{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,9]],"date-time":"2026-09-09T22:11:09Z","timestamp":1788991869760,"version":"build-2803163510"},"reference-count":60,"publisher":"Oxford University Press (OUP)","issue":"7","license":[{"start":{"date-parts":[[2000,7,1]],"date-time":"2000-07-01T00:00:00Z","timestamp":962409600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2000,7,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>The brittleness of bone in patients with osteogenesis imperfecta (OI) has been attributed to an aberrant collagen network. However, the role of collagen in the loss of tissue integrity has not been well established. To gain an insight into the biochemistry and structure of the collagen network, the cross-links hydroxylysylpyridinoline (HP) and lysylpyridinoline (LP) and the level of triple helical hydroxylysine (Hyl) were determined in bone of OI patients (types I, III, and IV) as well as controls. The amount of triple helical Hyl was increased in all patients. LP levels in OI were not significantly different; in contrast, the amount of HP (and as a consequence the HP\/LP ratio and the total pyridinoline level) was significantly increased. There was no relationship between the sum of pyridinolines and the amount of triple helical Hyl, indicating that lysyl hydroxylation of the triple helix and the telopeptides are under separate control. Cross-linking is the result of a specific three-dimensional arrangement of collagens within the fibril; only molecules that are correctly aligned are able to form cross-links. Inasmuch as the total amount of pyridinoline cross-links in OI bone is similar to control bone, the packing geometry of intrafibrillar collagen molecules is not disturbed in OI. Consequently, the brittleness of bone is not caused by a disorganized intrafibrillar collagen packing and\/or loss of cross-links. This is an unexpected finding, because mutant collagen molecules with a random distribution within the fibril are expected to result in disruptions of the alignment of neighboring collagen molecules. Pepsin digestion of OI bone revealed that collagen located at the surface of the fibril had lower cross-link levels compared with collagen located at the inside of the fibril, indicating that mutant molecules are not distributed randomly within the fibril but are located preferentially at the surface of the fibril.<\/jats:p>","DOI":"10.1359\/jbmr.2000.15.7.1330","type":"journal-article","created":{"date-parts":[[2006,4,26]],"date-time":"2006-04-26T20:30:23Z","timestamp":1146083423000},"page":"1330-1336","source":"Crossref","is-referenced-by-count":48,"title":["Pyridinium Cross-Links in Bone of Patients with Osteogenesis Imperfecta: Evidence of a Normal Intrafibrillar Collagen Packing"],"prefix":"10.1093","volume":"15","author":[{"given":"Ruud A.","family":"Bank","sequence":"first","affiliation":[{"name":"Gaubius Laboratory, Division of Vascular and Connective Tissue Research, Netherlands Organization for Applied Scientific Research (TNO), Prevention and Health, Leiden, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Johan M.","family":"Tekoppele","sequence":"additional","affiliation":[{"name":"Gaubius Laboratory, Division of Vascular and Connective Tissue Research, Netherlands Organization for Applied Scientific Research (TNO), Prevention and Health, Leiden, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guus J. M.","family":"Janus","sequence":"additional","affiliation":[{"name":"University Cluster of Orthopaedics, Department Orthopaedics, University Hospital, Utrecht, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maurice H. M.","family":"Wassen","sequence":"additional","affiliation":[{"name":"University Cluster of Orthopaedics, Department Orthopaedics, University Hospital, Utrecht, The Netherlands"},{"name":"Gaubius Laboratory, Division of Vascular and Connective Tissue Research, Netherlands Organization for Applied Scientific Research (TNO), Prevention and Health, Leiden, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hans E. H.","family":"Pruijs","sequence":"additional","affiliation":[{"name":"Wilhelmina