{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,5,13]],"date-time":"2025-05-13T17:08:01Z","timestamp":1747156081953,"version":"3.40.5"},"reference-count":36,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2024,9,1]],"date-time":"2024-09-01T00:00:00Z","timestamp":1725148800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,9,1]],"date-time":"2024-09-01T00:00:00Z","timestamp":1725148800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,7,16]],"date-time":"2024-07-16T00:00:00Z","timestamp":1721088000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemistry and Biophysics Reports"],"published-print":{"date-parts":[[2024,9]]},"DOI":"10.1016\/j.bbrep.2024.101790","type":"journal-article","created":{"date-parts":[[2024,7,19]],"date-time":"2024-07-19T19:13:07Z","timestamp":1721416387000},"page":"101790","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Generation of bone-specific lysyl hydroxylase 2 knockout mice and their phenotypes"],"prefix":"10.1016","volume":"39","author":[{"given":"Kenta","family":"Tsuneizumi","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Atsushi","family":"Kasamatsu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tomoaki","family":"Saito","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Reo","family":"Fukushima","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yuki","family":"Taga","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3354-6264","authenticated-orcid":false,"given":"Kazunori","family":"Mizuno","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Masataka","family":"Sunohara","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Katsuhiro","family":"Uzawa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mitsuo","family":"Yamauchi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbrep.2024.101790_bib1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1101\/cshperspect.a004978","article-title":"The collagen family","volume":"3","author":"Ricard-Blum","year":"2011","journal-title":"Cold Spring Harbor Perspect. Biol."},{"key":"10.1016\/j.bbrep.2024.101790_bib2","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1042\/bse0520113","article-title":"Lysine post-translational modifications of collagen","volume":"52","author":"Yamauchi","year":"2012","journal-title":"Essays Biochem."},{"key":"10.1016\/j.bbrep.2024.101790_bib3","doi-asserted-by":"crossref","first-page":"1716","DOI":"10.1172\/JCI117155","article-title":"A patient with Ehlers-Danlos syndrome type VI is a compound heterozygote for mutations in the lysyl hydroxylase gene","volume":"93","author":"Ha","year":"1994","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bbrep.2024.101790_bib4","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1006\/mgme.2000.3076","article-title":"Mutations in the lysyl hydroxylase 1 gene that result in enzyme deficiency and the clinical phenotype of Ehlers-Danlos syndrome type VI","volume":"71","author":"Yeowell","year":"2000","journal-title":"Mol. Genet. Metabol."},{"key":"10.1016\/j.bbrep.2024.101790_bib5","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.M111.333336","article-title":"Mutation in cyclophilin B that causes hyperelastosis cutis in american quarter horse does not affect peptidylprolyl cis-trans isomerase activity but shows altered cyclophilin b-protein interactions and affects collagen folding","volume":"287","author":"Ishikawa","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrep.2024.101790_bib6","doi-asserted-by":"crossref","first-page":"1639","DOI":"10.1359\/jbmr.2002.17.9.1639","article-title":"Regional alterations of type I collagen in rat tibia induced by skeletal unloading","volume":"17","author":"Shiiba","year":"2002","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bbrep.2024.101790_bib7","doi-asserted-by":"crossref","first-page":"40967","DOI":"10.1074\/jbc.M307380200","article-title":"Identification of PLOD2 as telopeptide lysyl hydroxylase, an important enzyme in fibrosis","volume":"278","author":"Van der Slot","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrep.2024.101790_bib8","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/j.matbio.2004.06.001","article-title":"Increased formation of pyridinoline cross-links due to higher telopeptide lysyl hydroxylase levels is a general fibrotic phenomenon","volume":"23","author":"van der Slot","year":"2004","journal-title":"Matrix Biol."},{"key":"10.1016\/j.bbrep.2024.101790_bib9","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbadis.2005.02.007","article-title":"The type of collagen cross-link determines the reversibility of experimental skin fibrosis","volume":"1740","author":"Van Der Slot-Verhoeven","year":"2005","journal-title":"Biochim. Biophys. Acta, Mol. Basis Dis."