{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T20:07:58Z","timestamp":1780517278835,"version":"3.54.1"},"reference-count":121,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2017,8,1]],"date-time":"2017-08-01T00:00:00Z","timestamp":1501545600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["MOP-142330"],"award-info":[{"award-number":["MOP-142330"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000156","name":"Fonds de Recherche du Qu\u00e9bec - Sant\u00e9","doi-asserted-by":"publisher","award":["28308"],"award-info":[{"award-number":["28308"]}],"id":[{"id":"10.13039\/501100000156","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["clinicalkey.fr","clinicalkey.jp","clinicalkey.es","clinicalkey.com.au","clinicalkey.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bone"],"published-print":{"date-parts":[[2017,8]]},"DOI":"10.1016\/j.bone.2017.04.007","type":"journal-article","created":{"date-parts":[[2017,4,18]],"date-time":"2017-04-18T02:16:41Z","timestamp":1492481801000},"page":"37-48","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":35,"special_numbering":"C","title":["Mineralization-inhibiting effects of transglutaminase-crosslinked polymeric osteopontin"],"prefix":"10.1016","volume":"101","author":[{"given":"Betty","family":"Hoac","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Valentin","family":"Nelea","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wenge","family":"Jiang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mari T.","family":"Kaartinen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marc D.","family":"McKee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"Suppl. 1","key":"10.1016\/j.bone.2017.04.007_bb0005","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1080\/03008200390152061","article-title":"Six genes expressed in bones and teeth encode the current members of the SIBLING family of proteins","volume":"44","author":"Fisher","year":"2003","journal-title":"Connect. Tissue Res."},{"issue":"23","key":"10.1016\/j.bone.2017.04.007_bb0010","doi-asserted-by":"crossref","first-page":"8819","DOI":"10.1073\/pnas.83.23.8819","article-title":"Cloning and sequence analysis of rat bone sialoprotein (osteopontin) cDNA reveals an Arg-Gly-Asp cell-binding sequence","volume":"83","author":"Oldberg","year":"1986","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bone.2017.04.007_bb0015","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1111\/j.1749-6632.1995.tb44629.x","article-title":"Osteopontin and the bone remodeling sequence. Colloidal-gold immunocytochemistry of an interfacial extracellular matrix protein","volume":"760","author":"McKee","year":"1995","journal-title":"Ann. N. Y. Acad. Sci."},{"issue":"4","key":"10.1016\/j.bone.2017.04.007_bb0020","doi-asserted-by":"crossref","first-page":"1686","DOI":"10.1172\/JCI116755","article-title":"Osteopontin is elevated during neointima formation in rat arteries and is a novel component of human atherosclerotic plaques","volume":"92","author":"Giachelli","year":"1993","journal-title":"J. Clin. Invest."},{"issue":"4","key":"10.1016\/j.bone.2017.04.007_bb0025","doi-asserted-by":"crossref","first-page":"1597","DOI":"10.1172\/JCI117501","article-title":"Diffuse calcification in human coronary arteries. Association of osteopontin with atherosclerosis","volume":"94","author":"Fitzpatrick","year":"1994","journal-title":"J. Clin. Invest."},{"issue":"1","key":"10.1016\/j.bone.2017.04.007_bb0030","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1073\/pnas.89.1.426","article-title":"Inhibition of calcium oxalate crystal growth in vitro by uropontin: another member of the aspartic acid-rich protein superfamily","volume":"89","author":"Shiraga","year":"1992","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"9","key":"10.1016\/j.bone.2017.04.007_bb0035","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1002\/jbmr.5650070905","article-title":"The calcium oxalate crystal growth inhibitor protein produced by mouse kidney cortical cells in culture is osteopontin","volume":"7","author":"Worcester","year":"1992","journal-title":"J. Bone Miner. Res."},{"issue":"20","key":"10.1016\/j.bone.2017.04.007_bb0040","doi-asserted-by":"crossref","first-page":"15180","DOI":"10.1016\/S0021-9258(18)82453-X","article-title":"Structure and expression of the mRNA encoding urinary stone protein (osteopontin)","volume":"268","author":"Kohri","year":"1993","journal-title":"J. Biol. Chem."},{"issue":"1\u20132","key":"10.1016\/j.bone.2017.04.007_bb0045","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/0167-4838(89)90092-7","article-title":"Purification of a human milk protein closely similar to tumor-secreted phosphoproteins and osteopontin","volume":"996","author":"Senger","year":"1989","journal-title":"Biochim. Biophys. Acta"},{"issue":"2","key":"10.1016\/j.bone.2017.04.007_bb0050","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1017\/S0022029900027503","article-title":"Purification and characterization of three proteins isolated from the proteose peptone fraction of bovine milk","volume":"60","author":"Sorensen","year":"1993","journal-title":"J. Dairy Res."