Children's Hospital, Utrecht, The Netherlands"},{"name":"University Cluster of Orthopaedics, Department Orthopaedics, University Hospital, Utrecht, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hans A. H.","family":"van der Sluijs","sequence":"additional","affiliation":[{"name":"Department of Orthopaedics, Academic Hospital Free Universitity, Amsterdam, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ralph J. B.","family":"Sakkers","sequence":"additional","affiliation":[{"name":"Wilhelmina Children's Hospital, Utrecht, The Netherlands"},{"name":"University Cluster of Orthopaedics, Department Orthopaedics, University Hospital, Utrecht, The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2009,12,2]]},"reference":[{"key":"2024020714092058200_bib1","doi-asserted-by":"crossref","first-page":"113","DOI":"10.3109\/07853899309164153","article-title":"Collagens and their abnormalities in a wide spectrum of diseases","volume":"25","author":"Kivirikko","year":"1993","journal-title":"Ann Med"},{"key":"2024020714092058200_bib2","first-page":"167","article-title":"Osteogenesis imperfecta as a consequence of naturally occurring and induced mutations of type I collagen","volume":"8","author":"Cole","year":"1994","journal-title":"J Bone Miner Res"},{"key":"2024020714092058200_bib3","first-page":"317","volume-title":"Connective Tissue and Its Heritable Disorders. Molecular, Genetic, and Medical Aspects","author":"Byers","year":"1993"},{"key":"2024020714092058200_bib4","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1007\/978-1-4757-9065-8_2","article-title":"Mutations in type I procollagen genes that cause osteogenesis imperfecta","volume":"19","author":"Prockop","year":"1990","journal-title":"Adv Hum Genet"},{"key":"2024020714092058200_bib5","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1002\/(SICI)1098-1004(1997)9:4<300::AID-HUMU2>3.0.CO;2-9","article-title":"Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels","volume":"9","author":"Kuivaniemi","year":"1997","journal-title":"Hum Mutat"},{"key":"2024020714092058200_bib6","first-page":"508","article-title":"Osteogenesis imperfecta type I is commonly due to a COL1A1 null allele of type I collagen","volume":"51","author":"Willing","year":"1992","journal-title":"Am J Hum Genet"},{"key":"2024020714092058200_bib7","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1172\/JCI119519","article-title":"Collagen from the osteogensis imperfecta mouse model (oim) shows reduced resistance against tensile stress","volume":"100","author":"Misof","year":"1997","journal-title":"J Clin Invest"},{"key":"2024020714092058200_bib8","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1016\/8756-3282(95)00076-P","article-title":"The strength of a calcified tissue depends in part on the molecular structure and organization of its constituent mineral crystals in their organic matrix","volume":"16","author":"Landis","year":"1995","journal-title":"Bone"},{"key":"2024020714092058200_bib9","doi-asserted-by":"crossref","first-page":"239","DOI":"10.3109\/03008209609005267","article-title":"Mineral characterization in calcifying tissues: Atomic, molecular and macromolecular perspectives","volume":"34","author":"Landis","year":"1996","journal-title":"Connect Tissue Res"},{"key":"2024020714092058200_bib10","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1002\/jbmr.5650080203","article-title":"Collagen crosslinks and mineral crystallinity in bone of patients with osteogenesis imperfecta","volume":"8","author":"Vetter","year":"1993","journal-title":"J Bone Miner Res"},{"key":"2024020714092058200_bib11","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/0945-053X(94)90200-3","article-title":"Ultrastructural studies of bones from patients with osteogenesis imperfecta","volume":"14","author":"Traub","year":"1994","journal-title":"Matrix Biol"},{"key":"2024020714092058200_bib12","doi-asserted-by":"crossref","first-page":"149","DOI":"10.3109\/03008208909050005","article-title":"The structure of mineralized collagen fibrils","volume":"21","author":"Katz","year":"1989","journal-title":"Connect