메뉴 건너뛰기




Volumn 28, Issue 5-6, 2013, Pages 313-320

Genetics of ectopia lentis

Author keywords

Ehler Danlos; Homocystinuria; Marfan; Subluxated lens; Sulfite oxidase deficiency; Weill marchesani

Indexed keywords

ARTICLE; ECTOPIA LENTIS; ECTOPIA LENTIS ET PUPILLAE; ECTOPIA LENTIS SIMPLEX; EHLERS DANLOS SYNDROME; ENZYME DEFICIENCY; GENETICS; HOMOCYSTINURIA; MARFAN SYNDROME; PRIORITY JOURNAL; SULFITE OXIDASE DEFICIENCY; WEILL MARCHESANI SYNDROME;

EID: 84886376585     PISSN: 08820538     EISSN: 17445205     Source Type: Journal    
DOI: 10.3109/08820538.2013.825276     Document Type: Article
Times cited : (56)

References (75)
  • 1
    • 0037479020 scopus 로고    scopus 로고
    • Hereditary subluxated lenses: Visual performances and long-term follow-up after surgery
    • Anteby I, Isaac M, BenEzra D. Hereditary subluxated lenses: visual performances and long-term follow-up after surgery. Ophthalmology 2003;110(7):1344-1348.
    • (2003) Ophthalmology , vol.110 , Issue.7 , pp. 1344-1348
    • Anteby, I.1    Isaac, M.2    Benezra, D.3
  • 2
    • 84907115234 scopus 로고
    • Unilateral lens dislocation and axial elongation in Marfan syndrome
    • Rasooly R, Benezra D. Unilateral lens dislocation and axial elongation in Marfan syndrome. Ophthalmic Paediatr Genet 1988;9(2):135-136.
    • (1988) Ophthalmic Paediatr Genet , vol.9 , Issue.2 , pp. 135-136
    • Rasooly, R.1    Benezra, D.2
  • 4
    • 0028900225 scopus 로고
    • The Marfan syndrome: Joint and skin manifestations are prevalent and correlated
    • Grahame R, Pyeritz RE. The Marfan syndrome: joint and skin manifestations are prevalent and correlated. Br J Rheumatol 1995;34(2):126-131.
    • (1995) Br J Rheumatol , vol.34 , Issue.2 , pp. 126-131
    • Grahame, R.1    Pyeritz, R.E.2
  • 5
    • 77956127537 scopus 로고    scopus 로고
    • The revised Ghent nosology for the Marfan syndrome
    • Loeys BL, Dietz HC, Braverman AC, et al. The revised Ghent nosology for the Marfan syndrome. J Med Genet 2010;47(7):476-485.
    • (2010) J Med Genet , vol.47 , Issue.7 , pp. 476-485
    • Loeys, B.L.1    Dietz, H.C.2    Braverman, A.C.3
  • 6
    • 0019754992 scopus 로고
    • The eye in the Marfan syndrome
    • Maumenee IH. The eye in the Marfan syndrome. Trans Am Ophthalmol Soc 1981;79:684-733.
    • (1981) Trans Am Ophthalmol Soc , vol.79 , pp. 684-733
    • Maumenee, I.H.1
  • 7
    • 0024396654 scopus 로고
    • Two-dimensional echocardiographic aortic root dimensions in normal children and adults
    • Roman MJ, Devereux RB, Kramer-Fox R, O'Loughlin J. Two-dimensional echocardiographic aortic root dimensions in normal children and adults. Am J Cardiol 1989; 64(8):507-512.
    • (1989) Am J Cardiol , vol.64 , Issue.8 , pp. 507-512
    • Roman, M.J.1    Devereux, R.B.2    Kramer-Fox, R.3    O'Loughlin, J.4
  • 8
    • 0020620407 scopus 로고
    • Mitral valve dysfunction in the Marfan syndrome: Clinical and echocardiographic study of prevalence and natural history
    • Pyeritz RE, Wappel MA. Mitral valve dysfunction in the Marfan syndrome: clinical and echocardiographic study of prevalence and natural history. Am J Med 1983; 74(5):797-807.
