Immunomodulatory Role of the Extracellular Matrix Within the Liver Disease Microenvironment
Open accessAbstract
Chronic liver disease when accompanied by underlying fibrosis, is characterised by an accumulation of extracellular matrix (ECM) proteins and chronic inflammation. Although traditionally considered as a passive and largely architectural structure, the ECM is now being recognised as a source of potent DAMPs with immune-active peptides and domains. In parallel, the ECM anchors a range of cytokines, chemokines and growth factors, all of which are capable of modulating the immune responses. A growing body of evidence shows that ECM proteins themselves are capable of interacting both directly, via a wide range of receptors including integrins and TLRs, and indirectly with immune cells. ECM deposition and remodelling during fibrosis can result in release or formation of ECM-DAMPs, which can drive immune cellular infiltration and sterile inflammation. Both the ECM and immune response are interlinked and integral in driving fibrosis, although their precise interactions in the context of chronic liver disease are poorly understood. This review aims to shed light on the ECM-immune interactions underlying liver disease, in particular fibrosis of different aetiologies, by describing the main ECM intact proteins and ECM-DAMPs with known immune regulatory activity. We also discuss how tissue engineering could provide new opportunities to explore ECM-immune cell interactions in bioreactor-based dynamic 3D models containing intact decellularized ECM scaffolds. A better understanding of these interactions would aid in the identification of new antifibrotic and immunomodulatory targets for treatment and biomarkers in liver disease.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
LMWHAs are released during ECM damage or degradation, act as DAMPs and drive inflammatory responses such as enhancing immune cell chemotaxis, DC maturation, and M1 polarization of macrophages via CD44 and TLRs.
“In contrast to HMWHAs, low molecular weight hyaluronic acids (LMWHAs) are released during ECM damage or degradation, which act as DAMPs and drive inflammatory responses such as enhancing immune cells chemotaxis, DCs maturation, and M1 polarization of macrophages via the same receptors (CD44 and TLRs) [63, 100].”
From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [100]
The “Low Molecular Weight-Hyaluronic Acid” section (page unavailable) says HA fragments arise during injury, identifies LMW-HA as an ECM-DAMP, and describes pro-inflammatory responses through TLR2, TLR4 and CD44. It reports antigen-presenting-cell maturation and cell migration, but does not specifically establish immune-cell chemotaxis or M1 macrophage polarization. (LLM, conf=0.88)
Experimental — accuracy not yet measuredActivation of TLRs and CD44 receptors by HMWHAs accompanies a decrease in DC maturation and promotion in the polarization of macrophages toward M2 phenotype besides differentiation of T cells into regulatory phenotype and induction of apoptosis in activated T cells.
“Activation of these receptors accompanies a decrease in DC maturation and promotion in the polarization of macrophages toward M2 phenotype besides differentiation of T cells into regulatory phenotype and induction of apoptosis in activated T cells.”
From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [100]
Split into 2 atoms — 0 confirmed, 2 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measuredImmunomodulatory traits of dECM scaffolds are largely attributed to the ability of their collagens to trigger LAIR-1 of immune cells and consequently downregulation of immune cell activity.
“Immunomodulatory traits of dECM scaffolds are largely attributed to the ability of their collagens to trigger leukocyte-associated immunoglobulin-like receptors-1 (LAIR-1) of immune cells and consequently downregulation of immune cell activity [100].”
From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [100]
The “Immunomodulatory Properties of the ECM” and “Collagen” sections say collagen binds LAIR-1 on immune cells and that this interaction suppresses immune activity (page unavailable). The Discussion addresses decellularized ECM scaffolds, but does not say their immunomodulatory traits are largely due to collagen–LAIR-1 signaling; it also describes other ECM immunomodulatory mechanisms. (LLM, conf=0.87)
Experimental — accuracy not yet measuredHMWHAs exert anti-inflammatory effects by impeding antigen-antibody interaction and triggering TLRs and CD44 receptors of innate and adaptive immune cells.
“In another example, high molecular weight hyaluronic acids (HMWHAs), well-known GAGs of dECM, exert anti-inflammatory effects by impeding antigen-antibody interaction and triggering toll-like receptors (TLRs), a subgroup of PRRs, and CD44 receptors of innate and adaptive immune cells.”
From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [100]
The High Molecular Weight-Hyaluronic Acid section describes HMW-HA as anti-inflammatory, says it limits antigen–antibody interactions, and reports immune-regulatory effects through CD44. It says HMW-HA inhibits TLR2 signaling, however, rather than triggering TLRs; the Low Molecular Weight-Hyaluronic Acid section attributes TLR2 and TLR4 activation to LMW-HA. (LLM, conf=0.90)
Experimental — accuracy not yet measuredECM is a reservoir for cryptic particles that activate or suppress inflammation and orchestrates innate and adaptive immune responses.
“ECM is a reservoir for the cryptic particles that activate or suppress inflammation and orchestrates innate and adaptive immune responses [100, 101].”
From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [100]
Harsh decellularization procedures may unveil certain cryptic helical and terminal antigenic sites of collagen, prompting initiation of antibody production against the ECM.
“For instance, harsh decellularization procedures may unveil certain cryptic helical and terminal antigenic sites of collagen, prompting the initiation of antibody production against the ECM [73].”
From Liver tissue engineering using decellularized scaffolds: Current progress, challenges, and opportunities (2024) · cites this paper as [73]
The Discussion (page unavailable) describes how decellularization can alter ECM composition and states that removing cellular content reduces the risk of negative immune responses. The Collagen section (page unavailable) describes collagen’s interactions with immune-cell receptors. Neither section addresses whether harsh decellularization exposes cryptic collagen antigenic sites or initiates antibody production; searches for those terms found no supporting passage. (LLM, conf=0.73)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Molecular Mechanisms of Stress-Responsive Changes in Collagen and Elastin Networks in Skin
Aziz, J., Shezali, H., Radzi, Z., Yahya, N. A., Abu Kassim, N. H., Czernuszka, J., & Rahman, M. T. (2016) · Skin Pharmacology and Physiology · doi:10.1159/000447017 · Cited by 7,323 · see citing works
Cellular senescence: when bad things happen to good cells
Campisi, J., & d'Adda di Fagagna, F. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2233 · Cited by 4,441 · see citing works
Mechanisms of hepatic stellate cell activation
Tsuchida, T., & Friedman, S. L. (2017) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2017.38 · Cited by 2,909 · see citing works
A complex secretory program orchestrated by the inflammasome controls paracrine senescence
Acosta, J. C., Banito, A., Wuestefeld, T., Georgilis, A., Janich, P., Morton, J. P., Athineos, D., Kang, T.-W., Lasitschka, F., Andrulis, M., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2784 · Cited by 2,278 · see citing works
Munger, 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 · see citing works
Senescence of activated stellate cells limits liver fibrosis
Krizhanovsky, V., Yon, M., Dickins, R. A., Hearn, S., Simon, J., Miething, C., Yee, H., Zender, L., & Lowe, S. W. (2008) · Cell · doi:10.1016/j.cell.2008.06.049 · Cited by 2,029 · see citing works
Senescence of Activated Stellate Cells Limits Liver Fibrosis
Krizhanovsky, V., Yon, M., Dickins, R. A., Hearn, S., Simon, J., Miething, C., Yee, H., Zender, L., & Lowe, S. W. (2008) · Cell · doi:10.1016/j.cell.2008.09.015 · Cited by 2,027
Pathogenesis of Liver Fibrosis
Hernandez-Gea, V., & Friedman, S. L. (2011) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-011110-130246 · Cited by 1,809 · see citing works
T-helper Type 2–driven Inflammation Defines Major Subphenotypes of Asthma
Woodruff, P. G., Modrek, B., Choy, D. F., Jia, G., Abbas, A. R., Ellwanger, A., Arron, J. R., Koth, L. L., & Fahy, J. V. (2009) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200903-0392oc · Cited by 1,806 · see citing works
Making sense of latent TGFβ activation
Annes, J. P., Munger, J. S., & Rifkin, D. B. (2002) · Journal of Cell Science · doi:10.1242/jcs.00229 · Cited by 1,624 · see citing works
Mechanobiology of YAP and TAZ in physiology and disease
Panciera, T., Azzolin, L., Cordenonsi, M., & Piccolo, S. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.87 · Cited by 1,461 · see citing works
Oligosaccharides of Hyaluronan Activate Dendritic Cells via Toll-like Receptor 4
Termeer, C., Benedix, F., Sleeman, J., Fieber, C., Voith, U., Ahrens, T., Miyake, K., Freudenberg, M., Galanos, C., & Simon, J. C. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20001858 · Cited by 1,378 · see citing works
Inflammatory networks during cellular senescence: causes and consequences.
