Frantz C, Stewart KM, Weaver VM. The extracellular matrix at a glance. J Cell Sci. 2010;123:4195–200.
Meran L, Baulies A, Li VSW. Intestinal Stem Cell Niche: the extracellular matrix and cellular components. Stem Cells Int. 2017;2017:7970385.
McKee TJ, Perlman G, Morris M, Komarova SV. Extracellular matrix composition of connective tissues: a systematic review and meta-analysis. Sci Rep. 2019;9:1–15.
Tonti OR, Larson H, Lipp SN, Luetkemeyer CM, Makam M, Vargas D, et al. Tissue-specific parameters for the design of ECM-mimetic biomaterials. Acta Biomater. 2021;132:83–102.
Rozario T, DeSimone DW. The extracellular matrix in development and morphogenesis: a dynamic view. Dev Biol. 2010;341:126–40.
Xing Y, Varghese B, Ling Z, Kar AS, Reinoso Jacome E, Ren X. Extracellular Matrix by Design: Native biomaterial fabrication and functionalization to boost tissue regeneration. Regen Eng Transl Med. 2022;8:55–74.
Theocharis AD, Skandalis SS, Gialeli C, Karamanos NK. Extracellular matrix structure. Adv Drug Deliv Rev. 2016;97:4–27.
Muiznieks LD, Keeley FW. Molecular assembly and mechanical properties of the extracellular matrix: a fibrous protein perspective. Biochim Biophys Acta. 2013;1832:866–75.
Mithieux SM, Wise SG, Weiss AS. Tropoelastin — a multifaceted naturally smart material. Adv Drug Deliv Rev. 2013;65:421–8.
Yeo GC, Keeley FW, Weiss AS. Coacervation of tropoelastin. Adv Coll Interface Sci. 2011;167:94–103.
Hinek A, Rabinovitch M. 67-kD elastin-binding protein is a protective companion of extracellular insoluble elastin and intracellular tropoelastin. J Cell Biol. 1994;126:563–74.
Gelse K, Pöschl E, Aigner T. Collagens–structure, function, and biosynthesis. Adv Drug Deliv Rev. 2003;55:1531–46.
Weihermann AC, Lorencini M, Brohem CA, de Carvalho CM. Elastin structure and its involvement in skin photoageing. Int J Cosmet Sci. 2017;39:241–7.
Kielty CM, Sherratt MJ, Marson A, Baldock C. Fibrillin microfibrils. Adv Protein Chem. 2005;70:405–36.
Papke CL, Yanagisawa H. Fibulin-4 and fibulin-5 in elastogenesis and beyond: Insights from mouse and human studies. Matrix Biol. 2014;37:142–9.
Kielty CM, Sherratt MJ, Shuttleworth CA. Elastic fibres. J Cell Sci. 2002;115:2817–28.
Hulmes DJS. Collagen Diversity, Synthesis and Assembly Collagen. Boston: Springer; 2008. p. 15–47.
Chute M, Aujla P, Jana S, Kassiri Z. The non-fibrillar side of fibrosis: contribution of the basement membrane, proteoglycans, and glycoproteins to myocardial fibrosis. J Cardiovasc Dev Dis. 2019;6:35.
Yurchenco PD, Ruben GC. Basement membrane structure in situ: evidence for lateral associations in the type IV collagen network. J Cell Biol. 1987;105:2559–68.
Yurchenco PD, Furthmayr H. Self-assembly of basement membrane collagen. Biochemistry. 1984;23:1839–50.
Aumailley M, Bruckner-Tuderman L, Carter WG, Deutzmann R, Edgar D, Ekblom P, et al. A simplified laminin nomenclature. Matrix Biol. 2005;24:326–32.
Halper J, Kjaer M. Basic components of connective tissues and extracellular matrix: elastin, fibrillin, fibulins, fibrinogen, fibronectin, laminin, tenascins and thrombospondins. Adv Exp Med Biol. 2014;802:31–47.
Rock MJ, Cain SA, Freeman LJ, Morgan A, Mellody K, Marson A, et al. Molecular basis of elastic fiber formation. critical interactions and a tropoelastin-fibrillin-1 cross-link. J Biol Chem. 2004;279:23748–58.
Rucker RB, Kosonen T, Clegg MS, Mitchell AE, Rucker BR, Uriu-Hare JY, et al. Copper, lysyl oxidase, and extracellular matrix protein cross-linking. Am J Clin Nutr. 1998;67:996S-1002S.
Yurchenco PD, Schittny JC. Molecular architecture of basement membranes. The FASEB Journal. 1990;4:1577–90.
Bosman FT, Stamenkovic I. Functional structure and composition of the extracellular matrix. J Pathol. 2003;200:423–8.
Martin GR, Timpl R. Laminin and other basement membrane components. Annu Rev Cell Biol. 1987;3:57–85.
Kruegel J, Miosge N. Basement membrane components are key players in specialized extracellular matrices. Cell Mol Life Sci. 2010;67:2879–95.
Faffe DS, Zin WA. Lung parenchymal mechanics in health and disease. Physiol Rev. 2009;89:759–75.
Toshima M, Ohtani Y, Ohtani O. Three-dimensional architecture of elastin and collagen fiber networks in the human and rat lung. Arch Histol Cytol. 2004;67:31–40.
Zhao XH, Laschinger C, Arora P, Szászi K, Kapus A, McCulloch CA. Force activates smooth muscle α-actin promoter activity through the Rho signaling pathway. J Cell Sci. 2007;120:1801–9.
