Update on the Genetics of Osteogenesis Imperfecta.

Marini JC, Cabral WA (2018) Osteogenesis imperfecta. Genet Bone Biol Skeletal Dis, pp 397–420

Jovanovic M, Guterman-Ram G, Marini JC (2022) Osteogenesis imperfecta: mechanisms and signaling pathways connecting classical and rare OI types. Endocr Rev 43(1):61–90

pubmed: 34007986 doi: 10.1210/endrev/bnab017

Raghunath M, Bruckner P, Steinmann B (1994) Delayed triple helix formation of mutant collagen from patient with osteogenesis imperfecta. J Mol Biol 236(3):940–949

pubmed: 8114103 doi: 10.1006/jmbi.1994.1199

Malfait F, Symoens S, De Backer J, Hermanns-Lê T, Sakalihasan N, Lapière CM et al (2007) Three arginine to cysteine substitutions in the pro-alpha (I)-collagen chain cause Ehlers-Danlos syndrome with a propensity to arterial rupture in early adulthood. Hum Mutat 28(4):387–395

pubmed: 17211858 doi: 10.1002/humu.20455

Cabral WA, Makareeva E, Letocha AD, Scribanu N, Fertala A, Steplewski A, et al (2007) Y‐position cysteine substitution in type I collagen (α1 (I) R888C/p. R1066C) is associated with osteogenesis imperfecta/Ehlers‐Danlos syndrome phenotype. Human Mutation 28(4):396–405

Gensure RC, Mäkitie O, Barclay C, Chan C, DePalma SR, Bastepe M et al (2005) A novel COL1A1 mutation in infantile cortical hyperostosis (Caffey disease) expands the spectrum of collagen-related disorders. J Clin Investig 115(5):1250–1257

pubmed: 15864348 pmcid: 1087158 doi: 10.1172/JCI22760

Cabral WA, Mertts MV, Makareeva E, Colige A, Tekin M, Pandya A et al (2003) Type I collagen triplet duplication mutation in lethal osteogenesis imperfecta shifts register of α chains throughout the Helix and Disrupts incorporation of mutant helices into fibrils and extracellular matrix. J Biol Chem 278(12):10006–10012

pubmed: 12538651 doi: 10.1074/jbc.M212523200

Pace JM, Atkinson M, Willing MC, Wallis G, Byers PH (2001) Deletions and duplications of Gly-Xaa-Yaa triplet repeats in the triple helical domains of type I collagen chains disrupt helix formation and result in several types of osteogenesis imperfecta. Hum Mutat 18(4):319–326

pubmed: 11668615 doi: 10.1002/humu.1193

Marini JC, Forlino A, Cabral WA, Barnes AM, San Antonio JD, Milgrom S et al (2007) Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans. Hum Mutat 28(3):209–221

pubmed: 17078022 pmcid: 4144349 doi: 10.1002/humu.20429

Garibaldi N, Besio R, Dalgleish R, Villani S, Barnes AM, Marini JC et al (2022) Dissecting the phenotypic variability of osteogenesis imperfecta. Dis Models Mech 15(5):dmm049398

Sałacińska K, Pinkier I, Rutkowska L, Chlebna-Sokół D, Jakubowska-Pietkiewicz E, Michałus I et al (2021) Novel mutations within collagen alpha1 (I) and alpha2 (I) ligand-binding sites, broadening the spectrum of osteogenesis imperfecta–current insights into collagen type I lethal regions. Front Genet 12:692978

pubmed: 34306033 pmcid: 8301378 doi: 10.3389/fgene.2021.692978

Willing MC, Deschenes SP, Scott DA, Byers PH, Slayton RL, Pitts SH et al (1994) Osteogenesis imperfecta type I: molecular heterogeneity for COL1A1 null alleles of type I collagen. Am J Hum Genet 55(4):638

pubmed: 7942841 pmcid: 1918287

Pihlajaniemi T, Dickson L, Pope F, Korhonen V, Nicholls A, Prockop D et al (1984) Osteogenesis imperfecta: cloning of a pro-alpha 2 (I) collagen gene with a frameshift mutation. J Biol Chem 259(21):12941–12944

pubmed: 6092353 doi: 10.1016/S0021-9258(18)90635-6

Schwarze U, Hata R-I, McKusick VA, Shinkai H, Hoyme HE, Pyeritz RE et al (2004) Rare autosomal recessive cardiac valvular form of Ehlers-Danlos syndrome results from mutations in the COL1A2 gene that activate the nonsense-mediated RNA decay pathway. Am J Human Genet 74(5):917–930

doi: 10.1086/420794

Forlino A, Porter FD, Lee EJ, Westphal H, Marini JC (1999) Use of the Cre/lox recombination system to develop a non-lethal knock-in murine model for osteogenesis imperfecta with an α1 (I) G349C substitution: variability in phenotype in BrtlIV mice. J Biol Chem 274(53):37923–37931

pubmed: 10608859 doi: 10.1074/jbc.274.53.37923

Kozloff KM, Carden A, Bergwitz C, Forlino A, Uveges TE, Morris MD et al (2004) Brittle IV mouse model for osteogenesis imperfecta IV demonstrates postpubertal adaptations to improve whole bone strength. J Bone Mineral Res 19(4):614–622

doi: 10.1359/JBMR.040111

Uveges TE, Collin-Osdoby P, Cabral WA, Ledgard F, Goldberg L, Bergwitz C et al (2008) Cellular mechanism of decreased bone in Brtl mouse model of OI: imbalance of decreased osteoblast function and increased osteoclasts and their precursors. J Bone Miner Res 23(12):1983–1994

pubmed: 18684089 pmcid: 2686922 doi: 10.1359/jbmr.080804

Davis MS, Kovacic BL, Marini JC, Shih AJ, Kozloff KM (2012) Increased susceptibility to microdamage in Brtl/+ mouse model for osteogenesis imperfecta. Bone 50(3):784–791

pubmed: 22207275 doi: 10.1016/j.bone.2011.12.007

Daley E, Streeten EA, Sorkin JD, Kuznetsova N, Shapses SA, Carleton SM et al (2010) Variable bone fragility associated with an Amish COL1A2 variant and a knock-in mouse model. J Bone Miner Res 25(2):247–261

pubmed: 19594296 doi: 10.1359/jbmr.090720

Kohler R, Tastad CA, Creecy A, Wallace JM (2021) Morphological and mechanical characterization of bone phenotypes in the Amish G610C murine model of osteogenesis imperfecta. PLoS ONE 16(8):e0255315

pubmed: 34449800 pmcid: 8396767 doi: 10.1371/journal.pone.0255315

Chipman SD, Sweet HO, McBride DJ Jr, Davisson MT, Marks SC Jr, Shuldiner AR et al (1993) Defective pro alpha 2 (I) collagen synthesis in a recessive mutation in mice: a model of human osteogenesis imperfecta. Proc Natl Acad Sci 90(5):1701–1705

pubmed: 8446583 pmcid: 45947 doi: 10.1073/pnas.90.5.1701

Thiele F, Cohrs CM, Flor A, Lisse TS, Przemeck GK, Horsch M et al (2012) Cardiopulmonary dysfunction in the Osteogenesis imperfecta mouse model Aga2 and human patients are caused by bone-independent mechanisms. Hum Mol Genet 21(16):3535–3545

pubmed: 22589248 pmcid: 3406754 doi: 10.1093/hmg/dds183

Lisse TS, Thiele F, Fuchs H, Hans W, Przemeck GKH, Abe K et al (2008) ER stress-mediated apoptosis in a new mouse model of osteogenesis imperfecta. PLoS Genet 4(2):e7

pubmed: 18248096 pmcid: 2222924 doi: 10.1371/journal.pgen.0040007

Chen F, Guo R, Itoh S, Moreno L, Rosenthal E, Zappitelli T et al (2014) First mouse model for combined osteogenesis imperfecta and Ehlers-Danlos syndrome. J Bone Miner Res 29(6):1412–1423

pubmed: 24443344 doi: 10.1002/jbmr.2177

Schnieke A, Harbers K, Jaenisch R (1983) Embryonic lethal mutation in mice induced by retrovirus insertion into the α 1 (I) collagen gene. Nature 304(5924):315–320

pubmed: 6308457 doi: 10.1038/304315a0

Bonadio J, Saunders TL, Tsai E, Goldstein SA, Morris-Wiman J, Brinkley L et al (1990) Transgenic mouse model of the mild dominant form of osteogenesis imperfecta. Proc Natl Acad Sci 87(18):7145–7149

pubmed: 2402497 pmcid: 54700 doi: 10.1073/pnas.87.18.7145

Bonadio J, Jepsen K, Mansoura M, Jaenisch R, Kuhn J, Goldstein S (1993) A murine skeletal adaptation that significantly increases cortical bone mechanical properties. Implications for human skeletal fragility. J Clin Investig 92(4):1697–705

Pollitt R, McMahon R, Nunn J, Bamford R, Afifi A, Bishop N et al (2006) Mutation analysis of COL1A1 and COL1A2 in patients diagnosed with osteogenesis imperfecta type I‐IV. Hum Mutat 27(7):716

