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“Variable expressivity of osteogenesis imperfecta in a Brazilian family due to p.G1079S mutation in the COL1A1 gene”, vol. 11, pp. 3246-3255, 2012.
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Alanay Y, Avaygan H, Camacho N, Utine GE, et al. (2010). Mutations in the gene encoding the RER protein FKBP65 cause autosomal-recessive osteogenesis imperfecta. Am. J. Hum. Genet. 86: 551-559.
http://dx.doi.org/10.1016/j.ajhg.2010.02.022
PMid:20362275 PMCid:2850430
Bateman JF, Moeller I, Hannagan M, Chan D, et al. (1992). Characterization of three osteogenesis imperfecta collagen α1(I) glycine to serine mutations demonstrating a position-dependent gradient of phenotypic severity. Biochem. J. 288: 131-135.
PMid:1445258 PMCid:1132089
Baum J and Brodsky B (1997). Real-time NMR investigations of triple-helix folding and collagen folding diseases. Fold. Des. 2: R53-R60.
http://dx.doi.org/10.1016/S1359-0278(97)00028-X
Beck K, Chan VC, Shenoy N, Kirkpatrick A, et al. (2000). Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine. Proc. Natl. Acad. Sci. U. S. A. 97: 4273-4278.
http://dx.doi.org/10.1073/pnas.070050097
PMid:10725403 PMCid:18226
Bhate M, Wang X, Baum J and Brodsky B (2002). Folding and conformational consequences of glycine to alanine replacements at different positions in a collagen model peptide. Biochemistry 41: 6539-6547.
http://dx.doi.org/10.1021/bi020070d
PMid:12009919
Buevich AV, Silva T, Brodsky B and Baum J (2004). Transformation of the mechanism of triple-helix peptide folding in the absence of a C-terminal nucleation domain and its implications for mutations in collagen disorders. J. Biol. Chem. 279: 46890-46895.
http://dx.doi.org/10.1074/jbc.M407061200
PMid:15299012
Cabral WA, Mertts MV, Makareeva E, Colige A, et al. (2003). Type I collagen triplet duplication mutation in lethal osteogenesis imperfecta shifts register of alpha chains throughout the helix and disrupts incorporation of mutant helices into fibrils and extracellular matrix. J. Biol. Chem. 278: 10006-10012.
http://dx.doi.org/10.1074/jbc.M212523200
PMid:12538651
Cabral WA, Chang W, Barnes AM, Weis M, et al. (2007). Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta. Nat. Genet. 39: 359-365.
http://dx.doi.org/10.1038/ng1968
PMid:17277775
Chang W, Barnes AM, Cabral WA, Bodurtha JN, et al. (2010). Prolyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complex. Hum. Mol. Genet. 19: 223-234.
http://dx.doi.org/10.1093/hmg/ddp481
PMid:19846465 PMCid:2796888
Cohen-Solal L, Zolezzi F, Pignatti PF and Mottes M (1996). Intrafamilial variable expressivity of osteogenesis imperfecta due to mosaicism for a lethal G382R substitution in the COL1A1 gene. Mol. Cell Probes 10: 219-225.
http://dx.doi.org/10.1006/mcpr.1996.0030
PMid:8799376
Dalgleish R (1998). The Human Collagen Mutation Database 1998. Nucleic Acids Res. 26: 253-255.
http://dx.doi.org/10.1093/nar/26.1.253
PMid:9399846 PMCid:147171
Deodhar AA and Woolf AD (2000). Fragile without fractures. Ann. Rheum. Dis. 59: 166-171.
http://dx.doi.org/10.1136/ard.59.3.166
PMid:10700422 PMCid:1753095
Forlino A, Cabral WA, Barnes AM and Marini JC (2011). New perspectives on osteogenesis imperfecta. Nat. Rev. Endocrinol. 7: 540-557.
http://dx.doi.org/10.1038/nrendo.2011.81
PMid:21670757 PMCid:3443407
Fraser RDB, MacRae TP and Suzuki E (1979). Chain conformation in the collagen molecule. J. Mol. Biol. 129: 463-481.
http://dx.doi.org/10.1016/0022-2836(79)90507-2
Galicka A, Wolczynski S, Gindzienski A, Surazynski A, et al. (2003). Gly511 to Ser substitution in the COL1A1 gene in osteogenesis imperfecta type III patient with increased turnover of collagen. Mol. Cell Biochem. 248: 49-56.
http://dx.doi.org/10.1023/A:1024197213525
PMid:12870654
Gauba V and Hartgerink JD (2008). Synthetic collagen heterotrimers: structural mimics of wild-type and mutant collagen type I. J. Am. Chem. Soc. 130: 7509-7515.
http://dx.doi.org/10.1021/ja801670v
PMid:18481852
Glorieux FH, Rauch F, Plotkin H, Ward L, et al. (2000). Type V osteogenesis imperfecta: a new form of brittle bone disease. J. Bone Miner. Res. 15: 1650-1658.
