, Y., & Tang, X. (2023) · Oncogene · doi:10.1038/s41388-023-02844-x · Cited by 125 · see citing works
Ferrara, B., Pignatelli, C., Cossutta, M., Citro, A., Courty, J., & Piemonti, L. (2021) · Cancers · doi:10.3390/cancers13174442 · Cited by 121 · see citing works
Towards extracellular matrix normalization for improved treatment of solid tumors
Abyaneh, H. S., Regenold, M., McKee, T. D., Allen, C. J., & Gauthier, M. A. (2020) · Theranostics · doi:10.7150/thno.39995 · Cited by 117 · see citing works
Signaling Mechanisms of Myofibroblastic Activation: Outside-in and Inside-Out
Zent, J. M., & Guo, L. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000493217 · Cited by 115 · see citing works
Nuclear deformation guides chromatin reorganization in cardiac development and disease
Seelbinder, B., Ghosh, S., Schneider, S. E., Scott, A. K., Berman, A. G., Goergen, C. J., Margulies, K. B., Bedi, K. C., Casas, E., Swearingen, A. R., et al. (2021) · Nature Biomedical Engineering · doi:10.1038/s41551-021-00823-9 · Cited by 115 · see citing works
Unravelling cell migration: defining movement from the cell surface
Merino-Casallo, F., Gómez‐Benito, M. J., Hervás-Raluy, S., & García‐Aznar, J. M. (2022) · Cell Adhesion & Migration · doi:10.1080/19336918.2022.2055520 · Cited by 114 · see citing works
Ten Years of Extracellular Matrix Proteomics: Accomplishments, Challenges, and Future Perspectives
Naba, A. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100528 · Cited by 112 · see citing works
Mittelheisser, V., Gensbittel, V., Bonati, L., Li, W., Tang, L., & Goetz, J. G. (2024) · Nature Nanotechnology · doi:10.1038/s41565-023-01535-8 · Cited by 109 · see citing works
Zheng, Y., Zhou, R., Cai, J., Yang, N., Wen, Z., Zhang, Z., Sun, H., Huang, G., Guan, Y., Huang, N., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-23-0025 · Cited by 105 · see citing works
From Design to Clinic: Engineered Nanobiomaterials for Immune Normalization Therapy of Cancer
Saeed, M., Chen, F., Ye, J., Shi, Y., Lammers, T., Geest, B. G. D., Xu, Z. P., & Yu, H. (2021) · Advanced Materials · doi:10.1002/adma.202008094 · Cited by 101 · see citing works
Extracellular matrix requirements for gastrointestinal organoid cultures
Rezakhani, S., Gjorevski, N., & Lutolf, M. P. (2021) · Biomaterials · doi:10.1016/j.biomaterials.2021.121020 · Cited by 100 · see citing works
TAGLN mediated stiffness-regulated ovarian cancer progression via RhoA/ROCK pathway
Xiao, W., Lou, H., Zhou, D., Jia, Y., Li, H., Huang, Q., Ma, J., Yang, Z., Sun, C., Meng, Y., et al. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02091-6 · Cited by 100 · see citing works
Understanding Multicellularity: The Functional Organization of the Intercellular Space
Bich, L., Pradeu, T., & Moreau, J. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.01170 · Cited by 99 · see citing works
The biophysics and mechanics of blood from a materials perspective
Qiu, Y., Myers, D. R., & Lam, W. A. (2019) · Nature Reviews Materials · doi:10.1038/s41578-019-0099-y · Cited by 96 · see citing works
Ewald, C. Y. (2019) · Gerontology · doi:10.1159/000504295 · Cited by 96 · see citing works
Circular RNAs in the tumour microenvironment
Ma, Z., Shuai, Y., Gao, X., Wen, X., & Ji, J. (2020) · Molecular Cancer · doi:10.1186/s12943-019-1113-0 · Cited by 96 · see citing works
Decellularized tissues as platforms for in vitro modeling of healthy and diseased tissues