},{"issue":"5","key":"10.1016\/j.bone.2017.04.007_bb0055","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1091\/mbc.5.5.565","article-title":"Adhesive properties of osteopontin: regulation by a naturally occurring thrombin-cleavage in close proximity to the GRGDS cell-binding domain","volume":"5","author":"Senger","year":"1994","journal-title":"Mol. Biol. Cell"},{"issue":"30","key":"10.1016\/j.bone.2017.04.007_bb0060","doi-asserted-by":"crossref","first-page":"28261","DOI":"10.1074\/jbc.M103608200","article-title":"Osteopontin, a novel substrate for matrix metalloproteinase-3 (stromelysin-1) and matrix metalloproteinase-7 (matrilysin)","volume":"276","author":"Agnihotri","year":"2001","journal-title":"J. Biol. Chem."},{"issue":"30","key":"10.1016\/j.bone.2017.04.007_bb0065","doi-asserted-by":"crossref","first-page":"18696","DOI":"10.1016\/S0021-9258(17)44808-3","article-title":"Physiological properties and differential glycosylation of phosphorylated and nonphosphorylated forms of osteopontin secreted by normal rat kidney cells","volume":"265","author":"Singh","year":"1990","journal-title":"J. Biol. Chem."},{"issue":"21","key":"10.1016\/j.bone.2017.04.007_bb0070","doi-asserted-by":"crossref","first-page":"14853","DOI":"10.1016\/S0021-9258(17)36541-9","article-title":"Dephosphorylation of osteopontin and bone sialoprotein by osteoclastic tartrate-resistant acid phosphatase. Modulation of osteoclast adhesion in vitro","volume":"269","author":"Ek-Rylander","year":"1994","journal-title":"J. Biol. Chem."},{"issue":"1\u20134","key":"10.1016\/j.bone.2017.04.007_bb0075","doi-asserted-by":"crossref","first-page":"223","DOI":"10.3109\/03008209609029195","article-title":"Extracellular processing of bone and dentin proteins in matrix mineralization","volume":"35","author":"Suzuki","year":"1996","journal-title":"Connect. Tissue Res."},{"issue":"4","key":"10.1016\/j.bone.2017.04.007_bb0080","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1007\/s00223-013-9698-6","article-title":"Role of osteopontin in modulation of hydroxyapatite formation","volume":"93","author":"Hunter","year":"2013","journal-title":"Calcif. Tissue Int."},{"issue":"2","key":"10.1016\/j.bone.2017.04.007_bb0085","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/j.bbrc.2012.02.024","article-title":"Post-translational modification of osteopontin: effects on in vitro hydroxyapatite formation and growth","volume":"419","author":"Boskey","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"6","key":"10.1016\/j.bone.2017.04.007_bb0090","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1016\/j.bone.2008.01.016","article-title":"Modulation of extracellular matrix protein phosphorylation alters mineralization in differentiating chick limb-bud mesenchymal cell micromass cultures","volume":"42","author":"Boskey","year":"2008","journal-title":"Bone"},{"issue":"1","key":"10.1016\/j.bone.2017.04.007_bb0095","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1007\/s00223-004-1288-1","article-title":"Importance of phosphorylation for osteopontin regulation of biomineralization","volume":"77","author":"Gericke","year":"2005","journal-title":"Calcif. Tissue Int."},{"issue":"26","key":"10.1016\/j.bone.2017.04.007_bb0100","doi-asserted-by":"crossref","first-page":"20197","DOI":"10.1074\/jbc.M909174199","article-title":"Phosphorylation of osteopontin is required for inhibition of vascular smooth muscle cell calcification","volume":"275","author":"Jono","year":"2000","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.bone.2017.04.007_bb0105","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1006\/bbrc.2000.4146","article-title":"Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin","volume":"280","author":"Fisher","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"2","key":"10.1016\/j.bone.2017.04.007_bb0110","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0056764","article-title":"Dynamic light scattering study of inhibition of nucleation and growth of hydroxyapatite crystals by osteopontin","volume":"8","author":"de Bruyn","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.bone.2017.04.007_bb0115","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.matbio.2016.01.007","article-title":"Intrinsically disordered proteins and biomineralization","volume":"52-54","author":"Boskey","year":"2016","journal-title":"Matrix Biol."},{"issue":"21","key":"10.1016\/j.bone.2017.04.007_bb0120","doi-asserted-by":"crossref","first-page":"15872","DOI":"10.1074\/jbc.M701116200","article-title":"Pyrophosphate inhibits mineralization of osteoblast cultures by binding to mineral, up-regulating osteopontin, and inhibiting alkaline phosphatase activity","volume":"282","author":"Addison","year":"2007","journal-title":"J. Biol. Chem."},{"issue":"5","key":"10.1016\/j.bone.2017.04.007_bb0125","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1093\/oxfordjournals.jbchem.a124240","article-title":"Calcium-binding properties of osteopontin derived from non-osteogenic sources","volume":"114","author":"Singh","year":"1993","journal-title":"J. Biochem."},{"issue":"2","key":"10.1016\/j.bone.2017.04.007_bb0130","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/S0169-6009(08)80225-5","article-title":"Osteopontin-hydroxyapatite interactions in vitro: inhibition of hydroxyapatite formation and growth in a gelatin-gel","volume":"22","author":"Boskey","year":"1993","journal-title":"Bone Miner."},{"key":"10.1016\/j.bone.2017.04.007_bb0135","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1111\/j.1749-6632.1995.tb44642.x","article-title":"The inhibitory activity of osteopontin on hydroxyapatite formation in vitro","volume":"760","author":"Goldberg","year":"1995","journal-title":"Ann. N. Y. Acad. Sci."