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The extracellular matrix as a multitasking player in disease
Abstract
Extracellular matrices (ECM s) are highly specialized and dynamic three‐dimensional (3D) scaffolds into which cells reside in tissues. ECM is composed of a variety of fibrillar components, such as collagens, fibronectin, and elastin, and non‐fibrillar molecules as proteoglycans, hyaluronan, and glycoproteins including matricellular proteins. These macromolecular components are interconnected forming complex networks that actively communicate with cells through binding to cell surface receptors and/or matrix effectors. ECM s exert diverse roles, either providing tissues with structural integrity and mechanical properties essential for tissue functions or regulating cell phenotype and functions to maintain tissue homeostasis. ECM molecular composition and structure vary among tissues, and is markedly modified during normal tissue repair as well as during the progression of various diseases. Actually, abnormal ECM remodeling occurring in pathologic circumstances drives disease progression by regulating cell–matrix interactions. The importance of matrix molecules to normal tissue functions is also highlighted by mutations in matrix genes that give rise to genetic disorders with diverse clinical phenotypes. In this review, we present critical and emerging issues related to matrix assembly in tissues and the multitasking roles for ECM in diseases such as osteoarthritis, fibrosis, cancer, and genetic diseases. The mechanisms underlying the various matrix‐based diseases are also discussed. Research focused on the highly dynamic 3D ECM networks will help to discover matrix‐related causative abnormalities of diseases as well as novel diagnostic tools and therapeutic targets.
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2 retracted
Stigliano, I. D., Puricelli, L., Filmus, J., Sogayar, M. C., Joffé, E. B. D. K., & Peters, M. G. (2008) · Breast Cancer Research and Treatment · doi:10.1007/s10549-008-0009-2 · Cited by 82
RetractedBuchanan, C., Stigliano, I. D., Garay-Malpartida, M., et al. (2009) · Breast Cancer Research and Treatment · doi:10.1007/s10549-009-0362-9 · Cited by 35
RetractedMatrix Metalloproteinases: Regulators of the Tumor Microenvironment
Kessenbrock, K., Plaks, V., & Werb, Z. (2010) · Cell · doi:10.1016/j.cell.2010.03.015 · Cited by 5,151
Tumour exosome integrins determine organotropic metastasis
Hoshino, A., Costa-Silva, B., Shen, T.-L., Rodrigues, G., Hashimoto, A., Tesic Mark, M., Molina, H., Kohsaka, S., Di Giannatale, A., Ceder, S., et al. (2015) · Nature · doi:10.1038/nature15756 · Cited by 5,101
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
Extracellular matrix structure
Theocharis, A. D., Skandalis, S. S., Gialeli, C., & Karamanos, N. K. (2016) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.11.001 · Cited by 2,598
Self-citationMunger, J. S., Huang, X., Kawakatsu, H., Griffiths, M. J. D., Dalton, S. L., Wu, J., Pittet, J.-F., Kaminski, N., Garat, C., Matthay, M. A., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80545-0 · Cited by 2,076
Collagen reorganization at the tumor-stromal interface facilitates local invasion
Provenzano, P. P., Eliceiri, K. W., Campbell, J. M., Inman, D. R., White, J. G., & Keely, P. J. (2006) · BMC Medicine · doi:10.1186/1741-7015-4-38 · Cited by 1,804
Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting
Gialeli, C., Theocharis, A. D., & Karamanos, N. K. (2011) · The FEBS Journal · doi:10.1111/j.1742-4658.2010.07919.x · Cited by 1,607
Self-citationGaggioli, C., Hooper, S., Hidalgo-Carcedo, C., Grosse, R., Marshall, J. F., Harrington, K., & Sahai, E. (2007) · Nature Cell Biology · doi:10.1038/ncb1658 · Cited by 1,589
Every step of the way: integrins in cancer progression and metastasis
Hamidi, H., & Ivaska, J. (2018) · Nature Reviews Cancer · doi:10.1038/s41568-018-0038-z · Cited by 1,493
Fibrosis–a common pathway to organ injury and failure
Rockey, D. C., Bell, P. D., & Hill, J. A. (2015) · New England Journal of Medicine · doi:10.1056/nejmra1300575 · Cited by 1,428
Targeted Disruption of Decorin Leads to Abnormal Collagen Fibril Morphology and Skin Fragility
Danielson, K. G., Baribault, H., Holmes, D. F., Graham, H., Kadler, K. E., & Iozzo, R. V. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.3.729 · Cited by 1,406
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
Aligned Collagen Is a Prognostic Signature for Survival in Human Breast Carcinoma
Conklin, M. W., Eickhoff, J. C., Riching, K. M., Pehlke, C. A., Eliceiri, K. W., Provenzano, P. P., Friedl, A., & Keely, P. J. (2011) · The American Journal of Pathology · doi:10.1016/j.ajpath.2010.11.076 · Cited by 1,285
Proteoglycan form and function: A comprehensive nomenclature of proteoglycans
Iozzo, R. V., & Schaefer, L. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.02.003 · Cited by 1,263
The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development
