Matricryptins and matrikines: biologically active fragments of the extracellular matrix
Open accessAbstract
Numerous extracellular proteins and glycosaminoglycans ( GAG s) undergo limited enzymatic cleavage resulting in the release of fragments exerting biological activities, which are usually different from those of the full‐length molecules. In this review, we define matrikines and matricryptins, which are bioactive fragments released from the extracellular matrix proteins, proteoglycans and GAG s and report their major biological activities. These fragments regulate a number of physiopathological processes including angiogenesis, cancer, fibrosis, inflammation, neurodegenerative diseases and wound healing. The challenges to translate these fragments from molecules biologically active in vitro and in experimental models to potential drugs are discussed in the last part of the review.
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Bioactive ECM byproducts (matricryptins/matrikines) are produced and propagate further inflammatory cascades due to their chemotactic properties.
“bioactive ECM byproducts, termed “matricryptins” or “matrikines”, are produced and propagate further inflammatory cascades due to their chemotactic properties17.”
From Bioengineered liver crosslinked with nano-graphene oxide enables efficient liver regeneration via MMP suppression and immunomodulation (2023) · cites this paper as [17]
Recent strategies for reducing immunogenicity of the dECM scaffold itself have been studied, such as genetic manipulation of organs or regulation of the inflammatory milieu.
“recent strategies for reducing the immunogenicity of the dECM scaffold itself have been studied, such as genetic manipulation of organs21, or regulation of the inflammatory milieu of bioengineered constructs17.”
From Bioengineered liver crosslinked with nano-graphene oxide enables efficient liver regeneration via MMP suppression and immunomodulation (2023) · cites this paper as [17]
Cites
1 retracted
Sudhakar, A. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24813 · Cited by 162 · see citing works
RetractedEndostatin: an endogenous inhibitor of angiogenesis and tumor growth
O'Reilly, M. S., Boehm, T., Shing, Y., Fukai, N., Vasios, G., Lane, W. S., Flynn, E., Birkhead, J. R., Olsen, B. R., & Folkman, J. (1997) · Cell · doi:10.1016/s0092-8674(00)81848-6 · Cited by 4,486 · see citing works
Ricard-Blum, S. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004978 · Cited by 2,305 · see citing works
Self-citationAngiogenesis Induced by Degradation Products of Hyaluronic Acid
West, D. C., HAMPSON, I. N., Arnold, F., & Kumar, S. (1985) · Science · doi:10.1126/science.2408340 · Cited by 1,140 · see citing works
Interactions between extracellular matrix and growth factors in wound healing
Schultz, G. S., & Wysocki, A. (2009) · Wound Repair and Regeneration · doi:10.1111/j.1524-475x.2009.00466.x · Cited by 1,126 · see citing works
Adipose tissue mass can be regulated through the vasculature
Rupnick, M. A., Panigrahy, D., Zhang, C.-Y., Dallabrida, S. M., Lowell, B. B., Langer, R., & Folkman, M. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162349799 · Cited by 845 · see citing works
Antiangiogenesis in cancer therapy—endostatin and its mechanisms of action
Folkman, J. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.11.015 · Cited by 657 · see citing works
Brooks, P. C., Silletti, S., Schalscha, T. V., Friedlander, M., & Cheresh, D. A. (1998) · Cell · doi:10.1016/s0092-8674(00)80931-9 · Cited by 623 · see citing works
Hamano, Y., Zeisberg, M., Sugimoto, H., Lively, J. C., Maeshima, Y., Yang, C., Hynes, R. O., Werb, Z., Sudhakar, A., & Kalluri, R. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00133-8 · Cited by 560 · see citing works
Canstatin, a Novel Matrix-derived Inhibitor of Angiogenesis and Tumor Growth
Kamphaus, G. D., Colorado, P. C., Panka, D. J., Hopfer, H., Ramchandran, R., de la Torre, A., Maeshima, Y., Mier, J. W., Sukhatme, V. P., & Kalluri, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.2.1209 · Cited by 470 · see citing works
Martino, M. M., Tortelli, F., Mochizuki, M., Traub, S., Ben-David, D., Kuhn, G. A., Müller, R., Livne, E., Eming, S. A., & Hubbell, J. A. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002614 · Cited by 459 · see citing works
Interaction of endostatin with integrins implicated in angiogenesis
Rehn, M., Veikkola, T., Kukk, E., Nakamura, H., Ilmonen, M., Lombardo, C. R., Pihlajaniemi, T. A., Alitalo, K. K., & Vuori, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.1024 · Cited by 455 · see citing works
Davis, G. E., Bayless, K. J., Davis, M. J., & Meininger, G. A. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65020-1 · Cited by 452 · see citing works
Kim, Y. M., Hwang, S., Kim, Y.-M., Pyun, B., Kim, T., Lee, S., Gho, Y. S., & Kwon, Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202771200 · Cited by 429 · see citing works
Anti-angiogenic cues from vascular basement membrane collagen.
Colorado, P. C., Torre, A., Kamphaus, G. D., Maeshima, Y., Hopfer, H., Takahashi, K., Volk, R., Zamborsky, E. D., Herman, S., Sarkar, P. K., et al. (2000) · PubMed · Cited by 421 · see citing works
Fragments of extracellular matrix as mediators of inflammation
Adair-Kirk, T. L., & Senior, R. M. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.12.005 · Cited by 362 · see citing works
Distinct Antitumor Properties of a Type IV Collagen Domain Derived from Basement Membrane
Maeshima, Y., Colorado, P. C., de la Torre, A., Holthaus, K. A., Grunkemeyer, J. A., Ericksen, M. B., Hopfer, H., Xiao, Y., Stillman, I. E., & Kalluri, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001956200 · Cited by 358 · see citing works
Adipocyte-derived endotrophin promotes malignant tumor progression
Park, J., & Scherer, P. E. (2012) · Journal of Clinical Investigation · doi:10.1172/jci63930 · Cited by 350 · see citing works
Endorepellin, a Novel Inhibitor of Angiogenesis Derived from the C Terminus of Perlecan
Mongiat, M., Sweeney, S. M., Antonio, J. D. S., Fu, J., & Iozzo, R. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210445200 · Cited by 341 · see citing works
Proteoglycans in health and disease: the multiple roles of syndecan shedding
Manon‐Jensen, T., Itoh, Y., & Couchman, J. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07798.x · Cited by 337 · see citing works
Extracellular matrix, inflammation, and the angiogenic response
Arroyo, A. G., & Iruela‐Arispe, M. L. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq049 · Cited by 336 · see citing works
Sasaki, T., Fukai, N., Mann, K., Göhring, W., Olsen, B. R., & Timpl, R. (1998) · The EMBO Journal · doi:10.1093/emboj/17.15.4249 · Cited by 330 · see citing works
Martino, M. M., & Hubbell, J. A. (2010) · The FASEB Journal · doi:10.1096/fj.09-151282 · Cited by 317 · see citing works
The High and Low Molecular Weight Forms of Hyaluronan Have Distinct Effects on CD44 Clustering
Yang, C., Cao, M., Liu, H., He, Y., Xu, J., Du, Y., Liu, Y., Wang, W., Cui, L., Hu, J., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.349209 · Cited by 310 · see citing works