Freund, A., Orjalo, A. V., Desprez, P.-Y., & Campisi, J. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.03.003 · Cited by 1,354 · see citing works
Proteoglycans as modulators of growth factor activities
Ruoslahti, E. I., & Yamaguchi, Y. (1991) · Cell · doi:10.1016/0092-8674(91)90308-l · Cited by 1,342 · see citing works
Liver fibrosis and repair: Immune regulation of wound healing in a solid organ
Pellicoro, A., Ramachandran, P., Iredale, J. P., & Fallowfield, J. A. (2014) · Nature Reviews Immunology · doi:10.1038/nri3623 · Cited by 1,310 · see citing works
Liver inflammation and fibrosis
Koyama, Y., & Brenner, D. A. (2017) · Journal of Clinical Investigation · doi:10.1172/jci88881 · Cited by 1,295 · see citing works
Seitz, H. K., Bataller, R., Cortez-Pinto, H., Gao, B., Gual, A., Lackner, C., Mathurin, P., Mueller, S., Szabo, G., & Tsukamoto, H. (2018) · Nature Reviews Disease Primers · doi:10.1038/s41572-018-0014-7 · Cited by 1,271 · see citing works
Daynes, R. A., Araneo, B. A., Ershler, W. B., Maloney, C., Li, G. Z., & Ryu, S. Y. (1993) · The Journal of Immunology · doi:10.4049/jimmunol.150.12.5219 · Cited by 1,264 · see citing works
CD36, a Scavenger Receptor Involved in Immunity, Metabolism, Angiogenesis, and Behavior
Silverstein, R. L., & Febbraio, M. (2009) · Science Signaling · doi:10.1126/scisignal.272re3 · Cited by 1,247 · see citing works
The Extra Domain A of Fibronectin Activates Toll-like Receptor 4
Okamura, Y., Watari, M., Jerud, E. S., Young, D. W., Ishizaka, S. T., Rose, J., Chow, J. C., & Strauss, J. F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100099200 · Cited by 1,217 · see citing works
Liver fibrosis: Pathophysiology, pathogenetic targets and clinical issues
Parola, M., & Pinzani, M. (2018) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2018.09.002 · Cited by 1,183 · see citing works
Immunology in the liver — from homeostasis to disease
Heymann, F., & Tacke, F. (2016) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2015.200 · Cited by 1,180 · see citing works
Interleukin‐10‐secreting type 1 regulatory T cells in rodents and humans
Roncarolo, M. G., Gregori, S., Battaglia, M., Bacchetta, R., Fleischhauer, K., & Levings, M. K. (2006) · Immunological Reviews · doi:10.1111/j.0105-2896.2006.00420.x · Cited by 1,174 · see citing works
Hyaluronan fragments: An information-rich system
Stern, R., Asari, A., & Sugahara, K. N. (2006) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2006.05.009 · Cited by 1,142 · see citing works
Angiogenesis 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
Eta-1 (Osteopontin): An Early Component of Type-1 (Cell-Mediated) Immunity
Ashkar, S., Weber, G. F., Panoutsakopoulou, V., Sanchirico, M. E., Jansson, M., Zawaideh, S., Rittling, S. R., Denhardt, D. T., Glimcher, M. J., & Cantor, H. (2000) · Science · doi:10.1126/science.287.5454.860 · Cited by 1,125 · see citing works
SUBEPITHELIAL FIBROSIS IN THE BRONCHI OF ASTHMATICS
Roche, W. R., Williams, J. H., Beasley, R. W., & Holgate, S. T. (1989) · The Lancet · doi:10.1016/s0140-6736(89)90067-6 · Cited by 1,121 · see citing works
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 · see citing works
Transforming growth factor-beta in disease: the dark side of tissue repair.
Border, W. A., & Ruoslahti, E. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115821 · Cited by 1,096 · see citing works
Collagen-based biomaterials for wound healing
Chattopadhyay, S., & Raines, R. T. (2014) · Biopolymers · doi:10.1002/bip.22486 · Cited by 1,041 · see citing works
Badylak, S. F., Taylor, D., & Uygun, K. (2011) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-071910-124743 · Cited by 1,041 · see citing works
TGF-β and immune cells: an important regulatory axis in the tumor microenvironment and progression
Yang, L., Pang, Y., & Moses, H. L. (2010) · Trends in Immunology · doi:10.1016/j.it.2010.04.002 · Cited by 1,023 · see citing works
Latent TGF-β structure and activation
Shi, M., Zhu, J., Wang, R., Chen, X., Mi, L., Walz, T., & Springer, T. A. (2011) · Nature · doi:10.1038/nature10152 · Cited by 1,013 · see citing works
Mechanisms of suppression by suppressor T cells
von Boehmer, H. (2005) · Nature Immunology · doi:10.1038/ni1180 · Cited by 1,005 · see citing works
Targeting hepatic macrophages to treat liver diseases
Tacke, F. (2017) · Journal of Hepatology · doi:10.1016/j.jhep.2017.02.026 · Cited by 1,003 · see citing works
Border, W. A., Noble, N. A., Yamamoto, T., Harper, J. R., Yamaguchi, Y., Pierschbacher, M. D., & Ruoslahti, E. I. (1992) · Nature · doi:10.1038/360361a0 · Cited by 972 · see citing works
Hepatic inflammation and fibrosis: Functional links and key pathways
Seki, E., & Schwabe, R. F. (2015) · Hepatology · doi:10.1002/hep.27332 · Cited by 972 · see citing works
Matricellular proteins: extracellular modulators of cell function
BORNSTEIN, P. K., & Sage, E. H. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(02)00361-7 · Cited by 966 · see citing works
Choi, Y. S., Kageyama, R., Eto, D. S., Escobar, T. C., Johnston, R. J., Monticelli, L. A., Lao, C., & Crotty, S. (2011) · Immunity · doi:10.1016/j.immuni.2011.03.023 · Cited by 953 · see citing works
Receptor-Ligand Interaction Between CD44 and Osteopontin (Eta-1)
Weber, G. F., Ashkar, S., Glimcher, M. J., & Cantor, H. (1996) · Science · doi:10.1126/science.271.5248.509 · Cited by 950 · see citing works
Tissue repair and the dynamics of the extracellular matrix
Midwood, K. S., Williams, L. V., & Schwarzbauer, J. E. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2003.12.003 · Cited by 919 · see citing works
Harmancı, A. S., Youngblood, M. W., Clark, V. E., Coşkun, S., Henegariu, O., Durán, D., Erson-Omay, Z., Kaulen, L. D., Lee, T. I., Abraham, B. J., et al. (2018) · Nature Communications · doi:10.1038/ncomms16215 · Cited by 907 · see citing works
Inflammasome inhibition prevents α-synuclein pathology and dopaminergic neurodegeneration in mice
Gordon, R., Albornoz, E. A., Christie, D. C., Langley, M. R., Kumar, V., Mantovani, S., Robertson, A. A. B., Butler, M. S., Rowe, D. B., O’Neill, L. A., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aah4066 · Cited by 897 · see citing works
Integrin-associated protein (CD47) and its ligands
Brown, E. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01906-1 · Cited by 880 · see citing works
Schaefer, L., Babelova, A., Kiss, E., Hausser, H.-J., Baliova, M., Krzyzankova, M., Marsche, G., Young, M. F., Mihalik, D., Götte, M., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23755 · Cited by 850 · see citing works
Lipotoxicity and the gut-liver axis in NASH pathogenesis
Marra, F., & Svegliati-Baroni, G. (2018) · Journal of Hepatology · doi:10.1016/j.jhep.2017.11.014 · Cited by 847 · see citing works
Kielty, C. M., Sherratt, M. J., & Shuttleworth, C. A. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.14.2817 · Cited by 841 · see citing works
Woodruff, P. G., Boushey, H. A., Dolganov, G. M., Barker, C. S., Yang, Y. H., Donnelly, S., Ellwanger, A., Sidhu, S. S., Dao-Pick, T. P., Pantoja, C., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707413104 · Cited by 828 · see citing works
McKee, C. M., Penno, M. B., Cowman, M. K., Burdick, M., Strieter, R. M., Bao, C., & Noble, P. W. (1996) · Journal of Clinical Investigation · doi:10.1172/jci119054 · Cited by 809 · see citing works
Feedback amplification of fibrosis through matrix stiffening and COX-2 suppression
Liu, F., Mih, J. D., Shea, B. S., Kho, A. T., Sharif, A. S., Tager, A. M., & Tschumperlin, D. J. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201004082 · Cited by 799 · see citing works
Xiong, G., Deng, L., Zhu, J., Rychahou, P. G., & Xu, R. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-1 · Cited by 756 · see citing works
Emerging Role of Endosomal Toll-Like Receptors in Rheumatoid Arthritis
Thwaites, R. S., Chamberlain, G., & Sacre, S. M. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00001 · Cited by 748 · see citing works
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 · see citing works
Hyaluronan Fragments Act as an Endogenous Danger Signal by Engaging TLR2
Scheibner, K. A., Lutz, M. A., Boodoo, S., Fenton, M. J., Powell, J. D., & Horton, M. R. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.2.1272 · Cited by 708 · see citing works
CCN proteins: multifunctional signalling regulators
Perbal, B. (2004) · The Lancet · doi:10.1016/s0140-6736(03)15172-0 · Cited by 704 · see citing works
Midwood, K. S., Sacre, S. M., Piccinini, A. M., Inglis, J. J., Trébaul, A., Chan, E., Drexler, S. K., Sofat, N., Kashiwagi, M., Orend, G., et al. (2009) · Nature Medicine · doi:10.1038/nm.1987 · Cited by 704 · see citing works
Fisher, L. W., Termine, J. D., & Young, M. F. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83781-4 · Cited by 703 · see citing works
Takayama, G., Arima, K., Kanaji, T., Toda, S., Tanaka, H., Shoji, S., McKenzie, A. N. J., Nagai, H., Hotokebuchi, T., & Izuhara, K. (2006) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2006.02.046 · Cited by 677 · see citing works
Oberhammer, F., Pavelka, M., Sharma, S., Tiefenbacher, R., Purchio, A. F., Bursch, W., & Schulte‐Hermann, R. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.12.5408 · Cited by 669 · see citing works
Bianco, P., Fisher, L. W., Young, M. F., Termine, J. D., & Robey, P. G. (1990) · Journal of Histochemistry & Cytochemistry · doi:10.1177/38.11.2212616 · Cited by 667 · see citing works
Periostin induces proliferation of differentiated cardiomyocytes and promotes cardiac repair
Kühn, B., del Monte, F., Hajjar, R. J., Chang, Y.-S., Lebeche, D., Arab, S., & Keating, M. T. (2007) · Nature Medicine · doi:10.1038/nm1619 · Cited by 658 · see citing works
Vieira, P. L., Christensen, J. R., Minaee, S., O’Neill, E. J., Barrat, F. J., Boonstra, A., Barthlott, T., Stockinger, B., Wraith, D. C., & O’Garra, A. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.10.5986 · Cited by 652 · see citing works