Sorushanova, A., Delgado, L. M., Wu, Z., Shologu, N., Kshirsagar, A., Raghunath, R., Mullen, A. M., Bayon, Y., Pandit, A., Raghunath, M., et al. (2019) · Advanced Materials · doi:10.1002/adma.201801651 · Cited by 1,151
Carcinoma-produced factors activate myeloid cells through TLR2 to stimulate metastasis
Kim, S., Takahashi, H., Lin, W.-W., Descargues, P., Grivennikov, S., Kim, Y., Luo, J.-L., & Karin, M. (2009) · Nature · doi:10.1038/nature07623 · Cited by 1,100
Barry-Hamilton, V., Spangler, R., Marshall, D., McCauley, S., Rodriguez, H. M., Oyasu, M., Mikels, A., Vaysberg, M., Ghermazien, H., Wai, C., et al. (2010) · Nature Medicine · doi:10.1038/nm.2208 · Cited by 870
Serini, G., Bochaton-Piallat, M.-L., Ropraz, P., Geinoz, A., Borsi, L., Zardi, L., & Gabbiani, G. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.3.873 · Cited by 847
Marini, J. C., Forlino, A., Bächinger, H. P., Bishop, N. J., Byers, P. H., Paepe, A. D., Fassier, F., Fratzl-Zelman, N., Kozloff, K. M., Krakow, D., et al. (2017) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2017.52 · Cited by 842
Kadler, K. E., Baldock, C., Bella, J., & Boot-Handford, R. P. (2007) · Journal of Cell Science · doi:10.1242/jcs.03453 · Cited by 823
A Stem Cell–Based Approach to Cartilage Repair
Johnson, K., Zhu, S., Tremblay, M. S., Payette, J. N., Wang, J., Bouchez, L. C., Meeusen, S., Althage, A., Cho, C. Y., Wu, X., et al. (2012) · Science · doi:10.1126/science.1215157 · Cited by 796
Extracellular control of TGFβ signalling in vascular development and disease
ten Dijke, P., & Arthur, H. M. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2262 · Cited by 778
Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators
Kadler, K. E., Hill, A., & Canty-Laird, E. G. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.06.008 · Cited by 756
Labernadie, A., Kato, T., Brugués, A., Serra-Picamal, X., Derzsi, S., Arwert, E., Weston, A., González-Tarragó, V., Elosegui-Artola, A., Albertazzi, L., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3478 · Cited by 747
Chakravarti, S., Magnuson, T., Lass, J. H., Jepsen, K. J., LaMantia, C., & Carroll, H. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.5.1277 · Cited by 731
The integrin αvβ8 mediates epithelial homeostasis through MT1-MMP–dependent activation of TGF-β1
Mu, D., Cambier, S., Fjellbirkeland, L., Baron, J. L., Munger, J. S., Kawakatsu, H., Sheppard, D., Broaddus, V. C., & Nishimura, S. L. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200109100 · Cited by 729
Zuo, F., Kaminski, N., Eugui, E., Allard, J., Yakhini, Z., Ben-Dor, A., Lollini, L., Morris, D., Kim, Y., DeLustro, B., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092134099 · Cited by 620
Liu, X., Wu, H., Byrne, M., Krane, S., & Jaenisch, R. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.5.1852 · Cited by 614
Targeted disruption of the biglycan gene leads to an osteoporosis-like phenotype in mice
Xu, T., Bianco, P., Fisher, L. W., Longenecker, G., Smith, E., Goldstein, S., Bonadio, J., Boskey, A., Heegaard, A.-M., Sommer, B., et al. (1998) · Nature Genetics · doi:10.1038/1746 · Cited by 612
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 608
Role of COL4A1 in Small-Vessel Disease and Hemorrhagic Stroke
Gould, D. B., Phalan, F. C., van Mil, S. E., Sundberg, J. P., Vahedi, K., Massin, P., Bousser, M. G., Heutink, P., Miner, J. H., Tournier-Lasserve, E., et al. (2006) · New England Journal of Medicine · doi:10.1056/nejmoa053727 · Cited by 581
The nature and biology of basement membranes
Pozzi, A., Yurchenco, P. D., & Iozzo, R. V. (2017) · Matrix Biology · doi:10.1016/j.matbio.2016.12.009 · Cited by 575
Glycosaminoglycans: key players in cancer cell biology and treatment
Afratis, N., Gialeli, C., Nikitovic, D., Tsegenidis, T., Karousou, E., Theocharis, A. D., Pavão, M. S., Tzanakakis, G. N., & Karamanos, N. K. (2012) · The FEBS Journal · doi:10.1111/j.1742-4658.2012.08529.x · Cited by 554
Self-citationCancer-associated fibroblasts promote directional cancer cell migration by aligning fibronectin
Erdogan, B., Ao, M., White, L. M., Means, A. L., Brewer, B. M., Yang, L., Washington, M. K., Shi, C., Franco, O. E., Weaver, A. M., et al. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201704053 · Cited by 552
Fibrotic extracellular matrix activates a profibrotic positive feedback loop
Parker, M. W., Rossi, D., Peterson, M., Smith, K., Sikström, K., White, E. S., Connett, J. E., Henke, C. A., Larsson, O., & Bitterman, P. B. (2014) · Journal of Clinical Investigation · doi:10.1172/jci71386 · Cited by 548
Mutations in Col4a1 Cause Perinatal Cerebral Hemorrhage and Porencephaly
Gould, D. B., Phalan, F. C., Breedveld, G. J., van Mil, S. E., Smith, R. S., Schimenti, J. C., Aguglia, U., van der Knaap, M. S., Heutink, P., & John, S. W. M. (2005) · Science · doi:10.1126/science.1109418 · Cited by 541
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
Durbeej, M. (2010) · Cell and Tissue Research · doi:10.1007/s00441-009-0838-2 · Cited by 500