},{"issue":"Pt 3","key":"10.1016\/j.bone.2017.04.007_bb0140","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1042\/bj3000723","article-title":"Modulation of crystal formation by bone phosphoproteins: structural specificity of the osteopontin-mediated inhibition of hydroxyapatite formation","volume":"300","author":"Hunter","year":"1994","journal-title":"Biochem. J."},{"issue":"7","key":"10.1016\/j.bone.2017.04.007_bb0145","doi-asserted-by":"crossref","first-page":"1619","DOI":"10.1016\/j.cell.2015.05.028","article-title":"A single kinase generates the majority of the secreted phosphoproteome","volume":"161","author":"Tagliabracci","year":"2015","journal-title":"Cell"},{"issue":"6085","key":"10.1016\/j.bone.2017.04.007_bb0150","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.1126\/science.1217817","article-title":"Secreted kinase phosphorylates extracellular proteins that regulate biomineralization","volume":"336","author":"Tagliabracci","year":"2012","journal-title":"Science"},{"issue":"3","key":"10.1016\/j.bone.2017.04.007_bb0155","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1002\/jbmr.1766","article-title":"Proteolytic processing of osteopontin by PHEX and accumulation of osteopontin fragments in Hyp mouse bone, the murine model of X-linked hypophosphatemia","volume":"28","author":"Barros","year":"2013","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bone.2017.04.007_bb0160","article-title":"Raine syndrome (OMIM #259775), caused by FAM20C mutation, is congenital sclerosing osteomalacia with cerebral calcification (OMIM 259660)","author":"Whyte","year":"2016","journal-title":"J. Bone Miner. Res."},{"issue":"3","key":"10.1016\/j.bone.2017.04.007_bb0165","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/j.jsb.2013.11.009","article-title":"Mineralisation of soft and hard tissues and the stability of biofluids","volume":"185","author":"Holt","year":"2014","journal-title":"J. Struct. Biol."},{"issue":"24","key":"10.1016\/j.bone.2017.04.007_bb0170","doi-asserted-by":"crossref","first-page":"18639","DOI":"10.1021\/la100401r","article-title":"The flexible polyelectrolyte hypothesis of protein-biomineral interaction","volume":"26","author":"Hunter","year":"2010","journal-title":"Langmuir"},{"issue":"2","key":"10.1016\/j.bone.2017.04.007_bb0175","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1038\/nrm1014","article-title":"Transglutaminases: crosslinking enzymes with pleiotropic functions","volume":"4","author":"Lorand","year":"2003","journal-title":"Nat. Rev. Mol. Cell Biol."},{"issue":"3","key":"10.1016\/j.bone.2017.04.007_bb0180","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1152\/physrev.00044.2008","article-title":"Transglutaminases and disease: lessons from genetically engineered mouse models and inherited disorders","volume":"89","author":"Iismaa","year":"2009","journal-title":"Physiol. Rev."},{"issue":"2","key":"10.1016\/j.bone.2017.04.007_bb0185","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1152\/physrev.00019.2013","article-title":"Transglutaminase regulation of cell function","volume":"94","author":"Eckert","year":"2014","journal-title":"Physiol. Rev."},{"issue":"4","key":"10.1016\/j.bone.2017.04.007_bb0190","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1007\/s10930-008-9128-1","article-title":"Size distribution and molecular associations of plasma fibronectin and fibronectin crosslinked by transglutaminase 2","volume":"27","author":"Nelea","year":"2008","journal-title":"Protein J."},{"issue":"12","key":"10.1016\/j.bone.2017.04.007_bb0195","doi-asserted-by":"crossref","first-page":"4717","DOI":"10.1021\/jf0637269","article-title":"Synthesis and resistance to in vitro proteolysis of transglutaminase cross-linked phaseolin, the major storage protein from Phaseolus vulgaris","volume":"55","author":"Mariniello","year":"2007","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.bone.2017.04.007_bb0200","doi-asserted-by":"crossref","first-page":"1591","DOI":"10.2741\/1907","article-title":"Transglutaminases in mineralized tissues","volume":"11","author":"Nurminskaya","year":"2006","journal-title":"Front. Biosci."},{"issue":"8","key":"10.1016\/j.bone.2017.04.007_bb0205","doi-asserted-by":"crossref","first-page":"1477","DOI":"10.1359\/jbmr.2001.16.8.1477","article-title":"Characterization of tissue transglutaminase in human osteoblast-like cells","volume":"16","author":"Heath","year":"2001","journal-title":"J. Bone Miner. Res."},{"issue":"12","key":"10.1016\/j.bone.2017.04.007_bb0210","doi-asserted-by":"crossref","first-page":"2161","DOI":"10.1359\/jbmr.2002.17.12.2161","article-title":"Tissue transglutaminase and its substrates in bone","volume":"17","author":"Kaartinen","year":"2002","journal-title":"J. Bone Miner. Res."},{"issue":"3","key":"10.1016\/j.bone.2017.04.007_bb0215","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.matbio.2005.11.001","article-title":"Transglutaminase activity regulates osteoblast differentiation and matrix mineralization in MC3T3-E1 osteoblast cultures","volume":"25","author":"Al-Jallad","year":"2006","journal-title":"Matrix Biol."