The extracellular matrix and transforming growth factor-β1: Tale of a strained relationship
Hinz, B. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.05.006 · Cited by 618 · see citing works
Complexity of Danger: The Diverse Nature of Damage-associated Molecular Patterns
Schaefer, L. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.619304 · Cited by 618 · see citing works
Shaping Gene Expression in Activated and Resting Primary Macrophages by IL-10
Lang, R., Patel, D. H., Morris, J. J., Rutschman, R. L., & Murray, P. J. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.5.2253 · Cited by 613 · see citing works
Eggert, T., Wolter, K., Ji, J., Ma, C., Yevsa, T., Klotz, S., Medina-Echeverz, J., Longerich, T., Forgues, M., Reisinger, F., et al. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.09.003 · Cited by 609 · see citing works
The epidemiology of non‐alcoholic fatty liver disease
Bellentani, S. (2017) · Liver International · doi:10.1111/liv.13299 · Cited by 607 · see citing works
The Long–Term Pathological Evolution of Chronic Hepatitis C
Yano, M., Kumada, H., Kage, M., Ikeda, K., Shimamatsu, K., INOUE, O., Hashimoto, E., Lefkowitch, J. H., Ludwig, J., & Okuda, K. (1996) · Hepatology · doi:10.1002/hep.510230607 · Cited by 598 · see citing works
Antielastin autoimmunity in tobacco smoking–induced emphysema
Lee, S., Goswami, S., Grudo, A., Song, L., Bandi, V., Goodnight-White, S., Green, L., Hacken, J. B., Huh, J., Bakaeen, F. G., et al. (2007) · Nature Medicine · doi:10.1038/nm1583 · Cited by 592 · see citing works
TGF-β and fibrosis in different organs — molecular pathway imprints
Pohlers, D., Brenmoehl, J., Loeffler, I., Müller, C. K., Leipner, C., Schultze–Mosgau, S., Stallmach, A., Kinne, R. W., & Wolf, G. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.06.004 · Cited by 576 · see citing works
Gillan, L., Matei, D. E., Fishman, D. A., Gerbin, C. S., Karlan, B. Y., & Chang, D. D. (2002) · PubMed · Cited by 560 · see citing works
Tenascins: regulation and putative functions during pathological stress
Chiquet-Ehrismann, R., & Chiquet, M. (2003) · Journal of Pathology · doi:10.1002/path.1415 · Cited by 557 · see citing works
Functions and mechanisms of action of CCN matricellular proteins
Chen, C.-C., & Lau, L. F. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.07.025 · Cited by 549 · see citing works
Hepatocyte telomere shortening and senescence are general markers of human liver cirrhosis
WIEMANN, S. U., SATYANARAYANA, A., TSAHURIDU, M., TILLMANN, H. L., ZENDER, L., KLEMPNAUER, J., FLEMMING, P., FRANCO, S., BLASCO, M. A., MANNS, M. P., et al. (2002) · The FASEB Journal · doi:10.1096/fj.01-0977com · Cited by 527 · see citing works
The role of osteopontin in inflammatory processes
Lund, S. A., Giachelli, C. M., & Scatena, M. (2009) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-009-0068-0 · Cited by 519 · see citing works
Hyaluronan, a Crucial Regulator of Inflammation
Petrey, A. C., & de la Motte, C. A. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00101 · Cited by 514 · see citing works
Cellular Binding of Hepatitis C Virus Envelope Glycoprotein E2 Requires Cell Surface Heparan Sulfate
Barth, H., Schäfer, C., Adah, M. I., Zhang, F., Linhardt, R. J., Toyoda, H., Kinoshita‐Toyoda, A., Toida, T., Kuppevelt, T. H. V., Depla, E., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302267200 · Cited by 499 · see citing works
The role of heparan sulphate in inflammation
Parish, C. R. (2006) · Nature reviews. Immunology · doi:10.1038/nri1918 · Cited by 498 · see citing works
Design of Antibacterial Agents: Alkyl Dihydroxybenzoates against Xanthomonas citri subsp. citri
Nazaré, A. C., Polaquini, C. R., Cavalca, L. B., Anselmo, D. B., Calmon, M. F., Monteiro, D. A., Zielińska, A., Rahal, P., Gomes, E., Scheffers, D., et al. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103050 · Cited by 475 · see citing works
Biglycan, a Danger Signal That Activates the NLRP3 Inflammasome via Toll-like and P2X Receptors
Bábelová, A., Moreth, K., Tsalastra, W., Zeng-Brouwers, J., Eickelberg, O., Young, M. F., Brückner, P., Pfeilschifter, J. M., Schaefer, R. M., Gröne, H., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014266 · Cited by 474 · see citing works
Schultz‐Cherry, S. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.122.4.923 · Cited by 468 · see citing works
Elastin fragments drive disease progression in a murine model of emphysema
Houghton, A. M. (2006) · Journal of Clinical Investigation · doi:10.1172/jci25617 · Cited by 462 · see citing works
Pierantonelli, I., & Svegliati‐Baroni, G. (2018) · Transplantation · doi:10.1097/tp.0000000000002480 · Cited by 459 · see citing works
Issa, R., Zhou, X., Constandinou, C. M., Fallowfield, J. A., Millward‐Sadler, H., Gaça, M. D. A., Sands, E., Suliman, I., Trim, N., & Knorr, A. (2004) · Gastroenterology · doi:10.1053/j.gastro.2004.03.009 · Cited by 455 · see citing works
Schulze, A., Gripon, P., & Urban, S. (2007) · Hepatology · doi:10.1002/hep.21896 · Cited by 445 · see citing works
The role of periostin in tissue remodeling across health and disease
Conway, S. J., Izuhara, K., Kudo, Y., Litvin, J., Markwald, R. R., Ouyang, G., Arron, J. R., Holweg, C. T. J., & Kudō, A. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1494-y · Cited by 423 · see citing works
Decellularized human liver as a natural 3D-scaffold for liver bioengineering and transplantation
Mazza, G., Rombouts, K., Rennie Hall, A., Urbani, L., Vinh Luong, T., Al-Akkad, W., Longato, L., Brown, D., Maghsoudlou, P., Dhillon, A. P., et al. (2015) · Scientific Reports · doi:10.1038/srep13079 · Cited by 415 · see citing works
Self-citationTransforming growth factor‐β in stem cells and tissue homeostasis
Xu, X., Zheng, L., Yuan, Q., Zhen, G., Crane, J. L., Zhou, X., & Cao, X. (2018) · Bone Research · doi:10.1038/s41413-017-0005-4 · Cited by 414 · see citing works
Soares, A. R., Martins‐Marques, T., Ribeiro‐Rodrigues, T., Ferreira, J. V., Catarino, S., Pinho, M. J., Zuzarte, M., Anjo, S. I., Manadas, B. J., Sluijter, J. P. G., et al. (2015) · Scientific Reports · doi:10.1038/srep14888 · Cited by 405 · see citing works
Periostin promotes chronic allergic inflammation in response to Th2 cytokines
増岡, 美., Shiraishi, H., Ohta, S., Suzuki, S., Arima, K., Aoki, S., Toda, S., Inagaki, N., Kurihara, Y., Hayashida, S., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci58978 · Cited by 389 · see citing works
Oligosaccharides of Hyaluronan Are Potent Activators of Dendritic Cells
Termeer, C., Hennies, J., Voith, U., Ahrens, T., Weiss, J. M., Prehm, P., & Simon, J. C. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.4.1863 · Cited by 388 · see citing works
Decorin Is a Biological Ligand for the Epidermal Growth Factor Receptor
Iozzo, R. V., Moscatello, D. K., McQuillan, D. J., & Eichstetter, I. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.4489 · Cited by 384 · 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
Götte, M. (2003) · The FASEB Journal · doi:10.1096/fj.02-0739rev · Cited by 346 · see citing works
Hur, E.-M., Youssef, S., Haws, M., Zhang, S. Y., Sobel, R. A., & Steinman, L. (2007) · Nature Immunology · doi:10.1038/ni1415 · Cited by 342 · see citing works
New insights into the roles of agrin
Bezáková, G., & Rüegg, M. A. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1074 · Cited by 341 · see citing works
Tenascin Is Increased in Airway Basement Membrane of Asthmatics and Decreased by an Inhaled Steroid
Laitinen, A., Altraja, A., Kämpe, M., LINDEN, M., Virtanen, I., & Laitinen, L. A. (1997) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.156.3.9610084 · Cited by 341 · see citing works
Collagens are functional, high affinity ligands for the inhibitory immune receptor LAIR-1
Lebbink, R. J., Ruiter, T. E.-D., Adelmeijer, J., Brenkman, A. B., van Helvoort, J. M. L. M., Koch, M., Farndale, R. W., Lisman, T., Sonnenberg, A., Lenting, P. J., et al. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20052554 · Cited by 339 · see citing works
Thrombospondin-1 regulation of latent TGF-β activation: A therapeutic target for fibrotic disease
Murphy-Ullrich, J. E., & Suto, M. J. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.12.009 · Cited by 337 · see citing works
Merline, R., Moreth, K., Beckmann, J., Nastase, M. V., Zeng-Brouwers, J., Tralhão, J. G., Lemarchand, P., Pfeilschifter, J., Schaefer, R. M., Iozzo, R. V., et al. (2011) · Science Signaling · doi:10.1126/scisignal.2001868 · Cited by 333 · see citing works
Noble, P. W., McKee, C. M., Cowman, M. K., & Shin, H. S. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.183.5.2373 · Cited by 323 · see citing works
Identification of Osteopontin as a Novel Marker for Early Hepatocellular Carcinoma
Shang, S., Plymoth, A., Ge, S., Feng, Z., Rosen, H. R., Sangrajrang, S., Hainaut, P. L., Marrero, J. A., & Beretta, L. (2011) · Hepatology · doi:10.1002/hep.24703 · Cited by 321 · see citing works
Porzionato, A., Stocco, E., Barbon, S., Grandi, F., Macchi, V., & De Caro, R. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19124117 · Cited by 319 · see citing works
Kanta, J. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00491 · Cited by 316 · see citing works
Replicative senescence in normal liver, chronic hepatitis C, and hepatocellular carcinomas
Paradis, V., Youssef, N., Dargère, D., Bâ, N., Bonvoust, F., Deschatrette, J., & Bedossa, P. (2001) · Human Pathology · doi:10.1053/hupa.2001.22747 · Cited by 314 · see citing works
MatrisomeDB: the ECM-protein knowledge database
Shao, X., Taha, I. N., Clauser, K. R., Gao, Y., & Naba, A. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz849 · Cited by 311 · see citing works
Liver extracellular matrix in health and disease
Bédossa, P., & Paradis, V. (2003) · The Journal of Pathology · doi:10.1002/path.1397 · Cited by 304 · see citing works
Inhibition of phagocytosis by high molecular weight hyaluronate.
