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Linked References

1. M. T. Longaker, N. S. Adzick, J. L. Hall et al., “Studies in fetal wound healing, VII. Fetal wound healing may be modulated by hyaluronic acid stimulating activity in amniotic fluid,” Journal of Pediatric Surgery, vol. 25, no. 4, pp. 430–433, 1990. View at Publisher · View at Google Scholar · View at Scopus
2. J. R. E. Fraser, T. C. Laurent, and U. B. G. Laurent, “Hyaluronan: its nature, distribution, functions and turnover,” Journal of Internal Medicine, vol. 242, no. 1, pp. 27–33, 1997. View at Scopus
3. B. P. Toole, “Hyaluronan in morphogenesis,” Journal of Internal Medicine, vol. 242, no. 1, pp. 35–40, 1997. View at Scopus
4. W. Y. J. Chen and G. Abatangelo, “Functions of hyaluronan in wound repair,” Wound Repair and Regeneration, vol. 7, no. 2, pp. 79–89, 1999. View at Publisher · View at Google Scholar · View at Scopus
5. E. A. Turley, P. W. Noble, and L. Y. W. Bourguignon, “Signaling properties of hyaluronan receptors,” The Journal of Biological Chemistry, vol. 277, no. 7, pp. 4589–4592, 2002. View at Publisher · View at Google Scholar · View at Scopus
6. K. R. Taylor, J. M. Trowbridge, J. A. Rudisill, C. C. Termeer, J. C. Simon, and R. L. Gallo, “Hyaluronan fragments stimulate endothelial recognition of injury through TLR4,” The Journal of Biological Chemistry, vol. 279, no. 17, pp. 17079–17084, 2004. View at Publisher · View at Google Scholar · View at Scopus
7. S. Kikuchi, C. T. Griffini, S. S. Wang, and D. M. Bissell, “Role of CD44 in epithelial wound repair: migration of rat hepatic stellate cells utilizes hyaluronic acid and CD44v6,” The Journal of Biological Chemistry, vol. 280, no. 15, pp. 15398–15404, 2005. View at Publisher · View at Google Scholar · View at Scopus
8. D. D. Allison and K. J. Grande-Allen, “Review. Hyaluronan: a powerful tissue engineering tool,” Tissue Engineering, vol. 12, no. 8, pp. 2131–2140, 2006. View at Publisher · View at Google Scholar · View at Scopus
9. G. D. Prestwich, “Simplifying the extracellular matrix for 3-D cell culture and tissue engineering: a pragmatic approach,” Journal of Cellular Biochemistry, vol. 101, no. 6, pp. 1370–1383, 2007. View at Publisher · View at Google Scholar · View at Scopus
10. G. D. Prestwich, “Evaluating drug efficacy and toxicology in three dimensions: using synthetic extracellular matrices in drug discovery,” Accounts of Chemical Research, vol. 41, no. 1, pp. 139–148, 2008. View at Publisher · View at Google Scholar · View at Scopus
11. G. D. Prestwich, “Hyaluronic acid-based clinical biomaterials derived for cell and molecule delivery in regenerative medicine,” Journal of Controlled Release, vol. 155, pp. 193–199, 2011. View at Publisher · View at Google Scholar · View at Scopus
12. G. Yang, L. Espandar, N. Mamalis, and G. D. Prestwich, “A cross-linked hyaluronan gel accelerates healing of corneal epithelial abrasion and alkali burn injuries in rabbits,” Veterinary Ophthalmology, vol. 13, no. 3, pp. 144–150, 2010. View at Publisher · View at Google Scholar · View at Scopus
13. G. Yang, G. D. Prestwich, and B. K. Mann, “Thiolated carboxymethyl hyaluronic acid-based biomaterials enhance wound healing in rats, dogs, and horses,” ISRN Veterinary Science, vol. 2011, Article ID 851593, 7 pages, 2011.