},{"issue":"1","key":"10.1016\/j.bone.2017.04.007_bb0220","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0015893","article-title":"Plasma membrane factor XIIIA transglutaminase activity regulates osteoblast matrix secretion and deposition by affecting microtubule dynamics","volume":"6","author":"Al-Jallad","year":"2011","journal-title":"PLoS One"},{"issue":"7","key":"10.1016\/j.bone.2017.04.007_bb0225","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1369\/jhc.6A7091.2007","article-title":"Expression and localization of plasma transglutaminase factor XIIIA in bone","volume":"55","author":"Nakano","year":"2007","journal-title":"J. Histochem. Cytochem."},{"issue":"3","key":"10.1016\/j.bone.2017.04.007_bb0230","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1016\/S0736-0266(01)00146-2","article-title":"Immunohistological analysis of transglutaminase factor XIIIA expression in mouse embryonic growth plate","volume":"20","author":"Nurminskaya","year":"2002","journal-title":"J. Orthop. Res."},{"issue":"1","key":"10.1016\/j.bone.2017.04.007_bb0235","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1007\/s00726-011-1131-8","article-title":"Transglutaminase 2 and factor XIII catalyze distinct substrates in differentiating osteoblastic cell line: utility of highly reactive substrate peptides","volume":"44","author":"Watanabe","year":"2013","journal-title":"Amino Acids"},{"key":"10.1016\/j.bone.2017.04.007_bb0240","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.bone.2014.11.008","article-title":"Serotonin (5-HT) inhibits factor XIII-A-mediated plasma fibronectin matrix assembly and crosslinking in osteoblast cultures via direct competition with transamidation","volume":"72","author":"Cui","year":"2015","journal-title":"Bone"},{"key":"10.1016\/j.bone.2017.04.007_bb0245","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/j.bone.2013.11.006","article-title":"Transglutaminase activity arising from factor XIIIA is required for stabilization and conversion of plasma fibronectin into matrix in osteoblast cultures","volume":"59","author":"Cui","year":"2014","journal-title":"Bone"},{"key":"10.1016\/j.bone.2017.04.007_bb0250","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/B978-0-12-394305-7.00001-X","article-title":"Cellular functions of tissue transglutaminase","volume":"294","author":"Nurminskaya","year":"2012","journal-title":"Int. Rev. Cell Mol. Biol."},{"issue":"10","key":"10.1016\/j.bone.2017.04.007_bb0255","doi-asserted-by":"crossref","first-page":"534","DOI":"10.1016\/S0968-0004(02)02182-5","article-title":"Transglutaminase 2: an enigmatic enzyme with diverse functions","volume":"27","author":"Fesus","year":"2002","journal-title":"Trends Biochem. Sci."},{"issue":"39","key":"10.1016\/j.bone.2017.04.007_bb0260","doi-asserted-by":"crossref","first-page":"11655","DOI":"10.1021\/bi970545e","article-title":"The core domain of the tissue transglutaminase Gh hydrolyzes GTP and ATP","volume":"36","author":"Iismaa","year":"1997","journal-title":"Biochemistry"},{"issue":"23","key":"10.1016\/j.bone.2017.04.007_bb0265","doi-asserted-by":"crossref","first-page":"23863","DOI":"10.1074\/jbc.M311919200","article-title":"Tissue transglutaminase has intrinsic kinase activity: identification of transglutaminase 2 as an insulin-like growth factor-binding protein-3 kinase","volume":"279","author":"Mishra","year":"2004","journal-title":"J. Biol. Chem."},{"issue":"9","key":"10.1016\/j.bone.2017.04.007_bb0270","doi-asserted-by":"crossref","first-page":"5532","DOI":"10.1074\/jbc.M506864200","article-title":"Phosphorylation of histones by tissue transglutaminase","volume":"281","author":"Mishra","year":"2006","journal-title":"J. Biol. Chem."},{"issue":"25","key":"10.1016\/j.bone.2017.04.007_bb0275","doi-asserted-by":"crossref","first-page":"18108","DOI":"10.1074\/jbc.M607413200","article-title":"Transglutaminase 2 kinase activity facilitates protein kinase A-induced phosphorylation of retinoblastoma protein","volume":"282","author":"Mishra","year":"2007","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.bone.2017.04.007_bb0280","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1046\/j.1432-1327.1999.00437.x","article-title":"The structural basis for the regulation of tissue transglutaminase by calcium ions","volume":"262","author":"Casadio","year":"1999","journal-title":"Eur. J. Biochem."},{"issue":"6","key":"10.1016\/j.bone.2017.04.007_bb0285","doi-asserted-by":"crossref","first-page":"3915","DOI":"10.1074\/jbc.275.6.3915","article-title":"Opposite effects of Ca(2+) and GTP binding on tissue transglutaminase tertiary structure","volume":"275","author":"Di Venere","year":"2000","journal-title":"J. Biol. Chem."},{"issue":"52","key":"10.1016\/j.bone.2017.04.007_bb0290","doi-asserted-by":"crossref","first-page":"19683","DOI":"10.1073\/pnas.0609283103","article-title":"Mechanism of allosteric regulation of transglutaminase 2 by GTP","volume":"103","author":"Begg","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"4","key":"10.1016\/j.bone.2017.04.007_bb0295","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/j.bone.2007.06.011","article-title":"ATP-mediated mineralization of MC3T3-E1 osteoblast cultures","volume":"41","author":"Nakano","year":"2007","journal-title":"Bone"},{"issue":"1","key":"10.1016\/j.bone.2017.04.007_bb0300","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1002\/jcp.22034","article-title":"Regulation of ATPase activity of transglutaminase 2 by MT1-MMP: implications for mineralization of MC3T3-E1 osteoblast cultures","volume":"223","author":"Nakano","year":"2010","journal-title":"J. Cell. Physiol."