{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,11]],"date-time":"2026-10-11T04:05:52Z","timestamp":1791691552678,"version":"4.3.4"},"reference-count":63,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2016,4,1]],"date-time":"2016-04-01T00:00:00Z","timestamp":1459468800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2016,4,1]],"date-time":"2016-04-01T00:00:00Z","timestamp":1459468800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2016,2,1]],"date-time":"2016-02-01T00:00:00Z","timestamp":1454284800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000274","name":"British Heart Foundation","doi-asserted-by":"publisher","award":["NH\/11\/1\/28922"],"award-info":[{"award-number":["NH\/11\/1\/28922"]}],"id":[{"id":"10.13039\/501100000274","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000274","name":"British Heart Foundation","doi-asserted-by":"publisher","award":["RG\/09\/003\/27122"],"award-info":[{"award-number":["RG\/09\/003\/27122"]}],"id":[{"id":"10.13039\/501100000274","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100004440","name":"Wellcome Trust","doi-asserted-by":"publisher","award":["094470\/Z\/10\/Z"],"award-info":[{"award-number":["094470\/Z\/10\/Z"]}],"id":[{"id":"10.13039\/100004440","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Peoples Programme of the EU 7th Framework Programme","award":["PIIF-GA-2013-624904"],"award-info":[{"award-number":["PIIF-GA-2013-624904"]}]},{"name":"EPSRC Medical Technologies IKC"},{"name":"ERC","award":["320598 3D-E"],"award-info":[{"award-number":["320598 3D-E"]}]}],"content-domain":{"domain":["clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.jp","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biomaterials"],"published-print":{"date-parts":[[2016,4]]},"DOI":"10.1016\/j.biomaterials.2016.01.044","type":"journal-article","created":{"date-parts":[[2016,1,23]],"date-time":"2016-01-23T02:31:40Z","timestamp":1453516300000},"page":"65-77","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":54,"special_numbering":"C","title":["The synthesis and coupling of photoreactive collagen-based peptides to restore integrin reactivity to an inert substrate, chemically-crosslinked collagen"],"prefix":"10.1016","volume":"85","author":[{"given":"Jean-Daniel","family":"Malcor","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel","family":"Bax","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Samir W.","family":"Hamaia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natalia","family":"Davidenko","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Serena M.","family":"Best","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruth E.","family":"Cameron","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6130-8808","authenticated-orcid":false,"given":"Richard W.","family":"Farndale","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dominique","family":"Bihan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.biomaterials.2016.01.044_bib1","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1016\/j.addr.2013.12.004","article-title":"Cell therapy, 3D culture systems and tissue engineering for cardiac regeneration","volume":"69\u201370","author":"Emmert","year":"2014","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0378-5173(01)00691-3","article-title":"Biomedical applications of collagen","volume":"221","author":"Lee","year":"2001","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib3","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1203\/PDR.0b013e31816c5bc3","article-title":"Collagen tissue engineering: development of novel biomaterials and applications","volume":"63","author":"Cen","year":"2008","journal-title":"Pediatr. Res."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib4","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.1002\/jbm.820200811","article-title":"Collagen-based wound dressings: control of the pore structure and morphology","volume":"20","author":"Doillon","year":"1986","journal-title":"J.\u00a0Biomed. Mater. Res."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib5","doi-asserted-by":"crossref","first-page":"2387","DOI":"10.1089\/ten.2006.0320","article-title":"Construction of collagen scaffolds that mimic the three-dimensional architecture of specific tissues","volume":"13","author":"Faraj","year":"2007","journal-title":"Tissue Eng."