Forrester, J. V., & Balazs, E. A. (1980) · PubMed · Cited by 303 · see citing works
Periostin in fibrillogenesis for tissue regeneration: periostin actions inside and outside the cell
Kudō, A. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0784-5 · Cited by 298 · see citing works
The small leucine‐rich proteoglycan biglycan modulates BMP‐4‐induced osteoblast differentiation
Chen, X., Fisher, L. W., Robey, P. G., & Young, M. F. (2004) · The FASEB Journal · doi:10.1096/fj.03-0899com · Cited by 295 · see citing works
Hyaluronan in human malignancies
Sironen, R. K., Tammi, M., Tammi, R., Auvinen, P., Anttila, M. A., & Kosma, V.-M. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.11.017 · Cited by 294 · see citing works
Interaction between Periostin and BMP-1 Promotes Proteolytic Activation of Lysyl Oxidase
Maruhashi, T., Kii, I., Saito, M., & Kudō, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.088864 · Cited by 294 · see citing works
The inhibitory collagen receptor LAIR-1 (CD305)
Meyaard, L. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0907609 · Cited by 290 · see citing works
Yamasaki, K., Muto, J., Taylor, K. R., Cogen, A. L., Audish, D., Bertin, J., Grant, E. P., Coyle, A. J., Misaghi, A., Hoffman, H. M., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806084200 · Cited by 288 · see citing works
McKee, C. M., Lowenstein, C. J., Horton, M. R., Wu, J., Bao, C., Chin, B. Y., Choi, A. M. K., & Noble, P. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.8013 · Cited by 283 · see citing works
Thrombospondin-1: Multiple Paths to Inflammation
Lopez-Dee, Z. P., Pidcock, K. A., & Gutierrez, L. S. (2011) · Mediators of Inflammation · doi:10.1155/2011/296069 · Cited by 283 · see citing works
Vaday, G. G., & Lider, O. (2000) · Journal of Leukocyte Biology · doi:10.1002/jlb.67.2.149 · Cited by 281 · see citing works
Kii, I., Nishiyama, T., Li, M., Matsumoto, K., Saito, M., Amizuka, N., & Kudō, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.051961 · Cited by 281 · see citing works
Periostin facilitates eosinophil tissue infiltration in allergic lung and esophageal responses
Blanchard, C., Mingler, M. K., McBride, M. L., Putnam, P. E., Collins, M. H., Chang, G., Stringer, K. F., Abonia, J. P., Molkentin, J. D., & Rothenberg, M. E. (2008) · Mucosal Immunology · doi:10.1038/mi.2008.15 · Cited by 281 · see citing works
Baril, P., Gangeswaran, R., Mahon, P. C., Caulee, K., Kocher, H. M., Harada, T., Zhu, M., Kalthoff, H., Crnogorac‐Jurcevic, T., & Lemoine, N. R. (2006) · Oncogene · doi:10.1038/sj.onc.1210009 · Cited by 275 · see citing works
Syn, W.-K., Choi, S. S., Liaskou, E., Karaca, G. F., Agboola, K. M., Oo, Y. H., Mi, Z., Pereira, T. A., Zdanowicz, M., Malladi, P., et al. (2011) · Hepatology · doi:10.1002/hep.23998 · Cited by 275 · see citing works
Schultz‐Cherry, S., Ribeiro, S. M. F., Gentry, L. E., & Murphy-Ullrich, J. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47086-x · Cited by 272 · see citing works
Biological interplay between proteoglycans and their innate immune receptors in inflammation
Frey, H., Schroeder, N., Manon‐Jensen, T., Iozzo, R. V., & Schaefer, L. (2013) · FEBS Journal · doi:10.1111/febs.12145 · Cited by 272 · see citing works
Mak, K. M., & Mei, R. (2017) · The Anatomical Record · doi:10.1002/ar.23567 · Cited by 269 · see citing works
Bird, T. G., Müller, M., Boulter, L., Vincent, D. F., Ridgway, R. A., Lopez-Guadamillas, E., Lu, W.-Y., Jamieson, T., Govaere, O., Campbell, A. D., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aan1230 · Cited by 261 · cited 1× · see citing works
“org 5 predominantly in hepatocytes in vivo, and this was amplified and transmitted between hepatocytes in a feedback loop TGF-b1dependent produced by macrophages (68).”
BackgroundMao, J. R., Taylor, G., Dean, W. B., Wagner, D. R., Afzal, V., Lotz, J. C., Rubin, E. M., & Bristow, J. (2002) · Nature Genetics · doi:10.1038/ng850 · Cited by 261 · see citing works
Kim, K.-H., Chen, C.-C., Monzon, R. I., & Lau, L. F. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00049-13 · Cited by 261 · see citing works
Lyon, M., Rushton, G., & Gallagher, J. T. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.29.18000 · Cited by 259 · see citing works
Urtasun, R., Lopategi, A., George, J., Leung, T. M., Lu, Y., Wang, X., Ge, X., Fiel, M. I., & Nieto, N. (2011) · Hepatology · doi:10.1002/hep.24701 · Cited by 257 · see citing works
Functions of lumican and fibromodulin: Lessons from knockout mice
Chakravarti, S. (2002) · Glycoconjugate Journal · doi:10.1023/a:1025348417078 · Cited by 248 · see citing works
Targeting of Bone Morphogenetic Protein Growth Factor Complexes to Fibrillin
Sengle, G., Charbonneau, N. L., Ono, R. N., Sasaki, T., Alvarez, J., Keene, D. R., Bächinger, H. P., & Sakai, L. Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707820200 · Cited by 245 · see citing works
The extracellular matrix as a key regulator of intracellular signalling networks
Hastings, J. F., Skhinas, J. N., Fey, D., Croucher, D. R., & Cox, T. R. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14195 · Cited by 243 · see citing works
Schober, J. M., Chen, N., Grzeszkiewicz, T. M., Jovanovic, I., Emeson, E. E., Ugarova, T. P., Ye, R. D., Lau, L. F., & Lam, S. C.-T. (2002) · Blood · doi:10.1182/blood.v99.12.4457 · Cited by 242 · 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
Hodge-Dufour, J., Noble, P. W., Horton, M. R., Bao, C., Wysocka, M., Burdick, M., Strieter, R. M., Trinchieri, G., & Puré, E. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.159.5.2492 · 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
Naba, A., Clauser, K. R., Whittaker, C. A., Carr, S. A., Tanabe, K. K., & Hynes, R. O. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-518 · Cited by 238 · see citing works
Extracellular Matrix Molecular Remodeling in Human Liver Fibrosis Evolution
Baiocchini, A., Montaldo, C., Conigliaro, A., Grimaldi, A., Correani, V., Mura, F., Ciccosanti, F., Rotiroti, N., Brenna, A., Montalbano, M., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0151736 · Cited by 238 · see citing works
Oldenborg, P. (2013) · ISRN Hematology · doi:10.1155/2013/614619 · Cited by 235 · see citing works
Yu-Wai-Man, P., Newman, N. J., Carelli, V., Moster, M. L., Biousse, V., Sadun, A. A., Klopstock, T., Vignal-Clermont, C., Sergott, R. C., Rudolph, G., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aaz7423 · Cited by 232 · see citing works
TLR-dependent cross talk between human Kupffer cells and NK cells
Tu, Z., Bozorgzadeh, A., Pierce, R. H., Kurtis, J. D., Crispe, I. N., & Orloff, M. S. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20072195 · Cited by 228 · see citing works
Goodall, K. J., Poon, I. K. H., Phipps, S., & Hulett, M. D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0109596 · Cited by 223 · see citing works
Engagement of αvβ3 Integrin Regulates Proliferation and Apoptosis of Hepatic Stellate Cells
Zhou, X., Murphy, F. R., Gehdu, N., Zhang, J., Iredale, J. P., & Benyon, R. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311668200 · Cited by 219 · see citing works
Immunosurveillance of senescent cells: the bright side of the senescence program
Sagiv, A., & Krizhanovsky, V. (2013) · Biogerontology · doi:10.1007/s10522-013-9473-0 · Cited by 208 · see citing works
Moreth, K., Brodbeck, R., Babelova, A., Gretz, N., Spieker, T., Zeng-Brouwers, J., Pfeilschifter, J., Young, M. F., Schaefer, R. M., & Schaefer, L. (2010) · Journal of Clinical Investigation · doi:10.1172/jci42213 · Cited by 207 · see citing works
The Prodomain of BMP-7 Targets the BMP-7 Complex to the Extracellular Matrix
Gregory, K. E., Ono, R. N., Charbonneau, N. L., Kuo, C.-L., Keene, D. R., Bächinger, H. P., & Sakai, L. Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504270200 · Cited by 207 · see citing works
Sugahara, K. N., Murai, T., Nishinakamura, H., Kawashima, H., Saya, H., & Miyasaka, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300347200 · Cited by 206 · see citing works
Proteome analysis of rat hepatic stellate cells
Kristensen, D. B., Kawada, N., Imamura, K., Miyamoto, Y., Tateno, C., Seki, S., Kuroki, T., & Yoshizato, K. (2000) · Hepatology · doi:10.1053/jhep.2000.9322 · Cited by 206 · see citing works