McCrary, M. W., Bousalis, D., Mobini, S., Song, Y. H., & Schmidt, C. E. (2020) · Acta Biomaterialia · doi:10.1016/j.actbio.2020.05.031 · Cited by 96 · see citing works
Incorporating mechanical strain in organs-on-a-chip: Lung and skin
Guenat, O. T., & Francois Berthiaume, B. (2018) · Biomicrofluidics · doi:10.1063/1.5024895 · Cited by 95 · see citing works
Giussani, M., Triulzi, T., Sozzi, G., & Tagliabue, E. (2019) · Cells · doi:10.3390/cells8020081 · Cited by 95 · see citing works
Yang, J., Wang, P., Zhang, Y., Zhang, M., Sun, Q., Chen, H., Dong, L., Chu, Z., Xue, B., Hoff, W. D., et al. (2024) · Cell stem cell · doi:10.1016/j.stem.2024.09.016 · Cited by 95 · see citing works
Optimized lipid nanoparticles (LNPs) for organ-selective nucleic acids delivery in vivo
Zhang, T., Yin, H., Li, Y., Yang, H., Ge, K., Zhang, J., Yuan, Q., Dai, X., Naeem, A., Weng, Y., et al. (2024) · iScience · doi:10.1016/j.isci.2024.109804 · Cited by 94 · see citing works
Mechanical checkpoint regulates monocyte differentiation in fibrotic niches
Vining, K. H., Marneth, A. E., Adu‐Berchie, K., Grolman, J. M., Tringides, C. M., Liu, Y., Wong, W. J., Pozdnyakova, O., Severgnini, M., Stafford, A. G., et al. (2022) · Nature Materials · doi:10.1038/s41563-022-01293-3 · Cited by 93 · see citing works
Charting the unexplored extracellular matrix in cancer
Filipe, E. C., Chitty, J. L., & Cox, T. R. (2018) · International Journal of Experimental Pathology · doi:10.1111/iep.12269 · Cited by 91 · see citing works
Selman, M., & Pardo, A. (2021) · European Respiratory Journal · doi:10.1183/13993003.04507-2020 · Cited by 91 · see citing works
Engineered Biomaterial Platforms to Study Fibrosis
Davidson, M. D., Burdick, J. A., & Wells, R. G. (2020) · Advanced Healthcare Materials · doi:10.1002/adhm.201901682 · Cited by 90 · see citing works
The aged extracellular matrix and the profibrotic role of senescence-associated secretory phenotype
Mebratu, Y. A., Soni, S., Rosas, L., Rojas, M. M., Horowitz, J. C., & Nho, R. S. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00124.2023 · Cited by 89 · see citing works
Deng, M., Lin, J., Nowsheen, S., Liu, T., Zhao, Y., Villalta, P. W., Sicard, D., Tschumperlin, D. J., Lee, S., Kim, J.-J., et al. (2020) · Science Advances · doi:10.1126/sciadv.abb2630 · Cited by 88 · see citing works
Tiskratok, W., Chuinsiri, N., Limraksasin, P., Kyawsoewin, M., & Jitprasertwong, P. (2025) · Polymers · doi:10.3390/polym17060822 · Cited by 88 · see citing works
Tan, W., Duong, M. T.-Q., Zuo, C., Qin, Y., Zhang, Y., Guo, Y., Hong, Y., Zheng, J. H., & Min, J. (2021) · Molecular Therapy · doi:10.1016/j.ymthe.2021.08.023 · Cited by 87 · see citing works
Taufalele, P., Wang, W., Simmons, A. J., Southard-Smith, A. N., Chen, B., Greenlee, J. D., King, M. R., Lau, K. S., Hassane, D. C., Bordeleau, F., et al. (2022) · Acta Biomaterialia · doi:10.1016/j.actbio.2022.04.031 · Cited by 87 · see citing works
Self-citationCollagen crosslinking: effect on structure, mechanics and fibrosis progression
Kong, W., Lyu, C., Liao, H., & Du, Y. (2021) · Biomedical Materials · doi:10.1088/1748-605x/ac2b79 · Cited by 85 · see citing works
Niche stiffness sustains cancer stemness via TAZ and NANOG phase separation
Liu, X., Ye, Y., Zhu, L., Xiao, X., Zhou, B., Gu, Y., Si, H., Liang, H., Liu, M., Li, J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-35856-y · Cited by 85 · see citing works
Mechanical signatures in cancer metastasis