    • (1983) Am J Med , vol.74 , Issue.5 , pp. 797-807
    • Pyeritz, R.E.1    Wappel, M.A.2
  • 9
    • 0033546937 scopus 로고    scopus 로고
    • Importance of dural ectasia in phenotypic assessment of Marfan's syndrome
    • Fattori R, Nienaber CA, Descovich B, et al. Importance of dural ectasia in phenotypic assessment of Marfan's syndrome. Lancet 1999;354(9182):910-913.
    • (1999) Lancet , vol.354 , Issue.9182 , pp. 910-913
    • Fattori, R.1    Nienaber, C.A.2    Descovich, B.3
  • 10
    • 0025886783 scopus 로고
    • Marfan syndrome caused by a recurrent de novo missense mutation in the fibrillin gene
    • Dietz HC, Cutting GR, Pyeritz RE, et al. Marfan syndrome caused by a recurrent de novo missense mutation in the fibrillin gene. Nature 1991;352(6333):337-339.
    • (1991) Nature , vol.352 , Issue.6333 , pp. 337-339
    • Dietz, H.C.1    Cutting, G.R.2    Pyeritz, R.E.3
  • 11
    • 84865805011 scopus 로고    scopus 로고
    • Identification of a novel FBN1 gene mutation in a large Pakistani family with Marfan syndrome
    • Micheal S, Khan MI, Akhtar F, et al. Identification of a novel FBN1 gene mutation in a large Pakistani family with Marfan syndrome. Mol Vis 2012;18:1918-1926.
    • (2012) Mol Vis , vol.18 , pp. 1918-1926
    • Micheal, S.1    Khan, M.I.2    Akhtar, F.3
  • 13
    • 0037373277 scopus 로고    scopus 로고
    • Dysregulation of TGF-beta activation contributes to patho-genesis in Marfan syndrome
    • Neptune ER, Frischmeyer PA, Arking DE, et al. Dysregulation of TGF-beta activation contributes to patho-genesis in Marfan syndrome. Nat Genet 2003;33(3):407-411.
    • (2003) Nat Genet , vol.33 , Issue.3 , pp. 407-411
    • Neptune, E.R.1    Frischmeyer, P.A.2    Arking, D.E.3
  • 14
    • 33646243773 scopus 로고    scopus 로고
    • FBN1, TGFBR1, and the Marfan-craniosynostosis/mental retardation disorders revisited
    • Ades LC, Sullivan K, Biggin A, et al. FBN1, TGFBR1, and the Marfan-craniosynostosis/mental retardation disorders revisited. American Journal of Medical Genetics 2006; 140(10):1047-1058.
    • (2006) American Journal of Medical Genetics , vol.140 , Issue.10 , pp. 1047-1058
    • Ades, L.C.1    Sullivan, K.2    Biggin, A.3
  • 15
    • 0036024994 scopus 로고    scopus 로고
    • Mutations of FBN1 and genotype-phenotype correlations in Marfan syndrome and related fibrillinopathies
    • Robinson PN, Booms P, Katzke S, et al. Mutations of FBN1 and genotype-phenotype correlations in Marfan syndrome and related fibrillinopathies. Hum Mutat 2002; 20(3):153-161.
    • (2002) Hum Mutat , vol.20 , Issue.3 , pp. 153-161
    • Robinson, P.N.1    Booms, P.2    Katzke, S.3
  • 16
    • 34548232284 scopus 로고    scopus 로고
    • Effect of mutation type and location on clinical outcome in 1013 probands with Marfan syndrome or related phenotypes and FBN1 mutations: An international study
    • Faivre L, Collod-Beroud G, Loeys BL, et al. Effect of mutation type and location on clinical outcome in 1013 probands with Marfan syndrome or related phenotypes and FBN1 mutations: an international study. American Journal of Human Genetics 2007;81(3):454-466.