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib6","doi-asserted-by":"crossref","first-page":"2508","DOI":"10.1016\/j.biomaterials.2010.12.026","article-title":"Stem-cell-capturing collagen scaffold promotes cardiac tissue regeneration","volume":"32","author":"Shi","year":"2011","journal-title":"Biomaterials"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib7","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1016\/j.biomaterials.2009.09.063","article-title":"The effect of mean pore size on cell attachment, proliferation and migration in collagen-glycosaminoglycan scaffolds for bone tissue engineering","volume":"31","author":"Murphy","year":"2010","journal-title":"Biomaterials"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib8","doi-asserted-by":"crossref","first-page":"2144","DOI":"10.1271\/bbb.63.2144","article-title":"Improvement of the physical properties of pepsin-solubilized elastin-collagen film by crosslinking","volume":"63","author":"Takahashi","year":"1999","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib9","doi-asserted-by":"crossref","first-page":"R47","DOI":"10.1186\/ar2202","article-title":"Bonding of articular cartilage using a combination of biochemical degradation and surface cross-linking","volume":"9","author":"Englert","year":"2007","journal-title":"Arthritis Res. Ther."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib10","doi-asserted-by":"crossref","first-page":"3080","DOI":"10.1016\/j.actbio.2012.05.006","article-title":"Crosslinking and composition influence the surface properties, mechanical stiffness and cell reactivity of collagen-based films","volume":"8","author":"Grover","year":"2012","journal-title":"Acta Biomater."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib11","doi-asserted-by":"crossref","first-page":"1569","DOI":"10.1007\/s10856-011-4336-1","article-title":"Extruded collagen fibres for tissue engineering applications: effect of crosslinking method on mechanical and biological properties","volume":"22","author":"Enea","year":"2011","journal-title":"J.\u00a0Mater. Sci. Mater. Med."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib12","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1074\/jbc.275.1.35","article-title":"The Collagen-binding A-domains of Integrins \u03b11\u03b21 and \u03b12\u03b21Recognize the Same Specific Amino Acid Sequence, GFOGER, in Native (Triple-helical) Collagens","volume":"275","author":"Knight","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib13","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1016\/S0142-9612(97)00103-8","article-title":"Enhancement of cell interactions with collagen\/glycosaminoglycan matrices by RGD derivatization","volume":"18","author":"Grzesiak","year":"1997","journal-title":"Biomaterials"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib14","first-page":"240","article-title":"Use of arginine\u2013glycine\u2013aspartic acid adhesion peptides coupled with a new collagen scaffold to engineer a myocardium-like tissue graft","volume":"6","author":"Schussler","year":"2009","journal-title":"Nat. Clin. Pract. Card."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib15","doi-asserted-by":"crossref","first-page":"4385","DOI":"10.1016\/S0142-9612(03)00343-0","article-title":"RGD modified polymers: biomaterials for stimulated cell adhesion and beyond","volume":"24","author":"Hersel","year":"2003","journal-title":"Biomaterials"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib16","doi-asserted-by":"crossref","DOI":"10.1039\/c2sm25903f","article-title":"Encoding cell-instructive cues to PEG-based hydrogels via triple helical peptide assembly","volume":"8","author":"Stahl","year":"2012","journal-title":"Soft Matter"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib17","doi-asserted-by":"crossref","first-page":"3228","DOI":"10.1016\/j.biomaterials.2007.04.003","article-title":"Biomolecular surface coating to enhance orthopaedic tissue healing and integration","volume":"28","author":"Reyes","year":"2007","journal-title":"Biomaterials"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib18","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1042\/BST0360241","article-title":"Cell-collagen interactions: the use of peptide toolkits to investigate collagen-receptor interactions","volume":"36","author":"Farndale","year":"2008","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib19","doi-asserted-by":"crossref","first-page":"3821","DOI":"10.1074\/jbc.M509818200","article-title":"Use of synthetic peptides to locate novel integrin \u03b12\u03b21-binding motifs in human collagen III","volume":"281","author":"Raynal","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib20","doi-asserted-by":"crossref","first-page":"26019","DOI":"10.1074\/jbc.M112.353144","article-title":"Mapping of potent and specific binding motifs, GLOGEN and GVOGEA, for integrin \u03b11\u03b21 using collagen toolkits II and III","volume":"287","author":"Hamaia","year":"2012","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib21","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1080\/03008200591008518","article-title":"Triple helical collagen-like peptides: engineering and applications in matrix biology","volume":"46","author":"Koide","year":"2005","journal-title":"Connect. Tissue Res."