Agrawal, A., Javanmardi, Y., Watson, S. A., Serwinski, B., Djordjevic, B., Li, W., Aref, A. R., Jenkins, R. W., & Moeendarbary, E. (2025) · npj Biological Physics and Mechanics. · doi:10.1038/s44341-024-00007-x · Cited by 85 · see citing works
The Complex Tumor Microenvironment in Ovarian Cancer: Therapeutic Challenges and Opportunities
Garlisi, B., Lauks, S., Aitken, C., Ogilvie, L. M., Lockington, C., Petrik, D., Eichhorn, J. S., & Petrik, J. (2024) · Current Oncology · doi:10.3390/curroncol31070283 · Cited by 83 · see citing works
RNA delivery biomaterials for the treatment of genetic and rare diseases
Zhao, W., Hou, X., Vick, O. G., & Dong, Y. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2019.119291 · Cited by 82 · see citing works
Cell matrix adhesion in cell migration
Conway, J. R. W., & Jacquemet, G. (2019) · Essays in Biochemistry · doi:10.1042/ebc20190012 · Cited by 82 · see citing works
Hyaluronidase: structure, mechanism of action, diseases and therapeutic targets
Lu, J., Zhao, Z., Pan, L., Wu, H. C., Wang, S., Tong, X., & Wu, S. (2025) · Molecular Biomedicine · doi:10.1186/s43556-025-00299-y · Cited by 82 · see citing works
Puls, T. J., Tan, X., Husain, M., Whittington, C. F., Fishel, M. L., & Voytik‐Harbin, S. L. (2018) · Scientific Reports · doi:10.1038/s41598-018-31138-6 · Cited by 81 · see citing works
Passive stiffness of fibrotic skeletal muscle in mdx mice relates to collagen architecture
Brashear, S. E., Wohlgemuth, R. P., Gonzalez, G., & Smith, L. (2020) · The Journal of Physiology · doi:10.1113/jp280656 · Cited by 78 · see citing works
Vascular stiffening and endothelial dysfunction in atherosclerosis
Hooglugt, A., Klatt, O. C., & Huveneers, S. (2022) · Current Opinion in Lipidology · doi:10.1097/mol.0000000000000852 · Cited by 77 · see citing works
Pradhan, S., & Slater, J. H. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2019.04.022 · Cited by 76 · see citing works
Mahmoud, M. M., Mayer, M., Cancel, L. M., Bartosch, A. M. W., Mathews, R., & Tarbell, J. M. (2020) · Cardiovascular Research · doi:10.1093/cvr/cvaa201 · Cited by 76 · see citing works
Deptuła, P., Łysik, D., Pogoda, K., Cieśluk, M., Namiot, A., Mystkowska, J., Król, G., Głuszek, S., Janmey, P. A., & Bucki, R. (2020) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.0c00975 · Cited by 74 · see citing works
Targeting transforming growth factor-β signaling for enhanced cancer chemotherapy
Chen, J., Ding, Z., Li, S., Liu, S., Xiao, C., Li, Z., Zhang, B., Chen, X., & Yang, X. (2020) · Theranostics · doi:10.7150/thno.51383 · Cited by 73 · see citing works
Targeting extracellular matrix stiffness for cancer therapy
Feng, X., Cao, F., Wu, X., Xie, W., Wang, P., & Jiang, H. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1467602 · Cited by 73 · see citing works
Matrix Mechanics as Regulatory Factors and Therapeutic Targets in Hepatic Fibrosis
Chen, G., Xia, B., Fu, Q., Xiang, H., Wang, F., Chen, Z., & Lv, Y. (2019) · International Journal of Biological Sciences · doi:10.7150/ijbs.37500 · Cited by 72 · see citing works
Injury- and inflammation-driven skin fibrosis: The paradigm of epidermolysis bullosa
Nyström, A., & Bruckner‐Tuderman, L. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.01.016 · Cited by 71 · see citing works
Fluctuation-Based Super-Resolution Traction Force Microscopy
Stubb, A., Laine, R. F., Miihkinen, M., Hamidi, H., Guzmán, C., Henriques, R., Jacquemet, G., & Ivaska, J. (2020) · Nano Letters · doi:10.1021/acs.nanolett.9b04083 · Cited by 70 · see citing works