Schenk, S., Hintermann, E., Bilban, M., Koshikawa, N., Hojilla, C., Khokha, R., & Quaranta, V. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200208145 · Cited by 309 · see citing works
Cell Surface Glypicans Are Low-Affinity Endostatin Receptors
Karumanchi, S. A., Jha, V., Ramchandran, R., Karihaloo, A. K., Tsiokas, L., Chan, B., Dhanabal, M., Hanai, J.-I., Venkataraman, G., Shriver, Z. H., et al. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00225-8 · Cited by 308 · see citing works
Cathepsin S Controls Angiogenesis and Tumor Growth via Matrix-derived Angiogenic Factors
Wang, B., Sun, J., Kitamoto, S., Yang, M., GRUBB, A. O., Chapman, H. A., Kalluri, R., & Shi, G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509134200 · Cited by 291 · see citing works
Antiangiogenic Activity of Restin, NC10 Domain of Human Collagen XV: Comparison to Endostatin
Ramchandran, R., Dhanabal, M., Volk, R., Waterman, M. J. F., Segal, M. S., Lu, H. A. J., Knebelmann, B., & Sukhatme, V. P. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0248 · Cited by 290 · see citing works
Erkan, M., Reiser–Erkan, C., Michalski, C. W., Deucker, S., Sauliunaite, D., Streit, S., Esposito, I., Friess, H., & Kleeff, J. H. (2009) · Neoplasia · doi:10.1593/neo.81618 · Cited by 289 · see citing works
Epidermal growth factor (EGF)-like repeats of human tenascin-C as ligands for EGF receptor
Swindle, C. S., Tran, K. T., Johnson, T. D., Banerjee, P., Mayes, A. M., Griffith, L., & Wells, A. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200103103 · Cited by 286 · see citing works
Diverse Cell Signaling Events Modulated by Perlecan
Whitelock, J. M., Melrose, J., & Iozzo, R. V. (2008) · Biochemistry · doi:10.1021/bi8013938 · Cited by 270 · see citing works
Bix, G. J., Fu, J., González, E. M. G., 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 · see citing works
Elastin‐Elastases and Inflamm‐Aging
Antonicelli, F. D., Bellon, G., Debelle, L., & Hornebeck, W. (2007) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(06)79005-6 · Cited by 241 · see citing works
Duca, L., Floquet, N., Alix, A. J. P., Haye, B., & Debelle, L. (2004) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2003.09.007 · Cited by 239 · see citing works
A fibronectin fragment inhibits tumor growth, angiogenesis, and metastasis
Yi, M., & Ruoslahti, E. I. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.2.620 · Cited by 232 · see citing works
Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs
Franzke, C.-W., Tasanen, K., Schäcke, H., Zhou, Z., Tryggvason, K., Mauch, C., Zigrino, P., Sunnarborg, S. W., Lee, D. C., Fahrenholz, F., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf532 · Cited by 230 · see citing works
Two RGD-independent αvβ3 Integrin Binding Sites on Tumstatin Regulate Distinct Anti-tumor Properties
Maeshima, Y., Colorado, P. C., & Kalluri, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000186200 · Cited by 229 · see citing works
Hashimoto, T., Wakabayashi, T., Watanabe, A., Kowa, H., Hosoda, R., Nakamura, A., Kanazawa, I., Arai, T., Takio, K., Mann, D. M. A., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/21.7.1524 · Cited by 223 · see citing works
Sasaki, T., Larsson, H. E., Tisi, D., Claesson, L., Hohenester, E., & Timpl, R. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3996 · Cited by 220 · see citing works
González, E. M., Reed, C. C., Bix, G. J., Fu, J., Zhang, Y., Gopalakrishnan, B., Greenspan, D. S., & Iozzo, R. V. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409841200 · Cited by 191 · see citing works
Hyaluronan oligosaccharides promote excisional wound healing through enhanced angiogenesis
Gao, F., Liu, Y., He, Y., Yang, C., Wang, Y., Shi, X., & Wei, G. (2009) · Matrix Biology · doi:10.1016/j.matbio.2009.11.002 · Cited by 185 · see citing works
Maquart, F.-X., Pickart, L., Laurent, M., Gillery, P., Monboisse, J.-C., & Borel, J.-P. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80509-x · Cited by 181 · see citing works
Proteolytic Post-translational Modification of Proteins: Proteomic Tools and Methodology
Rogers, L. D., & Overall, C. M. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.031310 · Cited by 173 · see citing works
The angiogenesis inhibitor endostatin impairs blood vessel maturation during wound healing
Bloch, W., Huggel, K., Sasaki, T., Grose, R. P., Bugnon, P., Addicks, K., Timpl, R., & Werner, S. (2000) · The FASEB Journal · doi:10.1096/fj.00-0490fje · Cited by 169 · see citing works
Nyberg, P., Heikkilä, P., Sorsa, T. A., Luostarinen, J., Heljäsvaara, R., Stenman, U., Pihlajaniemi, T. A., & Salo, T. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210325200 · Cited by 167 · see citing works
Distinct Recognition of Collagen Subtypes by α1β1 and α2β1Integrins
Nykvist, P., Tu, H., Ivaska, J., Käpylä, J., Pihlajaniemi, T. A., & Heino, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.8255 · Cited by 162 · see citing works
Fernando, N. T., Koch, M., Rothrock, C., Gollogly, L. K., D'Amore, P. A., Ryeom, S. W., & Yoon, S. S. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-4126 · Cited by 162 · see citing works
Magnon, C., Galaup, A., Mullan, B., Rouffiac, V., Bidart, J., Griscelli, F., Opolon, P., & Perricaudet, M. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-3536 · Cited by 152 · see citing works
Two Forms of Collagen XVII in Keratinocytes
Schäcke, H., Schumann, H., Hammami-Hauasli, N., Raghunath, M., & Bruckner‐Tuderman, L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.25937 · Cited by 152 · see citing works
Schor, S. L., & Schor, A. M. (2001) · Breast Cancer Research · doi:10.1186/bcr325 · Cited by 150 · see citing works
Perlecan domain V is neuroprotective and proangiogenic following ischemic stroke in rodents
Lee, B., Clarke, D. N., Al-Ahmad, A. J., Kahle, M., Parham, C. L., Auckland, L. D., Shaw, C. S., Fidanboylu, M., Orr, A. W., Ogunshola, O. O., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci46358 · Cited by 147 · see citing works
Matrikines and matricryptins: Implications for cutaneous cancers and skin repair
Tran, K. T., Lamb, P., & Deng, J. (2005) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2005.05.001 · Cited by 136 · see citing works
Ricard‐Blum, S., Féraud, O., Lortat‐Jacob, H., Rencurosi, A., Fukai, N., Dkhissi, F., Vittet, D., Imberty, A., Olsen, B. R., & REST, M. V. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309868200 · Cited by 135 · see citing works
Self-citationMatrix revolutions: ‘tails’ of basement-membrane components with angiostatic functions
Bix, G. J., & Iozzo, R. V. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.11.008 · Cited by 133 · see citing works
Laminin-111-derived peptides and cancer
Kikkawa, Y., Hozumi, K., Katagiri, F., Nomizu, M., Kleinman, H. K., & Koblinski, J. E. (2013) · Cell Adhesion & Migration · doi:10.4161/cam.22827 · Cited by 132 · see citing works
Zinc-dependent dimers observed in crystals of human endostatin