Lindert U, Gnoli M, Maioli M, Bedeschi M, Sangiorgi L, Rohrbach M et al (2018) Insight into the pathology of a COL1A1 signal peptide heterozygous mutation leading to severe osteogenesis imperfecta. Calcif Tissue Int 102:373–379

pubmed: 29101475 doi: 10.1007/s00223-017-0359-z

Cabral WA, Makareeva E, Colige A, Letocha AD, Ty JM, Yeowell HN et al (2005) Mutations near amino end of α1 (I) collagen cause combined osteogenesis imperfecta/Ehlers-Danlos syndrome by interference with N-propeptide processing. J Biol Chem 280(19):19259–19269

pubmed: 15728585 doi: 10.1074/jbc.M414698200

Malfait F, Symoens S, Goemans N, Gyftodimou Y, Holmberg E, López-González V et al (2013) Helical mutations in type I collagen that affect the processing of the amino-propeptide result in an Osteogenesis Imperfecta/Ehlers-Danlos Syndrome overlap syndrome. Orphanet J Rare Dis 8:1–10

doi: 10.1186/1750-1172-8-78

Lindahl K, Barnes AM, Fratzl-Zelman N, Whyte MP, Hefferan TE, Makareeva E et al (2011) COL1 C-propeptide cleavage site mutations cause high bone mass osteogenesis imperfecta. Hum Mutat 32(6):598–609

pubmed: 21344539 pmcid: 3103631 doi: 10.1002/humu.21475

Cundy T, Dray M, Delahunt J, Hald JD, Langdahl B, Li C et al (2018) Mutations that alter the carboxy-terminal-propeptide cleavage site of the chains of type I procollagen are associated with a unique osteogenesis imperfecta phenotype. J Bone Miner Res 33(7):1260–1271

pubmed: 29669177 doi: 10.1002/jbmr.3424

Symoens S, Hulmes DJ, Bourhis JM, Coucke PJ, De Paepe A, Malfait F (2014) Type I procollagen C-propeptide defects: study of genotype–phenotype correlation and predictive role of crystal structure. Hum Mutat 35(11):1330–1341

pubmed: 25146735

Barnes AM, Ashok A, Makareeva EN, Brusel M, Cabral WA, Weis M, et al (1865) COL1A1 C-propeptide mutations cause ER mislocalization of procollagen and impair C-terminal procollagen processing. Biochim Biophys Acta (BBA)-Molecular Basis Dis 1865(9):2210–2223

Martínez-Glez V, Valencia M, Caparrós-Martín JA, Aglan M, Temtamy S, Tenorio J et al (2012) Identification of a mutation causing deficient BMP1/mTLD proteolytic activity in autosomal recessive osteogenesis imperfecta. Hum Mutat 33(2):343–350

pubmed: 22052668 doi: 10.1002/humu.21647

Valencia M, Caparrós-Martin JA, Sirerol-Piquer MS, García-Verdugo JM, Martínez-Glez V, Lapunzina P et al (2014) Report of a newly indentified patient with mutations in BMP1 and underlying pathogenetic aspects. Am J Med Genet A 164(5):1143–1150

doi: 10.1002/ajmg.a.36427

Pollitt RC, Saraff V, Dalton A, Webb EA, Shaw NJ, Sobey GJ et al (2016) Phenotypic variability in patients with osteogenesis imperfecta caused by BMP1 mutations. Am J Med Genet A 170(12):3150–3156

pubmed: 27576954 doi: 10.1002/ajmg.a.37958

Semler O, Garbes L, Keupp K, Swan D, Zimmermann K, Becker J et al (2012) A mutation in the 5′-UTR of IFITM5 creates an in-frame start codon and causes autosomal-dominant osteogenesis imperfecta type V with hyperplastic callus. Am J Hum Genet 91(2):349–357

pubmed: 22863195 pmcid: 3415541 doi: 10.1016/j.ajhg.2012.06.011

Cho T-J, Lee K-E, Lee S-K, Song SJ, Kim KJ, Jeon D et al (2012) A single recurrent mutation in the 5′-UTR of IFITM5 causes osteogenesis imperfecta type V. Am J Hum Genet 91(2):343–348

pubmed: 22863190 pmcid: 3415533 doi: 10.1016/j.ajhg.2012.06.005

Moffatt P, Gaumond MH, Salois P, Sellin K, Bessette MC, Godin É et al (2008) Bril: a novel bone-specific modulator of mineralization. J Bone Miner Res 23(9):1497–1508

pubmed: 18442316 doi: 10.1359/jbmr.080412

Reich A, Bae AS, Barnes AM, Cabral WA, Hinek A, Stimec J et al (2015) Type V OI primary osteoblasts display increased mineralization despite decreased COL1A1 expression. J Clin Endocrinol Metab 100(2):E325–E332

pubmed: 25387264 doi: 10.1210/jc.2014-3082

Patoine A, Gaumond MH, Jaiswal PK, Fassier F, Rauch F, Moffatt P (2014) Topological mapping of BRIL reveals a type II orientation and effects of osteogenesis imperfecta mutations on its cellular destination. J Bone Miner Res 29(9):2004–2016

pubmed: 24715519 doi: 10.1002/jbmr.2243

Glorieux FH, Rauch F, Plotkin H, Ward L, Travers R, Roughley P et al (2000) Type V osteogenesis imperfecta: a new form of brittle bone disease. J Bone Miner Res 15(9):1650–1658

pubmed: 10976985 doi: 10.1359/jbmr.2000.15.9.1650

Rauch F, Moffatt P, Cheung M, Roughley P, Lalic L, Lund AM, et al (2013) Osteogenesis imperfecta type V: marked phenotypic variability despite the presence of the IFITM5 c.− 14C> T mutation in all patients. J Med Genet 50(1):21–24

Blouin S, Fratzl-Zelman N, Glorieux FH, Roschger P, Klaushofer K, Marini JC et al (2017) Hypermineralization and high osteocyte lacunar density in osteogenesis imperfecta type V bone indicate exuberant primary bone formation. J Bone Miner Res 32(9):1884–1892

pubmed: 28548288 doi: 10.1002/jbmr.3180

Hanagata N, Li X, Morita H, Takemura T, Li J, Minowa T (2011) Characterization of the osteoblast-specific transmembrane protein IFITM5 and analysis of IFITM5-deficient mice. J Bone Miner Metabol 29:279–290

doi: 10.1007/s00774-010-0221-0

Lietman CD, Marom R, Munivez E, Bertin TK, Jiang MM, Chen Y et al (2015) A transgenic mouse model of OI type V supports a neomorphic mechanism of the IFITM5 mutation. J Bone Miner Res 30(3):489–498

pubmed: 25251575 doi: 10.1002/jbmr.2363

Rauch F, Geng Y, Lamplugh L, Hekmatnejad B, Gaumond M-H, Penney J et al (2018) Crispr-Cas9 engineered osteogenesis imperfecta type V leads to severe skeletal deformities and perinatal lethality in mice. Bone 107:131–142

pubmed: 29174564 doi: 10.1016/j.bone.2017.11.013

Becker J, Semler O, Gilissen C, Li Y, Bolz HJ, Giunta C et al (2011) Exome sequencing identifies truncating mutations in human SERPINF1 in autosomal-recessive osteogenesis imperfecta. Am J Hum Genet 88(3):362–371

pubmed: 21353196 pmcid: 3059418 doi: 10.1016/j.ajhg.2011.01.015

Homan EP, Rauch F, Grafe I, Lietman C, Doll JA, Dawson B et al (2011) Mutations in SERPINF1 cause osteogenesis imperfecta type VI. J Bone Mineral Res 26(12):2798–2803

doi: 10.1002/jbmr.487

Glorieux FH, Ward LM, Rauch F, Lalic L, Roughley PJ, Travers R (2002) Osteogenesis imperfecta type VI: a form of brittle bone disease with a mineralization defect. J Bone Miner Res 17(1):30–38

pubmed: 11771667 doi: 10.1359/jbmr.2002.17.1.30

Fratzl-Zelman N, Schmidt I, Roschger P, Roschger A, Glorieux FH, Klaushofer K et al (2015) Unique micro-and nano-scale mineralization pattern of human osteogenesis imperfecta type VI bone. Bone 73:233–241

pubmed: 25554599 doi: 10.1016/j.bone.2014.12.023

Rauch F, Husseini A, Roughley P, Glorieux FH, Moffatt P (2012) Lack of circulating pigment epithelium-derived factor is a marker of osteogenesis imperfecta type VI. J Clin Endocrinol Metab 97(8):E1550–E1556

pubmed: 22669302 doi: 10.1210/jc.2012-1827

Dawson D, Volpert O, Gillis P, Crawford S, Xu H-J, Benedict W et al (1999) Pigment epithelium-derived factor: a potent inhibitor of angiogenesis. Science 285(5425):245–248

pubmed: 10398599 doi: 10.1126/science.285.5425.245

Meyer C, Notari L, Becerra SP (2002) Mapping the type I collagen-binding site on pigment epithelium-derived factor: Implications for its antiangiogenic activity. J Biol Chem 277(47):45400–45407

pubmed: 12237317 doi: 10.1074/jbc.M208339200

Hosomichi J, Yasui N, Koide T, Soma K, Morita I (2005) Involvement of the collagen I-binding motif in the anti-angiogenic activity of pigment epithelium-derived factor. Biochem Biophys Res Commun 335(3):756–761

pubmed: 16102727 doi: 10.1016/j.bbrc.2005.07.140

Bogan R, Riddle RC, Li Z, Kumar S, Nandal A, Faugere MC, Boskey A, Crawford SE, Clemens TL (2013) A mouse model for human osteogenesis imperfecta type VI. J Bone Miner Res 28(7):1531–1536