Xanthou, G., Alissafi, T., Semitekolou, M., Simoes, D., Economidou, E., Gaga, M., Lambrecht, B., Lloyd, C., & Panoutsakopoulou, V. (2007) · Nature Medicine · doi:10.1038/nm1580 · Cited by 205 · see citing works
Neutralization of Osteopontin Inhibits Obesity-Induced Inflammation and Insulin Resistance
Kiefer, F. W., Zeyda, M., Gollinger, K., Pfau, B., Neuhofer, A., Weichhart, T., Säemann, M. D., Geyeregger, R., Schlederer, M., Kenner, L., et al. (2010) · Diabetes · doi:10.2337/db09-0404 · Cited by 200 · see citing works
Hakuno, D., Kimura, N., Yoshioka, M., Mukai, M., Kimura, T., Okada, Y., Yozu, R., Shukunami, C., Hiraki, Y., Kudō, A., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci40973 · Cited by 199 · see citing works
Ruppert, S. M., Hawn, T. R., Arrigoni, A., Wight, T. N., & Bollyky, P. L. (2014) · Immunologic Research · doi:10.1007/s12026-014-8495-2 · Cited by 198 · see citing works
Interactions Between Hepatic Stellate Cells and the Immune System
Maher, J. J. (2001) · Seminars in Liver Disease · doi:10.1055/s-2001-17555 · Cited by 198 · see citing works
Correlation of Peripheral-Blood Gene Expression With the Extent of Coronary Artery Stenosis
Wingrove, J. A., Daniels, S. E., Sehnert, A. J., Tingley, W. G., Elashoff, M. R., Rosenberg, S. J., Buellesfeld, L., Grube, E., Newby, L. K., Ginsburg, G. S., et al. (2008) · Circulation Cardiovascular Genetics · doi:10.1161/circgenetics.108.782730 · Cited by 194 · see citing works
Extracellular Matrix‐Based Strategies for Immunomodulatory Biomaterials Engineering
Rowley, A. T., Nagalla, R. R., Wang, S., & Liu, W. F. (2019) · Advanced Healthcare Materials · doi:10.1002/adhm.201801578 · Cited by 193 · see citing works
Brassart, B., Fuchs, P., Huet, E., Alix, A. J. P., Wallach, J., Tamburro, A. M., Delacoux, F., Haye, B., Emonard, H., Hornebeck, W., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m003642200 · Cited by 190 · see citing works
Francki, A., Bradshaw, A. D., Bassuk, J. A., Howe, C. C., Couser, W. G., & Sage, E. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.45.32145 · Cited by 188 · see citing works
Ilkovitch, D., & Lopez, D. M. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4625 · Cited by 187 · see citing works
Kosinska, M. K., Ludwig, T. E., Liebisch, G., Zhang, R., Siebert, H.-C., Wilhelm, J., Kaesser, U., Dettmeyer, R. B., Klein, H., Ishaque, B., et al. (2015) · PLOS ONE · doi:10.1371/journal.pone.0125192 · Cited by 187 · see citing works
Frevert, C. W., Felgenhauer, J. L., Wygrecka, M., Nastase, M. V., & Schaefer, L. (2018) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155417740880 · Cited by 183 · see citing works
McCaffrey, T. A., Falcone, D. J., & Du, B. (1992) · Journal of Cellular Physiology · doi:10.1002/jcp.1041520226 · Cited by 182 · see citing works
C1q limits dendritic cell differentiation and activation by engaging LAIR-1
Son, M., Santiago‐Schwarz, F., Al‐Abed, Y., & Diamond, B. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1212753109 · Cited by 179 · see citing works
Physiological Regulation of the Immunological Synapse by Agrin
Khan, A. A., Böse, C., Yam, L. S., Soloski, M. J., & Rupp, F. (2001) · Science · doi:10.1126/science.1056594 · Cited by 177 · see citing works
Butcher, J. T., Norris, R. A., Hoffman, S., Mjaatvedt, C. H., & Markwald, R. R. (2007) · Developmental Biology · doi:10.1016/j.ydbio.2006.09.048 · Cited by 176 · see citing works
Bollyky, P. L., Lord, J. D., Masewicz, S., Evanko, S. P., Buckner, J. H., Wight, T. N., & Nepom, G. T. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.2.744 · Cited by 173 · see citing works
Horton, M. R., McKee, C. M., Bao, C., Liao, F., Farber, J. M., Hodge-Dufour, J., Puré, E., Oliver, B. L., Wright, T. M., & Noble, P. W. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.35088 · Cited by 173 · see citing works
Treatment with human metalloproteinase-8 gene delivery ameliorates experimental rat liver cirrhosis
Siller-López, F., Sandoval-Rodriguez, A. S., Salgado, S., Salazar, A., Bueno‐Topete, M. R., Garcı́a, J., Vera-Cruz, J. M., Gálvez, J., Hernández‐Cañaveral, I., & Ramos, M. H. (2004) · Gastroenterology · doi:10.1053/j.gastro.2003.12.045 · Cited by 173 · see citing works
Matricellular Protein CCN1 Activates a Proinflammatory Genetic Program in Murine Macrophages
Bai, T., Chen, C.-C., & Lau, L. F. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0902792 · Cited by 173 · see citing works
Cellular and molecular regulation of innate inflammatory responses
Liu, J., & Cao, X. (2016) · Cellular and Molecular Immunology · doi:10.1038/cmi.2016.58 · Cited by 171 · see citing works
Identification of Stromal Cells in Spleen Which Support Myelopoiesis
Lim, H. K., & O'Neill, H. C. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00001 · Cited by 169 · see citing works
Gilat, D., Hershkoviz, R., Mekori, Y. A., Vlodavsky, I., & Lider, O. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.153.11.4899 · Cited by 165 · see citing works
Tenascin, an extracellular matrix protein, exerts immunomodulatory activities.
Rüegg, C., Chiquet‐Ehrismann, R., & Alkan, Ş. Ş. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.19.7437 · Cited by 165 · see citing works
Matrix metalloproteinase functions in hepatic injury and fibrosis
Roderfeld, M. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.11.011 · Cited by 163 · 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
Mooring, M., Fowl, B. H., Lum, S. Z. C., Liu, Y., Yao, K., Softic, S., Kirchner, R., Bernstein, A., Singhi, A. D., Jay, D. G., et al. (2020) · Hepatology · doi:10.1002/hep.30928 · Cited by 162 · see citing works
Paracrine cellular senescence exacerbates biliary injury and impairs regeneration
Ferreira-Gonzalez, S., Lu, W.-Y., Raven, A., Dwyer, B., Man, T. Y., O’Duibhir, E., Lewis, P. J. S., Campana, L., Kendall, T. J., Bird, T. G., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03299-5 · Cited by 161 · see citing works
Patel, V., Knox, S. M., Likar, K. M., Lathrop, C. A., Hossain, R., Eftekhari, S., Whitelock, J., Elkin, M., Vlodavsky, I., & Hoffman, M. (2007) · Development · doi:10.1242/dev.011171 · Cited by 160 · see citing works
A role for decorin in cutaneous wound healing and angiogenesis
Järveläinen, H., Puolakkainen, P. A., Pakkanen, S. H., Brown, E. L., Höök, M., Iozzo, R. V., Sage, E. H., & Wight, T. N. (2006) · Wound Repair and Regeneration · doi:10.1111/j.1743-6109.2006.00150.x · Cited by 159 · see citing works
Regulation of Hyaluronan-Induced Chemokine Gene Expression by IL-10 and IFN-γ in Mouse Macrophages
Horton, M. R., Burdick, M. D., Strieter, R. M., Bao, C., & Noble, P. W. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.160.6.3023 · Cited by 154 · see citing works
Microenvironmental Regulation by Fibrillin-1
Sengle, G., Tsutsui, K., Keene, D. R., Tufa, S. F., Carlson, E. J., Charbonneau, N. L., Ono, R. N., Sasaki, T., Wirtz, M. K., Samples, J. R., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002425 · Cited by 152 · see citing works
Bollyky, P. L., Falk, B. A., Wu, R. P., Buckner, J. H., Wight, T. N., & Nepom, G. T. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.0109001 · Cited by 152 · see citing works
Charlton, M., Viker, K., Krishnan, A., Sanderson, S. O., Veldt, B. J., Kaalsbeek, A. J., Kendrick, M. L., Thompson, G. B., Que, F. G., Swain, J. M., et al. (2009) · Hepatology · doi:10.1002/hep.22927 · Cited by 152 · see citing works
Regulation of T-helper-cell lineage development by osteopontin: the inside story
Cantor, H., & Shinohara, M. L. (2008) · Nature reviews. Immunology · doi:10.1038/nri2460 · Cited by 151 · see citing works
Kawashima, R., Mochida, S., Matsui, A., YouLuTuZ, Y., Ishikawa, K., Toshima, K., Yamanobe, F., Inao, M., Ikeda, H., Ohno, A., et al. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0372 · Cited by 148 · see citing works
Periostin in Allergic Inflammation
Izuhara, K., Arima, K., Ohta, S., Suzuki, S., Inamitsu, M., & Yamamoto, K. (2014) · Allergology International · doi:10.2332/allergolint.13-rai-0663 · Cited by 147 · see citing works
Reactive Oxygen Species Contribute to Epidermal Hyaluronan Catabolism in Human Skin Organ Culture
Ågren, U. M., Tammi, R., & Tammi, M. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00098-1 · Cited by 144 · see citing works
Zhu, Q., Zou, L., Jagavelu, K., Simonetto, D. A., Huebert, R. C., Jiang, Z.-D., DuPont, H. L., & Shah, V. H. (2012) · Journal of Hepatology · doi:10.1016/j.jhep.2011.11.013 · Cited by 144 · see citing works