Gene therapy by skeletal muscle expression of decorin prevents fibrotic disease in rat kidney
Isaka, Y., Brees, D. K., Ikegaya, K., Kaneda, Y., Imai, E., Noble, N. A., & Border, W. A. (1996) · Nature Medicine · doi:10.1038/nm0496-418 · Cited by 482
Fallowfield, J. A., Mizuno, M., Kendall, T. J., Constandinou, C. M., Benyon, R. C., Duffield, J. S., & Iredale, J. P. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.8.5288 · Cited by 479
Biglycan, a Danger Signal That Activates the NLRP3 Inflammasome via Toll-like and P2X Receptors
Babelova, A., Moreth, K., Tsalastra-Greul, W., Zeng-Brouwers, J., Eickelberg, O., Young, M. F., Bruckner, P., Pfeilschifter, J., Schaefer, R. M., Gröne, H.-J., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014266 · Cited by 474
Glypican-3 Promotes the Growth of Hepatocellular Carcinoma by Stimulating Canonical Wnt Signaling
Capurro, M. I., Xiang, Y.-Y., Lobe, C., & Filmus, J. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4244 · Cited by 469
Corsi, A., Xu, T., Chen, X.-D., Boyde, A., Liang, J., Mankani, M., Sommer, B., Iozzo, R. V., Eichstetter, I., Robey, P. G., et al. (2002) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.2002.17.7.1180 · Cited by 465
Krishnan, Y., & Grodzinsky, A. J. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.05.005 · Cited by 443
Keloids: The paradigm of skin fibrosis — Pathomechanisms and treatment
Andrews, J. P., Marttala, J., Macarak, E., Rosenbloom, J., & Uitto, J. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.01.013 · Cited by 433
Glypican-3 as a Serum Marker for Hepatocellular Carcinoma
Capurro, M., & Filmus, J. (2005) · Cancer Research · doi:10.1158/0008-5472.372.65.1 · Cited by 432
Sandy, J. D., Flannery, C. R., Neame, P. J., & Lohmander, L. S. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115742 · Cited by 411
Matrix remodeling by MMPs during wound repair
Rohani, M. G., & Parks, W. C. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.03.002 · Cited by 407
Theocharis, A. D., Skandalis, S. S., Tzanakakis, G. N., & Karamanos, N. K. (2010) · The FEBS Journal · doi:10.1111/j.1742-4658.2010.07800.x · Cited by 403
Self-citationDe Wever, O., Nguyen, Q., Van Hoorde, L., Bracke, M., Bruyneel, E., Gespach, C., & Mareel, M. (2004) · The FASEB Journal · doi:10.1096/fj.03-1110fje · Cited by 402
Yeung, T.-L., Leung, C. S., Wong, K.-K., Samimi, G., Thompson, M. S., Liu, J., Zaid, T. M., Ghosh, S., Birrer, M. J., & Mok, S. C. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-0023 · Cited by 394
Revisiting the matricellular concept
Murphy-Ullrich, J. E., & Sage, E. H. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.07.005 · Cited by 392
Fibronectin, the extracellular glue
Zollinger, A. J., & Smith, M. L. (2017) · Matrix Biology · doi:10.1016/j.matbio.2016.07.011 · Cited by 383
Kleeff, J., Ishiwata, T., Kumbasar, A., Friess, H., Büchler, M. W., Lander, A. D., & Korc, M. (1998) · Journal of Clinical Investigation · doi:10.1172/jci4105 · Cited by 368
Proteoglycan Chemical Diversity Drives Multifunctional Cell Regulation and Therapeutics
Karamanos, N. K., Piperigkou, Z., Theocharis, A. D., Watanabe, H., Franchi, M., Baud, S., Brézillon, S., Götte, M., Passi, A., Vigetti, D., et al. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00354 · Cited by 367
Self-citationCapurro, M. I., Xu, P., Shi, W., Li, F., Jia, A., & Filmus, J. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.03.006 · Cited by 364
Glentis, A., Oertle, P., Mariani, P., Chikina, A., El Marjou, F., Attieh, Y., Zaccarini, F., Lae, M., Loew, D., Dingli, F., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00985-8 · Cited by 363
Mechanical forces regulate the interactions of fibronectin and collagen I in extracellular matrix
Kubow, K. E., Vukmirovic, R., Zhe, L., Klotzsch, E., Smith, M. L., Gourdon, D., Luna, S., & Vogel, V. (2015) · Nature Communications · doi:10.1038/ncomms9026 · Cited by 344
FBN1: The disease-causing gene for Marfan syndrome and other genetic disorders
Sakai, L. Y., Keene, D. R., Renard, M., & De Backer, J. (2016) · Gene · doi:10.1016/j.gene.2016.07.033 · Cited by 342
Cancer-associated fibroblasts lead tumor invasion through integrin-β3–dependent fibronectin assembly
Attieh, Y., Clark, A. G., Grass, C., Richon, S., Pocard, M., Mariani, P., Elkhatib, N., Betz, T., Gurchenkov, B., & Vignjevic, D. M. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201702033 · Cited by 338
McGuire, J. K., Li, Q., & Parks, W. C. (2003) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64318-0 · Cited by 322
Gao, D., Joshi, N., Choi, H., Ryu, S., Hahn, M., Catena, R., Sadik, H., Argani, P., Wagner, P., Vahdat, L. T., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-2905 · Cited by 307
Targeting renal fibrosis: Mechanisms and drug delivery systems
Nastase, M. V., Zeng-Brouwers, J., Wygrecka, M., & Schaefer, L. (2018) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2017.12.019 · Cited by 302
Mice lacking alpha 1 (IX) collagen develop noninflammatory degenerative joint disease.