    • (2007) American Journal of Human Genetics , vol.81 , Issue.3 , pp. 454-466
    • Faivre, L.1    Collod-Beroud, G.2    Loeys, B.L.3
  • 17
    • 33745737894 scopus 로고    scopus 로고
    • The molecular genetics of Marfan syndrome and related disorders
    • Robinson PN, Arteaga-Solis E, Baldock C, et al. The molecular genetics of Marfan syndrome and related disorders. J Med Genet 2006;43(10):769-787.
    • (2006) J Med Genet , vol.43 , Issue.10 , pp. 769-787
    • Robinson, P.N.1    Arteaga-Solis, E.2    Baldock, C.3
  • 18
    • 28844458691 scopus 로고    scopus 로고
    • Identification of 29 novel and nine recurrent fibrillin-1 (FBN1) mutations and genotype-phenotype correlations in 76 patients with Marfan syndrome
    • Rommel K, Karck M, Haverich A, et al. Identification of 29 novel and nine recurrent fibrillin-1 (FBN1) mutations and genotype-phenotype correlations in 76 patients with Marfan syndrome. Hum Mutat 2005;26(6):529-539.
    • (2005) Hum Mutat , vol.26 , Issue.6 , pp. 529-539
    • Rommel, K.1    Karck, M.2    Haverich, A.3
  • 19
    • 0013797979 scopus 로고
    • Homocystinuria in a mentally retarded child and her normal cousin
    • Spaeth GL, Barber GW. Homocystinuria in a mentally retarded child and her normal cousin. Trans Am Acad Ophthalmol Otolaryngol 1965;69(5):912-930.
    • (1965) Trans Am Acad Ophthalmol Otolaryngol , vol.69 , Issue.5 , pp. 912-930
    • Spaeth, G.L.1    Barber, G.W.2
  • 20
    • 0001573398 scopus 로고
    • Homocystinuria, an error in the metabolism of methionine
    • Gerritsen T, Waisman HA. Homocystinuria, an error in the metabolism of methionine. Pediatrics 1964;33:413-420.
    • (1964) Pediatrics , vol.33 , pp. 413-420
    • Gerritsen, T.1    Waisman, H.A.2
  • 21
    • 0021894152 scopus 로고
    • The natural history of homocystinuria due to cystathionine beta-synthase deficiency
    • Mudd SH, Skovby F, Levy HL, et al. The natural history of homocystinuria due to cystathionine beta-synthase deficiency. American Journal of Human Genetics 1985;37(1):1-31.
    • (1985) American Journal of Human Genetics , vol.37 , Issue.1 , pp. 1-31
    • Mudd, S.H.1    Skovby, F.2    Levy, H.L.3
  • 22
    • 0014574978 scopus 로고
    • The successful treatment of homo-cystinuria with pyridoxine
    • Barber GW, Spaeth GL. The successful treatment of homo-cystinuria with pyridoxine. J Pediatr 1969;75(3):463-478.
    • (1969) J Pediatr , vol.75 , Issue.3 , pp. 463-478
    • Barber, G.W.1    Spaeth, G.L.2
  • 23
    • 74049160847 scopus 로고    scopus 로고
    • Functional consequences of homocysteinylation of the elastic fiber proteins fibrillin-1 and tropoelastin
    • Hubmacher D, Cirulis JT, Miao M, et al. Functional consequences of homocysteinylation of the elastic fiber proteins fibrillin-1 and tropoelastin. J Biol Chem 2010; 285(2):1188-1198.
    • (2010) J Biol Chem , vol.285 , Issue.2 , pp. 1188-1198
    • Hubmacher, D.1    Cirulis, J.T.2    Miao, M.3
  • 25
    • 79959694166 scopus 로고    scopus 로고
    • Classical familial homocystinuria in an adult presenting as an isolated lens subluxation
    • Martinez-Gutierrez JD, Mencia-Gutierrez E, Gracia-Garcia-Miguel T, et al. Classical familial homocystinuria in an adult presenting as an isolated lens subluxation. Int Ophthalmol 2011;31(3):227-232.