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib22","doi-asserted-by":"crossref","first-page":"1237","DOI":"10.1039\/b920670a","article-title":"Synthesis and biological applications of collagen-model triple-helical peptides","volume":"8","author":"Fields","year":"2010","journal-title":"Org. Biomol. Chem."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib23","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/S0022-2836(02)01065-3","article-title":"The chain register in heterotrimeric collagen peptides affects triple helix stability and folding kinetics","volume":"324","author":"Sacca","year":"2002","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib24","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1002\/psc.385","article-title":"Synthesis of heterotrimeric collagen peptides containing the alpha1beta1 integrin recognition site of collagen type IV","volume":"8","author":"Sacca","year":"2002","journal-title":"J.\u00a0Pept. Sci."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib25","doi-asserted-by":"crossref","first-page":"13610","DOI":"10.1021\/bi9905157","article-title":"Synthesis and folding of native collagen III model peptides","volume":"38","author":"Henkel","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib26","doi-asserted-by":"crossref","first-page":"3153","DOI":"10.1021\/bm700587j","article-title":"The specific recognition of a cell binding sequence derived from type I collagen by Hep3B and L929 cells","volume":"8","author":"Khew","year":"2007","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib27","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1021\/bi702018v","article-title":"Template-assembled triple-helical peptide molecules: mimicry of collagen by molecular architecture and integrin-specific cell adhesion","volume":"47","author":"Khew","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib28","doi-asserted-by":"crossref","first-page":"5069","DOI":"10.1182\/blood-2010-01-260778","article-title":"Synergism between platelet collagen receptors defined using receptor-specific collagen-mimetic peptide substrata in flowing blood","volume":"115","author":"Pugh","year":"2010","journal-title":"Blood"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib29","doi-asserted-by":"crossref","first-page":"2574","DOI":"10.1016\/j.biomaterials.2009.12.008","article-title":"Coating of biomaterial scaffolds with the collagen-mimetic peptide GFOGER for bone defect repair","volume":"31","author":"Wojtowicz","year":"2010","journal-title":"Biomaterials"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib30","doi-asserted-by":"crossref","first-page":"892","DOI":"10.1002\/jms.1776","article-title":"Chemical cross-linking with a diazirine photoactivatable cross-linker investigated by MALDI- and ESI-MS\/MS","volume":"45","author":"Gomes","year":"2010","journal-title":"J.\u00a0Mass Spectrom."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib31","doi-asserted-by":"crossref","first-page":"554","DOI":"10.1016\/j.bmc.2011.06.066","article-title":"Diazirine based photoaffinity labeling","volume":"20","author":"Dubinsky","year":"2012","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib32","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1021\/bc00034a011","article-title":"Photoimmobilization of a bioactive laminin fragment and pattern-guided selective neuronal cell attachment","volume":"6","author":"Clemence","year":"1995","journal-title":"Bioconjug. Chem."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib33","doi-asserted-by":"crossref","first-page":"1077","DOI":"10.1016\/S0142-9612(03)00630-6","article-title":"Influence of freezing rate on pore structure in freeze-dried collagen-GAG scaffolds","volume":"25","author":"O'Brien","year":"2004","journal-title":"Biomaterials"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib34","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1002\/jbm.a.32415","article-title":"Design of a multiphase osteochondral scaffold. I. Control of chemical composition","volume":"92","author":"Lynn","year":"2010","journal-title":"J.\u00a0Biomed. Mater. Res. A"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib35","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1016\/S0142-9612(01)00211-3","article-title":"Use of collagen sponge incorporating transforming growth factor-beta1 to promote bone repair in skull defects in rabbits","volume":"23","author":"Ueda","year":"2002","journal-title":"Biomaterials"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib36","doi-asserted-by":"crossref","first-page":"1452","DOI":"10.1016\/j.biomaterials.2005.08.004","article-title":"Electrospinning of collagen nanofibers: effects on the behavior of normal human keratinocytes and early-stage wound healing","volume":"27","author":"Rho","year":"2006","journal-title":"Biomaterials"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib37","doi-asserted-by":"crossref","first-page":"1783","DOI":"10.1016\/S0142-9612(99)00073-3","article-title":"Biodegradable polymeric microcellular foams by modified thermally induced phase separation method","volume":"20","author":"Nam","year":"1999","journal-title":"Biomaterials"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib38","doi-asserted-by":"crossref","first-page":"4783","DOI":"10.1021\/nl103567y","article-title":"Self-assembly and biomaterials","volume":"10","author":"Stupp","year":"2010","journal-title":"Nano Lett."