Fässler, R., Schnegelsberg, P. N., Dausman, J., Shinya, T., Muragaki, Y., McCarthy, M. T., Olsen, B. R., & Jaenisch, R. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.11.5070 · Cited by 301
Extracellular matrix networks in bone remodeling
Alford, A. I., Kozloff, K. M., & Hankenson, K. D. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.05.008 · Cited by 300
Ikenaga, N., Peng, Z.-W., Vaid, K. A., Liu, S. B., Yoshida, S., Sverdlov, D. Y., Mikels-Vigdal, A., Smith, V., Schuppan, D., & Popov, Y. V. (2017) · Gut · doi:10.1136/gutjnl-2016-312473 · Cited by 295
Lotz, M. K. (2010) · Arthritis Research & Therapy · doi:10.1186/ar3046 · Cited by 294
Aggrecan Protects Cartilage Collagen from Proteolytic Cleavage
Pratta, M. A., Yao, W., Decicco, C., Tortorella, M. D., Liu, R.-Q., Copeland, R. A., Magolda, R., Newton, R. C., Trzaskos, J. M., & Arner, E. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303737200 · Cited by 292
Tenascin-C drives persistence of organ fibrosis
Bhattacharyya, S., Wang, W., Morales-Nebreda, L., Feng, G., Wu, M., Zhou, X., Lafyatis, R., Lee, J., Hinchcliff, M., Feghali-Bostwick, C., et al. (2016) · Nature Communications · doi:10.1038/ncomms11703 · Cited by 292
ADAMTS and ADAM metalloproteinases in osteoarthritis – looking beyond the ‘usual suspects’
Yang, C.-Y., Chanalaris, A., & Troeberg, L. (2017) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2017.02.791 · Cited by 291
Matsuda, K., Maruyama, H., Guo, F., Kleeff, J. H., Itakura, J., Matsumoto, Y., Lander, A. D., & Korc, M. (2001) · PubMed · Cited by 289
Syndecans – key regulators of cell signaling and biological functions
Afratis, N. A., Nikitovic, D., Multhaupt, H. A. B., Theocharis, A. D., Couchman, J. R., & Karamanos, N. K. (2017) · The FEBS Journal · doi:10.1111/febs.13940 · Cited by 283
Self-citationADAMTS proteins in human disorders
Mead, T. J., & Apte, S. S. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.06.002 · Cited by 279
Derksen, P. W. B., Keehnen, R. M. J., Evers, L. M., van Oers, M. H. J., Spaargaren, M., & Pals, S. T. (2002) · Blood · doi:10.1182/blood.v99.4.1405 · Cited by 274
Biological interplay between proteoglycans and their innate immune receptors in inflammation
Frey, H., Schroeder, N., Manon‐Jensen, T., Iozzo, R. V., & Schaefer, L. (2013) · The FEBS Journal · doi:10.1111/febs.12145 · Cited by 274
Wiberg, C., Klatt, A. R., Wagener, R., Paulsson, M., Bateman, J. F., Heinegård, D., & Mörgelin, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304638200 · Cited by 267
Shintani, Y., Fukumoto, Y., Chaika, N., Svoboda, R., Wheelock, M. J., & Johnson, K. R. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200708137 · Cited by 267
Delivery of matrix metalloproteinase-1 attenuates established liver fibrosis in the rat
Iimuro, Y., Nishio, T., Morimoto, T., Nitta, T., Stefanovic, B., Choi, S. K., Brenner, D. A., & Yamaoka, Y. (2003) · Gastroenterology · doi:10.1053/gast.2003.50063 · Cited by 263
A type X collagen mutation causes Schmid metaphyseal chondrodysplasia
Warman, M. L., Abbott, M., Apte, S. S., Hefferon, T., McIntosh, I., Cohn, D. H., Hecht, J. T., Olsen, B. R., & Francomano, C. A. (1993) · Nature Genetics · doi:10.1038/ng0993-79 · Cited by 261
The Ehlers–Danlos syndromes, rare types
Brady, A. F., Demirdas, S., Fournel‐Gigleux, S., Ghali, N., Giunta, C., Kapferer‐Seebacher, I., Kosho, T., Mendoza‐Londono, R., Pope, M. F., Rohrbach, M., et al. (2017) · American Journal of Medical Genetics Part C Seminars in Medical Genetics · doi:10.1002/ajmg.c.31550 · Cited by 258
Volk, S. W., Wang, Y., Mauldin, E. A., Liechty, K. W., & Adams, S. L. (2011) · Cells Tissues Organs · doi:10.1159/000322399 · Cited by 257
Matrix modeling and remodeling: A biological interplay regulating tissue homeostasis and diseases
Karamanos, N. K., Theocharis, A. D., Neill, T., & Iozzo, R. V. (2019) · Matrix Biology · doi:10.1016/j.matbio.2018.08.007 · Cited by 254
Self-citationBix, G., Fu, J., Gonzalez, E. M., Macro, L., Barker, A., Campbell, S., Zutter, M. M., Santoro, S. A., Kim, J. K., Höök, M., et al. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200401150 · Cited by 252
Matrix Metalloproteinase 3 Is a Mediator of Pulmonary Fibrosis
Yamashita, C. M., Dolgonos, L., Zemans, R. L., Young, S. K., Robertson, J., Briones, N., Suzuki, T., Campbell, M. N., Gauldie, J., Radisky, D. C., et al. (2011) · The American Journal of Pathology · doi:10.1016/j.ajpath.2011.06.041 · Cited by 247
Sites of Aggrecan Cleavage by Recombinant Human Aggrecanase-1 (ADAMTS-4)
Tortorella, M. D., Pratta, M., Liu, R.-Q., Austin, J., Ross, O. H., Abbaszade, I., Burn, T., & Arner, E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909383199 · Cited by 244
Osteopontin Expression Is Required for Myofibroblast Differentiation
Lenga, Y., Koh, A., Perera, A. S., McCulloch, C. A., Sodek, J., & Zohar, R. (2008) · Circulation Research · doi:10.1161/circresaha.107.160408 · Cited by 241
Troup, S., Njue, C., Kliewer, E. V., Parisien, M., Roskelley, C., Chakravarti, S., Roughley, P. J., Murphy, L. C., & Watson, P. H. (2003) · PubMed · Cited by 240
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
Cancer-Associated Fibroblasts Induce a Collagen Cross-link Switch in Tumor Stroma
Pankova, D., Chen, Y., Terajima, M., Schliekelman, M. J., Baird, B. N., Fahrenholtz, M., Sun, L., Gill, B. J., Vadakkan, T. J., Kim, M. P., et al. (2016) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-15-0307 · Cited by 232
The evolving relationship of wound healing and tumor stroma