},{"issue":"8","key":"10.1016\/j.bone.2017.04.007_bb0305","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1016\/S1357-2725(99)00045-X","article-title":"Tissue transglutaminase: an enzyme with a split personality","volume":"31","author":"Chen","year":"1999","journal-title":"Int. J. Biochem. Cell Biol."},{"issue":"4","key":"10.1016\/j.bone.2017.04.007_bb0310","doi-asserted-by":"crossref","first-page":"1901","DOI":"10.1016\/S0021-9258(19)75724-X","article-title":"Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity","volume":"262","author":"Achyuthan","year":"1987","journal-title":"J. Biol. Chem."},{"issue":"5","key":"10.1016\/j.bone.2017.04.007_bb0315","doi-asserted-by":"crossref","first-page":"2743","DOI":"10.1073\/pnas.042454899","article-title":"Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity","volume":"99","author":"Liu","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"4","key":"10.1016\/j.bone.2017.04.007_bb0320","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1369\/jhc.6A7087.2006","article-title":"Osteopontin upregulation and polymerization by transglutaminase 2 in calcified arteries of matrix Gla protein-deficient mice","volume":"55","author":"Kaartinen","year":"2007","journal-title":"J. Histochem. Cytochem."},{"issue":"3","key":"10.1016\/j.bone.2017.04.007_bb0325","doi-asserted-by":"crossref","first-page":"1205","DOI":"10.1016\/0006-291X(91)90669-X","article-title":"Osteopontin, a substrate for transglutaminase and factor XIII activity","volume":"177","author":"Prince","year":"1991","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"4","key":"10.1016\/j.bone.2017.04.007_bb0330","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1093\/oxfordjournals.jbchem.a124395","article-title":"Osteopontin: its transglutaminase-catalyzed posttranslational modifications and cross-linking to fibronectin","volume":"115","author":"Beninati","year":"1994","journal-title":"J. Biochem."},{"issue":"Pt 1","key":"10.1016\/j.bone.2017.04.007_bb0335","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1042\/bj3040013","article-title":"Localization of transglutaminase-reactive glutamine residues in bovine osteopontin","volume":"304","author":"Sorensen","year":"1994","journal-title":"Biochem. J."},{"key":"10.1016\/j.bone.2017.04.007_bb0340","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1111\/j.1749-6632.1995.tb44658.x","article-title":"Phosphorylation, glycosylation, and transglutaminase sites in bovine osteopontin","volume":"760","author":"Sorensen","year":"1995","journal-title":"Ann. N. Y. Acad. Sci."},{"issue":"11","key":"10.1016\/j.bone.2017.04.007_bb0345","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0113650","article-title":"Identification of transglutaminase reactive residues in human osteopontin and their role in polymerization","volume":"9","author":"Christensen","year":"2014","journal-title":"PLoS One"},{"issue":"2","key":"10.1016\/j.bone.2017.04.007_bb0350","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1021\/acs.biochem.5b01153","article-title":"Transglutaminase 2-catalyzed intramolecular cross-linking of Osteopontin","volume":"55","author":"Christensen","year":"2016","journal-title":"Biochemistry"},{"issue":"3","key":"10.1016\/j.bone.2017.04.007_bb0355","doi-asserted-by":"crossref","first-page":"1729","DOI":"10.1074\/jbc.274.3.1729","article-title":"Cross-linking of osteopontin by tissue transglutaminase increases its collagen binding properties","volume":"274","author":"Kaartinen","year":"1999","journal-title":"J. Biol. Chem."},{"issue":"36","key":"10.1016\/j.bone.2017.04.007_bb0360","doi-asserted-by":"crossref","first-page":"22736","DOI":"10.1074\/jbc.272.36.22736","article-title":"Transglutaminase-catalyzed cross-linking of osteopontin is inhibited by osteocalcin","volume":"272","author":"Kaartinen","year":"1997","journal-title":"J. Biol. Chem."},{"issue":"22","key":"10.1016\/j.bone.2017.04.007_bb0365","doi-asserted-by":"crossref","first-page":"14769","DOI":"10.1074\/jbc.M901515200","article-title":"Polymeric osteopontin employs integrin alpha9beta1 as a receptor and attracts neutrophils by presenting a de novo binding site","volume":"284","author":"Nishimichi","year":"2009","journal-title":"J. Biol. Chem."},{"issue":"13","key":"10.1016\/j.bone.2017.04.007_bb0370","doi-asserted-by":"crossref","first-page":"11170","DOI":"10.1074\/jbc.M110.189258","article-title":"Osteopontin undergoes polymerization in vivo and gains chemotactic activity for neutrophils mediated by integrin alpha9beta1","volume":"286","author":"Nishimichi","year":"2011","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.bone.2017.04.007_bb0375","doi-asserted-by":"crossref","first-page":"65","DOI":"10.4161\/cam.5.1.13369","article-title":"Transglutaminase-mediated oligomerization promotes osteoblast adhesive properties of osteopontin and bone sialoprotein","volume":"5","author":"Forsprecher","year":"2011","journal-title":"Cell Adhes. Migr."},{"issue":"14","key":"10.1016\/j.bone.2017.04.007_bb0380","doi-asserted-by":"crossref","first-page":"2697","DOI":"10.1016\/j.febslet.2007.05.018","article-title":"Enhanced biological activity of polymeric osteopontin","volume":"581","author":"Higashikawa","year":"2007","journal-title":"FEBS Lett."