14. N. E. Larsen, C. T. Pollak, K. Reiner, E. Leshchiner, and E. A. Balazs, “Hylan gel biomaterial: dermal and immunologic compatibility,” Journal of Biomedical Materials Research, vol. 27, no. 9, pp. 1129–1134, 1993. View at Scopus
15. L. Hallén, C. Johansson, and C. Laurent, “Cross-linked hyaluronan (hylan B gel): a new injectable remedy for treatment of vocal fold insufficiency—an animal study,” Acta Oto-Laryngologica, vol. 119, no. 1, pp. 107–111, 1999. View at Publisher · View at Google Scholar · View at Scopus
16. J. A. Burdick, C. Chung, X. Jia, M. A. Randolph, and R. Langer, “Controlled degradation and mechanical behavior of photopolymerized hyaluronic acid networks,” Biomacromolecules, vol. 6, no. 1, pp. 386–391, 2005. View at Publisher · View at Google Scholar · View at Scopus
17. J. B. Leach and C. E. Schmidt, “Characterization of protein release from photocrosslinkable hyaluronic acid-polyethylene glycol hydrogel tissue engineering scaffolds,” Biomaterials, vol. 26, no. 2, pp. 125–135, 2005. View at Publisher · View at Google Scholar · View at Scopus
18. S. Duflo, S. L. Thibeault, W. Li, X. Z. Shu, and G. D. Prestwich, “Vocal fold tissue repair in vivo using a synthetic extracellular matrix,” Tissue Engineering, vol. 12, no. 8, pp. 2171–2180, 2006. View at Publisher · View at Google Scholar · View at Scopus
19. Y. Liu, S. Ahmad, X. Z. Shu, R. K. Sanders, S. A. Kopesec, and G. D. Prestwich, “Accelerated repair of cortical bone defects using a synthetic extracellular matrix to deliver human demineralized bone matrix,” Journal of Orthopaedic Research, vol. 24, no. 7, pp. 1454–1462, 2006. View at Publisher · View at Google Scholar · View at Scopus
20. Y. Liu, X. Z. Shu, and G. D. Prestwich, “Osteochondral defect repair with autologous bone marrow-derived mesenchymal stem cells in an injectable, in situ, cross-linked synthetic extracellular matrix,” Tissue Engineering, vol. 12, no. 12, pp. 3405–3416, 2006. View at Publisher · View at Google Scholar · View at Scopus
21. Y. Liu, X. Z. Shu, and G. D. Prestwich, “Tumor engineering: orthotopic cancer models in mice using cell-loaded, injectable, cross-linked hyaluronan-derived hydrogels,” Tissue Engineering, vol. 13, no. 5, pp. 1091–1101, 2007. View at Publisher · View at Google Scholar · View at Scopus
22. X. Z. Shu, K. Ghosh, Y. Liu et al., “Attachment and spreading of fibroblasts on an RGD peptide-modified injectable hyaluronan hydrogel,” Journal of Biomedical Materials Research A, vol. 68, no. 2, pp. 365–375, 2004. View at Scopus
23. K. Ghosh, X. D. Ren, X. Z. Shu, G. D. Prestwich, and R. A. F. Clark, “Fibronectin functional domains coupled to hyaluronan stimulate adult human dermal fibroblast responses critical for wound healing,” Tissue Engineering, vol. 12, no. 3, pp. 601–613, 2006. View at Scopus
24. J. L. Vanderhooft, M. Alcoutlabi, J. J. Magda, and G. D. Prestwich, “Rheological properties of cross-linked hyaluronan-gelatin hydrogels for tissue engineering,” Macromolecular Bioscience, vol. 9, no. 1, pp. 20–28, 2009. View at Publisher · View at Google Scholar · View at Scopus
25. J. W. Gunn, S. D. Turner, and B. K. Mann, “Adhesive and mechanical properties of hydrogels influence neurite extension,” Journal of Biomedical Materials Research A, vol. 72, no. 1, pp. 91–97, 2005. View at Publisher · View at Google Scholar · View at Scopus
26. J. L. Vanderhooft, B. K. Mann, and G. D. Prestwich, “Synthesis and characterization of novel thiol-reactive poly(ethylene glycol) cross-linkers for extracellular-matrix-mimetic biomaterials,” Biomacromolecules, vol. 8, no. 9, pp. 2883–2889, 2007. View at Publisher · View at Google Scholar · View at Scopus
27. B. Jeong, Y. H. Bae, and S. W. Kim, “Thermoreversible gelation of PEG-PLGA-PEG triblock copolymer aqueous solutions,” Macromolecules, vol. 32, no. 21, pp. 7064–7069, 1999. View at Scopus
28. B. K. Mann, A. S. Gobin, A. T. Tsai, R. H. Schmedlen, and J. L. West, “Smooth muscle cell growth in photopolymerized hydrogels with cell adhesive and proteolytically degradable domains: synthetic ECM analogs for tissue engineering,” Biomaterials, vol. 22, no. 22, pp. 3045–3051, 2001. View at Publisher · View at Google Scholar · View at Scopus
29. A. S. Rowlands, P. A. George, and J. J. Cooper-White, “Directing osteogenic and myogenic differentiation of MSCs: interplay of stiffness and adhesive ligand presentation,” American Journal of Physiology, vol. 295, no. 4, pp. C1037–C1044, 2008. View at Publisher · View at Google Scholar · View at Scopus
30. T. M. Birkenmeier, J. J. McQuillan, E. D. Boedeker, W. S. Argraves, E. Ruoslahti, and D. C. Dean, “The α5β1 fibronectin receptor: characterization of the α5 gene promoter,” The Journal of Biological Chemistry, vol. 266, no. 30, pp. 20544–20549, 1991. View at Scopus
31. B. K. Mann and S. D. Turner, “Glycoproteins and adhesion peptides: properties and biomedical applications,” in Renewable Resources for Functional Polymers and Biomaterials: Polysaccharides, Proteins and Polyesters, P. A. Williams, Ed., Royal Society of Chemistry, London, UK, 2011.