Arora PD, Narani N, McCulloch CAG. The compliance of collagen gels regulates transforming growth factor-β induction of α-smooth muscle actin in fibroblasts. Am J Pathol. 1999;154:871–82.
Sandbo N, Lau A, Kach J, Ngam C, Yau D, Dulin NO. Delayed stress fiber formation mediates pulmonary myofibroblast differentiation in response to TGF-β. Am J Physiol Lung Cell. 2011;301:656–66.
Engler AJ, Sen S, Sweeney HL, Discher DE. Matrix elasticity directs stem cell lineage specification. Cell. 2006;126:677–89.
Schaefer L, Schaefer RM. Proteoglycans: from structural compounds to signaling molecules. Cell Tissue Res. 2010;339:237–46.
DeAngelis PL. Glycosaminoglycan polysaccharide biosynthesis and production: today and tomorrow. Appl Microbiol Biotechnol. 2012;94:295–305.
Sasisekharan R, Raman R, Prabhakar V. Glycomics approach to structure-function relationships of glycosaminoglycans. Annu Rev Biomed Eng. 2006;8:181–231.
Alberts B, Johnson A, Lewis J, Morgan D, Raff M, Roberts K, et al. Cell junctions and the extracellular matrix. Molecular Biology of the Cell (6th edition). New York: Garland Science; 2015. p. 1035–91.
Sterner E, Meli L, Kwon SJ, Dordick JS, Linhardt RJ. FGF-FGFR signaling mediated through glycosaminoglycans in microtiter plate and cell-based microarray platforms. Biochemistry. 2013;52:9009–19.
Sterner E, Masuko S, Li G, Li L, Green DE, Otto NJ, et al. Fibroblast growth factor-based signaling through synthetic heparan sulfate blocks copolymers studied using high cell density three-dimensional cell printing *. J Biol Chem. 2014;289:9754–65.
Schultz V, Suflita M, Liu X, Zhang X, Yu Y, Li L, et al. Heparan sulfate domains required for fibroblast growth factor 1 and 2 signaling through fibroblast growth factor receptor 1c *. J Biol Chem. 2017;292:2495–509.
Uhl FE, Zhang F, Pouliot RA, Uriarte JJ, Rolandsson Enes S, Han X, et al. Functional role of glycosaminoglycans in decellularized lung extracellular matrix. Acta Biomater. 2020;102:231–46.
Yamaguchi Y, Mann DM, Ruoslahti E. Negative regulation of transforming growth factor-beta by the proteoglycan decorin. Nature. 1990;346:281–4.
Godoy-Guzmán C, San Martin S, Pereda J. Proteoglycan and collagen expression during human air conducting system development. Eur J Histochem. 2012;56:179–84.
Kresse H, Schnherr E. Proteoglycans of the extracellular matrix and growth control. J Cell Physiol. 2001;189:266–74.
Naba A, Clauser KR, Hoersch S, Liu H, Carr SA, Hynes RO. The matrisome: in silico definition and in vivo characterization by proteomics of normal and tumor extracellular matrices. Mol Cell Proteomics. 2012;11(4):M111.014647.
Naba A, Clauser KR, Ding H, Whittaker CA, Carr SA, Hynes RO. The extracellular matrix: Tools and insights for the “omics” era. Matrix Biol. 2016;49:10–24.
Rosso F, Giordano A, Barbarisi M, Barbarisi A. From Cell–ECM interactions to tissue engineering. J Cell Physiol. 2004;199:174–80.
Clause KC, Barker TH. Extracellular matrix signaling in morphogenesis and repair. Curr Opin Biotechnol. 2013;24:830–3.
Giancotti FG, Ruoslahti E. Integrin signaling. Science. 1979;1999(285):1028–32.
Leitinger B. Discoidin domain receptor functions in physiological and pathological conditions. Int Rev Cell Mol Biol. 2014;310:39–87.
Ponta H, Sherman L, Herrlich PA. CD44: from adhesion molecules to signalling regulators. Nat Rev Mol Cell Biol. 2003;4:33–45.
Harada H, Takahashi M. CD44-dependent intracellular and extracellular catabolism of hyaluronic acid by hyaluronidase-1 and -2. J Biol Chem. 2007;282:5597–607.
Naor D, Sionov RV, Ish-Shalom D. CD44: Structure, function, and association with the malignant process. Adv Cancer Res. 1997;71:241–319.
Kreidberg JA, Donovan MJ, Goldstein SL, Rennke H, Shepherd K, Jones RC, et al. Alpha 3 beta 1 integrin has a crucial role in kidney and lung organogenesis. Development. 1996;122:3537–47.
Yamada KM, Even-Ram S. Integrin regulation of growth factor receptors. Nat Cell Biol. 2002;4(4):E75-6.
Moro L, Venturino M, Bozzo C, Silengo L, Altruda F, Beguinot L, et al. Integrins induce activation of EGF receptor: role in MAP kinase induction and adhesion-dependent cell survival. EMBO J. 1998;17:6622–32.
Byzova TV, Goldman CK, Pampori N, Thomas KA, Bett A, Shattil SJ, et al. A mechanism for modulation of cellular responses to vegf: activation of the integrins. Mol Cell. 2000;6:851–60.
de Castro Brás LE, Frangogiannis NG. Extracellular matrix-derived peptides in tissue remodeling and fibrosis. Matrix Biol. 2020;91–92:176–87.
Whitelock JM, Murdoch AD, Iozzo RV. Underwood PA. the degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases. J Biol Chem. 1996;271:10079–86.
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