},{"issue":"5","key":"10.1016\/j.bone.2017.04.007_bb0385","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1055\/s-2007-999043","article-title":"Tissue transglutaminase and factor XIII in cartilage and bone remodeling","volume":"22","author":"Aeschlimann","year":"1996","journal-title":"Semin. Thromb. Hemost."},{"issue":"1","key":"10.1016\/j.bone.2017.04.007_bb0390","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3109\/03008200009005638","article-title":"Protein crosslinking in assembly and remodelling of extracellular matrices: the role of transglutaminases","volume":"41","author":"Aeschlimann","year":"2000","journal-title":"Connect. Tissue Res."},{"issue":"10","key":"10.1016\/j.bone.2017.04.007_bb0395","doi-asserted-by":"crossref","first-page":"2040","DOI":"10.1002\/pro.5560041009","article-title":"Posttranslational modifications of bovine osteopontin: identification of twenty-eight phosphorylation and three O-glycosylation sites","volume":"4","author":"Sorensen","year":"1995","journal-title":"Protein Sci."},{"issue":"7","key":"10.1016\/j.bone.2017.04.007_bb0400","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1038\/nmeth.2089","article-title":"NIH image to imageJ: 25years of image analysis","volume":"9","author":"Schneider","year":"2012","journal-title":"Nat. Methods"},{"key":"10.1016\/j.bone.2017.04.007_bb0405","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/j.bone.2014.11.003","article-title":"Extracellular matrix mineralization in murine MC3T3-E1 osteoblast cultures: an ultrastructural, compositional and comparative analysis with mouse bone","volume":"71","author":"Addison","year":"2015","journal-title":"Bone"},{"issue":"8","key":"10.1016\/j.bone.2017.04.007_bb0410","doi-asserted-by":"crossref","first-page":"1462","DOI":"10.1177\/00220345940730081101","article-title":"The effect of supersaturation on apatite crystal formation in aqueous solutions at physiologic pH and temperature","volume":"73","author":"Ishikawa","year":"1994","journal-title":"J. Dent. Res."},{"issue":"1","key":"10.1016\/j.bone.2017.04.007_bb0415","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1007\/BF02546399","article-title":"The interaction of supersaturated calcium phosphate solutions with apatitic substrates","volume":"20","author":"Eanes","year":"1976","journal-title":"Calcif. Tissue Res."},{"issue":"6","key":"10.1016\/j.bone.2017.04.007_bb0420","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1359\/jbmr.1999.14.6.893","article-title":"Isolation and characterization of MC3T3-E1 preosteoblast subclones with distinct in vitro and in vivo differentiation\/mineralization potential","volume":"14","author":"Wang","year":"1999","journal-title":"J. Bone Miner. Res."},{"issue":"1","key":"10.1016\/j.bone.2017.04.007_bb0425","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1006\/bbrc.1994.1028","article-title":"Identification of two phosphorylation motifs in bovine osteopontin","volume":"198","author":"Sorensen","year":"1994","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"18","key":"10.1016\/j.bone.2017.04.007_bb0430","doi-asserted-by":"crossref","first-page":"6990","DOI":"10.1021\/bi050109p","article-title":"Comprehensive identification of post-translational modifications of rat bone osteopontin by mass spectrometry","volume":"44","author":"Keykhosravani","year":"2005","journal-title":"Biochemistry"},{"issue":"3","key":"10.1016\/j.bone.2017.04.007_bb0435","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1007\/s00223-008-9215-5","article-title":"Kinetics of calcium oxalate crystal growth in the presence of osteopontin isoforms: an analysis by scanning confocal interference microcopy","volume":"84","author":"Langdon","year":"2009","journal-title":"Calcif. Tissue Int."},{"issue":"1\u20134","key":"10.1016\/j.bone.2017.04.007_bb0440","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1159\/000151430","article-title":"Role of phosphate groups in inhibition of calcium oxalate crystal growth by osteopontin","volume":"189","author":"Hunter","year":"2009","journal-title":"Cells Tissues Organs"},{"issue":"1\u20134","key":"10.1016\/j.bone.2017.04.007_bb0445","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1159\/000151724","article-title":"Phosphorylation of osteopontin peptides mediates adsorption to and incorporation into calcium oxalate crystals","volume":"189","author":"O'Young","year":"2009","journal-title":"Cells Tissues Organs"},{"key":"10.1016\/j.bone.2017.04.007_bb0450","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.colsurfb.2012.03.015","article-title":"On the catalysis of calcium oxalate dihydrate formation by osteopontin peptides","volume":"96","author":"Chan","year":"2012","journal-title":"Colloids Surf. B: Biointerfaces"},{"issue":"1","key":"10.1016\/j.bone.2017.04.007_bb0455","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.jsb.2008.04.008","article-title":"Ultrastructural matrix-mineral relationships in avian eggshell, and effects of osteopontin on calcite growth in vitro","volume":"163","author":"Chien","year":"2008","journal-title":"J. Struct. Biol."},{"issue":"35","key":"10.1016\/j.bone.2017.04.007_bb0460","doi-asserted-by":"crossref","first-page":"23491","DOI":"10.1074\/jbc.M109.021899","article-title":"Modulation of calcium oxalate dihydrate growth by selective crystal-face binding of phosphorylated osteopontin and polyaspartate peptide showing occlusion by sectoral (compositional) zoning","volume":"284","author":"Chien","year":"2009","journal-title":"J. Biol. Chem."