Ding, Y., Javaherian, K., Lo, K.-M., Chopra, R., Boehm, T., Lanciotti, J., Harris, B. A., Li, Y., Shapiro, R., Hohenester, E., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10443 · Cited by 130 · see citing works
Therapeutic Efficacy of Endostatin Exhibits a Biphasic Dose-Response Curve
Celik, I., Sürücü, O., Dietz, C., Heymach, J. V., Force, J. M., Höschele, I., Becker, C. M., Folkman, J., & Kisker, O. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-2617 · Cited by 129 · see citing works
Elastin-Derived Peptides Are New Regulators of Insulin Resistance Development in Mice
Blaise, S. A., Romier, B., Kawecki, C., Ghirardi, M., Rabenoelina, F., Baud, S., Duca, L., Maurice, P., Heinz, A., Schmelzer, C. E. H., et al. (2013) · Diabetes · doi:10.2337/db13-0508 · Cited by 129 · see citing works
A Peptide Derived from Endostatin Ameliorates Organ Fibrosis
Yamaguchi, Y., Takihara, T., Chambers, R. A., Veraldi, K. L., Larregina, A. T., & Feghali‐Bostwick, C. A. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003421 · Cited by 127 · see citing works
Sugawara, K., Tsuruta, D., Ishii, M., Jones, J., & Kobayashi, H. (2008) · Experimental Dermatology · doi:10.1111/j.1600-0625.2008.00721.x · Cited by 125 · see citing works
Matricryptins derived from collagens and proteoglycans
Ricard‐Blum, S. (2010) · Frontiers in bioscience · doi:10.2741/3712 · Cited by 124 · see citing works
Self-citationEndostatin Overexpression Inhibits Lymphangiogenesis and Lymph Node Metastasis in Mice
Brideau, G., Mäkinen, M. J., Elamaa, H. P., Tu, H., Nilsson, G. P., Alitalo, K. K., Pihlajaniemi, T. A., & Heljäsvaara, R. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1458 · Cited by 124 · see citing works
A prototypic matricellular protein in the tumor microenvironment—Where there's SPARC, there's fire
Clark, C. J., & Sage, E. H. (2008) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21688 · Cited by 123 · see citing works
Towards definition of an ECM parts list: An advance on GO categories
Naba, A., Hoersch, S., & Hynes, R. O. (2012) · Matrix Biology · doi:10.1016/j.matbio.2012.11.008 · Cited by 118 · see citing works
Reynolds, A. R. (2010) · Dose-Response · doi:10.2203/dose-response.09-049.reynolds · Cited by 117 · see citing works
Goyal, A. K., Pal, N., Concannon, M., Paul, M. R., Doran, M., Poluzzi, C., Sekiguchi, K., Whitelock, J. M., Neill, T., & Iozzo, R. V. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.243626 · Cited by 117 · see citing works
Kuo, C. J., LaMontagne, K. R., García‐Cardeña, G., Ackley, B. D., Kalman, D., Park, S., Christofferson, R. H. B., Kamihara, J., Ding, Y., Lo, K.-M., et al. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.6.1233 · Cited by 116 · see citing works
Type XXIII Collagen, a New Transmembrane Collagen Identified in Metastatic Tumor Cells
Banyard, J., Bao, L., & Zetter, B. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210616200 · Cited by 116 · see citing works
Mydel, P. M., Shipley, J. M., Adair-Kirk, T. L., Kelley, D. G., Broekelmann, T. J., Mecham, R. P., & Senior, R. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706239200 · Cited by 115 · see citing works
Heinz, A., Jung, M. C., Duca, L., Sippl, W., Taddese, S., Ihling, C. H., Rusciani, A., Jahreis, G., Weiss, A. S., Neubert, R. H. H., et al. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07616.x · Cited by 112 · see citing works
Molecular Interplay between Endostatin, Integrins, and Heparan Sulfate
Faye, C., Moreau, C., Chautard, É., Edelmann, R. J., Fukai, N., Ruggiero, F., Humphries, M. J., Olsen, B. R., & Ricard‐Blum, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.002840 · Cited by 109 · see citing works
Self-citationPickart, L., Vasquez-Soltero, J. M., & Margolina, A. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/324832 · Cited by 108 · see citing works
The Angiogenesis Inhibitor, Endostatin, Does Not Affect Murine Cutaneous Wound Healing
Berger, A. C., Feldman, A. L., Gnant, M., Kruger, E. A., Sim, B. K. L., Hewitt, S. M., Figg, W. D., Alexander, H. R., & Libutti, S. K. (2000) · Journal of Surgical Research · doi:10.1006/jsre.2000.5890 · Cited by 108 · see citing works
Shedding of Collagen XVII/BP180 in Skin Depends on Both ADAM10 and ADAM9
Franzke, C.-W., Bruckner‐Tuderman, L., & Blobel, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.034090 · Cited by 104 · see citing works
Tu, H., Sasaki, T., Snellman, A., Göhring, W., Pirilä, P., Timpl, R., & Pihlajaniemi, T. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107583200 · Cited by 104 · see citing works
Cui, C., Mao, L., Chi, Z., Si, L., Sheng, X., Kong, Y., Li, S., Lian, B., Gu, K., Tao, M., et al. (2013) · Molecular Therapy · doi:10.1038/mt.2013.79 · Cited by 102 · see citing works
Metastatin: a hyaluronan-binding complex from cartilage that inhibits tumor growth.
Liu, N., Lapcevich, R., Underhill, C. B., Han, Z., Gao, F., Swartz, G., Plum, S., Zhang, L., & Green, S. J. (2001) · PubMed · Cited by 101 · see citing works
Endostatin induces autophagy in endothelial cells by modulating Beclin 1 and β‐catenin levels
Nguyen, T. M. B., Subramanian, I. V., Xiao, X., Ghosh, G., Nguyen, P. H., Kelekar, A., & Ramakrishnan, S. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00722.x · Cited by 100 · see citing works
Fuchs, K., Hippe, A., Schmaus, A., Homey, B., Sleeman, J. P., & Orian‐Rousseau, V. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.364 · Cited by 99 · see citing works
Role of laminins in physiological and pathological angiogenesis
Simon-Assmann, P. M., Orend, G., Mammadova‐Bach, E., Spenlé, C., & Lefèbvre, O. (2011) · The International Journal of Developmental Biology · doi:10.1387/ijdb.103223ps · Cited by 98 · see citing works
Ghazi, K., Deng-Pichon, U., Warnet, J., & Rat, P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048351 · Cited by 98 · see citing works
Biaoxue, R., Shuanying, Y., Li, W., Zhang, W., & Zongjuan, M. (2012) · World Journal of Surgical Oncology · doi:10.1186/1477-7819-10-170 · Cited by 94 · see citing works
Systems-based approaches toward wound healing
Tepole, A. B., & Ellen Kuhl, A. (2013) · Pediatric Research · doi:10.1038/pr.2013.3 · Cited by 93 · see citing works
The First Draft of the Endostatin Interaction Network
Faye, C., Chautard, É., Olsen, B. R., & Ricard‐Blum, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.002964 · Cited by 91 · see citing works
Self-citationThe C5 Domain of Col6A3 Is Cleaved Off from the Col6 Fibrils Immediately after Secretion
Aigner, T. G., Hambach, L., Söder, S., Schlötzer-Schrehardt, U. M., & Pöschl, E. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.6227 · Cited by 89 · see citing works
Reactive Oxygen Species Expose Cryptic Epitopes Associated with Autoimmune Goodpasture Syndrome
Kalluri, R., Cantley, L. G., Kerjaschki, D., & Neilson, E. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m904549199 · Cited by 88 · see citing works
Protein TAILS: when termini tell tales of proteolysis and function
Lange, P. F., & Overall, C. M. (2013) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2012.11.025 · Cited by 87 · see citing works
[Regulation of cell activity by the extracellular matrix: the concept of matrikines].