},{"year":"1998","series-title":"Altered Posttranslational Modifications of Collagen in Keloid","author":"Uzawa","key":"10.1016\/j.bbrep.2024.101790_bib10"},{"key":"10.1016\/j.bbrep.2024.101790_bib11","doi-asserted-by":"crossref","DOI":"10.1016\/j.ajhg.2008.09.004","article-title":"A connective tissue disorder caused by mutations of the lysyl hydroxylase 3 gene","volume":"83","author":"Salo","year":"2008","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.bbrep.2024.101790_bib12","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0137639","article-title":"Lysyl hydroxylase 3 localizes to epidermal basement membrane and is reduced in patients with recessive dystrophic epidermolysis bullosa","volume":"10","author":"Watt","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.bbrep.2024.101790_bib13","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1004465","article-title":"Abnormal type I collagen post-translational modification and crosslinking in a cyclophilin B KO mouse model of recessive osteogenesis imperfecta","volume":"10","author":"Cabral","year":"2014","journal-title":"PLoS Genet."},{"key":"10.1016\/j.bbrep.2024.101790_bib14","doi-asserted-by":"crossref","first-page":"25799","DOI":"10.1074\/jbc.M116.759803","article-title":"Lysyl hydroxylase 2 is secreted by tumor cells and can modify collagen in the extracellular space","volume":"291","author":"Chen","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrep.2024.101790_bib15","doi-asserted-by":"crossref","first-page":"2914","DOI":"10.1021\/acs.jproteome.7b00190","article-title":"Cyclophilin B deficiency causes abnormal dentin collagen matrix","volume":"16","author":"Terajima","year":"2017","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.bbrep.2024.101790_bib16","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1008196","article-title":"Cyclophilin B control of lysine post-translational modifications of skin type I collagen","volume":"15","author":"Terajima","year":"2019","journal-title":"PLoS Genet."},{"key":"10.1016\/j.bbrep.2024.101790_bib17","doi-asserted-by":"crossref","first-page":"1272","DOI":"10.1359\/jbmr.1999.14.8.1272","article-title":"Differential expression of human lysyl hydroxylase genes, lysine hydroxylation, and cross-linking of type I collagen during osteoblastic differentiation in vitro","volume":"14","author":"Uzawa","year":"1999","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bbrep.2024.101790_bib18","doi-asserted-by":"crossref","first-page":"1349","DOI":"10.1359\/JBMR.040323","article-title":"Lysyl hydroxylase-2b directs collagen cross-linking pathways in MC3T3-E1 cells","volume":"19","author":"Pornprasertsuk","year":"2004","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bbrep.2024.101790_bib19","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1042\/EBC20180051","article-title":"Collagen cross-linking mediated by lysyl hydroxylase 2: an enzymatic battlefield to combat fibrosis","volume":"63","author":"Piersma","year":"2019","journal-title":"Essays Biochem."},{"key":"10.1016\/j.bbrep.2024.101790_bib20","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-022-18165-0","article-title":"Lysyl hydroxylase 2 mediated collagen post-translational modifications and functional outcomes","volume":"12","author":"Terajima","year":"2022","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbrep.2024.101790_bib21","doi-asserted-by":"crossref","first-page":"7142","DOI":"10.1073\/pnas.1600074113","article-title":"Disentangling mechanisms involved in collagen pyridinoline cross-linking: the immunophilin FKBP65 is critical for dimerization of lysyl hydroxylase 2","volume":"113","author":"Gjaltema","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbrep.2024.101790_bib22","article-title":"FKBP65-dependent peptidyl-prolyl isomerase activity potentiates the lysyl hydroxylase 2-driven collagen cross-link switch","volume":"7","author":"Chen","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbrep.2024.101790_bib23","doi-asserted-by":"crossref","first-page":"1815","DOI":"10.1002\/ajmg.a.62718","article-title":"Bruck syndrome in 13 new patients: identification of five novel FKBP10 and PLOD2 variants and further expansion of the phenotypic spectrum","volume":"188","author":"Otaify","year":"2022","journal-title":"Am. J. Med. Genet."