},{"issue":"30","key":"10.1016\/j.bone.2017.04.007_bb0465","doi-asserted-by":"crossref","first-page":"9151","DOI":"10.1021\/jp804282u","article-title":"Phosphorylation of osteopontin is required for inhibition of calcium oxalate crystallization","volume":"112","author":"Wang","year":"2008","journal-title":"J. Phys. Chem. B"},{"issue":"1","key":"10.1016\/j.bone.2017.04.007_bb0470","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1046\/j.1523-1755.2001.00772.x","article-title":"Phosphorylated osteopontin peptides suppress crystallization by inhibiting the growth of calcium oxalate crystals","volume":"60","author":"Hoyer","year":"2001","journal-title":"Kidney Int."},{"key":"10.1016\/j.bone.2017.04.007_bb0475","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.bone.2014.05.020","article-title":"Osteopontin binds multiple calcium ions with high affinity and independently of phosphorylation status","volume":"66","author":"Klaning","year":"2014","journal-title":"Bone"},{"issue":"4","key":"10.1016\/j.bone.2017.04.007_bb0480","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1359\/jbmr.090832","article-title":"Phosphorylation-dependent inhibition of mineralization by osteopontin ASARM peptides is regulated by PHEX cleavage","volume":"25","author":"Addison","year":"2010","journal-title":"J. Bone Miner. Res."},{"issue":"Pt 1","key":"10.1016\/j.bone.2017.04.007_bb0485","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1042\/BJ20050341","article-title":"Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications","volume":"390","author":"Christensen","year":"2005","journal-title":"Biochem. J."},{"issue":"1\u20134","key":"10.1016\/j.bone.2017.04.007_bb0490","doi-asserted-by":"crossref","first-page":"145","DOI":"10.3109\/03008209609029185","article-title":"Posttranslational modification in rat bone osteopontin","volume":"35","author":"Neame","year":"1996","journal-title":"Connect. Tissue Res."},{"issue":"1","key":"10.1016\/j.bone.2017.04.007_bb0495","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1042\/BJ20071021","article-title":"Post-translational modification and proteolytic processing of urinary osteopontin","volume":"411","author":"Christensen","year":"2008","journal-title":"Biochem. J."},{"issue":"3","key":"10.1016\/j.bone.2017.04.007_bb0500","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1016\/j.bone.2012.05.009","article-title":"Structural disorder in proteins brings order to crystal growth in biomineralization","volume":"51","author":"Kalmar","year":"2012","journal-title":"Bone"},{"issue":"5","key":"10.1016\/j.bone.2017.04.007_bb0505","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1016\/j.bone.2003.11.027","article-title":"Osteopontin is a negative regulator of proliferation and differentiation in MC3T3-E1 pre-osteoblastic cells","volume":"34","author":"Huang","year":"2004","journal-title":"Bone"},{"issue":"3","key":"10.1016\/j.bone.2017.04.007_bb0510","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1093\/jb\/mvh136","article-title":"In vitro and in vivo effects of the overexpression of osteopontin on osteoblast differentiation using a recombinant adenoviral vector","volume":"136","author":"Kojima","year":"2004","journal-title":"J. Biochem."},{"issue":"3","key":"10.1016\/j.bone.2017.04.007_bb0515","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1042\/BJ20140702","article-title":"Osteopontin mediates mineralization and not osteogenic cell development in vitro","volume":"464","author":"Holm","year":"2014","journal-title":"Biochem. J."},{"issue":"8","key":"10.1016\/j.bone.2017.04.007_bb0520","doi-asserted-by":"crossref","first-page":"1440","DOI":"10.1359\/jbmr.2000.15.8.1440","article-title":"Developmental expression and tissue distribution of Phex protein: effect of the Hyp mutation and relationship to bone markers","volume":"15","author":"Ruchon","year":"2000","journal-title":"J. Bone Miner. Res."},{"issue":"12","key":"10.1016\/j.bone.2017.04.007_bb0525","doi-asserted-by":"crossref","first-page":"2027","DOI":"10.1359\/jbmr.1999.14.12.2027","article-title":"Coordinated maturational regulation of PHEX and renal phosphate transport inhibitory activity: evidence for the pathophysiological role of PHEX in X-linked hypophosphatemia","volume":"14","author":"Nesbitt","year":"1999","journal-title":"J. Bone Miner. Res."},{"issue":"1","key":"10.1016\/j.bone.2017.04.007_bb0530","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1016\/j.actbio.2013.10.010","article-title":"Multifunctional role of osteopontin in directing intrafibrillar mineralization of collagen and activation of osteoclasts","volume":"10","author":"Rodriguez","year":"2014","journal-title":"Acta Biomater."},{"issue":"3\u20135","key":"10.1016\/j.bone.2017.04.007_bb0535","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.mser.2007.05.001","article-title":"Bone structure and formation: a new perspective","volume":"58","author":"Olszta","year":"2007","journal-title":"Mater. Sci. Eng. R. Rep."},{"issue":"1","key":"10.1016\/j.bone.2017.04.007_bb0540","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1006\/jsbi.1993.1003","article-title":"Mineral and organic matrix interaction in normally calcifying tendon visualized in three dimensions by high-voltage electron microscopic tomography and graphic image reconstruction","volume":"110","author":"Landis","year":"1993","journal-title":"J. Struct. Biol."