Foster, D. S., Jones, R. E., Ransom, R. C., Longaker, M. T., & Norton, J. A. (2018) · JCI Insight · doi:10.1172/jci.insight.99911 · Cited by 223
Provisional matrix: A role for versican and hyaluronan
Wight, T. N. (2017) · Matrix Biology · doi:10.1016/j.matbio.2016.12.001 · Cited by 222
Deshmukh, V., Hu, H., Barroga, C., Bossard, C., KC, S., Dellamary, L., Stewart, J., Chiu, K., Ibanez, M., Pedraza, M., et al. (2018) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2017.08.015 · Cited by 222
Agrin as a Mechanotransduction Signal Regulating YAP through the Hippo Pathway
Chakraborty, S., Njah, K., Pobbati, A. V., Lim, Y. B., Raju, A., Lakshmanan, M., Tergaonkar, V., Lim, C. T., & Hong, W. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.041 · Cited by 220
Deep dermal fibroblasts contribute to hypertrophic scarring
Wang, J., Dodd, C., Shankowsky, H. A., Scott, P. G., & Tredget, E. E. (2008) · Laboratory Investigation · doi:10.1038/labinvest.2008.101 · Cited by 218
Clinical significance of the integrin α6β4 in human malignancies
Stewart, R. L., & O'Connor, K. L. (2015) · Laboratory Investigation · doi:10.1038/labinvest.2015.82 · Cited by 218
van der Slot, A. J., Zuurmond, A.-M., van den Bogaerdt, A. J., Ulrich, M. M. W., Middelkoop, E., Boers, W., Karel Ronday, H., DeGroot, J., Huizinga, T. W. J., & Bank, R. A. (2004) · Matrix Biology · doi:10.1016/j.matbio.2004.06.001 · Cited by 216
A current view of perlecan in physiology and pathology: A mosaic of functions
Gubbiotti, M. A., Neill, T., & Iozzo, R. V. (2017) · Matrix Biology · doi:10.1016/j.matbio.2016.09.003 · Cited by 216
Heparanase regulation of cancer, autophagy and inflammation: new mechanisms and targets for therapy
Sanderson, R. D., Elkin, M., Rapraeger, A. C., Ilan, N., & Vlodavsky, I. (2017) · The FEBS Journal · doi:10.1111/febs.13932 · Cited by 216
Bosse, K. R., Raman, P., Zhu, Z., Lane, M., Martinez, D., Heitzeneder, S., Rathi, K. S., Kendsersky, N. M., Randall, M., Donovan, L., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.08.003 · Cited by 215
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
Van Laer, L., Dietz, H., & Loeys, B. (2014) · Advances in Experimental Medicine and Biology · doi:10.1007/978-94-007-7893-1_7 · Cited by 214
Elastin in lung development and disease pathogenesis
Mecham, R. P. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.01.005 · Cited by 208
Decorin causes autophagy in endothelial cells via Peg3
Buraschi, S., Neill, T., Goyal, A., Poluzzi, C., Smythies, J., Owens, R. T., Schaefer, L., Torres, A., & Iozzo, R. V. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305732110 · Cited by 205
Extracellular vesicles are integral and functional components of the extracellular matrix
Rilla, K., Mustonen, A.-M., Arasu, U. T., Härkönen, K., Matilainen, J., & Nieminen, P. (2019) · Matrix Biology · doi:10.1016/j.matbio.2017.10.003 · Cited by 204
Current and upcoming therapies to modulate skin scarring and fibrosis
Coentro, J. Q., Pugliese, E., Hanley, G., Raghunath, M., & Zeugolis, D. I. (2019) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2018.08.009 · Cited by 204
Glypican‐3: a marker and a therapeutic target in hepatocellular carcinoma
Filmus, J., & Capurro, M. (2013) · The FEBS Journal · doi:10.1111/febs.12126 · Cited by 203
Roles and targeting of the HAS/hyaluronan/CD44 molecular system in cancer
Karousou, E., Misra, S., Ghatak, S., Dobra, K., Götte, M., Vigetti, D., Passi, A., Karamanos, N. K., & Skandalis, S. S. (2017) · Matrix Biology · doi:10.1016/j.matbio.2016.10.001 · Cited by 203
Self-citationProteoglycans remodeling in cancer: Underlying molecular mechanisms
Theocharis, A. D., & Karamanos, N. K. (2019) · Matrix Biology · doi:10.1016/j.matbio.2017.10.008 · Cited by 203
Self-citationZhu, J.-X., Goldoni, S., Bix, G., Owens, R. T., McQuillan, D. J., Reed, C. C., & Iozzo, R. V. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503833200 · Cited by 201
Cysteine cathepsins in extracellular matrix remodeling: Extracellular matrix degradation and beyond
Vizovišek, M., Fonović, M., & Turk, B. (2019) · Matrix Biology · doi:10.1016/j.matbio.2018.01.024 · Cited by 200
Congenital Stromal Dystrophy of the Cornea Caused by a Mutation in the Decorin Gene
Bredrup, C., Knappskog, P. M., Majewski, J., Rødahl, E., & Boman, H. (2005) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.04-0804 · Cited by 199
Santra, M., Mann, D. M., Mercer, E. W., Skorski, T., Calabretta, B., & Iozzo, R. V. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119507 · Cited by 196
Arikawa-Hirasawa, E., Le, A. H., Nishino, I., Nonaka, I., Ho, N. C., Francomano, C. A., Govindraj, P., Hassell, J. R., Devaney, J. M., Spranger, J., et al. (2002) · The American Journal of Human Genetics · doi:10.1086/340390 · Cited by 195
Fogelgren, B., Polgár, N., Szauter, K. M., Újfaludi, Z., Laczkó, R., Fong, K. S. K., & Csiszar, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412979200 · Cited by 191
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 191
Glypican-1 modulates the angiogenic and metastatic potential of human and mouse cancer cells
Aikawa, T., Whipple, C. A., Lopez, M. E., Gunn, J., Young, A., Lander, A. D., & Korc, M. (2008) · Journal of Clinical Investigation · doi:10.1172/jci32412 · Cited by 189
Fibronectin-guided migration of carcinoma collectives
Gopal, S., Veracini, L., Grall, D., Butori, C., Schaub, S., Audebert, S., Camoin, L., Baudelet, E., Radwanska, A., Beghelli-de la Forest Divonne, S., et al. (2017) · Nature Communications · doi:10.1038/ncomms14105 · Cited by 189