},{"key":"10.1016\/j.bbrep.2024.101790_bib24","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1016\/j.bbrc.2019.03.091","article-title":"Deficiency of lysyl hydroxylase 2 in mice causes systemic endoplasmic reticulum stress leading to early embryonic lethality","volume":"512","author":"Kasamatsu","year":"2019","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbrep.2024.101790_bib25","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.bbrc.2021.11.100","article-title":"Lysyl hydroxylase 2 deficiency promotes filopodia formation and fibroblast migration","volume":"587","author":"Nozaki","year":"2022","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbrep.2024.101790_bib26","article-title":"Deep coverage and quantification of the bone proteome provides enhanced opportunities for new discoveries in skeletal biology and disease","volume":"2022","author":"Rose","year":"2023","journal-title":"bioRxiv"},{"key":"10.1016\/j.bbrep.2024.101790_bib27","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1016\/S0006-291X(03)01262-2","article-title":"Identification, expression, and tissue distribution of the three rat lysyl hydroxylase isoforms","volume":"307","author":"Mercer","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbrep.2024.101790_bib28","doi-asserted-by":"crossref","first-page":"1349","DOI":"10.1359\/JBMR.040323","article-title":"Lysyl hydroxylase-2b directs collagen cross-linking pathways in MC3T3-E1 cells","volume":"19","author":"Pornprasertsuk","year":"2004","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bbrep.2024.101790_bib29","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/j.bbadis.2005.02.007","article-title":"The type of collagen cross-link determines the reversibility of experimental skin fibrosis","volume":"1740","author":"Van Der Slot-Verhoeven","year":"2005","journal-title":"Biochim. Biophys. Acta, Mol. Basis Dis."},{"key":"10.1016\/j.bbrep.2024.101790_bib30","doi-asserted-by":"crossref","first-page":"1930","DOI":"10.1002\/jbmr.2977","article-title":"Loss of type I collagen telopeptide lysyl hydroxylation causes musculoskeletal abnormalities in a zebrafish model of Bruck syndrome","volume":"31","author":"Gistelinck","year":"2016","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bbrep.2024.101790_bib31","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.1002\/jbmr.3742","article-title":"Osteocyte death and bone overgrowth in mice lacking fibroblast growth factor receptors 1 and 2 in mature osteoblasts and osteocytes","volume":"34","author":"McKenzie","year":"2019","journal-title":"J. Bone Miner. Res."},{"key":"10.1016\/j.bbrep.2024.101790_bib32","article-title":"Osteogenic differentiation potential of porcine bone marrow mesenchymal stem cell subpopulations selected in different basal media","volume":"9","author":"Kannan","year":"2020","journal-title":"Biol. Open."},{"key":"10.1016\/j.bbrep.2024.101790_bib33","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1007\/s11914-018-0455-7","article-title":"Mouse Cre models for the study of bone diseases","volume":"16","author":"Dallas","year":"2018","journal-title":"Curr. Osteoporos. Rep."},{"key":"10.1016\/j.bbrep.2024.101790_bib34","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/S0003-9969(97)00114-3","article-title":"The effects of oestrogen on osteocalcin production by human periodontal ligament cells","volume":"43","author":"Morishita","year":"1998","journal-title":"Arch. Oral Biol."},{"key":"10.1016\/j.bbrep.2024.101790_bib35","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1007\/s00223-013-9725-7","article-title":"Association of calcium and phosphate ions with collagen in the mineralization of vertebrate tissues","volume":"93","author":"Landis","year":"2013","journal-title":"Calcif. Tissue Int."},{"key":"10.1016\/j.bbrep.2024.101790_bib36","doi-asserted-by":"crossref","DOI":"10.1002\/jbm4.10454","article-title":"Abnormal bone collagen cross-linking in osteogenesis imperfecta\/bruck syndrome caused by compound heterozygous PLOD2 mutations","volume":"5","author":"Gistelinck","year":"2021","journal-title":"JBMR Plus"}],"container-title":["Biochemistry and Biophysics Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2405580824001547?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2405580824001547?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,10,9]],"date-time":"2024-10-09T06:10:02Z","timestamp":1728454202000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2405580824001547"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,9]]},"references-count":36,"alternative-id":["S2405580824001547"],"URL":"https:\/\/doi.org\/10.1016\/j.bbrep.2024.101790","relation":{},"ISSN":["2405-5808"],"issn-type":[{"type":"print","value":"2405-5808"}],"subject":[],"published":{"date-parts":[[2024,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Generation of bone-specific lysyl hydroxylase 2 knockout mice and their phenotypes","name":"articletitle","label":"Article Title"},{"value":"Biochemistry and Biophysics Reports","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbrep.2024.101790","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"101790"}}