Tissue Res"},{"key":"2024020714092058200_bib13","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1021\/bi00117a013","article-title":"Cross-linking connectivity in bone collagen fibrils: The COOH-terminal locus of free aldehyde","volume":"31","author":"Otsubo","year":"1992","journal-title":"Biochemistry"},{"key":"2024020714092058200_bib14","doi-asserted-by":"crossref","first-page":"81","DOI":"10.3109\/03008209309014236","article-title":"The post-translational chemistry and molecular packing of mineralizing tendon collagens","volume":"29","author":"Yamauchi","year":"1993","journal-title":"Connect Tissue Res"},{"key":"2024020714092058200_bib15","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1007\/BF00316875","article-title":"Bone strength: The bottom line","volume":"51","author":"Einhorn","year":"1992","journal-title":"Calcif Tissue Int"},{"key":"2024020714092058200_bib16","doi-asserted-by":"crossref","first-page":"365S","DOI":"10.1016\/8756-3282(95)00328-B","article-title":"Reduced concentrations of collagen cross-links are associated with reduced strength of bone","volume":"17","author":"Oxlund","year":"1995","journal-title":"Bone"},{"key":"2024020714092058200_bib17","doi-asserted-by":"crossref","first-page":"4907","DOI":"10.1021\/bi00365a027","article-title":"Intermolecular cross-linking and streospecific molecular packing in type I collagen fibrils of the periodontal ligament","volume":"25","author":"Yamauchi","year":"1986","journal-title":"Biochemistry"},{"key":"2024020714092058200_bib18","doi-asserted-by":"crossref","first-page":"26508","DOI":"10.1074\/jbc.271.43.26508","article-title":"Molecular site specificity of pyridinoline and pyrrole cross-links in type I collagen in human bone","volume":"271","author":"Hanson","year":"1996","journal-title":"J Biol Chem"},{"key":"2024020714092058200_bib19","doi-asserted-by":"crossref","first-page":"401","DOI":"10.3109\/03008209609029218","article-title":"Disrupted collagen architecture in the crystal structure of a triple helical peptide with a Gly\u2192Ala substitution","volume":"35","author":"Bella","year":"1996","journal-title":"Connect Tissue Res"},{"key":"2024020714092058200_bib20","doi-asserted-by":"crossref","first-page":"19249","DOI":"10.1016\/S0021-9258(18)37416-7","article-title":"A substitution of cysteine for glycine 748 of the \u03b11 chain produces a kink at this site in the procollagen I molecule and an altered N-proteinase cleavage site over 225 nm away","volume":"263","author":"Vogel","year":"1988","journal-title":"J Biol Chem"},{"key":"2024020714092058200_bib21","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1097\/00003086-198109000-00004","article-title":"Osteogenesis imperfecta: An expanding panorama of variants","volume":"159","author":"Sillence","year":"1981","journal-title":"Clin Orthop"},{"key":"2024020714092058200_bib22","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1136\/jmg.16.2.101","article-title":"Genetic heterogeneity in osteogenesis imperfecta","volume":"16","author":"Sillence","year":"1979","journal-title":"J Med Genet"},{"key":"2024020714092058200_bib23","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/S0378-4347(97)00391-5","article-title":"Sensitive fluorometric quantitation of pyridinium and pentosidine crosslinks in biological samples using a single HPLC-run","volume":"703","author":"Bank","year":"1997","journal-title":"J Chromatogr B Biomed Appl"},{"key":"2024020714092058200_bib24","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1006\/abio.1996.0346","article-title":"Amino acid analysis by reverse-phase high-performance liquid chromatography: Improved derivatization and detection conditions with 9-fluorenylmethyl chloroformate","volume":"240","author":"Bank","year":"1996","journal-title":"Anal Biochem"},{"key":"2024020714092058200_bib25","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1042\/bj2400699","article-title":"Collagen defects in lethal perinathal osteogenesis imperfecta","volume":"240","author":"Bateman","year":"1986","journal-title":"Biochem