http://dx.doi.org/10.1359/jbmr.2000.15.9.1650
PMid:10976985
Glorieux FH, Ward LM, Rauch F, Lalic L, et al. (2002). Osteogenesis imperfecta type VI: a form of brittle bone disease with a mineralization defect. J. Bone Miner. Res. 17: 30-38.
http://dx.doi.org/10.1359/jbmr.2002.17.1.30
PMid:11771667
Hartikka H, Kuurila K, Korkko J, Kaitila I, et al. (2004). Lack of correlation between the type of COL1A1 or COL1A2 mutation and hearing loss in osteogenesis imperfecta patients. Hum. Mutat. 24: 147-154.
http://dx.doi.org/10.1002/humu.20071
PMid:15241796
Kaneko H, Kitoh H, Matsuura T, Masuda A, et al. (2011). Hyperuricemia cosegregating with osteogenesis imperfecta is associated with a mutation in GPATCH8. Hum. Genet. 130: 671-683.
http://dx.doi.org/10.1007/s00439-011-1006-9
PMid:21594610
Körkkö J, Ala-Kokko L, De PA, Nuytinck L, et al. (1998). Analysis of the COL1A1 and COL1A2 genes by PCR amplification and scanning by conformation-sensitive gel electrophoresis identifies only COL1A1 mutations in 15 patients with osteogenesis imperfecta type I: identification of common sequences of null-allele mutations. Am. J. Hum. Genet. 62: 98-110.
http://dx.doi.org/10.1086/301689
PMid:9443882 PMCid:1376813
Marini JC, Forlino A, Cabral WA, Barnes AM, 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: 209-221.
http://dx.doi.org/10.1002/humu.20429
PMid:17078022
Morello R, Bertin TK, Chen Y, Hicks J, et al. (2006). CRTAP is required for prolyl 3- hydroxylation and mutations cause recessive osteogenesis imperfecta. Cell 127: 291-304.
http://dx.doi.org/10.1016/j.cell.2006.08.039
PMid:17055431
Mottes M, Sangalli A, Valli M, Gomez LM, et al. (1992). Mild dominant osteogenesis imperfecta with intrafamilial variability: the cause is a serine for glycine α1(I) 901 substitution in a type-I collagen gene. Hum. Genet. 89: 480-484.
http://dx.doi.org/10.1007/BF00219169
PMid:1634225
Namikawa C, Suzumori K, Fukushima Y, Sasaki M, et al. (1995). Recurrence of osteogenesis imperfecta because of paternal mosaicism: Gly862→Ser substitution in a type I collagen gene (COL1A1). Hum. Genet. 95: 666-670.
http://dx.doi.org/10.1007/BF00209484
PMid:7789952
Primorac D, Rowe DW, Mottes M, Barisic I, et al. (2001). Osteogenesis imperfecta at the beginning of bone and joint decade. Croat Med. J. 42: 393-415.
PMid:11471191
Roschger P, Fratzl-Zelman N, Misof BM, Glorieux FH, et al. (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.
http://dx.doi.org/10.1007/s00223-008-9113-x
PMid:18311573
Sillence DO, Senn A and Danks DM (1979). Genetic heterogeneity in osteogenesis imperfecta. J. Med. Genet. 16: 101-116.
http://dx.doi.org/10.1136/jmg.16.2.101
PMid:458828 PMCid:1012733
Van Dijk FS, Nesbitt IM, Zwikstra EH, Nikkels PG, et al. (2009). PPIB mutations cause severe osteogenesis imperfecta. Am. J. Hum. Genet. 85: 521-527.
http://dx.doi.org/10.1016/j.ajhg.2009.09.001
PMid:19781681 PMCid:2756556
Ward LM, Rauch F, Travers R, Chabot G et al. (2002). Osteogenesis imperfecta type VII: an autosomal recessive form of brittle bone disease. Bone 31: 12-18.
http://dx.doi.org/10.1016/S8756-3282(02)00790-1
Westerhausen A, Kishi J and Prockop DJ (1990). Mutations that substitute serine for glycine alpha 1-598 and glycine α1- 631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks. J. Biol. Chem. 265: 13995-14000.
PMid:2116413
Witecka J, Augusciak-Duma AM, Kruczek A, Szydlo A, et al. (2008). Two novel COL1A1 mutations in patients with osteogenesis imperfecta (OI) affect the stability of the collagen type I triple-helix. J. Appl. Genet. 49: 283-295.
http://dx.doi.org/10.1007/BF03195625
PMid:18670065
Zhang ZL, Zhang H, Ke YH, Yue H, et al. (2012). The identification of novel mutations in COL1A1, COL1A2, and LEPRE1 genes in Chinese patients with osteogenesis imperfecta. J. Bone Miner. Metab. 30: 69-77.
http://dx.doi.org/10.1007/s00774-011-0284-6
PMid:21667357
“A novel COL1A1 gene-splicing mutation (c.1875+1G>C) in a Brazilian patient with osteogenesis imperfecta”, vol. 8, pp. 173-178, 2009.
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