Kang H, Aryal Ac S, Barnes AM, Martin A, David V, Crawford SE et al (2020) Antagonism Between PEDF and TGF-β Contributes to Type VI Osteogenesis Imperfecta Bone and Vascular Pathogenesis. J Bone Miner Res 37(5):925–937

doi: 10.1002/jbmr.4540

Mackie E, Ahmed Y, Tatarczuch L, Chen K-S, Mirams M (2008) Endochondral ossification: how cartilage is converted into bone in the developing skeleton. Int J Biochem Cell Biol 40(1):46–62

pubmed: 17659995 doi: 10.1016/j.biocel.2007.06.009

Belinsky GS, Sreekumar B, Andrejecsk JW, Saltzman WM, Gong J, Herzog RI et al (2016) Pigment epithelium–derived factor restoration increases bone mass and improves bone plasticity in a model of osteogenesis imperfecta type VI via Wnt3a blockade. FASEB J 30(8):2837

pubmed: 27127101 pmcid: 4970601 doi: 10.1096/fj.201500027R

Farber CR, Reich A, Barnes AM, Becerra P, Rauch F, Cabral WA et al (2014) A novel IFITM5 mutation in severe atypical osteogenesis imperfecta type VI impairs osteoblast production of pigment epithelium-derived factor. J Bone Mineral Res 29(6):1402–1411

doi: 10.1002/jbmr.2173

Lindsay SE, Nicol LE, Gamayo AC, Raney EM (2021) An unusual presentation of osteogenesis imperfecta: a case report. JBJS Case Connector 11(4):e21

doi: 10.2106/JBJS.CC.21.00480

Grebennikova TA, Gavrilova AO, Tiulpakov AN, Tarbaeva NV, Belaya ZE, Melnichenko GA (2020) First description of a type v osteogenesis imperfecta clinical case with severe skeletal deformities caused by a mutation p. 119C> T in IFITM5 gene in Russia. Osteoporosis Bone Dis 22(2):32–37

Hoyer-Kuhn H, Semler O, Garbes L, Zimmermann K, Becker J, Wollnik B, Schoenau E, Netzer C (2014) A nonclassical IFITM5 mutation located in the coding region causes severe osteogenesis imperfecta with prenatal onset. J Bone Miner Res 29(6):1387–1391

Guillén-Navarro E, Ballesta-Martínez MJ, Valencia M, Bueno AM, Martinez-Glez V, López-González V et al (2014) Two mutations in IFITM5 causing distinct forms of osteogenesis imperfecta. Am J Med Genet A 164(5):1136–1142

doi: 10.1002/ajmg.a.36409

Rodriguez Celin M, Moosa S, Fano V (2018) Uncommon IFITM5 mutation associated with severe skeletal deformity in osteogenesis imperfecta. Ann Hum Genet 82(6):477–481

pubmed: 30039845 doi: 10.1111/ahg.12275

Liu Y, Asan, Ma D, Lv F, Xu X, Wang J, et al (2017) Gene mutation spectrum and genotype-phenotype correlation in a cohort of Chinese osteogenesis imperfecta patients revealed by targeted next generation sequencing. Osteoporosis Int 28:2985–2995

Dagdeviren D, Tamimi F, Lee B, Sutton R, Rauch F, Retrouvey JM (2019) Dental and craniofacial characteristics caused by the p. Ser40Leu mutation in IFITM5. Am J Med Genet A 179(1):65–70

Chandler N, Best S, Hayward J, Faravelli F, Mansour S, Kivuva E et al (2018) Rapid prenatal diagnosis using targeted exome sequencing: a cohort study to assess feasibility and potential impact on prenatal counseling and pregnancy management. Genet Med 20(11):1430–1437

pubmed: 29595812 doi: 10.1038/gim.2018.30

He Y, Yan J-M, Liu Y-H, Han J, Li D-Z (2017) A prenatal case of osteogenesis imperfecta diagnosed with next-generation sequencing. J Obstet Gynaecol 37(6):809–810

pubmed: 28319678 doi: 10.1080/01443615.2017.1286304

Guterman-Ram G, Hedjazi G, Stephan C, Blouin S, Zwerina J, Kozloff KM, Fratzl-Zelman N, Marini JC (2021) Atypical type VI Osteogenesis Imperfecta mouse models the intersection of IFITM5 and SERPINF1 pathways in patients. Bone Rep 14:100805

Hedjazi G, Guterman-Ram G, Blouin S, Schemenz V, Wagermaier W, Fratzl P, et al (2022) Alterations of bone material properties in growing Ifitm5/BRIL p. S42 knock-in mice, a new model for atypical type VI osteogenesis imperfecta. Bone 162:116451

Myllyharju J, Kivirikko KI (2004) Collagens, modifying enzymes and their mutations in humans, flies and worms. Trends Genet 20(1):33–43

pubmed: 14698617 doi: 10.1016/j.tig.2003.11.004

Vranka JA, Sakai LY, Bächinger HP (2004) Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes. J Biol Chem 279(22):23615–23621

pubmed: 15044469 doi: 10.1074/jbc.M312807200

Tryggvason K, Majamaa K, Risteli J, Kivirikko KI (1979) Partial purification and characterization of chick-embryo prolyl 3-hydroxylase. Biochem J 183(2):303–307

pubmed: 230821 pmcid: 1161559 doi: 10.1042/bj1830303

Marini JC, Cabral WA, Barnes AM, Chang W (2007) Components of the collagen prolyl 3-hydroxylation complex are crucial for normal bone development. Cell Cycle 6(14):1675–1681

pubmed: 17630507 doi: 10.4161/cc.6.14.4474

Morello R, Bertin TK, Chen Y, Hicks J, Tonachini L, Monticone M et al (2006) CRTAP is required for prolyl 3-hydroxylation and mutations cause recessive osteogenesis imperfecta. Cell 127(2):291–304

pubmed: 17055431 doi: 10.1016/j.cell.2006.08.039

Ward L, Rauch F, Travers R, Chabot G, Azouz E, Lalic L et al (2002) Osteogenesis imperfecta type VII: an autosomal recessive form of brittle bone disease. Bone 31(1):12–18

pubmed: 12110406 doi: 10.1016/S8756-3282(02)00790-1

Barnes AM, Chang W, Morello R, Cabral WA, Weis M, Eyre DR et al (2006) Deficiency of cartilage-associated protein in recessive lethal osteogenesis imperfecta. N Engl J Med 355(26):2757–2764

pubmed: 17192541 pmcid: 7509984 doi: 10.1056/NEJMoa063804

Baldridge D, Schwarze U, Morello R, Lennington J, Bertin TK, Pace JM et al (2008) CRTAP and LEPRE1 mutations in recessive osteogenesis imperfecta. Hum Mutat 29(12):1435–1442

pubmed: 18566967 pmcid: 2671575 doi: 10.1002/humu.20799

Marini JC, Cabral WA, Barnes AM (2010) Null mutations in LEPRE1 and CRTAP cause severe recessive osteogenesis imperfecta. Cell Tissue Res 339:59–70

pubmed: 19862557 doi: 10.1007/s00441-009-0872-0

Cabral WA, Chang W, Barnes AM, Weis M, Scott MA, Leikin S et al (2007) Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta. Nat Genet 39(3):359–365

pubmed: 17277775 pmcid: 7510175 doi: 10.1038/ng1968

Willaert A, Malfait F, Symoens S, Gevaert K, Kayserili H, Megarbane A et al (2009) Recessive osteogenesis imperfecta caused by LEPRE1 mutations: clinical documentation and identification of the splice form responsible for prolyl 3-hydroxylation. J Med Genet 46(4):233–241

pubmed: 19088120 doi: 10.1136/jmg.2008.062729

Wassenhove-McCarthy DJ, McCarthy KJ (1999) Molecular characterization of a novel basement membrane-associated proteoglycan, leprecan. J Biol Chem 274(35):25004–25017

pubmed: 10455179 doi: 10.1074/jbc.274.35.25004

Kantaputra PN, Dejkhamron P, Intachai W, Ngamphiw C, Cairns JRK, Kawasaki K et al (2021) A novel P3H1 mutation is associated with osteogenesis imperfecta type VIII and dental anomalies. Oral Surg Oral Med Oral Pathol Oral Radiol 132(6):e198–e207

pubmed: 33737016 doi: 10.1016/j.oooo.2021.01.023

Dimori M, Heard-Lipsmeyer ME, Byrum SD, Mackintosh SG, Kurten RC, Carroll JL et al (2020) Respiratory defects in the Crtap KO mouse model of osteogenesis imperfecta. Am J Physiol-Lung Cell Molec Physiol 318(4):L592–L605

doi: 10.1152/ajplung.00313.2019

Chang W, Barnes AM, Cabral WA, Bodurtha JN, Marini JC (2010) Prolyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complex. Hum Mol Genet 19(2):223–234

pubmed: 19846465 doi: 10.1093/hmg/ddp481

Cabral WA, Fratzl-Zelman N, Weis M, Perosky JE, Alimasa A, Harris R et al (2020) Substitution of murine type I collagen A1 3-hydroxylation site alters matrix structure but does not recapitulate osteogenesis imperfecta bone dysplasia. Matrix Biol 90:20–39

pubmed: 32112888 pmcid: 7476075 doi: 10.1016/j.matbio.2020.02.003

Homan EP, Lietman C, Grafe I, Lennington J, Morello R, Napierala D et al (2014) Differential effects of collagen prolyl 3-hydroxylation on skeletal tissues. PLoS Genet 10(1):e1004121