J"},{"key":"2024020714092058200_bib26","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1042\/bj3180497","article-title":"Cross-link analysis of the C-telopeptide domain from type III collagen","volume":"318","author":"Henkel","year":"1996","journal-title":"Biochem J"},{"key":"2024020714092058200_bib27","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/0221-8747(82)90022-4","article-title":"Composition, cross-linking and thermal stability of bone and skin collagens in patients with osteogenesis imperfecta","volume":"4","author":"Herbage","year":"1982","journal-title":"Metab Bone Dis Rel Res"},{"key":"2024020714092058200_bib28","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1007\/978-1-4757-9113-6_38","article-title":"The qualitative and quantitative crosslink chemistry of collagen matrices","volume":"86B","author":"Mechanic","year":"1977","journal-title":"Adv Exp Med Biol"},{"key":"2024020714092058200_bib29","first-page":"271","article-title":"Osteogenesis imperfecta: Biochemical studies of bone collagen","volume":"124","author":"Fujii","year":"1977","journal-title":"Clin Orthop"},{"key":"2024020714092058200_bib30","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1136\/ard.58.1.35","article-title":"Lysyl hydroxylation and nonreducible crosslinking of human supraspinatus tendon collagen: Changes with age and in chronic rotator cuff tendinitis","volume":"58","author":"Bank","year":"1999","journal-title":"Ann Rheum Dis"},{"key":"2024020714092058200_bib31","doi-asserted-by":"crossref","first-page":"275","DOI":"10.3109\/00365519609088617","article-title":"Changes with age in the urinary excretion of hydroxylysylpyridinoline (HP) and lysylpyridinoline (LP)","volume":"56","author":"A\u00e7il","year":"1996","journal-title":"Scand J Clin Lab Invest"},{"key":"2024020714092058200_bib32","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/0945-053X(94)90189-9","article-title":"Deposition and selective degradation of structurally abnormal type I collagen in a collagen matrix produced by osteogenesis imperfecta fibroblasts in vitro","volume":"14","author":"Bateman","year":"1994","journal-title":"Matrix Biol"},{"key":"2024020714092058200_bib33","doi-asserted-by":"crossref","first-page":"5081","DOI":"10.1021\/bi00234a035","article-title":"A type I collagen with substitution of a cysteine for glycine-748 in the \u03b11(I) chain copolymerizes with normal type I collagen and can generate fractallike structures","volume":"30","author":"Kadler","year":"1991","journal-title":"Biochemistry"},{"key":"2024020714092058200_bib34","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1111\/j.1365-2362.1981.tb01763.x","article-title":"Disorder of collagen metabolism in a patient with osteogenesis imperfecta (lethal type): Increased degree of hydroxylation of lysine in collagen types I and III","volume":"11","author":"Kirsch","year":"1981","journal-title":"Eur J Clin Invest"},{"key":"2024020714092058200_bib35","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1146\/annurev.bi.53.070184.003441","article-title":"Cross-linking in collagen and elastin","volume":"53","author":"Eyre","year":"1984","journal-title":"Annu Rev Biochem"},{"key":"2024020714092058200_bib36","doi-asserted-by":"crossref","first-page":"1054","DOI":"10.1073\/pnas.96.3.1054","article-title":"Defective collagen crosslinking in bone, but not in ligament or cartilage, in Bruck syndrome: Indications for a bone-specific telopeptide lysyl hydroxylase on chromosome 17","volume":"96","author":"Bank","year":"1999","journal-title":"Proc Natl Acad Sci U S A"},{"key":"2024020714092058200_bib37","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1172\/JCI114253","article-title":"Biochemical analysis of callus tissue in osteogenesis imperfecta type IV. Evidence for transient overmodification in collagen types I and III","volume":"84","author":"Brenner","year":"1989","journal-title":"J Clin Invest"},{"key":"2024020714092058200_bib38","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1042\/bj2820313","article-title":"Lysyl hydroxylation in collagens from hyperplastic callus and embryonic bones","volume":"282","author":"Lehmann","year":"1992","journal-title":"Biochem