Maquart, F., Siméon, A., Brassart‐Pasco, S., & Monboisse, J. (1999) · PubMed · Cited by 84 · see citing works
Jia, H., Li, Y., Zhao, T., Li, X., Hu, J., Yin, D., Guo, B., Kopecko, D. J., Zhao, X., Zhang, L., et al. (2012) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-012-1256-y · Cited by 81 · see citing works
Régulation de l’activité cellulaire par la matrice extracelulaire : le concept de matrikines
Maquart, F., Siméon, A., Pasco, S., & Monboisse, J. (1999) · Journal de la Société de Biologie · doi:10.1051/jbio/1999193040423 · Cited by 81 · see citing works
Chang, J.-H., Javier, J., Chang, G., Oliveira, H. B., & Azar, D. T. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.05.043 · Cited by 81 · see citing works
Demidova‐Rice, T. N., Wolf, L. N., Deckenback, J., Hamblin, M. R., & Herman, I. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032146 · Cited by 79 · see citing works
Iyer, A. K. V., Tran, K. T., Griffith, L. G., & Wells, A. H. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21232 · Cited by 78 · see citing works
Floquet, N., Brassart‐Pasco, S., Ramont, L., Derreumaux, P., Laronze, J. Y., Nuzillard, J., Maquart, F. X., Alix, A. J. P., & Monboisse, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307736200 · Cited by 78 · see citing works
Novel roles for collagens in wiring the vertebrate nervous system
Fox, M. A. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.05.003 · Cited by 77 · see citing works
Briknarová, K., Åkerman, M. E., Hoyt, D. W., Ruoslahti, E. I., & Ely, K. R. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00890-8 · Cited by 76 · see citing works
Demidova‐Rice, T. N., Geevarghese, A., & Herman, I. M. (2010) · Wound Repair and Regeneration · doi:10.1111/j.1524-475x.2010.00642.x · Cited by 76 · see citing works
The nuclear translocation of endostatin is mediated by its receptor nucleolin in endothelial cells
Song, N., Ding, Y., Zhuo, W., He, T., Fu, Z., Chen, Y., Song, X., Fu, Y., & Luo, Y. (2012) · Angiogenesis · doi:10.1007/s10456-012-9284-y · Cited by 74 · see citing works
Antiangiogenic proteins require plasma fibronectin or vitronectin for in vivo activity
Yi, M., Sakai, T., Fässler, R., & Ruoslahti, E. I. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1635112100 · Cited by 74 · see citing works
Chang, J. W., Kang, U., Kim, D., Yi, J. K., Lee, J. W., Noh, D., Lee, C., & Yu, M. (2007) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.200780049 · Cited by 73 · see citing works
Cysteine Cathepsins S and L Modulate Anti-angiogenic Activities of Human Endostatin
Veillard, F., Saidi, A., Burden, R. E., Scott, C. J., Gillet, L., Lecaille, F., & Lalmanach, G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.284869 · Cited by 71 · see citing works
Mechanical factors influence the expression of endostatin—an inhibitor of angiogenesis—in tendons
Pufe, T., Petersen, W. J., Kurz, B., Tsokos, M., Tillmann, B. N., & Mentlein, R. (2003) · Journal of Orthopaedic Research® · doi:10.1016/s0736-0266(02)00262-0 · Cited by 71 · see citing works
Angiosuppressive and angiostimulatory effects exerted by synthetic partial sequences of endostatin.
Morbidelli, L., Donnini, S., Chillemi, F., Giachetti, A., & Ziche, M. (2003) · PubMed · Cited by 71 · see citing works
Endostatin, an angiogenesis inhibitor, ameliorates bleomycin-induced pulmonary fibrosis in rats
Wan, Y., Tian, G., Guo, H.-S., Kang, Y., Yao, Z., Li, X.-L., Liu, Q., & Lin, D. (2013) · Respiratory Research · doi:10.1186/1465-9921-14-56 · Cited by 68 · see citing works
Collagen XVII Is Destabilized by a Glycine Substitution Mutation in the Cell Adhesion Domain Col15
Tasanen, K., Eble, J. A., Aumailley, M., Schumann, H., Baetge, J., Tu, H., Brückner, P., & Bruckner‐Tuderman, L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3093 · Cited by 68 · see citing works
Extracellular matrix in angiogenesis: dynamic structures with translational potential
Eming, S. A., & Hubbell, J. A. (2011) · Experimental Dermatology · doi:10.1111/j.1600-0625.2011.01309.x · Cited by 66 · see citing works
Tetrastatin, the NC1 Domain of the α4(IV) Collagen Chain: A Novel Potent Anti-Tumor Matrikine
Brassart‐Pasco, S., Sénéchal, K., Thévenard, J., Ramont, L., Devy, J., Stefano, L. D., Dupont-Deshorgue, A., Brézillon, S., Feru, J., Jazeron, J.-F., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029587 · Cited by 66 · see citing works
Self-citationKaragiannis, E. D., & Popel, A. S. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.12.231 · Cited by 66 · see citing works
John, H., Radtke, K., Ständker, L., & Forssmann, W. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.10.013 · Cited by 63 · see citing works
Hyaluronan Fragments Promote Inflammation by Down-Regulating the Anti-inflammatory A2a Receptor
Collins, S. L., Black, K. E., Chan‐Li, Y., Ahn, Y., Cole, P. A., Powell, J. D., & Horton, M. R. (2011) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2010-0387oc · Cited by 62 · see citing works
Farwick, M., Grether‐Beck, S., Marini, A., Maczkiewitz, U., Lange, J., Köhler, T., Lersch, P., Falla, T., Felsner, I., Brenden, H., et al. (2011) · Experimental Dermatology · doi:10.1111/j.1600-0625.2011.01307.x · Cited by 58 · see citing works
Kranenburg, O., Kroon-Batenburg, L. M. J., Reijerkerk, A., Wu, Y., Voest, E. E., & Gebbink, M. F. B. G. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00218-7 · Cited by 57 · see citing works
Bioactive oligopeptides in dermatology: Part I
Reddy, B. Y., Jow, T., & Hantash, B. M. (2012) · Experimental Dermatology · doi:10.1111/j.1600-0625.2012.01528.x · Cited by 56 · see citing works
Arul, V., Gopinath, D., Gomathi, K., & Jayakumar, R. (2005) · Journal of Biomedical Materials Research Part B: Applied Biomaterials · doi:10.1002/jbm.b.30246 · Cited by 56 · see citing works
Altered angiogenic balance in keloids: a key to therapeutic intervention
Mogili, N. S., Krishnaswamy, V. R., Jayaraman, M., Rajaram, R., Venkatraman, A., & Korrapati, P. S. (2011) · Translational research · doi:10.1016/j.trsl.2011.10.002 · Cited by 55 · see citing works
Shedding of Collagen XXIII Is Mediated by Furin and Depends on the Plasma Membrane Microenvironment
Veit, G., Павловна, З. Е., Franzke, C.-W., Kutsch, S., Siebolds, U., Gordon, M. K., Bruckner‐Tuderman, L., & Koch, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703425200 · Cited by 55 · see citing works
Angiogenic laminin-derived peptides stimulate wound healing
Malinda, K. M., Wysocki, A. B., Koblinski, J. E., Kleinman, H. K., & Ponce, M. L. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.05.025 · Cited by 54 · see citing works
Booms, P., Ney, A., Barthel, F., Moroy, G., Counsell, D., Gille, C., Guo, G., Pregla, R., Mundlos, S., & Alix, A. J. P. (2006) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2005.11.009 · Cited by 54 · see citing works
Endotrophin - Linking Obesity with Aggressive Tumor Growth