pubmed: 24465224 pmcid: 3900401 doi: 10.1371/journal.pgen.1004121

Price ER, Zydowsky LD, Jin M, Baker CH, McKeon FD, Walsh CT (1991) Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence. Proc Natl Acad Sci 88(5):1903–1907

pubmed: 2000394 pmcid: 51134 doi: 10.1073/pnas.88.5.1903

Yao Q, Li M, Yang H, Chai H, Fisher W, Chen C (2005) Roles of cyclophilins in cancers and other organ systems. World J Surg 29:276–280

pubmed: 15706440 doi: 10.1007/s00268-004-7812-7

Smith T, Ferreira LR, Hebert C, Norris K, Sauk JJ (1995) Hsp47 and cyclophilin B traverse the endoplasmic reticulum with procollagen into pre-Golgi intermediate vesicles: a role for Hsp47 and cyclophilin B in the export of procollagen from the endoplasmic reticulum. J Biol Chem 270(31):18323–18328

pubmed: 7629154 doi: 10.1074/jbc.270.31.18323

van Dijk FS, Nesbitt IM, Zwikstra EH, Nikkels PG, Piersma SR, Fratantoni SA et al (2009) PPIB mutations cause severe osteogenesis imperfecta. Am J Hum Genet 85(4):521–527

pubmed: 19781681 pmcid: 2756556 doi: 10.1016/j.ajhg.2009.09.001

Barnes AM, Carter EM, Cabral WA, Weis M, Chang W, Makareeva E et al (2010) Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding. N Engl J Med 362(6):521–528

pubmed: 20089953 pmcid: 3156560 doi: 10.1056/NEJMoa0907705

Pyott SM, Schwarze U, Christiansen HE, Pepin MG, Leistritz DF, Dineen R et al (2011) Mutations in PPIB (cyclophilin B) delay type I procollagen chain association and result in perinatal lethal to moderate osteogenesis imperfecta phenotypes. Hum Mol Genet 20(8):1595–1609

pubmed: 21282188 pmcid: 3063987 doi: 10.1093/hmg/ddr037

Cabral WA, Perdivara I, Weis M, Terajima M, Blissett AR, Chang W et al (2014) Abnormal type I collagen post-translational modification and crosslinking in a cyclophilin B KO mouse model of recessive osteogenesis imperfecta. PLoS Genet 10(6):e1004465

pubmed: 24968150 pmcid: 4072593 doi: 10.1371/journal.pgen.1004465

Christiansen HE, Schwarze U, Pyott SM, AlSwaid A, Al Balwi M, Alrasheed S et al (2010) Homozygosity for a missense mutation in SERPINH1, which encodes the collagen chaperone protein HSP47, results in severe recessive osteogenesis imperfecta. Am J Hum Genet 86(3):389–398

pubmed: 20188343 pmcid: 2833387 doi: 10.1016/j.ajhg.2010.01.034

Marshall C, Lopez J, Crookes L, Pollitt RC, Balasubramanian M (2016) A novel homozygous variant in SERPINH1 associated with a severe, lethal presentation of osteogenesis imperfecta with hydranencephaly. Gene 595(1):49–52

pubmed: 27677223 doi: 10.1016/j.gene.2016.09.035

Syx D, Ishikawa Y, Gebauer J, Boudko SP, Guillemyn B, Van Damme T et al (2021) Aberrant binding of mutant HSP47 affects posttranslational modification of type I collagen and leads to osteogenesis imperfecta. PLoS Genet 17(2):e1009339

pubmed: 33524049 pmcid: 7877763 doi: 10.1371/journal.pgen.1009339

Macdonald JR, Bächinger HP (2001) HSP47 binds cooperatively to triple helical type I collagen but has little effect on the thermal stability or rate of refolding. J Biol Chem 276(27):25399–25403

pubmed: 11333272 doi: 10.1074/jbc.M102471200

Bonfanti L, Mironov AA, Martínez-Menárguez JA, Martella O, Fusella A, Baldassarre M et al (1998) Procollagen traverses the Golgi stack without leaving the lumen of cisternae: evidence for cisternal maturation. Cell 95(7):993–1003

pubmed: 9875853 doi: 10.1016/S0092-8674(00)81723-7

Nagai N, Hosokawa M, Itohara S, Adachi E, Matsushita T, Hosokawa N et al (2000) Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis. J Cell Biol 150(6):1499–1506

pubmed: 10995453 pmcid: 2150697 doi: 10.1083/jcb.150.6.1499

Ishida Y, Kubota H, Yamamoto A, Kitamura A, Bächinger HP, Nagata K (2006) Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fibrillogenesis. Mol Biol Cell 17(5):2346–2355

pubmed: 16525016 pmcid: 1446091 doi: 10.1091/mbc.e05-11-1065

Ishikawa Y, Vranka J, Wirz J, Nagata K, Bächinger HP (2008) The rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens. J Biol Chem 283(46):31584–31590

pubmed: 18786928 doi: 10.1074/jbc.M802535200

Alanay Y, Avaygan H, Camacho N, Utine GE, Boduroglu K, Aktas D et al (2010) Mutations in the gene encoding the RER protein FKBP65 cause autosomal-recessive osteogenesis imperfecta. Am J Hum Genet 86(4):551–559

pubmed: 20362275 pmcid: 2850430 doi: 10.1016/j.ajhg.2010.02.022

Barnes AM, Cabral WA, Weis M, Makareeva E, Mertz EL, Leikin S et al (2012) Absence of FKBP10 in recessive type XI osteogenesis imperfecta leads to diminished collagen cross-linking and reduced collagen deposition in extracellular matrix. Hum Mutat 33(11):1589–1598

pubmed: 22718341 pmcid: 3470738 doi: 10.1002/humu.22139

Schwarze U, Cundy T, Pyott SM, Christiansen HE, Hegde MR, Bank RA et al (2013) Mutations in FKBP10, which result in Bruck syndrome and recessive forms of osteogenesis imperfecta, inhibit the hydroxylation of telopeptide lysines in bone collagen. Hum Mol Genet 22(1):1–17

pubmed: 22949511 doi: 10.1093/hmg/dds371

Kelley BP, Malfait F, Bonafe L, Baldridge D, Homan E, Symoens S et al (2011) Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck syndrome. J Bone Miner Res 26(3):666–672

pubmed: 20839288 doi: 10.1002/jbmr.250

Shaheen R, Al-Owain M, Sakati N, Alzayed ZS, Alkuraya FS (2010) FKBP10 and Bruck syndrome: phenotypic heterogeneity or call for reclassification? Am J Hum Gene 87(2):306–307

doi: 10.1016/j.ajhg.2010.05.020

Shaheen R, Al-Owain M, Faqeih E, Al-Hashmi N, Awaji A, Al-Zayed Z et al (2011) Mutations in FKBP10 cause both Bruck syndrome and isolated osteogenesis imperfecta in humans. Am J Med Genet A 155(6):1448–1452

doi: 10.1002/ajmg.a.34025

Otaify GA, Abdel-Hamid MS, Hassib NF, Elhossini RM, Abdel-Ghafar SF, Aglan MS (2022) Bruck syndrome in 13 new patients: Identification of five novel FKBP10 and PLOD2 variants and further expansion of the phenotypic spectrum. Am J Med Genet A 188(6):1815–1825

pubmed: 35278031 doi: 10.1002/ajmg.a.62718

Barnes AM, Duncan G, Weis M, Paton W, Cabral WA, Mertz EL et al (2013) Kuskokwim syndrome, a recessive congenital contracture disorder, extends the phenotype of FKBP10 mutations. Hum Mutat 34(9):1279–1288

pubmed: 23712425 pmcid: 3770534 doi: 10.1002/humu.22362

Duran I, Nevarez L, Sarukhanov A, Wu S, Lee K, Krejci P et al (2015) HSP47 and FKBP65 cooperate in the synthesis of type I procollagen. Hum Mol Genet 24(7):1918–1928

pubmed: 25510505 doi: 10.1093/hmg/ddu608

Efthymiou S, Herman I, Rahman F, Anwar N, Maroofian R, Yip J et al (2021) Two novel bi-allelic KDELR2 missense variants cause osteogenesis imperfecta with neurodevelopmental features. Am J Med Genet A 185(7):2241–2249

pubmed: 33964184 pmcid: 8436746 doi: 10.1002/ajmg.a.62221

Van Dijk FS, Semler O, Etich J, Köhler A, Jimenez-Estrada JA, Bravenboer N et al (2020) Interaction between KDELR2 and HSP47 as a key determinant in osteogenesis imperfecta caused by bi-allelic variants in KDELR2. Am J Hum Genet 107(5):989–999

pubmed: 33053334 pmcid: 7675035 doi: 10.1016/j.ajhg.2020.09.009

Capitani M, Sallese M (2009) The KDEL receptor: new functions for an old protein. FEBS Lett 583(23):3863–3871

pubmed: 19854180 doi: 10.1016/j.febslet.2009.10.053

Bräuer P, Parker JL, Gerondopoulos A, Zimmermann I, Seeger MA, Barr FA et al (2019) Structural basis for pH-dependent retrieval of ER proteins from the Golgi by the KDEL receptor. Science 363(6431):1103–1107

pubmed: 30846601 doi: 10.1126/science.aaw2859

Dickinson ME, Flenniken AM, Ji X, Teboul L, Wong MD, White JK et al (2016) High-throughput discovery of novel developmental phenotypes. Nature 537(7621):508–514