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib39","doi-asserted-by":"crossref","first-page":"908","DOI":"10.1038\/nmat2022","article-title":"Microfluidic scaffolds for tissue engineering","volume":"6","author":"Choi","year":"2007","journal-title":"Nat. Mater."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib40","doi-asserted-by":"crossref","first-page":"337","DOI":"10.2147\/IJN.S38635","article-title":"Techniques for fabrication and construction of three-dimensional scaffolds for tissue engineering","volume":"8","author":"Lu","year":"2013","journal-title":"Int. J. Nanomed."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib41","doi-asserted-by":"crossref","first-page":"6621","DOI":"10.1016\/j.biomaterials.2011.05.025","article-title":"The effect of purity upon the triple-helical stability of collagenous peptides","volume":"32","author":"Slatter","year":"2011","journal-title":"Biomaterials"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib42","doi-asserted-by":"crossref","first-page":"1629","DOI":"10.1242\/jcs.108.4.1629","article-title":"Integrin alpha 2 I-domain is a binding site for collagens","volume":"108","author":"Tuckwell","year":"1995","journal-title":"J.\u00a0Cell Sci."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib43","doi-asserted-by":"crossref","first-page":"24560","DOI":"10.1074\/jbc.M004111200","article-title":"Micromolar Ca2+ concentrations are essential for Mg2+-dependent binding of collagen by the integrin alpha2beta1 in human platelets","volume":"275","author":"Onley","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib44","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1016\/0142-9612(96)81413-X","article-title":"Cross-linking of dermal sheep collagen using a water-soluble carbodiimide","volume":"17","author":"Olde Damink","year":"1996","journal-title":"Biomaterials"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib45","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1038\/ki.1993.341","article-title":"Polymerase chain reaction and focal contact formation indicate integrin expression in mesangial cells","volume":"44","author":"Petermann","year":"1993","journal-title":"Kidney Int."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib46","doi-asserted-by":"crossref","first-page":"29873","DOI":"10.1074\/jbc.M304073200","article-title":"Prolyl hydroxylation of collagen type I is required for efficient binding to integrin \u03b11\u03b21 and platelet glycoprotein VI but not to \u03b12\u03b21","volume":"278","author":"Perret","year":"2003","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib47","doi-asserted-by":"crossref","first-page":"33287","DOI":"10.1074\/jbc.273.50.33287","article-title":"Identification in collagen type I of an integrin \u03b12\u03b21-binding site containing an essential GER sequence","volume":"273","author":"Knight","year":"1998","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib48","doi-asserted-by":"crossref","first-page":"47763","DOI":"10.1074\/jbc.M404685200","article-title":"Integrin activation state determines selectivity for novel recognition sites in fibrillar collagens","volume":"279","author":"Siljander","year":"2004","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib49","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.peptides.2012.04.013","article-title":"The properties conferred upon triple-helical collagen-mimetic peptides by the presence of cysteine residues","volume":"36","author":"Slatter","year":"2012","journal-title":"Peptides"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib50","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1038\/nmeth752","article-title":"Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells","volume":"2","author":"Suchanek","year":"2005","journal-title":"Nat. Methods"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib51","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1002\/jbm.a.10550","article-title":"Engineering integrin-specific surfaces with a triple-helical collagen-mimetic peptide","volume":"65A","author":"Reyes","year":"2003","journal-title":"J.