Lebbink, R. J., van den Berg, M. C. W., Ruiter, T. E.-D., Raynal, N., van Roon, J. A. G., Lenting, P. J., Jin, B., & Meyaard, L. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.3.1662 · Cited by 144 · see citing works
The extra domain A of fibronectin stimulates murine mast cells via Toll-like receptor 4
Gondokaryono, S. P., Ushio, H., Niyonsaba, F., Hara, M., Takenaka, H., Jayawardana, S. T. M., Ikeda, S., Okumura, K., & Ogawa, H. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.1206730 · Cited by 144 · see citing works
Specific expression of GPR56 by human cytotoxic lymphocytes
Peng, Y.-M., van de Garde, M. D. B., Cheng, K.-F., Baars, P. A., Remmerswaal, E. B. M., van Lier, R. A. W., Mackay, C. R., Lin, H., & Hamann, J. (2011) · Journal of Leukocyte Biology · doi:10.1189/jlb.0211092 · Cited by 142 · see citing works
Regulation of Innate and Adaptive Immunity by TGFβ
Kelly, A., Houston, S. A., Sherwood, E., Casulli, J., & Travis, M. A. (2017) · Advances in immunology · doi:10.1016/bs.ai.2017.01.001 · Cited by 142 · see citing works
Elastin fragmentation and atherosclerosis progression: The elastokine concept
Maurice, P., Blaise, S. A., Gayral, S., Debelle, L., Laffargue, M., Hornebeck, W., & Duca, L. (2013) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2012.12.004 · Cited by 142 · see citing works
Horton, M. R., Burdick, M., Strieter, R. M., Bao, C., & Noble, P. W. (1998) · PubMed · Cited by 141 · see citing works
Droguett, R., Cabello‐Verrugio, C., Riquelme, C. A., & Brandan, E. (2006) · Matrix Biology · doi:10.1016/j.matbio.2006.04.004 · Cited by 140 · see citing works
Al‐Sharif, A., Jamal, M., Zhang, L. X., Larson, K. M., Schmidt, T. A., Jay, G. D., & Elsaid, K. A. (2015) · Arthritis & Rheumatology · doi:10.1002/art.39087 · Cited by 140 · see citing works
Human papillomavirus in a necessary cause of invasive cervical cancer worldwide
(1999) · Pure Amsterdam UMC · doi:10.1002/(sici)1096-9896(199909)189:1 · Cited by 140 · see citing works
Fan, W., Liu, T., Chen, W. L., Hammad, S., Longerich, T., Haußer, I., Fu, Y., Li, N., He, Y., Liu, C., et al. (2019) · Gastroenterology · doi:10.1053/j.gastro.2019.07.036 · Cited by 140 · see citing works
Effect of intracellular lipid accumulation in a new model of non-alcoholic fatty liver disease
Chávez-Tapia, N. C., Rosso, N., & Tiribelli, C. (2012) · BMC Gastroenterology · doi:10.1186/1471-230x-12-20 · Cited by 138 · see citing works
Induction and Regulation of Macrophage Metalloelastase by Hyaluronan Fragments in Mouse Macrophages
Horton, M. R., Shapiro, S. D., Bao, C., Lowenstein, C. J., & Noble, P. W. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.7.4171 · Cited by 138 · see citing works
Bollyky, P. L., Wu, R. P., Falk, B. A., Lord, J. D., Long, S. A., Preisinger, A., Teng, B. J., Holt, G. E., Standifer, N. E., Braun, K. R., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017360108 · Cited by 136 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Fibroblasts: Origins, definitions, and functions in health and disease
Plikus, M. V., Wang, X., Sinha, S., Forte, E., Thompson, S. M., Herzog, E. L., Driskell, R. R., Rosenthal, N. A., Biernaskie, J. A., & Horsley, V. (2021) · Cell · doi:10.1016/j.cell.2021.06.024 · Cited by 1,162 · see citing works
The extracellular matrix and the immune system: A mutually dependent relationship
Sutherland, T. E., Dyer, D. P., & Allen, J. E. (2023) · Science · doi:10.1126/science.abp8964 · Cited by 519 · see citing works
Kasravi, M., Ahmadi, A., Babajani, A., Mazloomnejad, R., Hatamnejad, M. R., Shariatzadeh, S., Bahrami, S., & Niknejad, H. (2023) · Biomaterials Research · doi:10.1186/s40824-023-00348-z · Cited by 316 · see citing works
Bhattacharya, M., & Ramachandran, P. (2023) · Nature Immunology · doi:10.1038/s41590-023-01551-9 · Cited by 148 · see citing works
The Role of Epithelial Damage in the Pulmonary Immune Response
Burgoyne, R. A., Fisher, A. J., & Borthwick, L. A. (2021) · Cells · doi:10.3390/cells10102763 · Cited by 146 · see citing works
Pathophysiology and Treatment Options for Hepatic Fibrosis: Can It Be Completely Cured?
Khanam, A., Saleeb, P. G., & Kottilil, S. (2021) · Cells · doi:10.3390/cells10051097 · Cited by 132 · see citing works
Damage-associated molecular patterns (DAMPs) in diseases: implications for therapy
Lin, H., Xiong, W. G., Fu, L., Yi, J., & Yang, J. (2025) · Molecular Biomedicine · doi:10.1186/s43556-025-00305-3 · Cited by 118 · see citing works
The extracellular matrix in hepatocellular carcinoma: Mechanisms and therapeutic vulnerability
Roy, A. M., Iyer, R. V., & Chakraborty, S. (2023) · Cell Reports Medicine · doi:10.1016/j.xcrm.2023.101170 · Cited by 110 · see citing works
Rodríguez, M. J., Sabaj, M., Tolosa, G., Vielma, F. H., Zúñiga, M. J., González, D. R., & Zúñiga‐Hernández, J. (2021) · Cells · doi:10.3390/cells10123406 · Cited by 80 · see citing works
Tissue CD14+CD8+T-cells reprogrammed by myeloid cells and modulated by LPS
Pallett, L., Swadling, L., Diniz, M., Maini, A. A., Schwabenland, M., Gasull, A. D., Davies, J., Kucykowicz, S., Skelton, J., Thomas, N., et al. (2023) · Nature · doi:10.1038/s41586-022-05645-6 · Cited by 68 · see citing works
Regulation of tumor immunity and immunotherapy by the tumor collagen extracellular matrix
Flies, D. B., Langermann, S., Jensen, C., Karsdal, M. A., & Willumsen, N. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1199513 · Cited by 76 · see citing works
Mechanical homeostasis imbalance in hepatic stellate cells activation and hepatic fibrosis
Zhao, Y.-Q., Deng, X.-W., Xu, G.-Q., Lin, J., Lu, H.-Z., & Chen, J. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1183808 · Cited by 71 · see citing works
Lamb, C. A., Saifuddin, A., Powell, N., & Rieder, F. (2022) · Gastroenterology · doi:10.1053/j.gastro.2021.09.077 · Cited by 66 · see citing works
Extracellular matrix scaffold-immune microenvironment modulates tissue regeneration
Yu, Y., Zhang, W., Liu, X., Wang, H., Shen, J., Xiao, H., Mei, J., Chai, Y., & Wen, G. (2021) · Composites Part B Engineering · doi:10.1016/j.compositesb.2021.109524 · Cited by 63 · see citing works
Recent advances in liver engineering with decellularized scaffold
Dai, Q., Jiang, W., Huang, F., Song, F., Zhang, J., & Zhao, H. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.831477 · Cited by 57 · see citing works
The extracellular matrix in cancer: from understanding to targeting
Chitty, J. L., & Cox, T. R. (2025) · Trends in cancer · doi:10.1016/j.trecan.2025.05.003 · Cited by 56 · see citing works
Guo, S., Feng, Y., Zhu, X., Zhang, X., Wang, H., Wang, R., Zhang, Q., Li, Y., Ren, Y., Gao, X., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41832-3 · Cited by 51 · see citing works
Recent Advancements in Antifibrotic Therapies for Regression of Liver Fibrosis
Jangra, A., Kothari, A., Sarma, P., Medhi, B., Omar, B. J., & Kaushal, K. (2022) · Cells · doi:10.3390/cells11091500 · Cited by 48 · see citing works
Inflammation and Fibrogenesis in MAFLD: Role of the Hepatic Immune System
Torre, P., Motta, B. M., Sciorio, R., Masarone, M., & Persico, M. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.781567 · Cited by 47 · see citing works
Constructing biomimetic liver models through biomaterials and vasculature engineering
Lv, W., Zhou, H., Aazmi, A., Yu, M., Xu, X., Yang, H., Huang, Y. Y. S., & Ma, L. (2022) · Regenerative Biomaterials · doi:10.1093/rb/rbac079 · Cited by 45 · see citing works
Trussoni, C. E., O’Hara, S. P., & LaRusso, N. F. (2022) · Seminars in Immunopathology · doi:10.1007/s00281-022-00909-9 · Cited by 43 · see citing works
Vascular Derived ECM Improves Therapeutic Index of BMP‐2 and Drives Vascularized Bone Regeneration
Chen, J., Zhou, X., Sun, W., Zhang, Z., Teng, W., Wang, F., Sun, H., Zhang, W., Wang, J., Yu, X., et al. (2022) · Small · doi:10.1002/smll.202107991 · Cited by 43 · see citing works
Nanodrug removes physical barrier to promote T-cell infiltration for enhanced cancer immunotherapy
Xiao, Z., Tan, Y., Cai, Y., Huang, J., Wang, X., Li, B., Lin, L., Wang, Y., Shuai, X., & Zhu, K. (2023) · Journal of Controlled Release · doi:10.1016/j.jconrel.2023.02.029 · Cited by 41 · see citing works
H3K18 lactylation accelerates liver fibrosis progression through facilitating SOX9 transcription.