pubmed: 27626380 pmcid: 5295821 doi: 10.1038/nature19356

Lapunzina P, Aglan M, Temtamy S, Caparrós-Martín JA, Valencia M, Letón R et al (2010) Identification of a frameshift mutation in Osterix in a patient with recessive osteogenesis imperfecta. Am J Hum Genet 87(1):110–114

pubmed: 20579626 pmcid: 2896769 doi: 10.1016/j.ajhg.2010.05.016

Fiscaletti M, Biggin A, Bennetts B, Wong K, Briody J, Pacey V et al (2018) Novel variant in Sp7/Osx associated with recessive osteogenesis imperfecta with bone fragility and hearing impairment. Bone 110:66–75

pubmed: 29382611 doi: 10.1016/j.bone.2018.01.031

Hayat A, Hussain S, Bilal M, Kausar M, Almuzzaini B, Abbas S et al (2020) Biallelic variants in four genes underlying recessive osteogenesis imperfecta. Eur J Med Genet 63(8):103954

pubmed: 32413570 doi: 10.1016/j.ejmg.2020.103954

Harrington J, AlSubaihin A, Dupuis L, Kannu P, Mendoza-Londono R, Howard A (2021) Diagnostic utility of next-generation sequence genetic panel testing in children presenting with a clinically significant fracture history. Arch Osteoporos 16(1):88

pubmed: 34091789 doi: 10.1007/s11657-021-00943-4

Ludwig K, Ward LM, Khan N, Robinson M-E, Miranda V, Bardai G et al (2022) Dominant osteogenesis imperfecta with low bone turnover caused by a heterozygous SP7 variant. Bone 160:116400

pubmed: 35367406 doi: 10.1016/j.bone.2022.116400

Tung JY-l, Ho JL-i, Wong R, Fung S-c (2022) Dental phenotype in an adolescent with osteogenesis imperfecta type XII. BMJ Case Reports CP 15(4):e246554

Al-Mutairi DA, Jarragh AA, Alsabah BH, Wein MN, Mohammed W, Alkharafi L (2024) A homozygous SP7/OSX mutation causes osteogenesis and dentinogenesis imperfecta with craniofacial anomalies. JBMR Plus 8(5):ziae026

Lui JC, Raimann A, Hojo H, Dong L, Roschger P, Kikani B et al (2022) A neomorphic variant in SP7 alters sequence specificity and causes a high-turnover bone disorder. Nat Commun 13(1):700

pubmed: 35121733 pmcid: 8816926 doi: 10.1038/s41467-022-28318-4

Whyte MP, Campeau PM, McAlister WH, Roodman GD, Kurihara N, Nenninger A et al (2020) Juvenile Paget’s disease from heterozygous mutation of SP7 encoding Osterix (specificity protein 7, transcription factor SP7). Bone 137:115364

pubmed: 32298837 pmcid: 8054448 doi: 10.1016/j.bone.2020.115364

Ortuño MJ, Susperregui AR, Artigas N, Rosa JL, Ventura F (2013) Osterix induces Col1a1 gene expression through binding to Sp1 sites in the bone enhancer and proximal promoter regions. Bone 52(2):548–556

pubmed: 23159876 doi: 10.1016/j.bone.2012.11.007

Cao Z, Liu R, Zhang H, Liao H, Zhang Y, Hinton RJ et al (2015) Osterix controls cementoblast differentiation through downregulation of Wnt-signaling via enhancing DKK1 expression. Int J Biol Sci 11(3):335

pubmed: 25678852 pmcid: 4323373 doi: 10.7150/ijbs.10874

Tohmonda T, Miyauchi Y, Ghosh R, Yoda M, Uchikawa S, Takito J et al (2011) The IRE1α–XBP1 pathway is essential for osteoblast differentiation through promoting transcription of Osterix. EMBO Rep 12(5):451–457

pubmed: 21415858 pmcid: 3090012 doi: 10.1038/embor.2011.34

Nakashima K, Zhou X, Kunkel G, Zhang Z, Deng JM, Behringer RR et al (2002) The novel zinc finger-containing transcription factor osterix is required for osteoblast differentiation and bone formation. Cell 108(1):17–29

pubmed: 11792318 doi: 10.1016/S0092-8674(01)00622-5

Volodarsky M, Markus B, Cohen I, Staretz-Chacham O, Flusser H, Landau D et al (2013) A deletion mutation in TMEM 38 B associated with autosomal recessive Osteogenesis imperfecta. Hum Mutat 34(4):582–586

pubmed: 23316006

Shaheen R, Alazami AM, Alshammari MJ, Faqeih E, Alhashmi N, Mousa N et al (2012) Study of autosomal recessive osteogenesis imperfecta in Arabia reveals a novel locus defined by TMEM38B mutation. J Med Genet 49(10):630–635

pubmed: 23054245 doi: 10.1136/jmedgenet-2012-101142

Rubinato E, Morgan A, D’Eustacchio A, Pecile V, Gortani G, Gasparini P et al (2014) A novel deletion mutation involving TMEM38B in a patient with autosomal recessive osteogenesis imperfecta. Gene 545(2):290–292

pubmed: 24835313 doi: 10.1016/j.gene.2014.05.028

Cabral WA, Ishikawa M, Garten M, Makareeva EN, Sargent BM, Weis M et al (2016) Absence of the ER cation channel TMEM38B/TRIC-B disrupts intracellular calcium homeostasis and dysregulates collagen synthesis in recessive osteogenesis imperfecta. PLoS Genet 12(7):e1006156

pubmed: 27441836 pmcid: 4956114 doi: 10.1371/journal.pgen.1006156

Lv F, Xu X-j, Wang J-y, Liu Y, Wang J-w, Song L-j et al (2016) Two novel mutations in TMEM38B result in rare autosomal recessive osteogenesis imperfecta. J Hum Genet 61(6):539–545

Kodama Y, Meiri S, Asada T, Matsuyama M, Makino S, Iwai M et al (2023) Novel splice site variant of TMEM38B in osteogenesis imperfecta type XIV. Human Genome Variation 10(1):25

pubmed: 37696855 pmcid: 10495319 doi: 10.1038/s41439-023-00252-x

Webb EA, Balasubramanian M, Fratzl-Zelman N, Cabral WA, Titheradge H, Alsaedi A et al (2017) Phenotypic spectrum in osteogenesis imperfecta due to mutations in TMEM38B: unraveling a complex cellular defect. J Clin Endocrinol Metab 102(6):2019–2028

pubmed: 28323974 pmcid: 5470761 doi: 10.1210/jc.2016-3766

Yazawa M, Ferrante C, Feng J, Mio K, Ogura T, Zhang M et al (2007) TRIC channels are essential for Ca2+ handling in intracellular stores. Nature 448(7149):78–82

pubmed: 17611541 doi: 10.1038/nature05928

Jovanovic M, Mitra A, Besio R, Contento BM, Wong KW, Derkyi A et al (2023) Absence of TRIC-B from type XIV Osteogenesis Imperfecta osteoblasts alters cell adhesion and mitochondrial function–a multi-omics study. Matrix Biol 121:127–148

pubmed: 37348683 pmcid: 10634967 doi: 10.1016/j.matbio.2023.06.004

Yamazaki D, Komazaki S, Nakanishi H, Mishima A, Nishi M, Yazawa M, Yamazaki T, Taguchi R, Takeshima H (2009) Essential role of the TRIC-B channel in Ca2+ handling of alveolar epithelial cells and in perinatal lung maturation. Development 136(14):2355–2361

Zhao C, Ichimura A, Qian N, Iida T, Yamazaki D, Noma N et al (2016) Mice lacking the intracellular cation channel TRIC-B have compromised collagen production and impaired bone mineralization. Sci Signal 9(428):ra49-ra

Besio R, Contento BM, Garibaldi N, Filibian M, Sonntag S, Shmerling D et al (2023) CaMKII inhibition due to TRIC-B loss-of-function dysregulates SMAD signaling in osteogenesis imperfecta. Matrix Biol 120:43–59

pubmed: 37178987 pmcid: 11123566 doi: 10.1016/j.matbio.2023.05.002

Doubravska L, Krausova M, Gradl D, Vojtechova M, Tumova L, Lukas J et al (2011) Fatty acid modification of Wnt1 and Wnt3a at serine is prerequisite for lipidation at cysteine and is essential for Wnt signalling. Cell Signal 23(5):837–848

pubmed: 21244856 doi: 10.1016/j.cellsig.2011.01.007

Fahiminiya S, Majewski J, Mort J, Moffatt P, Glorieux FH, Rauch F (2013) Mutations in WNT1 are a cause of osteogenesis imperfecta. J Med Genet 50(5):345–348

pubmed: 23434763 doi: 10.1136/jmedgenet-2013-101567

Keupp K, Beleggia F, Kayserili H, Barnes AM, Steiner M, Semler O et al (2013) Mutations in WNT1 cause different forms of bone fragility. Am J Hum Genet 92(4):565–574

pubmed: 23499309 pmcid: 3617378 doi: 10.1016/j.ajhg.2013.02.010

Pyott SM, Tran TT, Leistritz DF, Pepin MG, Mendelsohn NJ, Temme RT et al (2013) WNT1 mutations in families affected by moderately severe and progressive recessive osteogenesis imperfecta. Am J Hum Genet 92(4):590–597

pubmed: 23499310 pmcid: 3617391 doi: 10.1016/j.ajhg.2013.02.009

Laine CM, Joeng KS, Campeau PM, Kiviranta R, Tarkkonen K, Grover M et al (2013) WNT1 mutations in early-onset osteoporosis and osteogenesis imperfecta. N Engl J Med 368(19):1809–1816