Park, J., & Scherer, P. E. (2012) · Oncotarget · doi:10.18632/oncotarget.796 · Cited by 53 · see citing works
Deininger, M. H., Fimmen, B. A., Thal, D. R., Schluesener, H. J., & Meyermann, R. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-24-10621.2002 · Cited by 52 · see citing works
Transglutaminase-2: a new endostatin partner in the extracellular matrix of endothelial cells
Faye, C., Inforzato, A., Bignon, M., Hartmann, D. J., Muller, L., Ballut, L., Olsen, B. R., Day, A. J., & Ricard‐Blum, S. (2010) · Biochemical Journal · doi:10.1042/bj20091594 · Cited by 52 · see citing works
Self-citationRodrigues, M., Yates, C. C., Nuschke, A., Griffith, L. G., & Wells, A. H. (2013) · Tissue Engineering Part A · doi:10.1089/ten.tea.2012.0568 · Cited by 50 · see citing works
Antiangiogenic Properties of Fibstatin, an Extracellular FGF-2–Binding Polypeptide
Bossard, C., Berghe, L. V. D., Laurell, H., Castano, C., Cérutti, M., Prats, A., & Prats, H. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0287 · Cited by 48 · see citing works
Extended interaction network of procollagen C-proteinase enhancer-1 in the extracellular matrix
Salza, R., Peysselon, F., Chautard, É., Faye, C., Moschcovich, L., Weiss, T., Perrin‐Cocon, L., Lotteau, V., Kessler, E., & Ricard‐Blum, S. (2013) · Biochemical Journal · doi:10.1042/bj20130295 · Cited by 47 · see citing works
Self-citationThe shed ectodomain of type XIII collagen affects cell behaviour in a matrix-dependent manner
Väisänen, M., Väisänen, T., & Pihlajaniemi, T. A. (2004) · Biochemical Journal · doi:10.1042/bj20031974 · Cited by 47 · see citing works
The NC1 domain of type XIX collagen inhibits in vivo melanoma growth
Ramont, L., Brassart‐Pasco, S., Thévenard, J., Dupont-Deshorgue, A., Ventéo, L., Laronze, J. Y., Pluot, M., Monboisse, J., & Maquart, F. (2007) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-06-0207 · Cited by 46 · see citing works
Conway, R. E., Joiner, K., Patterson, A., Bourgeois, D. S., Rampp, R., Hannah, B. C., McReynolds, S., Elder, J. M., Gilfilen, H., & Shapiro, L. H. (2013) · Angiogenesis · doi:10.1007/s10456-013-9360-y · Cited by 46 · see citing works
Target-Derived Matricryptins Organize Cerebellar Synapse Formation Through α3β1 Integrins
Su, J., Stenbjorn, R. S., Gorse, K., Su, K., Hauser, K., Ricard-Blum, S., Pihlajaniemi, T., & Fox, M. A. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.07.001 · Cited by 45 · see citing works
Self-citationEvaluation of angiogenic activities of hyaluronan oligosaccharides of defined minimum size
Cui, X., Xu, H., Zhou, S., Zhao, T., Liu, A., Guo, X., Tang, W., & Wang, F. (2009) · Life Sciences · doi:10.1016/j.lfs.2009.08.010 · Cited by 44 · see citing works
Structural characterization of human elastin derived peptides containing the GXXP sequence
Moroy, G., Alix, A. J. P., & Héry‐Huynh, S. (2005) · Biopolymers · doi:10.1002/bip.20276 · Cited by 43 · see citing works
Ambesi, A., & McKeown‐Longo, P. J. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-08-0195 · Cited by 42 · see citing works
Burgess, J. K., & Weckmann, M. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.02.002 · Cited by 41 · see citing works
Endostatin inhibits hypertrophic scarring in a rabbit ear model
Ren, H., Hu, H., Li, Y., Jiang, H.-F., Hu, X., & Han, C. (2013) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b1200077 · Cited by 40 · see citing works
Angiogenic and Vascular Modulation by Extracellular Matrix Cleavage Products
Suhr, F., Brixius, K., & Bloch, W. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209787315756 · Cited by 37 · see citing works
Fukuda, H., Mochizuki, S., Abe, H., Okano, H. J., Hara‐Miyauchi, C., Okano, H., Yamaguchi, N., Nakayama, M., D'Armiento, J. M., & Okada, Y. (2011) · British Journal of Cancer · doi:10.1038/bjc.2011.431 · Cited by 37 · see citing works
Mercurius, K. O., & Morla, A. O. (2001) · BMC Cell Biology · doi:10.1186/1471-2121-2-18 · Cited by 37 · see citing works
Grahovac, J., Becker, D., & Wells, A. H. (2012) · Journal of Investigative Dermatology · doi:10.1038/jid.2012.263 · Cited by 36 · see citing works
Chen, J., Yao, Q., Li, D., Zhang, J., Wang, T., Yu, M., Zhou, X., Huan, Y., Wang, J., & Wang, L. (2013) · BMC Cancer · doi:10.1186/1471-2407-13-248 · Cited by 36 · see citing works
CXCL4L1–fibstatin cooperation inhibits tumor angiogenesis, lymphangiogenesis and metastasis
Prats, A., Berghe, L. V. D., Rayssac, A., Ainaoui, N., Morfoisse, F., Pujol, F., Gonidec, S. L., Bikfalvi, A., Prats, H., Pyronnet, S., et al. (2013) · Microvascular Research · doi:10.1016/j.mvr.2013.05.005 · Cited by 36 · see citing works
Opposite effects of endostatin on different endothelial cells
Schmidt, A., Addicks, K., & Bloch, W. (2004) · Cancer Biology & Therapy · doi:10.4161/cbt.3.11.1219 · Cited by 34 · see citing works
Javaherian, K., Lee, T.-Y., Sjin, R. M. T. T., Parris, G. E., & Hlatky, L. (2010) · Dose-Response · doi:10.2203/dose-response.10-020.javaherian · Cited by 34 · see citing works
Gunda, V., Verma, R. K., & Sudhakar, Y. A. (2013) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.12-10870 · Cited by 30 · see citing works
Lamstatin – a novel inhibitor of lymphangiogenesis derived from collagen IV
Weckmann, M., Moir, L. M., Heckman, C. A., Black, J. L., Oliver, B. G. G., & Burgess, J. K. (2012) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2012.01648.x · Cited by 28 · see citing works
Screening of integrin-binding peptides from the laminin α4 and α5 chain G domain peptide library
Katagiri, F., Ishikawa, M., Yamada, Y., Hozumi, K., Kikkawa, Y., & Nomizu, M. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2012.02.017 · Cited by 28 · see citing works
Väisänen, M., Väisänen, T., Tu, H., Pirilä, P., Sormunen, R. T., & Pihlajaniemi, T. A. (2005) · Biochemical Journal · doi:10.1042/bj20051073 · Cited by 25 · see citing works
Parham, C. L., Auckland, L. D., Rachwal, J., Clarke, D. N., & Bix, G. J. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130683 · Cited by 24 · see citing works
Bioactive oligopeptides in dermatology: Part II
Reddy, B. Y., Jow, T., & Hantash, B. M. (2012) · Experimental Dermatology · doi:10.1111/j.1600-0625.2012.01527.x · Cited by 24 · see citing works
Denis, C. J., Deiteren, K., Mortier, A., Tounsi, A., Fransén, E., Proost, P., Renauld, J., & Lambeir, A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034199 · Cited by 23 · see citing works
Al-Ahmad, A. J., Lee, B., Stack, J. P., Parham, C. L., Campbell, J., Clarke, D. N., Fertala, A., & Bix, G. J. (2010) · Brain Research · doi:10.1016/j.brainres.2010.09.023 · Cited by 21 · see citing works
Luo, Y., Li-JuanYao, Zhao, L., Sun, A.-Y., Dong, H., Du, J., Wu, S., & Hu, W. (2010) · Clinica Chimica Acta · doi:10.1016/j.cca.2010.01.001 · Cited by 21 · see citing works
Perlecan Domain V Therapy for Stroke: A Beacon of Hope?