32. A. S. G. Curtis and J. V. Forrester, “The competitive effects of serum proteins on cell adhesion,” Journal of Cell Science, vol. 71, pp. 17–35, 1984. View at Scopus
33. G. E. Davis, “Affinity of integrins for damaged extracellular matrix: α(v)β3 binds to denatured collagen type I through RGD sites,” Biochemical and Biophysical Research Communications, vol. 182, no. 3, pp. 1025–1031, 1992. View at Scopus
34. M. H. Zaman, “Understanding the molecular basis for differential binding of integrins to collagen and gelatin,” Biophysical Journal, vol. 92, no. 2, pp. L17–L19, 2007. View at Publisher · View at Google Scholar · View at Scopus
35. S. Johansson, G. Svineng, K. Wennerberg, A. Armulik, and L. Lohikangas, “Fibronectin-integrin interactions,” Frontiers in Bioscience, vol. 2, pp. d126–d146, 1997. View at Scopus
36. T. Yeung, P. C. Georges, L. A. Flanagan et al., “Effects of substrate stiffness on cell morphology, cytoskeletal structure, and adhesion,” Cell Motility and the Cytoskeleton, vol. 60, no. 1, pp. 24–34, 2005. View at Publisher · View at Google Scholar · View at Scopus
37. T. S. Panetti, D. F. Hannah, C. Avraamides et al., “Extracellular matrix molecules regulate endothelial cell migration stimulated by lysophosphatidic acid,” Journal of Thrombosis and Haemostasis, vol. 2, no. 9, pp. 1645–1656, 2004. View at Publisher · View at Google Scholar · View at Scopus
38. M. Kubo, R. A. F. Clark, A. B. Katz et al., “Transduction of β3 integrin subunit cDNA confers on human keratinocytes the ability to adhere to gelatin,” Archives of Dermatological Research, vol. 299, no. 1, pp. 13–24, 2007. View at Publisher · View at Google Scholar · View at Scopus
39. I. A. Potapova, I. S. Cohen, and S. V. Doronin, “Von willebrand factor increases endothelial cell adhesiveness for human mesenchymal stem cells by activating p38 mitogen-activated protein kinase,” Stem Cell Research and Therapy, vol. 1, no. 5, article 35, 2010. View at Publisher · View at Google Scholar · View at Scopus
40. M. M. Martino, M. Mochizuki, D. A. Rothenfluh, S. A. Rempel, J. A. Hubbell, and T. H. Barker, “Controlling integrin specificity and stem cell differentiation in 2D and 3D environments through regulation of fibronectin domain stability,” Biomaterials, vol. 30, no. 6, pp. 1089–1097, 2009. View at Publisher · View at Google Scholar · View at Scopus
41. G. C. Hunt, P. Singh, and J. E. Schwarzbauer, “Endogenous production of fibronectin is required for self-renewal of cultured mouse embryonic stem cells,” Experimental Cell Research, vol. 318, pp. 1820–1831, 2012.
42. J. Veevers-Lowe, S. G. Ball, A. Shuttleworth, and C. M. Kielty, “Mesenchymal stem cell migration is regulated by fibronectin through a5b1-integrin-mediated activation of PDGFR-β and potentiation of growth factor signals,” Journal of Cell Science, vol. 124, no. 8, pp. 1288–1300, 2011. View at Publisher · View at Google Scholar · View at Scopus
43. M. C. Markowski, A. C. Brown, and T. H. Barker, “Directing epithelial to mesenchymal transition through engineered microenvironments displaying orthogonal adhesive and mechanical cues,” Journal of Biomedical Materials Research A, vol. 100, pp. 2119–2127, 2012.
44. G. D. Nicodemus, S. C. Skaalure, and S. J. Bryant, “Gel structure has an impact on pericellular and extracellular matrix deposition, which subsequently alters metabolic activities in chondrocyte-laden PEG hydrogels,” Acta Biomaterialia, vol. 7, no. 2, pp. 492–504, 2011. View at Publisher · View at Google Scholar · View at Scopus