\u00a0Biomed. Mater. Res. A"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib52","doi-asserted-by":"crossref","first-page":"1468","DOI":"10.1002\/jps.20815","article-title":"Protect from light: photodegradation and protein biologics","volume":"96","author":"Kerwin","year":"2007","journal-title":"J.\u00a0Pharm. Sci."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib53","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.bpj.2009.01.065","article-title":"Flash photolysis of cutinase: identification and decay kinetics of transient intermediates formed upon UV excitation of aromatic residues","volume":"97","author":"Neves-Petersen","year":"2009","journal-title":"Biophys. J."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib54","series-title":"Molecular Photochemistry \u2013 Various Aspects","article-title":"UV light effects on proteins: from photochemistry to nanomedicine","author":"Teresa","year":"2012"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib55","doi-asserted-by":"crossref","first-page":"3505","DOI":"10.1172\/JCI45913","article-title":"OSCAR is a collagen receptor that costimulates osteoclastogenesis in DAP12-deficient humans and mice","volume":"121","author":"Barrow","year":"2011","journal-title":"J.\u00a0Clin. Investig."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib56","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.jmbbm.2012.02.028","article-title":"Investigating the morphological, mechanical and degradation properties of scaffolds comprising collagen, gelatin and elastin for use in soft tissue engineering","volume":"10","author":"Grover","year":"2012","journal-title":"J.\u00a0Mech. Behav. Biomed."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib57","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1038\/223512a0","article-title":"Cell spreading and cell movement: an active or a passive process?","volume":"223","author":"Wolpert","year":"1969","journal-title":"Nature"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib58","doi-asserted-by":"crossref","first-page":"1863","DOI":"10.1091\/mbc.9.7.1863","article-title":"Activation of Rac and Cdc42 by integrins mediates cell spreading","volume":"9","author":"Price","year":"1998","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib59","first-page":"642","article-title":"Regulation of the actin cytoskeleton in cancer cell migration and invasion","volume":"1773","author":"Yamaguchi","year":"2007","journal-title":"BBA \u2013 Mol. Cell Res."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib60","doi-asserted-by":"crossref","first-page":"e27958","DOI":"10.4161\/sgtp.27958","article-title":"The on-off relationship of Rho and Rac during integrin-mediated adhesion and cell migration","volume":"5","author":"Lawson","year":"2014","journal-title":"Small GTPases"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib61","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.actbio.2015.07.034","article-title":"Control of crosslinking for tailoring collagen-based scaffolds stability and mechanics","volume":"25","author":"Davidenko","year":"2015","journal-title":"Acta Biomater."},{"key":"10.1016\/j.biomaterials.2016.01.044_bib62","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1182\/blood-2002-12-3882","article-title":"Platelet-collagen interaction: is GPVI the central receptor?","volume":"102","author":"Nieswandt","year":"2003","journal-title":"Blood"},{"key":"10.1016\/j.biomaterials.2016.01.044_bib63","doi-asserted-by":"crossref","first-page":"e52209","DOI":"10.1371\/journal.pone.0052209","article-title":"Discoidin domain receptors promote alpha1beta1- and alpha2beta1-integrin mediated cell adhesion to collagen by enhancing integrin activation","volume":"7","author":"Xu","year":"2012","journal-title":"PLoS One"}],"container-title":["Biomaterials"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0142961216000582?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0142961216000582?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,26]],"date-time":"2025-09-26T16:14:35Z","timestamp":1758903275000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0142961216000582"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,4]]},"references-count":63,"alternative-id":["S0142961216000582"],"URL":"https:\/\/doi.org\/10.1016\/j.biomaterials.2016.01.044","relation":{},"ISSN":["0142-9612"],"issn-type":[{"value":"0142-9612","type":"print"}],"subject":[],"published":{"date-parts":[[2016,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The synthesis and coupling of photoreactive collagen-based peptides to restore integrin reactivity to an inert substrate, chemically-crosslinked collagen","name":"articletitle","label":"Article Title"},{"value":"Biomaterials","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.biomaterials.2016.01.044","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2016 The Authors. Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}]}}