Wu, S., Li, J., & Zhan, Y.-T. (2024) · Experimental Cell Research · doi:10.1016/j.yexcr.2024.114135 · Cited by 42 · see citing works
The Material World of 3D‐Bioprinted and Microfluidic‐Chip Models of Human Liver Fibrosis
Carvalho, A. M., Bansal, R., Barrias, C. C., & Sarmento, B. F. C. C. (2023) · Advanced Materials · doi:10.1002/adma.202307673 · Cited by 36 · see citing works
In vitro modelling of the physiological and diseased female reproductive system
Stejskalová, A., Vankelecom, H. E. J., Sourouni, M., Ho, M. Y., Götte, M., & Almquist, B. D. (2021) · Acta Biomaterialia · doi:10.1016/j.actbio.2021.04.032 · Cited by 35 · see citing works
Long, J., Qin, Z., Chen, G., Song, B., & Zhang, Z. (2022) · Biomaterials Science · doi:10.1039/d2bm01204a · Cited by 35 · see citing works
Liver fibrosis: pathological features, clinical treatment and application of therapeutic nanoagents
Chen, L., Guo, W., Mao, C., Shen, J., & Wan, M. (2024) · Journal of Materials Chemistry B · doi:10.1039/d3tb02790b · Cited by 33 · see citing works
Liu, Z., Chen, J., Jo, M., Viola Vogel, B., Chen, J., Rogers, J. A., & Li, S. (2026) · Nature Reviews Bioengineering · doi:10.1038/s44222-025-00391-6 · Cited by 37 · see citing works
Human Three-Dimensional Hepatic Models: Cell Type Variety and Corresponding Applications
Xu, Q. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.730008 · Cited by 36 · see citing works
3D printed tissue models: From hydrogels to biomedical applications
Cadamuro, F., Nicotra, F., & Russo, L. (2023) · Journal of Controlled Release · doi:10.1016/j.jconrel.2023.01.048 · Cited by 34 · see citing works
Poulis, N., Martin, M., Hoerstrup, S. P., Emmert, M. Y., & Fioretta, E. S. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.952178 · Cited by 30 · see citing works
Sukei, T., Palma, E., & Urbani, L. (2021) · Cancers · doi:10.3390/cancers13215586 · Cited by 29 · see citing works
Self-citationExamination of the role of necroptotic damage-associated molecular patterns in tissue fibrosis
Liu, X., Lu, F., & Chen, X. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.886374 · Cited by 29 · see citing works
Hussein, K. H., Ahmadzada, B., Correa, J. C., Sultan, A., Wilken, S., Amiot, B., & Nyberg, S. L. (2024) · Bioactive Materials · doi:10.1016/j.bioactmat.2024.06.001 · Cited by 28 · see citing works
“ECM contains different cryptic peptides that can either stimulate or inhibit the host immune response [73].”
BackgroundA Perfusion Bioreactor for Longitudinal Monitoring of Bioengineered Liver Constructs
Sassi, L., Ajayi, O., Campinoti, S., Natarajan, D., McQuitty, C., Siena, R. R., Mantero, S., Coppi, P. D., Pellegata, A. F., Chokshi, S., et al. (2021) · Nanomaterials · doi:10.3390/nano11020275 · Cited by 27 · see citing works
Self-citationTenascin-C induction exacerbates post-stroke brain damage
Chelluboina, B., Chokkalla, A. K., Mehta, S. L., Morris-Blanco, K. C., Bathula, S., Sankar, S., Park, J. S., & Vemuganti, R. (2021) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x211056392 · Cited by 26 · see citing works
The Prospect of Hepatic Decellularized Extracellular Matrix as a Bioink for Liver 3D Bioprinting
Shi, W. T., Zhang, Z., & Wang, X. (2024) · Biomolecules · doi:10.3390/biom14081019 · Cited by 25 · see citing works
Liver scaffolds obtained by decellularization: A transplant perspective in liver bioengineering
Dias, M. L., Paranhos, B. A., & Goldenberg, R. C. D. S. (2022) · Journal of Tissue Engineering · doi:10.1177/20417314221105305 · Cited by 24 · see citing works
Melaibari, M., Alkreathy, H. M., Esmat, A., Rajeh, N. A., Shaik, R. A., Alghamdi, A. A., & Ahmad, A. (2023) · Biomedicines · doi:10.3390/biomedicines11051342 · Cited by 24 · see citing works
Advances in the Insulin–Heart Axis: Current Therapies and Future Directions
Caturano, A., Vetrano, E., Galiero, R., Sardu, C., Rinaldi, L., Russo, V., Monda, M., Marfella, R., & Sasso, F. C. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251810173 · Cited by 23 · see citing works
The extracellular matrix in inflammation and cancer
Zhang, W., Xiang, Y., Lu, C., Wang, F., Ren, H., Wu, H., & Yan, M. (2026) · Molecular Biomedicine · doi:10.1186/s43556-026-00415-6 · Cited by 32 · see citing works
Maghin, E., Carraro, E., Boso, D., Dedja, A., Giagante, M., Caccin, P., Barna, R.-A.-M., Bresolin, S., Cani, A., Borile, G., et al. (2022) · npj Regenerative Medicine · doi:10.1038/s41536-022-00222-x · Cited by 19 · see citing works
Model of Liver Fibrosis Induction by Thioacetamide in Rats for Regenerative Therapy Studies
Enciso, N., Amiel-Pérez, J., Domínguez, F. F., Pando, J., Rojas, N., Cisneros-Huamaní, C., Nava, E., & Enciso, J. (2022) · Analytical Cellular Pathology · doi:10.1155/2022/2841894 · Cited by 18 · see citing works
Bhattacharya, T., Kumari, M., Kaur, K., Kaity, S., Arumugam, S., Ravichandiran, V., & Roy, S. (2024) · Journal of Materials Chemistry B · doi:10.1039/d4tb00680a · Cited by 18 · see citing works
Cao, L. L., Zhou, Y., Lin, S., Yang, C., Guan, Z., Li, X., Yang, S., Gao, T., Zhao, J., Fan, N., et al. (2024) · Journal of Extracellular Vesicles · doi:10.1002/jev2.12499 · Cited by 17 · see citing works
Waugh, S., Ranasinghe, A., Gomez, A., Houston, S., Lithgow, K., Eshghi, A., Fleetwood, J., Conway, K. M. E., Reynolds, L. A., & Cameron, C. E. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1254342 · Cited by 15 · see citing works
Effect of Uncaria rhynchophylla against Thioacetamide‐Induced Acute Liver Injury in Rat
Shin, M.-R., Kim, M. J., Lee, J. A., & Roh, S. (2021) · Canadian Journal of Gastroenterology and Hepatology · doi:10.1155/2021/5581816 · Cited by 16 · see citing works
Liver Extracellular Matrix in Colorectal Liver Metastasis
Morabito, M., Thibodot, P., Gigandet, A., Compagnon, P., Toso, C., Berishvili, E., Lacotte, S., & Peloso, A. (2025) · Cancers · doi:10.3390/cancers17060953 · Cited by 17 · see citing works
The role of matrix metalloproteinases in liver function and disease
Mitropoulou, G., Kompoura, V., Saffioti, F., & Mavroeidis, V. K. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl27127 · Cited by 14 · see citing works
Blackman, S. A., Miles, D., Suresh, J., Calve, S., & Bryant, S. J. (2024) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.3c01393 · Cited by 14 · see citing works
Matricellular proteins in intrahepatic cholangiocarcinoma
Sirica, A. E. (2022) · Advances in cancer research · doi:10.1016/bs.acr.2022.01.010 · Cited by 14 · see citing works
Preliminary Study on the Antigen-Removal from Extracellular Matrix via Different Decellularization
Wu, H. C., Yin, G., Pu, X., Wang, J., Liao, X., & Huang, Z. (2022) · Tissue Engineering Part C Methods · doi:10.1089/ten.tec.2022.0025 · Cited by 14 · see citing works
Bahcivanci, B., Shafiha, R., Gkoutos, G. V., & Acharjee, A. (2022) · Cancer Medicine · doi:10.1002/cam4.4941 · Cited by 13 · see citing works
Maddali, P., Ambesi, A., & McKeown‐Longo, P. J. (2023) · PLoS ONE · doi:10.1371/journal.pone.0286390 · Cited by 12 · see citing works
Decellularized Green and Brown Macroalgae as Cellulose Matrices for Tissue Engineering
Berry-Kilgour, C., Oey, I., Cabral, J. D., Dowd, G. C., & Wise, L. M. (2024) · Journal of Functional Biomaterials · doi:10.3390/jfb15120390 · Cited by 12 · see citing works
Xu, M., Xu, K., Yin, S., Chang, C., Sun, W., Wang, G., Zhang, K., Mu, J., Wu, M., Xing, B., et al. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100574 · Cited by 12 · see citing works
Bate, T. S. R., Shanahan, W. R., Casillo, J. P., Grant, R., Forbes, S. J., & Callanan, A. (2022) · Journal of Biomedical Materials Research Part B Applied Biomaterials · doi:10.1002/jbm.b.35115 · Cited by 12 · see citing works
Lin, S., Wang, J., Mukherjee, P. K., Veisman, I., Massey, W. J., Mao, R., Chandra, J., Fiocchi, C., & Rieder, F. (2025) · Matrix Biology · doi:10.1016/j.matbio.2025.05.001 · Cited by 11 · see citing works
Multiscale analysis of human tissue engineered matrices for next generation heart valve applications
Poulis, N., Breitenstein, P., Hofstede, S., Hoerstrup, S. P., Emmert, M. Y., & Fioretta, E. S. (2023) · Acta Biomaterialia · doi:10.1016/j.actbio.2023.01.007 · Cited by 11 · see citing works
Carnazzo, V., Pignalosa, S., Tagliaferro, M., Gragnani, L., Zignego, A. L., Racco, C., Biase, L. D., Basile, V., Rapaccini, G. L., Santo, R. D., et al. (2024) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2024.110861 · Cited by 10 · see citing works
Mir, T. A., Alzhrani, A., Nakamura, M., Iwanaga, S., Wani, S. I., Altuhami, A., Kazmi, S., Arai, K., Shamma, T., Obeid, D. A., et al. (2023) · Bioengineering · doi:10.3390/bioengineering10101126 · Cited by 9 · see citing works
Deng, L., Cheng, S., Jiang, L., Xu, X., Hao, X., Fan, Y., & Mu, S. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113919 · Cited by 10 · see citing works