Specific ECM degradation potentiates the antitumor activity of CAR-T cells in solid tumors
Zheng, R., Shen, K., Liang, S., Lyu, Y., Zhang, S., Dong, H., Li, Y., Han, Y., Zhao, X., Zhang, Y., et al. (2024) · Cellular and Molecular Immunology · doi:10.1038/s41423-024-01228-9 · Cited by 69 · see citing works
Multiscale Mechanobiology in Brain Physiology and Diseases
Procès, A., Luciano, M., Kalukula, Y., Ris, L., & Gabriele, S. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.823857 · Cited by 68 · see citing works
Lyu, C., Kong, W., Liu, Z., Wang, S., Zhao, P., Liang, K., Niu, Y., Yang, W., Xiang, C., Hu, X., et al. (2023) · Nature Biomedical Engineering · doi:10.1038/s41551-023-01019-z · Cited by 67 · see citing works
Staunton, J. R., So, W. Y., Paul, C. D., & Tanner, K. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1814271116 · Cited by 67 · see citing works
Ke, W., Wang, B., Liao, Z., Song, Y., Li, G., Ma, L., Wang, K., Li, S., Hua, W., & Cao, Y. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04590-w · Cited by 66 · see citing works
Chen, H., Qian, Z., Zhang, S., Tang, J. X., Fang, L., Jiang, F., Ge, D., Chang, J., Cao, J., Yang, L., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101774 · Cited by 65 · see citing works
Chronic lung diseases: entangled in extracellular matrix
Burgess, J. K., & Harmsen, M. C. (2022) · European Respiratory Review · doi:10.1183/16000617.0202-2021 · Cited by 65 · see citing works
Progress in the mechanical modulation of cell functions in tissue engineering
Dey, K., Roca, E., Ramorino, G., & Sartore, L. (2020) · Biomaterials Science · doi:10.1039/d0bm01255f · Cited by 64 · see citing works
New insights into the Hippo/YAP pathway in idiopathic pulmonary fibrosis
Sun, M., Sun, Y., Feng, Z., Kang, X., Yang, W., Wang, Y., & Luo, Y. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105635 · Cited by 64 · see citing works
Matrix Stiffness and Colorectal Cancer
Liu, C., Pei, H., & Tan, F. (2020) · OncoTargets and Therapy · doi:10.2147/ott.s231010 · Cited by 63 · see citing works
- Authors
- Lampi, M. C., & Reinhart-King, C. A.
- Affiliations
- Cornell University (US)
- Department of Biomedical Engineering, Vanderbilt University, Nashville, TN 37212, USA.
- Venue
- Science Translational Medicine
- Published
- 2018-01-03
- Volume
- 10
- Issue
- 422
- ISSN
- 1946-6234 (ISSN-L)
- 1946-6242
- OpenAlex
- W2781877987
- Cited by
- 551
- References
- 159
- Citations by year
- 2026: 50 · 2025: 68 · 2024: 57 · 2023: 77 · 2022: 81 · 2021: 69 · 2020: 72 · 2019: 43 · 2018: 32
- FWCI
- 6.09
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science Translational Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation (award333523, 1435755, award333525, 2013155462)
- Ford Foundation (award333526)
- National Heart, Lung, and Blood Institute (award333524, HL127499)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Health Sciences › Medicine › Surgery › Tissue Engineering and Regenerative Medicine
- Physical Sciences › Engineering › Biomedical Engineering › Elasticity and Material Modeling
- Keywords
- extracellular matrix stiffness, tissue stiffening, mechanotransduction, myofibroblasts, TGF-beta, tumor progression, fibrosis, cardiovascular disease, aging, pharmacological interventions, drug development, clinical trials
- MeSH terms
- Animals, Cell Differentiation, Extracellular Matrix, Fibrosis, Humans, Transforming Growth Factor beta, Myofibroblasts
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