pubmed: 23656646 pmcid: 3709450 doi: 10.1056/NEJMoa1215458

Stephen J, Girisha KM, Dalal A, Shukla A, Shah H, Srivastava P et al (2015) Mutations in patients with osteogenesis imperfecta from consanguineous Indian families. Eur J Med Genet 58(1):21–27

pubmed: 25450603 doi: 10.1016/j.ejmg.2014.10.001

Umair M, Alhaddad B, Rafique A, Jan A, Haack TB, Graf E et al (2017) Exome sequencing reveals a novel homozygous splice site variant in the WNT1 gene underlying osteogenesis imperfecta type 3. Pediatr Res 82(5):753–758

pubmed: 28665926 doi: 10.1038/pr.2017.149

Kausar M, Siddiqi S, Yaqoob M, Mansoor S, Makitie O, Mir A et al (2018) Novel mutation G324C in WNT1 mapped in a large Pakistani family with severe recessively inherited Osteogenesis Imperfecta. J Biomed Sci 25:1–10

doi: 10.1186/s12929-018-0481-x

Lu Y, Ren X, Wang Y, Bardai G, Sturm M, Dai Y et al (2018) Novel WNT1 mutations in children with osteogenesis imperfecta: clinical and functional characterization. Bone 114:144–149

pubmed: 29935254 doi: 10.1016/j.bone.2018.06.018

Shang L, Shi W, Xu Y, Nong T, Li X, Li Z et al (2024) A novel compound heterozygous variation in the FKBP10 gene causes Bruck syndrome without congenital contractures: a case report. Heliyon 10(7)

Kantaputra PN, Sirirungruangsarn Y, Visrutaratna P, Petcharunpaisan S, Carlson BM, Intachai W et al (2019) WNT1-associated osteogenesis imperfecta with atrophic frontal lobes and arachnoid cysts. J Hum Genet 64(4):291–296

pubmed: 30692598 doi: 10.1038/s10038-019-0565-9

Nampoothiri S, Guillemyn B, Elcioglu N, Jagadeesh S, Yesodharan D, Suresh B et al (2019) Ptosis as a unique hallmark for autosomal recessive WNT1-associated osteogenesis imperfecta. Am J Med Genet A 179(6):908–914

pubmed: 30896082 doi: 10.1002/ajmg.a.61119

Mäkitie RE, Haanpää M, Valta H, Pekkinen M, Laine CM, Lehesjoki AE et al (2016) Skeletal characteristics of WNT1 osteoporosis in children and young adults. J Bone Miner Res 31(9):1734–1742

pubmed: 27005318 doi: 10.1002/jbmr.2841

Alhamdi S, Lee YC, Chowdhury S, Byers PH, Gottschalk M, Taft RJ et al (2018) Heterozygous WNT1 variant causing a variable bone phenotype. Am J Med Genet A 176(11):2419–2424

pubmed: 30246918 pmcid: 6289778 doi: 10.1002/ajmg.a.40347

McMahon AP, Bradley A (1990) The Wnt-1 (int-1) proto-oncogene is required for development of a large region of the mouse brain. Cell 62(6):1073–1085

pubmed: 2205396 doi: 10.1016/0092-8674(90)90385-R

Joeng KS, Lee Y-C, Jiang M-M, Bertin TK, Chen Y, Abraham AM et al (2014) The swaying mouse as a model of osteogenesis imperfecta caused by WNT1 mutations. Hum Mol Genet 23(15):4035–4042

pubmed: 24634143 pmcid: 4082367 doi: 10.1093/hmg/ddu117

Joeng KS, Lee Y-C, Lim J, Chen Y, Jiang M-M, Munivez E et al (2017) Osteocyte-specific WNT1 regulates osteoblast function during bone homeostasis. J Clin Investig 127(7):2678–2688

pubmed: 28628032 pmcid: 5490765 doi: 10.1172/JCI92617

Symoens S, Malfait F, D’hondt S, Callewaert B, Dheedene A, Steyaert W et al (2013) Deficiency for the ER-stress transducer OASIS causes severe recessive osteogenesis imperfecta in humans. Orphanet J Rare Dis 8:1–6

Lindahl K, Åström E, Dragomir A, Symoens S, Coucke P, Larsson S et al (2018) Homozygosity for CREB3L1 premature stop codon in first case of recessive osteogenesis imperfecta associated with OASIS-deficiency to survive infancy. Bone 114:268–277

pubmed: 29936144 doi: 10.1016/j.bone.2018.06.019

Keller RB, Tran TT, Pyott SM, Pepin MG, Savarirayan R, McGillivray G et al (2018) Monoallelic and biallelic CREB3L1 variant causes mild and severe osteogenesis imperfecta, respectively. Genet Med 20(4):411–419

pubmed: 28817112 doi: 10.1038/gim.2017.115

Cayami FK, Maugeri A, Treurniet S, Setijowati ED, Teunissen BP, Eekhoff EM et al (2019) The first family with adult osteogenesis imperfecta caused by a novel homozygous mutation in CREB3L1. Mol Genet Genomic Med 7(8):e823

pubmed: 31207160 pmcid: 6687637 doi: 10.1002/mgg3.823

Guillemyn B, Kayserili H, Demuynck L, Sips P, De Paepe A, Syx D et al (2019) A homozygous pathogenic missense variant broadens the phenotypic and mutational spectrum of CREB3L1-related osteogenesis imperfecta. Hum Mol Genet 28(11):1801–1809

pubmed: 30657919 doi: 10.1093/hmg/ddz017

Andersson K, Malmgren B, Åström E, Nordgren A, Taylan F, Dahllöf G (2020) Mutations in COL1A1/A2 and CREB3L1 are associated with oligodontia in osteogenesis imperfecta. Orphanet J Rare Dis 15:1–12

doi: 10.1186/s13023-020-01361-4

DeMasters DP, Paulus AO, Scott JN (2023) Osteogenesis imperfecta diagnosed in an active duty female due to CREB3L1 heterozygosity. Mil Med 188(7–8):e2802–e2804

pubmed: 35978537 doi: 10.1093/milmed/usac245

Murakami T, Kondo S, Ogata M, Kanemoto S, Saito A, Wanaka A et al (2006) Cleavage of the membrane-bound transcription factor OASIS in response to endoplasmic reticulum stress. J Neurochem 96(4):1090–1100

pubmed: 16417584 doi: 10.1111/j.1471-4159.2005.03596.x

Murakami T, Saito A, Hino S-i, Kondo S, Kanemoto S, Chihara K, et al (2009) Signalling mediated by the endoplasmic reticulum stress transducer OASIS is involved in bone formation. Nature Cell Biol 11(10):1205–1211

Lindert U, Cabral WA, Ausavarat S, Tongkobpetch S, Ludin K, Barnes AM et al (2016) MBTPS2 mutations cause defective regulated intramembrane proteolysis in X-linked osteogenesis imperfecta. Nat Commun 7(1):11920

pubmed: 27380894 pmcid: 4935805 doi: 10.1038/ncomms11920

Oeffner F, Fischer G, Happle R, König A, Betz RC, Bornholdt D et al (2009) IFAP syndrome is caused by deficiency in MBTPS2, an intramembrane zinc metalloprotease essential for cholesterol homeostasis and ER stress response. Am J Hum Genet 84(4):459–467

pubmed: 19361614 pmcid: 2667992 doi: 10.1016/j.ajhg.2009.03.014

Naiki M, Mizuno S, Yamada K, Yamada Y, Kimura R, Oshiro M et al (2012) MBTPS2 mutation causes BRESEK/BRESHECK syndrome. Am J Med Genet A 158(1):97–102

doi: 10.1002/ajmg.a.34373

Aten E, Brasz LC, Bornholdt D, Hooijkaas IB, Porteous ME, Sybert VP et al (2010) Keratosis follicularis spinulosa decalvans is caused by mutations in MBTPS2. Hum Mutat 31(10):1125–1133

pubmed: 20672378 doi: 10.1002/humu.21335

Lim PJ, Marfurt S, Lindert U, Opitz L, Ndarugendamwo T, Srikanthan P et al (2021) Omics profiling of S2P mutant fibroblasts as a mean to unravel the pathomechanism and molecular signatures of X-linked MBTPS2 osteogenesis imperfecta. Front Genet 12:662751

pubmed: 34093655 pmcid: 8176293 doi: 10.3389/fgene.2021.662751

Lim PJ, Marcionelli G, Srikanthan P, Ndarugendamwo T, Pinner J, Rohrbach M et al (2023) Perturbations in fatty acid metabolism and collagen production infer pathogenicity of a novel MBTPS2 variant in Osteogenesis imperfecta. Front Endocrinol 14:1195704

doi: 10.3389/fendo.2023.1195704

Kondo Y, Fu J, Wang H, Hoover C, McDaniel JM, Steet R et al (2018) Site-1 protease deficiency causes human skeletal dysplasia due to defective inter-organelle protein trafficking. JCI Insight 3(14)