Radosavljević, T. S., Vukićević, D., Djuretić, J., Gopčević, K., Labudović‐Borović, M., Stankovic, S. D., Samardžić, J., Radosavljević, M., Vučević, D. B., & Jakovljevic, V. L. (2024) · Biomedicines · doi:10.3390/biomedicines12061337 · Cited by 9 · see citing works
Ock, S. A., Kim, S.-Y., Kim, Y.-I., Ju, W. S., & Lee, P. (2024) · Cells · doi:10.3390/cells13151303 · Cited by 9 · see citing works
Setayesh, T., Hu, Y., Vaziri, F., Wei, D., & Wan, Y. Y. (2024) · Biomarker Research · doi:10.1186/s40364-024-00660-3 · Cited by 9 · see citing works
Chaulagain, R. P., Padder, A. M., Shrestha, H., Gupta, R., Bhandari, R., Shrestha, Y., Moqbel, A. Q., Gautam, S., Lal, N., & Jin, S. (2025) · Cureus · doi:10.7759/cureus.82171 · Cited by 9 · see citing works
Farzaneh, Z., Khojastehpour, F., Keivan, M., & Farzaneh, M. (2022) · Current Stem Cell Research & Therapy · doi:10.2174/1574888x17666220614160957 · Cited by 9 · see citing works
Jeon, H. J., Chun, H. J., Choi, H. S., Keum, B., Kim, H. B., & Kim, J. H. (2024) · Cancers · doi:10.3390/cancers16071389 · Cited by 8 · see citing works
Ryu, Y., Seo, J. H., Kim, H. S., Nam, Y. J., Noh, K. B., Oh, S., Hwang, J. S., & Shin, Y. J. (2024) · Matrix Biology · doi:10.1016/j.matbio.2024.10.001 · Cited by 7 · see citing works
Dressed in Collagen: 2D and 3D Cardiac Fibrosis Models
Cardona-Timoner, M., Gomes, R. N., & Nascimento, D. S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26073038 · Cited by 8 · see citing works
Research progress on damage-associated molecular patterns in acute kidney injury
Li, J., & Hu, Z. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1590822 · Cited by 7 · see citing works
Xie, H., Lu, Y., Zhang, A., Zheng, A., Rao, B., Yang, C., Li, A., Guo, W., Hu, L., Huang, X., et al. (2025) · Clinical and Translational Medicine · doi:10.1002/ctm2.70541 · Cited by 7 · see citing works
Decellularized diseased tissues: current state‐of‐the‐art and future directions
Li, X., Shan, J., Chen, X., Cui, H., Wen, G., & Yu, Y. (2023) · MedComm · doi:10.1002/mco2.399 · Cited by 6 · see citing works
Salmonella ‐driven intestinal edema in mice is characterized by tensed fibronectin fibers
Rappold, R., Kalogeropoulos, K., Keller, U. A. D., Viola Vogel, B., & Slack, E. M. C. (2024) · FEBS Journal · doi:10.1111/febs.17120 · Cited by 6 · see citing works
Fan, Y., Xue, M., Shan, T., Bai, Y., Zhang, H., Liu, M., Wang, P., Liang, X., & Liang, H. (2023) · Food Bioscience · doi:10.1016/j.fbio.2023.103454 · Cited by 6 · see citing works
Kim, H. J., Lee, K., Park, K. H., Choi, B. Y., Cho, I., & Lee, M. J. (2024) · American Journal of Reproductive Immunology · doi:10.1111/aji.13913 · Cited by 6 · see citing works
Kołakowski, A., Dziemitko, S., Chmielecka, A., Żywno, H., Bzdęga, W., Charytoniuk, T., Chabowski, A., & Konstantynowicz-Nowicka, K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911380 · Cited by 6 · see citing works
Froghi, S., de Andrade, M. O., Mohammad-Hadi, L., Gélat, P., Rashidi, H., Quaglia, A., Fuller, B. J., Saffari, N., & Davidson, B. R. (2023) · Bioengineering · doi:10.3390/bioengineering10020276 · Cited by 6 · see citing works
Li, F., Yan, T., Wang, S., & Wen, X. (2023) · Clinical and Experimental Medicine · doi:10.1007/s10238-023-01122-0 · Cited by 6 · see citing works
Liver fibrosis pathologies and potentials of RNA based therapeutics modalities
Diwan, R., Gaytan, S. L., Bhatt, H. N., Pena‐Zacarias, J., & Nurunnabi, M. (2024) · Drug Delivery and Translational Research · doi:10.1007/s13346-024-01551-8 · Cited by 6 · see citing works
Liver Stiffness Values to Predict Occurrence and Recurrence of Hepatocellular Carcinoma
Stasi, C., & Brillanti, S. (2024) · Life · doi:10.3390/life14030342 · Cited by 6 · see citing works
Application of pulsed electric field technology to skin engineering
Berry-Kilgour, C., Wise, L., King, J., & Oey, I. (2024) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2024.1386725 · Cited by 6 · see citing works
The native liver as inspiration to create superior in vitro hepatic models
Carpentier, N., Urbani, L., Dubruel, P., & Vlierberghe, S. V. (2023) · Biomaterials Science · doi:10.1039/d2bm01646j · Cited by 6 · see citing works
Self-citationChen, M., Wu, Z., Du, Z., Sun, S., Wu, J., & Luo, J. (2021) · Gastroenterología y Hepatología · doi:10.1016/j.gastrohep.2021.10.001 · Cited by 5 · see citing works
The construction and validation of ECM-related prognosis model in laryngeal squamous cell carcinoma
Jiang, X., & Jiang, W. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e19907 · Cited by 5 · see citing works
Utilising an in silico model to predict outcomes in senescence-driven acute liver injury
Ashmore‐Harris, C., Antonopoulou, E., Aird, R. E., Man, T. Y., Finney, S. M., Speel, A. M., Lu, W., Forbes, S. J., Gadd, V. L., & Waters, S. L. (2024) · npj Regenerative Medicine · doi:10.1038/s41536-024-00371-1 · Cited by 5 · see citing works
Andreeva, E. R., Zhidkova, O., Константиновна, М. Д., Gornostaeva, A. N., Lobanova, M. V., & Buravkova, L. B. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26136301 · Cited by 4 · see citing works
El‐Fakharany, E. M., El-Sayed, M. H., Ali, H. M., Omar, S. M., Sayed, A. M., Atwa, A. M., Alfaifi, M. Y., Shati, A. A., Elbehairi, S. E. I., Alrayes, Z. R., et al. (2025) · Medical Oncology · doi:10.1007/s12032-025-03100-w · Cited by 4 · see citing works
Heydarifard, Z., Shokri, S., Mahmoudvand, S., Heydarifard, F., Parnian, R., & Mirzaei, H. (2026) · Reviews in Medical Virology · doi:10.1002/rmv.70178 · Cited by 4 · see citing works
Dias, M. L., Wajsenzon, I. J. R., Alves, G. B. N., Paranhos, B. A., de Andrade, C. B. V., Monteiro, V. R. D. S., de Sousa, R. M. R., Pereira, E. N. G. D. S., Rodrigues, K. L., Daliry, A., et al. (2023) · Cells · doi:10.3390/cells12070976 · Cited by 3 · see citing works
Ghobrial, D. K., El-Nikhely, N. A., Sheta, E., Ragab, H. M., Rostom, S. A. F., Saeed, H. M. S., & Wahid, A. M. (2023) · Antioxidants · doi:10.3390/antiox12030637 · Cited by 4 · see citing works
Murphy, S. L., Balzer, N. R., Ranheim, T., Sagen, E. L., Huse, C., Bjerkeli, V., Michelsen, A. E., Finbråten, A., Heggelund, L., Dyrhol‐Riise, A. M., et al. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1379570 · Cited by 4 · see citing works
Parkinson, J. E., Bryant, M., Ghafoor, M., Dodd, R. J., Tompkins, H. E., Fergie, M., Burgess, M. O., Rattray, M., & Sutherland, T. E. (2026) · Molecular Systems Biology · doi:10.1038/s44320-026-00234-5 · Cited by 4 · see citing works
Mirosław, P., Kosowska, K., Serafin, W., Piwowar, R., Romanik-Chruścielewska, A., Westphal, K., Wszola, M., & Klak, M. (2025) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2025.1680938 · Cited by 3 · see citing works
Natural medicines for treating liver fibrosis by modulating post-translational modifications
Niu, Q., Mou, Y., Wang, K., Dong, H., Zeng, Z., & Li, H. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1660908 · Cited by 3 · see citing works
Yuri, G., Sanhueza, S., Paredes, A., Morales, G., Cifuentes, M., & Ormazabal, P. (2023) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2023.111882 · Cited by 3 · see citing works
Sun, A., Sheng, X., Tang, J., Yu, Z., & Zhang, J. (2021) · Journal of Immunology Research · doi:10.1155/2021/7876489 · Cited by 3 · see citing works
Xu, S.-J., Ye, L., Wang, W., Chen, Y., Dong, J. W., Mao, X., & Li, S.-W. (2021) · Stem Cells International · doi:10.1155/2021/5513309 · Cited by 3 · see citing works
Tang, L. Y., Yu, X., Zou, L., Li, S., Cheng, Y., Wu, Y., Xing, L., & Fang, H. (2023) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2023/5642713 · Cited by 3 · see citing works
- Authors
- McQuitty, C. E., Williams, R., Chokshi, S., & Urbani, L.
- Affiliations
- King's College London (GB)
- Corresponding author
- Urbani, Luca
- Venue
- Frontiers in Immunology
- Publisher
- Frontiers Media SA
- Published
- 2020-11-11
- Volume
- 11
- Pages
- 574276-574276
- ISSN
- 1664-3224 (ISSN-L)
- PMC
- PMC7686550
- OpenAlex
- W3098031338
- Cited by
- 146
- References
- 446
- Citations by year
- 2026: 23 · 2025: 22 · 2024: 34 · 2023: 31 · 2022: 19 · 2021: 17
- FWCI
- 2.23
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Immunology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Health Sciences › Medicine › Hepatology › Liver physiology and pathology
- Health Sciences › Medicine › Hepatology › Liver Diseases and Immunity
- Health Sciences › Medicine › Surgery › Tissue Engineering and Regenerative Medicine
- Keywords
- extracellular matrix, chronic liver disease, liver fibrosis, damage-associated molecular patterns, sterile inflammation, integrins, TLRs, immune cell infiltration, tissue engineering, biomarkers
- MeSH terms
- Anti-Inflammatory Agents, Extracellular Matrix, Humans, Inflammation, Liver, Liver Cirrhosis, Liver Diseases, Cytokines, Extracellular Matrix Proteins, Immunomodulation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review