Bix, G. J. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300197y · Cited by 20 · see citing works
Peptides derived from the human laminin α4 and α5 chains exhibit antimicrobial activity
Senyürek, I., Klein, G., Kalbacher, H., Deeg, M., & Schittek, B. (2010) · Peptides · doi:10.1016/j.peptides.2010.04.016 · Cited by 20 · see citing works
Sharma, B. K., Srinivasan, R., Kapil, S., Singla, B., Saini, N., Chawla, Y. K., Chakraborti, A., Duseja, A. K., Kalra, N., & Dhiman, R. K. (2013) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1759-7 · Cited by 20 · see citing works
Crystal Structure of the LG3 Domain of Endorepellin, an Angiogenesis Inhibitor
Le, B. V., Kim, H., Choi, J., Kim, J.-H., Hahn, M., Lee, C., Kim, K. K., & Hwang, H. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.09.048 · Cited by 20 · see citing works
Endostatin and anastellin inhibit distinct aspects of the angiogenic process
Neskey, D. M., Ambesi, A., Pumiglia, K. M., & McKeown‐Longo, P. J. (2008) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/1756-9966-27-61 · Cited by 20 · see citing works
Novel insight into the biological functions of syndecan ectodomain core proteins
Rossi, G. D., & Whiteford, J. R. (2013) · BioFactors · doi:10.1002/biof.1104 · Cited by 19 · see citing works
Endogenous Matrix-Derived Inhibitors of Angiogenesis
Sund, M., Nyberg, P., & Eikesdal, H. P. (2010) · Pharmaceuticals · doi:10.3390/ph3103021 · Cited by 17 · see citing works
Qiu, Z., Hu, J., Xu, H., Wang, W., Caihui, N., & Wang, X. (2013) · Anti-Cancer Drugs · doi:10.1097/cad.0b013e328361b7ad · Cited by 16 · see citing works
Lin, J. (2010) · International Journal of Oncology · doi:10.3892/ijo.2010.871 · Cited by 16 · see citing works
Endostatin enhances radioresponse in breast cancer cells via alteration of substance P levels
Aydemir, E. A. (2011) · Oncology Letters · doi:10.3892/ol.2011.335 · Cited by 12 · see citing works
Endostar Injection Inhibits Rabbit Ear Hypertrophic Scar Formation
ZhiYong, W., Song, F., LianJu, X., Yingkai, L., Chun, Q., Lu, S., & XiQiao, W. (2012) · The International Journal of Lower Extremity Wounds · doi:10.1177/1534734612463698 · Cited by 10 · see citing works
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Frangogiannis, N. G. (2021) · Cardiovascular Research · doi:10.1093/cvr/cvaa324 · Cited by 1,229 · see citing works
A guide to the composition and functions of the extracellular matrix
Karamanos, N. K., Theocharis, A. D., Piperigkou, Z., Manou, D., Passi, A. G., Skandalis, S. S., Vynios, D. H., Orian‐Rousseau, V., Ricard‐Blum, S., Schmelzer, C. E. H., et al. (2021) · FEBS Journal · doi:10.1111/febs.15776 · Cited by 1,100 · see citing works
Self-citationThe extracellular matrix: tools and insights for the "omics" era
Naba, A., Clauser, K. R., Ding, H., Whittaker, C. A., Carr, S. A., & Hynes, R. O. (2016) · Matrix Biology · doi:10.1016/j.matbio.2015.06.003 · Cited by 1,037 · see citing works
The big five in fibrosis: Macrophages, myofibroblasts, matrix, mechanics, and miscommunication
Pakshir, P., & Hinz, B. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.01.019 · Cited by 396 · see citing works
The Interplay between Extracellular Matrix Remodeling and Cancer Therapeutics
Prakash, J., & Shaked, Y. (2024) · Cancer Discovery · doi:10.1158/2159-8290.cd-24-0002 · Cited by 391 · see citing works
González-Ávila, G., Sommer, B., Mendoza-Posada, D. A., Ramos, C., García-Hernández, A. A., & Falfán‐Valencia, R. (2019) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2019.02.010 · Cited by 378 · see citing works
Emerging roles of ECM remodeling processes in cancer
Mohan, V., Das, A., & Sagi, I. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.09.004 · Cited by 339 · see citing works
Mechanisms of Assembly and Remodeling of the Extracellular Matrix
Naba, A. (2024) · Nature reviews. Molecular cell biology · doi:10.1038/s41580-024-00767-3 · Cited by 311 · see citing works
Collagen interactions: Drug design and delivery
An, B., Lin, Y., & Brodsky, B. (2015) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.11.013 · Cited by 245 · see citing works
Matrix Metalloproteinases in Bone Resorption, Remodeling, and Repair
Paiva, K. B. S., & Granjeiro, J. M. (2017) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.05.001 · Cited by 237 · see citing works
Glioma infiltration and extracellular matrix: key players and modulators
Ferrer, V. P., Moura‐Neto, V., & Mentlein, R. (2018) · Glia · doi:10.1002/glia.23309 · Cited by 223 · see citing works
Extracellular Matrix, a Hard Player in Angiogenesis
Mongiat, M., Andreuzzi, E., Tarticchio, G., & Paulitti, A. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17111822 · Cited by 221 · see citing works
Eckhard, U., Huesgen, P. F., Schilling, O., Bellac, C. L., Butler, G. S., Cox, J. H., Dufour, A., Goebeler, V., Kappelhoff, R., Keller, U. A. D., et al. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.09.003 · Cited by 208 · see citing works
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 · see citing works
From Structure to Phenotype: Impact of Collagen Alterations on Human Health
Arseni, L., Lombardi, A., & Orioli, D. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051407 · Cited by 186 · see citing works
“The ectodomains of syndecans 1–4 are also matricryptins, whereas fragments derived from hyaluronan degradation regulate inflammation and wound healing ([28] and references therein).”
BackgroundEndostatin's emerging roles in angiogenesis, lymphangiogenesis, disease, and clinical applications
Walia, A., Yang, J., Huang, Y.-H., Rosenblatt, M. I., Chang, J., & Azar, D. T. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.09.007 · Cited by 182 · see citing works
Pivotal role for decorin in angiogenesis
Järveläinen, H., Sainio, A., & Wight, T. N. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.01.023 · Cited by 182 · see citing works
Molecular and tissue alterations of collagens in fibrosis
Ricard‐Blum, S., Baffet, G., & Théret, N. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.02.004 · Cited by 170 · see citing works
Self-citationPacelli, S., Basu, S., Whitlow, J., Chakravarti, A. R., Acosta, F. M., Varshney, A., Modaresi, S., Berkland, C. J., & Paul, A. (2017) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2017.07.011 · Cited by 166 · see citing works
Extracellular matrix-mediated cellular communication in the heart
Valiente-Alandí, Í., Schafer, A. E., & Blaxall, B. C. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.01.011 · Cited by 164 · see citing works
Lindsey, M. L., Iyer, R. P., Zamilpa, R., Yabluchanskiy, A., DeLeon‐Pennell, K. Y., Hall, M. E., Kaplan, A., Zouein, F. A., Bratton, D. R., Flynn, E. R., et al. (2015) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2015.07.035 · Cited by 160 · see citing works
Dynamic matrisome: ECM remodeling factors licensing cancer progression and metastasis
Yuzhalin, A. E., Lim, S. Y., Кутихин, А. Г., & Gordon-Weeks, A. N. (2018) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2018.09.002 · Cited by 146 · see citing works
Heljäsvaara, R., Aikio, M., Ruotsalainen, H. J., & Pihlajaniemi, T. A. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.10.002 · Cited by 142 · see citing works
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 143 · see citing works
Self-citationGomes, A., Teixeira, C. A. S., Ferraz, R., Prudêncio, C., & Gomes, P. A. C. (2017) · Molecules · doi:10.3390/molecules22101743 · Cited by 140 · see citing works
Extracellular Matrix Components in the Pathogenesis of Type 1 Diabetes
Bogdani, M., Korpos, É., Simeonovic, C. J., Parish, C. R., Sorokin, L. M., & Wight, T. N. (2014) · Current Diabetes Reports · doi:10.1007/s11892-014-0552-7 · Cited by 126 · see citing works
Topical Collagen-Based Biomaterials for Chronic Wounds: Rationale and Clinical Application
Gould, L. J. (2015) · Advances in Wound Care · doi:10.1089/wound.2014.0595 · Cited by 126 · see citing works