Patra D, Xing X, Davies S, Bryan J, Franz C, Hunziker EB et al (2007) Site-1 protease is essential for endochondral bone formation in mice. J Cell Biol 179(4):687–700

pubmed: 18025304 pmcid: 2080931 doi: 10.1083/jcb.200708092

Mendoza-Londono R, Fahiminiya S, Majewski J, Tétreault M, Nadaf J, Kannu P et al (2015) Recessive osteogenesis imperfecta caused by missense mutations in SPARC. Am J Hum Genet 96(6):979–985

pubmed: 26027498 pmcid: 4457955 doi: 10.1016/j.ajhg.2015.04.021

Durkin A, DeVile C, Arundel P, Bull M, Walsh J, Bishop NJ et al (2022) Expanding the phenotype of SPARC-related osteogenesis imperfecta: clinical findings in two patients with pathogenic variants in SPARC and literature review. J Med Genet 59(8):810–816

pubmed: 34462290 doi: 10.1136/jmedgenet-2021-107942

Termine JD, Kleinman HK, Whitson SW, Conn KM, McGarvey ML, Martin GR (1981) Osteonectin, a bone-specific protein linking mineral to collagen. Cell 26(1):99–105

pubmed: 7034958 doi: 10.1016/0092-8674(81)90037-4

MAYER U, Aumailley M, Mann K, Timpl R, Engel J (1991) Calcium‐dependent binding of basement membrane protein BM‐40 (osteonectin, SPARC) to basement membrane collagen type IV. Euro J Biochem 198(1):141–150

Delany A, Amling M, Priemel M, Howe C, Baron R, Canalis E (2000) Osteopenia and decreased bone formation in osteonectin-deficient mice. J Clin Investig 105(7):915–923

pubmed: 10749571 pmcid: 377474 doi: 10.1172/JCI7039

Bradshaw AD, Puolakkainen P, Wight TN, Sage EH, Dasgupta J, Davidson JM (2003) SPARC-null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength. J Investig Dermatol 120(6):949–955

pubmed: 12787119 doi: 10.1046/j.1523-1747.2003.12241.x

Trombetta-eSilva J, Rosset EA, Hepfer RG, Wright GJ, Baicu C, Yao H et al (2015) Decreased mechanical strength and collagen content in SPARC-null periodontal ligament is reversed by inhibition of transglutaminase activity. J Bone Miner Res 30(10):1914–1924

pubmed: 25827352 doi: 10.1002/jbmr.2522

Doyard M, Bacrot S, Huber C, Di Rocco M, Goldenberg A, Aglan MS et al (2018) FAM46A mutations are responsible for autosomal recessive osteogenesis imperfecta. J Med Genet 55(4):278–284

pubmed: 29358272 doi: 10.1136/jmedgenet-2017-104999

Kuchta K, Muszewska A, Knizewski L, Steczkiewicz K, Wyrwicz LS, Pawlowski K et al (2016) FAM46 proteins are novel eukaryotic non-canonical poly (A) polymerases. Nucleic Acids Res 44(8):3534–3548

pubmed: 27060136 pmcid: 4857005 doi: 10.1093/nar/gkw222

Gewartowska O, Aranaz-Novaliches G, Krawczyk PS, Mroczek S, Kusio-Kobiałka M, Tarkowski B et al (2021) Cytoplasmic polyadenylation by TENT5A is required for proper bone formation. Cell Reports 35(3)

Tüysüz B, Elkanova L, Alkaya DU, Güleç Ç, Toksoy G, Güneş N et al (2022) Osteogenesis imperfecta in 140 Turkish families: molecular spectrum and comparison of long-term clinical outcome of those with COL1A1/A2 and biallelic variants. Bone 155:116293

pubmed: 34902613 doi: 10.1016/j.bone.2021.116293

Cormier-Daire V, Munnich A, Lyonnet S, Rustin P, Delezoide A-L, Maroteaux P et al (1998) Presentation of six cases of Stüve-Wiedemann syndrome. Pediatr Radiol 28:776–780

pubmed: 9799300 doi: 10.1007/s002470050464

Diener S, Bayer S, Sabrautzki S, Wieland T, Mentrup B, Przemeck GK et al (2016) Exome sequencing identifies a nonsense mutation in Fam46a associated with bone abnormalities in a new mouse model for skeletal dysplasia. Mamm Genome 27:111–121

pubmed: 26803617 doi: 10.1007/s00335-016-9619-x

Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A et al (2004) Functional proteomics mapping of a human signaling pathway. Genome Res 14(7):1324–1332

pubmed: 15231748 pmcid: 442148 doi: 10.1101/gr.2334104

Barragan I, Borrego S, Abd El-Aziz M, El-Ashry M, Abu-Safieh L, Bhattacharya S et al (2008) Genetic analysis of FAM46A in Spanish families with autosomal recessive retinitis pigmentosa: characterisation of novel VNTRs. Ann Hum Genet 72(1):26–34

pubmed: 17803723 doi: 10.1111/j.1469-1809.2007.00393.x

Etokebe GE, Jotanovic Z, Mihelic R, Mulac-Jericevic B, Nikolic T, Balen S et al (2015) Susceptibility to large-joint osteoarthritis (hip and knee) is associated with BAG6 rs3117582 SNP and the VNTR polymorphism in the second exon of the FAM46A gene on chromosome 6. J Orthop Res 33(1):56–62

pubmed: 25231575 doi: 10.1002/jor.22738

Min K, Li Y, Wu Z, Dai Z, Feng Z, Qian Z et al (2023) A genetic variant of FAM46A is associated with the development of adolescent idiopathic scoliosis in the Chinese Population. Spine 48(17):1253–1258

pubmed: 37141460 pmcid: 10412078

Moosa S, Yamamoto GL, Garbes L, Keupp K, Beleza-Meireles A, Moreno CA et al (2019) Autosomal-recessive mutations in MESD cause osteogenesis imperfecta. Am J Hum Genet 105(4):836–843

pubmed: 31564437 pmcid: 6817720 doi: 10.1016/j.ajhg.2019.08.008

Tran TT, Keller RB, Guillemyn B, Pepin M, Corteville JE, Khatib S et al (2021) Biallelic variants in MESD, which encodes a WNT-signaling-related protein, in four new families with recessively inherited osteogenesis imperfecta. Human Genet Genom Adv 2(4)

Stürznickel J, Rolvien T, Delsmann A, Butscheidt S, Barvencik F, Mundlos S et al (2020) Clinical phenotype and relevance of LRP5 and LRP6 variants in patients with early-onset osteoporosis (EOOP). J Bone Miner Res 36(2):271–282

pubmed: 33118644 doi: 10.1002/jbmr.4197

Uludağ Alkaya D, Uyguner ZO, Güneş N, Tüysüz B (2022) Long-term follow-up findings in a Turkish girl with osteogenesis imperfecta type XX caused by a homozygous MESD variant. Am J Med Genet A 188(5):1639–1646

pubmed: 35092157 doi: 10.1002/ajmg.a.62664

Hsieh J-C, Lee L, Zhang L, Wefer S, Brown K, DeRossi C et al (2003) Mesd encodes an LRP5/6 chaperone essential for specification of mouse embryonic polarity. Cell 112(3):355–367

pubmed: 12581525 doi: 10.1016/S0092-8674(03)00045-X

Ghosh DK, Udupa P, Shrikondawar AN, Bhavani GS, Shah H, Ranjan A et al (2023) Mutant MESD links cellular stress to type I collagen aggregation in osteogenesis imperfecta type XX. Matrix Biol 115:81–106

pubmed: 36526215 doi: 10.1016/j.matbio.2022.12.001

Dubail J, Brunelle P, Baujat G, Huber C, Doyard M, Michot C et al (2020) Homozygous loss-of-function mutations in CCDC134 are responsible for a severe form of osteogenesis imperfecta. J Bone Miner Res 35(8):1470–1480

pubmed: 32181939 doi: 10.1002/jbmr.4011

Holick MF, Shirvani A, Charoenngam N (2021) Fetal fractures in an infant with maternal Ehlers-Danlos syndrome, CCDC134 pathogenic mutation and a negative genetic test for osteogenesis imperfecta. Children 8(6):512

pubmed: 34204301 pmcid: 8235512 doi: 10.3390/children8060512

Ali TM, Linnenkamp BD, Yamamoto GL, Honjo RS, Cabral de Menezes Filho H, Kim CA et al (2022) The recurrent homozygous translation start site variant in CCDC134 in an individual with severe osteogenesis imperfecta of non‐Morrocan ancestry. Am J Med Genet A 188(5):1545–1549

Huang J, Shi T, Ma T, Zhang Y, Ma X, Lu Y et al (2008) CCDC134, a novel secretory protein, inhibits activation of ERK and JNK, but not p38 MAPK. Cell Mol Life Sci 65:338–349

pubmed: 18087676 doi: 10.1007/s00018-007-7448-5

Kim J-M, Yang Y-S, Park KH, Oh H, Greenblatt MB, Shim J-H (2019) The ERK MAPK pathway is essential for skeletal development and homeostasis. Int J Mol Sci 20(8):1803

pubmed: 31013682 pmcid: 6514701 doi: 10.3390/ijms20081803

Kang H, Jha S, Deng Z, Fratzl-Zelman N, Cabral WA, Ivovic A et al (2018) Somatic activating mutations in MAP2K1 cause melorheostosis. Nat Commun 9(1):1390

pubmed: 29643386 pmcid: 5895796 doi: 10.1038/s41467-018-03720-z

Yu B, Zhang T, Xia P, Gong X, Qiu X, Huang J (2018) CCDC134 serves a crucial role in embryonic development. Int J Mol Med 41(1):381–390

pubmed: 29115376

Claeys L, Storoni S, Eekhoff M, Elting M, Wisse L, Pals G et al (2021) Collagen transport and related pathways in Osteogenesis Imperfecta. Hum Genet 140(8):1121–1141

pubmed: 34169326 pmcid: 8263409 doi: 10.1007/s00439-021-02302-2

Lekszas C, Foresti O, Raote I, Liedtke D, König E-M, Nanda I et al (2020) Biallelic TANGO1 mutations cause a novel syndromal disease due to hampered cellular collagen secretion. Elife 9:e51319

pubmed: 32101163 pmcid: 7062462 doi: 10.7554/eLife.51319

Besio R, Iula G, Garibaldi N, Cipolla L, Sabbioneda S, Biggiogera M, et al (2018) 4-PBA ameliorates cellular homeostasis in fibroblasts from osteogenesis imperfecta patients by enhancing autophagy and stimulating protein secretion. Biochim Biophys Acta (BBA)-Molecular Basis Dis 1864(5):1642–1652