Schnittert, J., Bansal, R., Storm, G., & Prakash, J. (2018) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2018.01.020 · Cited by 188
Ehlers-Danlos syndrome, classical type
Bowen, J. M., Sobey, G. J., Burrows, N. P., Colombi, M., Lavallee, M. E., Malfait, F., & Francomano, C. A. (2017) · American Journal of Medical Genetics Part C: Seminars in Medical Genetics · doi:10.1002/ajmg.c.31548 · Cited by 184
Lysyl hydroxylase 2 induces a collagen cross-link switch in tumor stroma
Chen, Y., Terajima, M., Yang, Y., Sun, L., Ahn, Y.-H., Pankova, D., Puperi, D. S., Watanabe, T., Kim, M. P., Blackmon, S. H., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci74725 · Cited by 181
Seidler, D. G., Goldoni, S., Agnew, C., Cardi, C., Thakur, M. L., Owens, R. T., McQuillan, D. J., & Iozzo, R. V. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602853200 · Cited by 180
Sanderson, R. D., Bandari, S. K., & Vlodavsky, I. (2019) · Matrix Biology · doi:10.1016/j.matbio.2017.10.007 · Cited by 180
Induction of cardiac fibroblast lysyl oxidase by TGF-β1 requires PI3K/Akt, Smad3, and MAPK signaling
Voloshenyuk, T. G., Landesman, E. S., Khoutorova, E., Hart, A. D., & Gardner, J. D. (2011) · Cytokine · doi:10.1016/j.cyto.2011.03.024 · Cited by 177
Hu, F., a Dzaye, O. D., Hahn, A., Yu, Y., Scavetta, R. J., Dittmar, G., Kaczmarek, A. K., Dunning, K. R., Ricciardelli, C., Rinnenthal, J. L., et al. (2015) · Neuro-Oncology · doi:10.1093/neuonc/nou324 · Cited by 173
Identification of an Agrin Mutation that Causes Congenital Myasthenia and Affects Synapse Function
Huzé, C., Bauché, S., Richard, P., Chevessier, F., Goillot, E., Gaudon, K., Ben Ammar, A., Chaboud, A., Grosjean, I., Lecuyer, H.-A., et al. (2009) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2009.06.015 · Cited by 172
SPARC Represses E-Cadherin and Induces Mesenchymal Transition during Melanoma Development
Robert, G., Gaggioli, C., Bailet, O., Chavey, C., Abbe, P., Aberdam, E., Sabatié, E., Cano, A., Garcia de Herreros, A., Ballotti, R., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3189 · Cited by 172
Massive aggrecan and versican accumulation in thoracic aortic aneurysm and dissection
Cikach, F. S., Koch, C. D., Mead, T. J., Galatioto, J., Willard, B. B., Emerton, K. B., Eagleton, M. J., Blackstone, E. H., Ramirez, F., Roselli, E. E., et al. (2018) · JCI Insight · doi:10.1172/jci.insight.97167 · Cited by 171
Thomson, J., Singh, M., Eckersley, A., Cain, S. A., Sherratt, M. J., & Baldock, C. (2019) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2018.07.016 · Cited by 170
Yan, W., & Shao, R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601856200 · Cited by 169
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
Gleghorn, L., Ramesar, R., Beighton, P., & Wallis, G. (2005) · The American Journal of Human Genetics · doi:10.1086/444401 · Cited by 168
CCN2 (Connective Tissue Growth Factor) Promotes Fibroblast Adhesion to Fibronectin
Chen, Y., Abraham, D. J., Shi-wen, X., Pearson, J. D., Black, C. M., Lyons, K. M., & Leask, A. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-06-0490 · Cited by 167
New insights into the structure and function of the plasminogen/plasmin system
Law, R. H., Abu-Ssaydeh, D., & Whisstock, J. C. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.10.006 · Cited by 166
Insights into the key roles of proteoglycans in breast cancer biology and translational medicine
Theocharis, A. D., Skandalis, S. S., Neill, T., Multhaupt, H. A. B., Hubo, M., Frey, H., Gopal, S., Gomes, A. M., Afratis, N. A., Lim, H. C., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2015.03.006 · Cited by 165
Self-citationBlood-induced joint damage: A human in vitro study
Roosendaal, G., Vianen, M. E., Marx, J. J. M., van den Berg, H. M., Lafeber, F. P. J. G., & Bijlsma, J. W. J. (1999) · Arthritis & Rheumatism · Cited by 163
Matricellular proteins: priming the tumour microenvironment for cancer development and metastasis
Wong, G. S., & Rustgi, A. K. (2013) · British Journal of Cancer · doi:10.1038/bjc.2012.592 · Cited by 162
An oncogenic role of Agrin in regulating focal adhesion integrity in hepatocellular carcinoma
Chakraborty, S., Lakshmanan, M., Swa, H. L. F., Chen, J., Zhang, X., Ong, Y. S., Loo, L. S., Akıncılar, S. C., Gunaratne, J., Tergaonkar, V., et al. (2015) · Nature Communications · doi:10.1038/ncomms7184 · Cited by 162
Stattin, E.-L., Wiklund, F., Lindblom, K., Önnerfjord, P., Jonsson, B.-A., Tegner, Y., Sasaki, T., Struglics, A., Lohmander, S., Dahl, N., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2009.12.018 · Cited by 161
Jolly, L. A., Novitskiy, S. V., Owens, P., Massoll, N. A., Cheng, N., Fang, W. B., Moses, H. L., & Franco, A. T. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-2351 · Cited by 161
Schaefer, L., Macakova, K., Raslik, I., Micegova, M., Gröne, H.-J., Schönherr, E., Robenek, H., Echtermeyer, F. G., Grässel, S., Bruckner, P., et al. (2002) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64937-1 · Cited by 160
Mundhenke, C., Meyer, K. K., Drew, S. A., & Friedl, A. (2002) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64362-3 · Cited by 160
Kohan, M., Muro, A. F., White, E. S., & Berkman, N. (2010) · The FASEB Journal · doi:10.1096/fj.10-154435 · Cited by 160
Proteoglycan neofunctions: regulation of inflammation and autophagy in cancer biology
Schaefer, L., Tredup, C., Gubbiotti, M. A., & Iozzo, R. V. (2016) · FEBS Journal · doi:10.1111/febs.13963 · Cited by 160
Cancer associated fibroblasts: is the force the path to the dark side?