},{"issue":"6","key":"10.1016\/j.bone.2017.04.007_bb0545","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1055\/s-0037-1613342","article-title":"Targeted inactivation of the mouse locus encoding coagulation factor XIII-A: hemostatic abnormalities in mutant mice and characterization of the coagulation deficit","volume":"88","author":"Lauer","year":"2002","journal-title":"Thromb. Haemost."},{"issue":"23","key":"10.1016\/j.bone.2017.04.007_bb0550","doi-asserted-by":"crossref","first-page":"20673","DOI":"10.1074\/jbc.M010846200","article-title":"Targeted inactivation of Gh\/tissue transglutaminase II","volume":"276","author":"Nanda","year":"2001","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.bone.2017.04.007_bb0555","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1128\/MCB.21.1.148-155.2001","article-title":"Gene disruption of tissue transglutaminase","volume":"21","author":"De Laurenzi","year":"2001","journal-title":"Mol. Cell. Biol."},{"issue":"4","key":"10.1016\/j.bone.2017.04.007_bb0560","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1007\/s00726-008-0133-7","article-title":"FXIIIA and TGF-beta over-expression produces normal musculo-skeletal phenotype in TG2\u2212\/\u2212 mice","volume":"36","author":"Tarantino","year":"2009","journal-title":"Amino Acids"},{"key":"10.1016\/j.bone.2017.04.007_bb0565","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.matbio.2015.02.001","article-title":"Normal bone deposition occurs in mice deficient in factor XIII-A and transglutaminase 2","volume":"43","author":"Cordell","year":"2015","journal-title":"Matrix Biol."},{"key":"10.1016\/j.bone.2017.04.007_bb0570","doi-asserted-by":"crossref","DOI":"10.1038\/cdd.2017.21","article-title":"Transglutaminases factor XIII-A and TG2 regulate resorption, adipogenesis and plasma fibronectin homeostasis in bone and bone marrow","author":"Mousa","year":"2017","journal-title":"Cell Death Differ."},{"issue":"2\u20133","key":"10.1016\/j.bone.2017.04.007_bb0575","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1007\/s00726-011-1021-0","article-title":"Characterization of the transglutaminase gene family in zebrafish and in vivo analysis of transglutaminase-dependent bone mineralization","volume":"42","author":"Deasey","year":"2012","journal-title":"Amino Acids"},{"issue":"2","key":"10.1016\/j.bone.2017.04.007_bb0580","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1007\/s00223-001-1121-z","article-title":"Osteopontin deficiency increases mineral content and mineral crystallinity in mouse bone","volume":"71","author":"Boskey","year":"2002","journal-title":"Calcif. Tissue Int."},{"issue":"6","key":"10.1016\/j.bone.2017.04.007_bb0585","doi-asserted-by":"crossref","first-page":"1564","DOI":"10.1016\/j.bone.2010.02.014","article-title":"Osteopontin deficiency increases bone fragility but preserves bone mass","volume":"46","author":"Thurner","year":"2010","journal-title":"Bone"},{"issue":"2","key":"10.1016\/j.bone.2017.04.007_bb0590","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1359\/jbmr.061103","article-title":"Impaired angiogenesis, early callus formation, and late stage remodeling in fracture healing of osteopontin-deficient mice","volume":"22","author":"Duvall","year":"2007","journal-title":"J. Bone Miner. Res."},{"issue":"1","key":"10.1016\/j.bone.2017.04.007_bb0595","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1002\/jbm.a.31081","article-title":"Osteopontin deficiency and aging on nanomechanics of mouse bone","volume":"83","author":"Kavukcuoglu","year":"2007","journal-title":"J. Biomed. Mater. Res. A"},{"issue":"8","key":"10.1016\/j.bone.2017.04.007_bb0600","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1038\/nmat1428","article-title":"Sacrificial bonds and hidden length dissipate energy as mineralized fibrils separate during bone fracture","volume":"4","author":"Fantner","year":"2005","journal-title":"Nat. Mater."},{"issue":"47","key":"10.1016\/j.bone.2017.04.007_bb0605","doi-asserted-by":"crossref","first-page":"19178","DOI":"10.1073\/pnas.1201513109","article-title":"Dilatational band formation in bone","volume":"109","author":"Poundarik","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."}],"container-title":["Bone"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S8756328217301461?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S8756328217301461?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,6,23]],"date-time":"2024-06-23T16:17:45Z","timestamp":1719159465000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S8756328217301461"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,8]]},"references-count":121,"alternative-id":["S8756328217301461"],"URL":"https:\/\/doi.org\/10.1016\/j.bone.2017.04.007","relation":{},"ISSN":["8756-3282"],"issn-type":[{"value":"8756-3282","type":"print"}],"subject":[],"published":{"date-parts":[[2017,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Mineralization-inhibiting effects of transglutaminase-crosslinked polymeric osteopontin","name":"articletitle","label":"Article Title"},{"value":"Bone","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bone.2017.04.007","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}