Besio R, Garibaldi N, Leoni L, Cipolla L, Sabbioneda S, Biggiogera M et al (2019) Cellular stress due to impairment of collagen prolyl hydroxylation complex is rescued by the chaperone 4-phenylbutyrate. Dis Models Mech 12(6):dmm038521

Gremminger VL, Jeong Y, Cunningham RP, Meers GM, Rector RS, Phillips CL (2019) Compromised exercise capacity and mitochondrial dysfunction in the osteogenesis imperfecta murine (oim) mouse model. J Bone Miner Res 34(9):1646–1659

pubmed: 30908713 doi: 10.1002/jbmr.3732

Moffatt P, Boraschi-Diaz I, Bardai G, Rauch F (2021) Muscle transcriptome in mouse models of osteogenesis imperfecta. Bone 148:115940

pubmed: 33812081 doi: 10.1016/j.bone.2021.115940

Gorrell L, Makareeva E, Omari S, Otsuru S, Leikin S (2022) ER, Mitochondria, and ISR regulation by mt-HSP70 and ATF5 upon procollagen misfolding in osteoblasts. Adv Sci 9(29):2201273

doi: 10.1002/advs.202201273

Prinz WA, Toulmay A, Balla T (2020) The functional universe of membrane contact sites. Nat Rev Mol Cell Biol 21(1):7–24

pubmed: 31732717 doi: 10.1038/s41580-019-0180-9

Abrisch RG, Gumbin SC, Wisniewski BT, Lackner LL, Voeltz GK (2020) Fission and fusion machineries converge at ER contact sites to regulate mitochondrial morphology. J Cell Biol 219(4):e201911122

pubmed: 32328629 pmcid: 7147108 doi: 10.1083/jcb.201911122

Lim J, Grafe I, Alexander S, Lee B (2017) Genetic causes and mechanisms of osteogenesis imperfecta. Bone 102:40–49

pubmed: 28232077 pmcid: 5607741 doi: 10.1016/j.bone.2017.02.004

Ha-Vinh R, Alanay Y, Bank RA, Campos-Xavier AB, Zankl A, Superti-Furga A et al (2004) Phenotypic and molecular characterization of Bruck syndrome (osteogenesis imperfecta with contractures of the large joints) caused by a recessive mutation in PLOD2. Am J Med Genet A 131(2):115–120

pubmed: 15523624 doi: 10.1002/ajmg.a.30231

Roschger P, Fratzl-Zelman N, Misof BM, Glorieux FH, Klaushofer K, Rauch F (2008) Evidence that abnormal high bone mineralization in growing children with osteogenesis imperfecta is not associated with specific collagen mutations. Calcif Tissue Int 82:263–270

pubmed: 18311573 doi: 10.1007/s00223-008-9113-x

Weber M, Roschger P, Fratzl-Zelman N, Schöberl T, Rauch F, Glorieux FH et al (2006) Pamidronate does not adversely affect bone intrinsic material properties in children with osteogenesis imperfecta. Bone 39(3):616–622

pubmed: 16644299 doi: 10.1016/j.bone.2006.02.071

Fratzl-Zelman N, Morello R, Lee B, Rauch F, Glorieux F, Misof B et al (2010) CRTAP deficiency leads to abnormally high bone matrix mineralization in a murine model and in children with osteogenesis imperfecta type VII. Bone 46(3):820–826

pubmed: 19895918 doi: 10.1016/j.bone.2009.10.037

Marini JC, Reich A, Smith SM (2014) Osteogenesis imperfecta due to mutations in non-collagenous genes: lessons in the biology of bone formation. Curr Opin Pediatr 26(4):500–507

pubmed: 25007323 pmcid: 4183132 doi: 10.1097/MOP.0000000000000117

Hoyer-Kuhn H, Semler O, Schoenau E, Roschger P, Klaushofer K, Rauch F (2013) Hyperosteoidosis and hypermineralization in the same bone: bone tissue analyses in a boy with a homozygous BMP1 mutation. Calcif Tissue Int 93:565–570

pubmed: 24091809 doi: 10.1007/s00223-013-9799-2

Palomo T, Al-Jallad H, Moffatt P, Glorieux FH, Lentle B, Roschger P et al (2014) Skeletal characteristics associated with homozygous and heterozygous WNT1 mutations. Bone 67:63–70

pubmed: 25010833 doi: 10.1016/j.bone.2014.06.041

Stürznickel J, Jähn-Rickert K, Zustin J, Hennig F, Delsmann MM, Schoner K et al (2020) Compound heterozygous frameshift mutations in MESD cause a lethal syndrome suggestive of osteogenesis imperfecta type XX. J Bone Miner Res 36(6):1077–1087

doi: 10.1002/jbmr.4277

Sarathchandra P, Pope F, Kayser M, Ali S (2000) A light and electron microscopic study of osteogenesis imperfecta bone samples, with reference to collagen chemistry and clinical phenotype. J Pathol 192(3):385–395

pubmed: 11054723 doi: 10.1002/1096-9896(2000)9999:9999<::AID-PATH704>3.0.CO;2-U

Grafe I, Yang T, Alexander S, Homan EP, Lietman C, Jiang MM et al (2014) Excessive transforming growth factor-β signaling is a common mechanism in osteogenesis imperfecta. Nat Med 20(6):670–675

pubmed: 24793237 pmcid: 4048326 doi: 10.1038/nm.3544

Zimmerman SM, Dimori M, Heard Lipsmeyer ME, Morello R (2019) The osteocyte transcriptome is extensively dysregulated in mouse models of osteogenesis imperfecta. J Bone Miner Res Plus 3(7):e10171

Folkestad L, Hald JD, Canudas-Romo V, Gram J, Hermann AP, Langdahl B et al (2016) Mortality and causes of death in patients with osteogenesis imperfecta: a register-based nationwide cohort study. J Bone Miner Res 31(12):2159–2166

pubmed: 27345018 doi: 10.1002/jbmr.2895

Widmann RF, Bitan FD, Laplaza FJ, Burke SW, DiMaio MF, Schneider R (1999) Spinal deformity, pulmonary compromise, and quality of life in osteogenesis imperfecta. Spine 24(16):1673

pubmed: 10472101 doi: 10.1097/00007632-199908150-00008

Khan SI, Yonko EA, Carter EM, Dyer D, Sandhaus RA, Raggio CL (2020) Cardiopulmonary status in adults with osteogenesis imperfecta: intrinsic lung disease may contribute more than scoliosis. Clin Orthop Relat Res 478(12):2833–2843

Gochuico BR, Hossain M, Talvacchio SK, Zuo MXG, Barton M, Do AND et al (2023) Pulmonary function and structure abnormalities in children and young adults with osteogenesis imperfecta point to intrinsic and extrinsic lung abnormalities. J Med Genet 60(11):1067–1075

pubmed: 37197785 doi: 10.1136/jmg-2022-109009

Hortop J, Tsipouras P, Hanley J, Maron B, Shapiro J (1986) Cardiovascular involvement in osteogenesis imperfecta. Circulation 73(1):54–61

pubmed: 3940669 doi: 10.1161/01.CIR.73.1.54

Bonita RE, Cohen IS, Berko BA (2010) Valvular heart disease in osteogenesis imperfecta: presentation of a case and review of the literature. Echocardiography 27(1):69–73

pubmed: 19725849 doi: 10.1111/j.1540-8175.2009.00973.x

Lamanna A, Fayers T, Clarke S, Parsonage W (2013) Valvular and aortic diseases in osteogenesis imperfecta. Heart Lung Circ 22(10):801–810

pubmed: 23791715 doi: 10.1016/j.hlc.2013.05.640

Rush ET, Li L, Goodwin JL, Kreikemeier RM, Craft M, Danford DA et al (2017) Echocardiographic phenotype in osteogenesis imperfecta varies with disease severity. Heart 103(6):443–448

pubmed: 27647171 doi: 10.1136/heartjnl-2016-310099

Verdonk SJ, Storoni S, Micha D, van den Aardweg JG, Versacci P, Celli L, et al (2024) Is Osteogenesis imperfecta associated with cardiovascular abnormalities? A systematic review of the literature. Calcified Tissue Int, pp 1–12

Folkestad L, Hald JD, Gram J, Langdahl BL, Hermann AP, Diederichsen AC et al (2016) Cardiovascular disease in patients with osteogenesis imperfecta—a nationwide, register-based cohort study. Int J Cardiol 225:250–257

pubmed: 27741483 doi: 10.1016/j.ijcard.2016.09.107

Update on the Genetics of Osteogenesis Imperfecta.

Journal

Informations de publication

Résumé

Identifiants

Types de publication

Langues

Sous-ensembles de citation

Subventions

Informations de copyright

Références

Auteurs

Milena Jovanovic (M)

Joan C Marini (JC)

Classifications MeSH