J"},{"key":"2024020714092058200_bib39","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1002\/jbmr.5650060512","article-title":"Osteogenesis imperfecta: changes in noncollagenous proteins in bone","volume":"6","author":"Vetter","year":"1991","journal-title":"J Bone Miner Res"},{"key":"2024020714092058200_bib40","doi-asserted-by":"crossref","first-page":"800","DOI":"10.1002\/jbmr.5650110611","article-title":"Long-term extracellular matrix metabolism by cultured human osteogenesis imperfecta osteoblasts","volume":"11","author":"Fedarko","year":"1996","journal-title":"J Bone Miner Res"},{"key":"2024020714092058200_bib41","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1002\/(SICI)1096-8628(19960503)63:1<161::AID-AJMG28>3.0.CO;2-L","article-title":"Deficient expression of the small proteoglycan decorin in a case of severe\/lethal osteogenesis imperfecta","volume":"63","author":"Dyne","year":"1996","journal-title":"Am J Med Genet"},{"key":"2024020714092058200_bib42","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1016\/S0945-053X(97)90023-8","article-title":"Altered collagen of human pathological fibroblasts impairs the synthesis of fibronectin","volume":"15","author":"Lebb\u00e9","year":"1997","journal-title":"Matrix Biol"},{"key":"2024020714092058200_bib43","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1002\/jbmr.5650110709","article-title":"Role of nonenzymatic glycosylation of type I collagen in diabetic osteopenia","volume":"11","author":"Katayama","year":"1996","journal-title":"J Bone Miner Res"},{"key":"2024020714092058200_bib44","doi-asserted-by":"crossref","first-page":"1139","DOI":"10.1002\/jbmr.5650110813","article-title":"The role of type I collagen in the regulation of the osteoblast phenotype","volume":"11","author":"Shi","year":"1996","journal-title":"J Bone Miner Res"},{"key":"2024020714092058200_bib45","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1002\/jcp.1041530205","article-title":"Growth on type I collagen promotes expression of the osteoblastic phenotype in human osteosarcoma MG-63 cells","volume":"153","author":"Andriano","year":"1992","journal-title":"J Cell Physiol"},{"key":"2024020714092058200_bib46","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1006\/excr.1995.1005","article-title":"The influence of type I collagen on the development and maintenance of the osteoblast phenotype in primary and passaged rat calvarial osteoblasts: modification of expression of genes supporting cell growth, adhesion, and extracellular matrix mineralization","volume":"216","author":"Lynch","year":"1995","journal-title":"Exp Cell Res"},{"key":"2024020714092058200_bib47","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1002\/jcp.1041430304","article-title":"Progressive development of the rat osteoblast phenotype in vitro: Reciprocal relationship in expression of genes associated with proliferation and differentiation during formation of the boneextracellular matrix","volume":"143","author":"Owen","year":"1990","journal-title":"J Cell Physiol"},{"key":"2024020714092058200_bib48","doi-asserted-by":"crossref","first-page":"357","DOI":"10.3109\/03008209609029212","article-title":"Matrix proteins and mineralization: An overview","volume":"35","author":"Boskey","year":"1996","journal-title":"Connect Tissue Res"},{"key":"2024020714092058200_bib49","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1002\/(SICI)1096-8628(19960503)63:1<167::AID-AJMG29>3.0.CO;2-L","article-title":"Tracing the pathway between mutation and phenotype in osteogenesis imperfecta: Isolation of mineralization-specific genes","volume":"63","author":"Culbert","year":"1996","journal-title":"Am J Med Genet"},{"key":"2024020714092058200_bib50","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1007\/BF01212948","article-title":"Composition and posttranslational modification of individual collagen chains from osteosarcomas and osteofibrous dysplasias","volume":"121","author":"Lehmann","year":"1995","journal-title":"J Cancer Res Clin