    • (2011) Int Ophthalmol , vol.31 , Issue.3 , pp. 227-232
    • Martinez-Gutierrez, J.D.1    Mencia-Gutierrez, E.2    Gracia-Garcia-Miguel, T.3
  • 26
    • 71649116022 scopus 로고    scopus 로고
    • A revisit to the natural history of homocystinuria due to cystathionine beta-synthase deficiency
    • Skovby F, Gaustadnes M, Mudd SH. A revisit to the natural history of homocystinuria due to cystathionine beta-synthase deficiency. Mol Genet Metab 2010;99(1):1-3.
    • (2010) Mol Genet Metab , vol.99 , Issue.1 , pp. 1-3
    • Skovby, F.1    Gaustadnes, M.2    Mudd, S.H.3
  • 27
    • 0021331753 scopus 로고
    • Homocystinuria: Biogenesis of cystathionine beta-synthase subunits in cultured fibroblasts and in an in vitro translation system programmed with fibroblast messenger RNA
    • Skovby F, Kraus JP, Rosenberg LE. Homocystinuria: biogenesis of cystathionine beta-synthase subunits in cultured fibroblasts and in an in vitro translation system programmed with fibroblast messenger RNA. American Journal of Human Genetics 1984;36(2):452-459.
    • (1984) American Journal of Human Genetics , vol.36 , Issue.2 , pp. 452-459
    • Skovby, F.1    Kraus, J.P.2    Rosenberg, L.E.3
  • 28
    • 0032848774 scopus 로고    scopus 로고
    • Assignment of enzymatic functions to specific regions of the PLP-dependent heme protein cystathionine beta-synthase
    • Taoka S, Widjaja L, Banerjee R. Assignment of enzymatic functions to specific regions of the PLP-dependent heme protein cystathionine beta-synthase. Biochemistry 1999; 38(40):13155-13161.
    • (1999) Biochemistry , vol.38 , Issue.40 , pp. 13155-13161
    • Taoka, S.1    Widjaja, L.2    Banerjee, R.3
  • 29
    • 0023939665 scopus 로고
    • The gene for cystathionine beta-synthase (CBS) maps to the subtelo-meric region on human chromosome 21q and to proximal mouse chromosome 17
    • Munke M, Kraus JP, Ohura T, Francke U. The gene for cystathionine beta-synthase (CBS) maps to the subtelo-meric region on human chromosome 21q and to proximal mouse chromosome 17. American Journal of Human Genetics 1988;42(4):550-559.
    • (1988) American Journal of Human Genetics , vol.42 , Issue.4 , pp. 550-559
    • Munke, M.1    Kraus, J.P.2    Ohura, T.3    Francke, U.4
  • 30
    • 77954109889 scopus 로고    scopus 로고
    • Cystathionine beta-synthase mutations: Effect of mutation topology on folding and activity
    • Kozich V, Sokolova J, Klatovska V, et al. Cystathionine beta-synthase mutations: effect of mutation topology on folding and activity. Hum Mutat 2010;31(7):809-819.
    • (2010) Hum Mutat , vol.31 , Issue.7 , pp. 809-819
    • Kozich, V.1    Sokolova, J.2    Klatovska, V.3
  • 31
    • 0035653286 scopus 로고    scopus 로고
    • Cystathionine beta-synthase deficiency in Central Europe: Discrepancy between biochemical and molecular genetic screening for homocystinuric alleles
    • Sokolova J, Janosikova B, Terwilliger JD, et al. Cystathionine beta-synthase deficiency in Central Europe: discrepancy between biochemical and molecular genetic screening for homocystinuric alleles. Hum Mutat 2001; 18(6):548-549.
    • (2001) Hum Mutat , vol.18 , Issue.6 , pp. 548-549
    • Sokolova, J.1    Janosikova, B.2    Terwilliger, J.D.3
  • 32
    • 0029156096 scopus 로고
    • High frequency (71%) of cystathionine beta-synthase mutation G307S in Irish homocystinuria patients
    • Gallagher PM, Ward P, Tan S, et al. High frequency (71%) of cystathionine beta-synthase mutation G307S in Irish homocystinuria patients. Hum Mutat 1995;6(2): 177-180.