Launay, G., Salza, R., Multedo, D., Thierry‐Mieg, N., & Ricard‐Blum, S. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1091 · Cited by 124 · see citing works
Self-citationExtracellular matrix dynamics: tracking in biological systems and their implications
Hu, M. M., Ling, Z., & Ren, X. (2022) · Journal of Biological Engineering · doi:10.1186/s13036-022-00292-x · Cited by 128 · see citing works
Matrix Metalloproteinases’ Role in Tumor Microenvironment
González-Ávila, G., Sommer, B., García-Hernández, A. A., & Ramos, C. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-40146-7_5 · Cited by 121 · see citing works
Brás, L. E. D. C., & Frangogiannis, N. (2020) · Matrix Biology · doi:10.1016/j.matbio.2020.04.006 · Cited by 105 · see citing works
Collagen Biosynthesis, Processing, and Maturation in Lung Ageing
Onursal, C., Dick, E., Angelidis, I., Schiller, H. B., & Staab-Weijnitz, C. A. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.593874 · Cited by 122 · 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
Tumor Interstitial Fluid Formation, Characterization, and Clinical Implications
Wagner, M., & Wiig, H. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00115 · Cited by 111 · see citing works
Versican: A Dynamic Regulator of the Extracellular Matrix
Islam, S., & Watanabe, H. (2020) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155420953922 · Cited by 105 · see citing works
Stromal Versican Regulates Tumor Growth by Promoting Angiogenesis
Asano, K., Nelson, C. M., Nandadasa, S., Aramaki‐Hattori, N., Lindner, D. J., Alban, T. J., Inagaki, J., Ohtsuki, T., Oohashi, T., Apte, S., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-17613-6 · Cited by 101 · see citing works
Exploring the extracellular matrix in health and disease using proteomics
Taha, I. N., & Naba, A. (2019) · Essays in Biochemistry · doi:10.1042/ebc20190001 · Cited by 100 · see citing works
The cartilage extracellular matrix as a transient developmental scaffold for growth plate maturation
Melrose, J., Shu, C., Whitelock, J. M., & Lord, M. S. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.01.008 · Cited by 96 · 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
Decellularized Matrices As Cell-Instructive Scaffolds to Guide Tissue-Specific Regeneration
Robb, K. P., Shridhar, A., & Flynn, L. E. (2017) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.7b00619 · Cited by 90 · see citing works
Natural myocardial ECM patch drives cardiac progenitor based restoration even after scarring
Sarig, U., Sarig, H., de-Berardinis, E., Chaw, S. Y., Nguyen, E. B.-V., Vaibavi, S. R., Vu, T. D., Al‐Haddawi, M., Liao, S., Seliktar, D., et al. (2016) · Acta Biomaterialia · doi:10.1016/j.actbio.2016.08.031 · Cited by 88 · see citing works
Extracellular Matrix in Ischemic Heart Disease, Part 4/4
Frangogiannis, N. G., & Kovacic, J. C. (2020) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2020.03.020 · Cited by 88 · see citing works
Fighting the Fiber: Targeting Collagen in Lung Fibrosis
Staab-Weijnitz, C. A. (2021) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2021-0342tr · Cited by 83 · see citing works
Cartilage extracellular matrix-derived matrikines in osteoarthritis
Rapp, A. E., & Zaucke, F. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00464.2022 · Cited by 83 · see citing works
Ma, H., Wu, X., Li, Y., & Xia, Y. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.963054 · Cited by 78 · see citing works
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Ricard‐Blum, S., & Vallet, S. D. (2015) · Biochimie · doi:10.1016/j.biochi.2015.09.016 · Cited by 76 · see citing works
Self-citationMatricryptins Network with Matricellular Receptors at the Surface of Endothelial and Tumor Cells
Ricard‐Blum, S., & Vallet, S. D. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2016.00011 · Cited by 72 · see citing works
Self-citationKim, M., Kim, K., Jung, H. Y., Jo, H., Jeong, S.-W., Lee, J., Kim, C. H., Kim, H., Cho, D.-H., & Park, H. J. (2015) · Experimental Dermatology · doi:10.1111/exd.12745 · Cited by 71 · see citing works
Perlecan, a modular instructive proteoglycan with diverse functional properties
Melrose, J. (2020) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2020.105849 · Cited by 69 · see citing works
Matrix Metalloproteinase-1 Activation Contributes to Airway Smooth Muscle Growth and Asthma Severity
Naveed, S.-U.-N., Clements, D., Jackson, D. J., Philp, C. J., Billington, C. K., Soomro, I. N., Reynolds, C., Harrison, T., Johnston, S. L., Shaw, D. E., et al. (2017) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201604-0822oc · Cited by 68 · see citing works
Basement membrane fragments in the context of the epithelial-to-mesenchymal transition
Horejs, C. (2016) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2016.06.002 · Cited by 66 · see citing works
Etich, J., Koch, M., Wagener, R., Zaucke, F., Fabri, M., & Brachvogel, B. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20205086 · Cited by 64 · 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
Boucherat, O., Yokokawa, T., Krishna, V., Kalyana-Sundaram, S., Martineau, S., Breuils-Bonnet, S., Azhar, N., Bonilla, F., Gutstein, D., Potus, F., et al. (2022) · Nature Cardiovascular Research · doi:10.1038/s44161-022-00113-w · Cited by 64 · see citing works
Renaud, L., da Silveira, W. A., Takamura, N., Hardiman, G., & Feghali‐Bostwick, C. A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00383 · Cited by 59 · see citing works
Extracellular matrix in cancer progression and therapy
He, X., Lee, B., & Jiang, Y. (2022) · Medical Review · doi:10.1515/mr-2021-0028 · Cited by 56 · see citing works
The Role of Collagen-Based Biomaterials in Chronic Wound Healing and Sports Medicine Applications
Yeung, D. A., & Kelly, N. H. (2021) · Bioengineering · doi:10.3390/bioengineering8010008 · Cited by 56 · see citing works
Maiti, G., Frikeche, J., Lam, C. Y.-M., Biswas, A., Shinde, V. M., Samanovic, M. I., Kagan, J. C., Mulligan, M. J., & Chakravarti, S. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2100999118 · Cited by 53 · see citing works
Mostovenko, E., Young, T. L., Muldoon, P. P., Bishop, L. M., Canal, C. G., Vucetic, A., Zeidler-Erdely, P. C., Erdely, A., Campen, M. J., & Ottens, A. K. (2019) · Particle and Fibre Toxicology · doi:10.1186/s12989-019-0304-6 · Cited by 52 · see citing works
Kim, D.-H., Kim, M.-J., Kwak, S.-Y., Jeong, J., Choi, D., Choi, S. W., Ryu, J., & Kang, K.-S. (2023) · Nature Communications · doi:10.1038/s41467-023-35941-2 · Cited by 53 · see citing works
Matrix remodeling in chronic lung diseases
Gu, B., Madison, M. C., Corry, D. B., & Kheradmand, F. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.03.012 · Cited by 50 · see citing works
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Mohindra, R., Agrawal, D. K., & Thankam, F. G. (2021) · Journal of Cardiovascular Translational Research · doi:10.1007/s12265-020-10091-8 · Cited by 50 · see citing works
Integrin signalling in joint development, homeostasis and osteoarthritis
Miao, M. Z., Lee, J. S., Yamada, K. M., & Loeser, R. F. (2024) · Nature Reviews Rheumatology · doi:10.1038/s41584-024-01130-8 · Cited by 48 · see citing works
Dentinogenic effects of extracted dentin matrix components digested with matrix metalloproteinases
Okamoto, M., Takahashi, Y., Komichi, S., Cooper, P. R., & Hayashi, M. (2018) · Scientific Reports · doi:10.1038/s41598-018-29112-3 · Cited by 47 · see citing works
Docking software performance in protein-glycosaminoglycan systems
Uciechowska‐Kaczmarzyk, U., de Beauchêne, I. C., & Samsonov, S. A. (2019) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2019.04.001 · Cited by 47 · see citing works
Cardiac ECM: Its Epigenetic Regulation and Role in Heart Development and Repair
Song, R., & Zhang, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228610 · Cited by 47 · see citing works
Mazloomnejad, R., Babajani, A., Kasravi, M., Ahmadi, A., Shariatzadeh, S., Bahrami, S., & Niknejad, H. (2023) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2023.1103727 · Cited by 46 · see citing works