Barbazán, J., & Matic Vignjevic, D. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2018.09.002 · Cited by 160
Fibulin-4 and fibulin-5 in elastogenesis and beyond: Insights from mouse and human studies
Papke, C. L., & Yanagisawa, H. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.02.004 · Cited by 156
Xia, L., Huang, W., Tian, D., Zhang, L., Qi, X., Chen, Z., Shang, X. C., Nie, Y., & Wu, K. (2013) · Hepatology · doi:10.1002/hep.26735 · Cited by 156
Serglycin: At the Crossroad of Inflammation and Malignancy
Korpetinou, A., Skandalis, S. S., Labropoulou, V., Smirlaki, G., Noulas, A., Karamanos, N. K., & Theocharis, A. D. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2013.00327 · Cited by 155
Self-citationRicciardelli, C., Brooks, J. H., Suwiwat, S., et al. (2002) · PubMed · Cited by 154
Type VI Collagen Regulates Dermal Matrix Assembly and Fibroblast Motility
Theocharidis, G., Drymoussi, Z., Kao, A. P., Barber, A. H., Lee, D. A., Braun, K. M., & Connelly, J. T. (2015) · Journal of Investigative Dermatology · doi:10.1038/jid.2015.352 · Cited by 153
Immunoregulatory roles of versican proteolysis in the myeloma microenvironment
Hope, C. L., Foulcer, S. J., Jagodinsky, J. C., Chen, S. X., Jensen, J. L., Patel, S., Leith, C. P., Maroulakou, I. G., Callander, N. S., Miyamoto, S., et al. (2016) · Blood · doi:10.1182/blood-2016-03-705780 · Cited by 153
Glypican-1 Is Frequently Overexpressed in Human Gliomas and Enhances FGF-2 Signaling in Glioma Cells
Su, G., Meyer, K. K., Nandini, C., Qiao, D., Salamat, S. M., & Friedl, A. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.050800 · Cited by 152
Dang, C., Beanes, S. R., Lee, H., Zhang, X., Soo, C. B., & Ting, K. (2003) · Plastic & Reconstructive Surgery · doi:10.1097/01.prs.0000060102.57809.da · Cited by 152
Beauvais, D. M., & Rapraeger, A. C. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(03)00126-5 · Cited by 150
Glypican-5 stimulates rhabdomyosarcoma cell proliferation by activating Hedgehog signaling
Li, F., Shi, W., Capurro, M., & Filmus, J. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201008087 · Cited by 150
Amini‐Nik, S., Yousuf, Y., & Jeschke, M. G. (2017) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2017.07.017 · Cited by 150
Dynamic matrisome: ECM remodeling factors licensing cancer progression and metastasis
Yuzhalin, A. E., Lim, S. Y., Kutikhin, A. G., & Gordon-Weeks, A. N. (2018) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2018.09.002 · Cited by 150
Fragments generated upon extracellular matrix remodeling: Biological regulators and potential drugs
Ricard‐Blum, S., & Vallet, S. D. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.11.005 · Cited by 149
Decorin as a multivalent therapeutic agent against cancer
Neill, T., Schaefer, L., & Iozzo, R. V. (2015) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.10.016 · Cited by 146
Tompson, S. W. J., Merriman, B., Funari, V. A., Fresquet, M., Lachman, R. S., Rimoin, D. L., Nelson, S. F., Briggs, M. D., Cohn, D. H., & Krakow, D. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2008.12.001 · Cited by 146
Hyaluronan Regulates Transforming Growth Factor-β1 Receptor Compartmentalization
Ito, T., Williams, J. D., Fraser, D. J., & Phillips, A. O. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403135200 · Cited by 145
Heljäsvaara, R., Aikio, M., Ruotsalainen, H. J., & Pihlajaniemi, T. A. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.10.002 · Cited by 145
Matrix molecules and skin biology
Nyström, A., & Bruckner-Tuderman, L. (2019) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2018.07.025 · Cited by 144
Fullár, A., Dudás, J., Oláh, L., Hollósi, P., Papp, Z., Sobel, G., Karászi, K., Paku, S., Baghy, K., & Kovalszky, I. (2015) · BMC Cancer · doi:10.1186/s12885-015-1272-3 · Cited by 144
Tenascin-C Is a Major Component of the Fibrogenic Niche in Kidney Fibrosis
Fu, H., Tian, Y., Zhou, L., Zhou, D. F., Tan, R. J., Stolz, D. B., & Liu, Y. (2016) · Journal of the American Society of Nephrology · doi:10.1681/asn.2016020165 · Cited by 144
Involvement of Hyaluronan in Regulation of Fibroblast Phenotype
Meran, S., Thomas, D. W., Stephens, P., MARTIN, J. T., Bowen, T., Phillips, A. O., & Steadman, R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700773200 · Cited by 143
Supramolecular Interactions in the Dermo-epidermal Junction Zone
Villone, D., Fritsch, A., Koch, M., Bruckner‐Tuderman, L., Hansen, U. J., & Brückner, P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802415200 · Cited by 143
Comparative analysis of lysyl oxidase (like) family members in pulmonary fibrosis
Aumiller, V., Strobel, B., Romeike, M., Schuler, M. J., Stierstorfer, B., & Kreuz, S. (2017) · Scientific Reports · doi:10.1038/s41598-017-00270-0 · Cited by 143