Oncol"},{"key":"2024020714092058200_bib51","doi-asserted-by":"crossref","first-page":"964","DOI":"10.2106\/00004623-198062060-00013","article-title":"Changes in tissue morphology and collagen composition during the repair of cortical bone and in the adult chicken","volume":"62A","author":"Glimcher","year":"1980","journal-title":"J Bone Joint Surg"},{"key":"2024020714092058200_bib52","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1042\/bj2890829","article-title":"Fulvic acid supplementation and selenium deficiency disturb the structural integrity of mouse skeletal tissue. An animal model to study the molecular defects of Kashin-Beck disease","volume":"289","author":"Yang","year":"1993","journal-title":"Biochem J"},{"key":"2024020714092058200_bib53","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1172\/JCI114994","article-title":"Cartilage expression of a type II collagen mutation in an inherited form of osteoarthritis associated with a mild chondrodysplasia","volume":"87","author":"Eyre","year":"1991","journal-title":"J Clin Invest"},{"key":"2024020714092058200_bib54","first-page":"5","article-title":"Type II collagen defects in the chondrodysplasias. I. Spondyloepiphyseal dysplasias","volume":"45","author":"Murray","year":"1989","journal-title":"Am J Hum Genet"},{"key":"2024020714092058200_bib55","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1016\/0006-291X(92)91697-O","article-title":"Post-translational modifications in the collagen of human osteoporotic femoral head","volume":"185","author":"Bailey","year":"1992","journal-title":"Biochem Biophys Res Commun"},{"key":"2024020714092058200_bib56","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1111\/j.1365-2362.1992.tb01450.x","article-title":": Compositional analysis of the collagenous bone matrix. A study on adult normal and osteoponic bone tissue","volume":"22","author":"B\u00e4tge","year":"1992","journal-title":"Eur J Clin Invest"},{"key":"2024020714092058200_bib57","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1007\/s002239900271","article-title":"Alteration in the extent of collagen I hydroxylation, isolated from femoral heads of women with a femoral neck fracture caused by osteoporosis","volume":"60","author":"K\u00f6wotz","year":"1997","journal-title":"Calcif Tissue Int"},{"key":"2024020714092058200_bib58","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1042\/bj3101045","article-title":"Biochemical changes in the collagenous matrix of osteoporotic avian bone","volume":"310","author":"Knott","year":"1995","journal-title":"Biochem J"},{"key":"2024020714092058200_bib59","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/S0065-3101(24)00183-X","article-title":"Osteogenesis imperfecta: Comprehensive management","volume":"35","author":"Marini","year":"1988","journal-title":"Adv Pediatr"},{"key":"2024020714092058200_bib60","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1056\/NEJM199810013391402","article-title":"Cyclic administration of pamidronate in children with severe osteogenesis imperfecta","volume":"339","author":"Glorieux","year":"1998","journal-title":"N Engl J Med"}],"container-title":["Journal of Bone and Mineral Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1359%2Fjbmr.2000.15.7.1330","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/academic.oup.com\/jbmr\/article-pdf\/15\/7\/1330\/56602369\/5650150710.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/jbmr\/article-pdf\/15\/7\/1330\/56602369\/5650150710.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,3,13]],"date-time":"2024-03-13T15:00:54Z","timestamp":1710342054000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/jbmr\/article\/15\/7\/1330-1336\/7515366"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2000,7,1]]},"references-count":60,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2009,12,2]]},"published-print":{"date-parts":[[2000,7,1]]}},"URL":"https:\/\/doi.org\/10.1359\/jbmr.2000.15.7.1330","relation":{},"ISSN":["0884-0431","1523-4681"],"issn-type":[{"value":"0884-0431","type":"print"},{"value":"1523-4681","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2000,7,1]]},"published":{"date-parts":[[2000,7,1]]}}}