Kazemi, A., Fathy, M., Jahanian, A., Khanali, J., Ostadi, Y., Babajani, A., Tayebi, T., & Niknejad, H. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118457 · Cited by 48 · see citing works
Mutgan, A. C., Jandl, K., & Kwapiszewska, G. (2020) · Cells · doi:10.3390/cells9092029 · Cited by 45 · see citing works
Liang, D., Liu, L., Zhao, Y., Luo, Z., He, Y., Li, Y., Tang, S., Tang, J., & Chen, N. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1186712 · Cited by 43 · see citing works
Functional Insights from the Proteomic Inventory of Ovine Forestomach Matrix
Dempsey, S. G., Miller, C. H., Hill, R. C., Hansen, K. C., & May, B. C. H. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00908 · Cited by 42 · see citing works
Huynh, M., Pak, C., Markovina, S. S., Callander, N. S., Chng, K. S., Wuerzberger‐Davis, S. M., Bakshi, D. D., Kink, J. A., Hematti, P., Hope, C. L., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000667 · Cited by 41 · see citing works
Cardiomyogenesis Modeling Using Pluripotent Stem Cells: The Role of Microenvironmental Signaling
Leitolis, A., Robert, A. W., Pereira, I. T., Correa, A., & Stimamiglio, M. A. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00164 · Cited by 38 · see citing works
Exploring the roles of MACIT and multiplexin collagens in stem cells and cancer
Izzi, V., Heljäsvaara, R., Heikkinen, A., Karppinen, S., Koivunen, J. T., & Pihlajaniemi, T. A. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.08.033 · Cited by 35 · see citing works
Levy, C., Brooks, J. M., Chen, J., Su, J., & Fox, M. A. (2014) · The Journal of Comparative Neurology · doi:10.1002/cne.23701 · Cited by 38 · see citing works
Elmansi, A. M., Awad, M. E., Eisa, N. H., Kondrikov, D., Hussein, K. A., Aguilar‐Perez, A., Herberg, S., Periyasamy‐Thandavan, S., Fulzele, S., Hamrick, M. W., et al. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.02.005 · Cited by 38 · see citing works
Tanaka, H. Y., Nakazawa, T., Enomoto, A., Masamune, A., & Kano, M. R. (2023) · Cancers · doi:10.3390/cancers15030724 · Cited by 40 · see citing works
Barallobre‐Barreiro, J., Lynch, M., Yin, X., & Mayr, M. (2016) · Cardiovascular Research · doi:10.1093/cvr/cvw206 · Cited by 37 · see citing works
Decellularized Diaphragmatic Muscle Drives a Constructive Angiogenic Response In Vivo
Fallas, M. E. A., Piccoli, M., Franzin, C., Sgrò, A., Dedja, A., Urbani, L., Bertin, E., Trevisan, C., Gamba, P., Burns, A. J., et al. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051319 · Cited by 37 · see citing works
Petersen, E. V., Chudakova, D. A., Skorova, E., Anikin, V., Решетов, И. В., & Mynbaev, O. A. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.575569 · Cited by 36 · see citing works
Steiner, D., Winkler, S., Heltmann‐Meyer, S., Trossmann, V. T., Fey, T., Scheibel, T., Horch, R. E., & Arkudas, A. (2021) · Biofabrication · doi:10.1088/1758-5090/ac0d9b · Cited by 35 · see citing works
Miao, M. Z., Su, Q. P., Cui, Y., Bahnson, E. M., Li, G., Wang, M., Yang, Y., Collins, J. A., Wu, D., Gu, Q., et al. (2023) · Science Signaling · doi:10.1126/scisignal.adf8299 · Cited by 36 · see citing works
Masoumifeshani, B., Kenari, A. A., Sottorff, I., Crüsemann, M., & Moghaddam, J. A. (2025) · Marine Drugs · doi:10.3390/md23040162 · Cited by 34 · see citing works
Haywood, J., Qi, J., Chen, C., Lu, G., Liu, Y., Yan, J., Shi, Y., & Gao, G. F. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1522572113 · Cited by 32 · see citing works
Ricciardelli, C., Lokman, N. A., Ween, M. P., & Oehler, M. K. (2016) · Endocrine Related Cancer · doi:10.1530/erc-16-0320 · Cited by 32 · see citing works
Joshi, R., Goihberg, E., Ren, W., Pilichowska, M. E., & Mathew, P. F. (2016) · Cell Adhesion & Migration · doi:10.1080/19336918.2016.1212139 · Cited by 31 · see citing works
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González-Ávila, G., Sommer, B., García-Hernández, A. A., Ramos, C., & Flores‐Soto, E. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.918789 · Cited by 30 · see citing works
Melrose, J., Fuller, E. S., & Little, C. B. (2017) · Connective Tissue Research · doi:10.1080/03008207.2017.1284824 · Cited by 30 · see citing works
The Effects of a Novel Series of KTTKS Analogues on Cytotoxicity and Proteolytic Activity
Tałałaj, U., Uścinowicz, P., Bruzgo, I., Surażyński, A., Zaręba, I., & Markowska, A. (2019) · Molecules · doi:10.3390/molecules24203698 · Cited by 28 · see citing works
Any route for melanoblasts to colonize the skin!
Petit, V., & Larue, L. (2016) · Experimental Dermatology · doi:10.1111/exd.13061 · Cited by 27 · see citing works
A tissue-specific, injectable acellular gel for the treatment of chronic vocal fold scarring
Xu, C. C., & Mau, T. (2019) · Acta Biomaterialia · doi:10.1016/j.actbio.2019.08.025 · Cited by 27 · see citing works
Proteomic Analysis of Porcine-Derived Collagen Membrane and Matrix
Lee, J., Mitulović, G., Panahipour, L., & Gruber, R. (2020) · Materials · doi:10.3390/ma13225187 · Cited by 24 · see citing works
Granzyme B as a therapeutic target: an update in 2022
Aubert, A., Lane, M. D., Jung, K., & Granville, D. J. (2022) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2022.2161890 · Cited by 24 · see citing works
Paracrine Role for Somatostatin Interneurons in the Assembly of Perisomatic Inhibitory Synapses
Su, J., Basso, D., Iyer, S., Su, K., Wei, J., & Fox, M. A. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.0613-20.2020 · Cited by 24 · see citing works
Hußler, W., Höhn, L., Stolz, C., Vielhaber, S., Garz, C., Schmitt, F. C., Gundelfinger, E. D., Schreiber, S., & Seidenbecher, C. I. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.838432 · Cited by 23 · see citing works
Engineered basement membranes: fromin vivoconsiderations to cell-based assays
Perry, G., Xiao, W., Welsh, G. I., Perriman, A. W., & Lennon, R. (2018) · Integrative Biology · doi:10.1039/c8ib00138c · Cited by 23 · see citing works
Systemic cell therapy for muscular dystrophies
Ausems, C. R. M., van Engelen, B. G. M., van Bokhoven, H., & Wansink, D. G. (2020) · Stem Cell Reviews and Reports · doi:10.1007/s12015-020-10100-y · Cited by 22 · see citing works
Smith, M. M., & Melrose, J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26189182 · Cited by 21 · see citing works
Cells and mediators of inflammation as effectors of epithelial repair in the inflamed intestine
Crifò, B., & MacNaughton, W. K. (2021) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00194.2021 · Cited by 19 · see citing works
Yuan, Y., Zhang, X., Zhan, Y., Tang, S., Deng, P., Wang, Z., & Li, J. (2022) · Stem Cell Research & Therapy · doi:10.1186/s13287-022-02907-y · Cited by 20 · see citing works
- Authors
- Ricard‐Blum, S., & Salza, R.
- Affiliations
- Lyon 1 Université (FR)
- Corresponding author
- Ricard‐Blum, Sylvie
- Venue
- Experimental Dermatology
- Publisher
- Wiley
- Published
- 2014-07
- Volume
- 23
- Issue
- 7
- Pages
- 457-463
- ISSN
- 0906-6705 (ISSN-L)
- 1600-0625
- OpenAlex
- W2011478609
- Cited by
- 224
- References
- 161
- Citations by year
- 2026: 20 · 2025: 15 · 2024: 19 · 2023: 17 · 2022: 19 · 2021: 19 · 2020: 20 · 2019: 22 · 2018: 20 · 2017: 17 · 2016: 19 · 2015: 13 · 2014: 4
- FWCI
- 1.78
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Experimental Dermatology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Connective Tissue Growth Factor Research
- Keywords
- matrikines, extracellular matrix, proteoglycans, glycosaminoglycans, enzymatic cleavage, angiogenesis, cancer, fibrosis, inflammation, neurodegenerative diseases, wound healing, drug development
- MeSH terms
- Animals, Extracellular Matrix, Glycosaminoglycans, Humans, Inflammation, Models, Theoretical, Neoplasms, Neovascularization, Pathologic, Proteoglycans, Skin Diseases, Wound Healing, Extracellular Matrix Proteins, Protein Structure, Tertiary, Neurodegenerative Diseases, Proteomics, Systems Biology, Mice
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