Herum, K. M., Lunde, I. G., Skrbic, B., Florholmen, G., Behmen, D., Sjaastad, I., Carlson, C. R., Gomez, M. F., & Christensen, G. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.11.006 · Cited by 142
Congenital muscular dystrophy: molecular and cellular aspects
Jimenez-Mallebrera, C., Brown, S., Sewry, C. A., & Muntoni, F. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4510-4 · Cited by 141
TNF-α–stimulated fibroblasts secrete lumican to promote fibrocyte differentiation
Pilling, D., Vakil, V., Cox, N., & Gomer, R. H. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1507387112 · Cited by 140
Yang, N., Mosher, R., Seo, S., Beebe, D. J., & Friedl, A. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.11.039 · Cited by 139
Li, N., Fu, H., Hewitt, S. M., Dimitrov, D. S., & Ho, M. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1706055114 · Cited by 137
Webber, J. P., Meran, S., Steadman, R., & Phillips, A. O. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806989200 · Cited by 136
Endostatin and endorepellin: A common route of action for similar angiostatic cancer avengers
Poluzzi, C., Iozzo, R. V., & Schaefer, L. (2015) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.10.012 · Cited by 136
Lumican, an extracellular matrix proteoglycan, is a novel requisite for hepatic fibrosis
Krishnan, A., Li, X., Kao, W.-Y., Viker, K., Butters, K. A., Masuoka, H. C., Knudsen, B. E., Gores, G. J., & Charlton, M. (2012) · Laboratory Investigation · doi:10.1038/labinvest.2012.121 · Cited by 135
Oxidative Stress Alters Syndecan-1 Distribution in Lungs with Pulmonary Fibrosis
Kliment, C. R., Englert, J. M., Gochuico, B. R., Yu, G., Kaminski, N., Rosas, I. O., & Oury, T. D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807001200 · Cited by 135
Meester, J., Vandeweyer, G., Pintelon, I., Lammens, M. M. Y., Hoorick, L. V., Belder, S. D., Waitzman, K., Young, L., Markham, L. W., Vogt, J., et al. (2016) · Genetics in Medicine · doi:10.1038/gim.2016.126 · Cited by 135
Theocharis, A. D., Vynios, D. H., Papageorgakopoulou, N., Skandalis, S. S., & Theocharis, D. A. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(02)00264-9 · Cited by 134
Self-citationGeneration and Characterization of Aggrecanase
Arner, E. C., Pratta, M. A., Trzăskos, J. M., Decicco, C. P., & Tortorella, M. D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.10.6594 · Cited by 132
Wu, Y., Chen, L., Zheng, P., & Yang, B. B. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110748200 · Cited by 130
Granzyme B in skin inflammation and disease
Turner, C. T., Lim, D. J., & Granville, D. J. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.12.005 · Cited by 130
Li, Y., Wang, Y., Chubinskaya, S., Schoeberl, B., Florine, E. M., Kopesky, P. W., & Grodzinsky, A. J. (2014) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2014.11.006 · Cited by 129
Collagen IV diseases: A focus on the glomerular basement membrane in Alport syndrome
Cosgrove, D. E., & Liu, S. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.08.005 · Cited by 128
Modulation of TGFβ1-Dependent Myofibroblast Differentiation by Hyaluronan
Webber, J. P., Jenkins, R. L., Meran, S., Phillips, A. O., & Steadman, R. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.080837 · Cited by 127
Vanhoutte, D., Schellings, M. W. M., Götte, M., Swinnen, M., Hérias, V., Wild, M. K., Vestweber, D., Chorianopoulos, E., Cortés, V., Rigotti, A., et al. (2007) · Circulation · doi:10.1161/circulationaha.106.644609 · Cited by 126
Guo, J.-Y., Hsu, H.-S., Tyan, S.-W., Li, F.-Y., Shew, J.-Y., Lee, W.-H., & Chen, J.-Y. (2016) · Oncogene · doi:10.1038/onc.2016.404 · Cited by 126
Osteogenesis imperfecta and therapeutics
Morello, R. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.03.010 · Cited by 125
Scott, P. G., Dodd, C. M., Tredget, E. E., Ghahary, A., & Rahemtulla, F. G. (1995) · Histopathology · doi:10.1111/j.1365-2559.1995.tb00249.x · Cited by 124
Syndecan-1 couples the insulin-like growth factor-1 receptor to inside-out integrin activation
Beauvais, D. M., & Rapraeger, A. C. (2010) · Journal of Cell Science · doi:10.1242/jcs.067645 · Cited by 123
Wang, X., Zhou, Y., Tan, R., Xiong, M., He, W., Fang, L., Wen, P., Jiang, L., & Yang, J. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00216.2010 · Cited by 122
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Metadata
- Authors
- Theocharis, A. D., Manou, D., & Karamanos, N. K.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2019-04-11
- Volume
- 286
- Issue
- 15
- Pages
- 2830-2869
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W2938801784
- Cited by
- 511
- References
- 343
- FWCI
- 26.71
- Type
- journal article
- Language
- en
- Open access
- closed
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 ›
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.