    • (1995) Hum Mutat , vol.6 , Issue.2 , pp. 177-180
    • Gallagher, P.M.1    Ward, P.2    Tan, S.3
  • 33
    • 33646440610 scopus 로고    scopus 로고
    • The p.T191M mutation of the CBS gene is highly prevalent among homocystinuric patients from Spain, Portugal and South America
    • Urreizti R, Asteggiano C, Bermudez M, et al. The p.T191M mutation of the CBS gene is highly prevalent among homocystinuric patients from Spain, Portugal and South America. J Hum Genet 2006;51(4):305-313.
    • (2006) J Hum Genet , vol.51 , Issue.4 , pp. 305-313
    • Urreizti, R.1    Asteggiano, C.2    Bermudez, M.3
  • 34
    • 1242338015 scopus 로고    scopus 로고
    • Characterization of cystathionine beta-synthase gene mutations in homocystinuric Venezuelan patients: Identification of one novel mutation in exon 6
    • De Lucca M, Casique L. Characterization of cystathionine beta-synthase gene mutations in homocystinuric Venezuelan patients: identification of one novel mutation in exon 6. Mol Genet Metab 2004;81(3):209-215.
    • (2004) Mol Genet Metab , vol.81 , Issue.3 , pp. 209-215
    • De Lucca, M.1    Casique, L.2
  • 35
    • 0347624606 scopus 로고    scopus 로고
    • Cystathionine beta-synthase deficiency in Georgia (USA): Correlation of clinical and biochemical phenotype with genotype
    • Kruger WD, Wang L, Jhee KH, et al. Cystathionine beta-synthase deficiency in Georgia (USA): correlation of clinical and biochemical phenotype with genotype. Hum Mutat 2003;22(6):434-441.
    • (2003) Hum Mutat , vol.22 , Issue.6 , pp. 434-441
    • Kruger, W.D.1    Wang, L.2    Jhee, K.H.3
  • 36
    • 28844436017 scopus 로고    scopus 로고
    • Identification and functional analysis of cystathionine beta-synthase gene mutations in patients with homocystinuria
    • Lee SJ, Lee DH, Yoo HW, et al. Identification and functional analysis of cystathionine beta-synthase gene mutations in patients with homocystinuria. J Hum Genet 2005; 50(12):648-654.
    • (2005) J Hum Genet , vol.50 , Issue.12 , pp. 648-654
    • Lee, S.J.1    Lee, D.H.2    Yoo, H.W.3
  • 38
    • 9844226203 scopus 로고    scopus 로고
    • Functional modeling of vitamin responsiveness in yeast: A common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria
    • Kim CE, Gallagher PM, Guttormsen AB, et al. Functional modeling of vitamin responsiveness in yeast: a common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria. Hum Mol Genet 1997; 6(13):2213-2221.
    • (1997) Hum Mol Genet , vol.6 , Issue.13 , pp. 2213-2221
    • Kim, C.E.1    Gallagher, P.M.2    Guttormsen, A.B.3
  • 39
    • 10744219755 scopus 로고    scopus 로고
    • Clinical homogeneity and genetic heterogeneity in Weill-Marchesani syndrome
    • Faivre L, Dollfus H, Lyonnet S, et al. Clinical homogeneity and genetic heterogeneity in Weill-Marchesani syndrome. American Journal of Medical Genetics 2003; 123A(2):204-207.
    • (2003) American Journal of Medical Genetics , vol.123 A , Issue.2 , pp. 204-207
    • Faivre, L.1    Dollfus, H.2    Lyonnet, S.3
  • 40
    • 84886394435 scopus 로고    scopus 로고
    • Weill-marchesani syndrome
    • [Internet]. Seattle (WA): University of Washington Seattle; 1993-2013
    • TM [Internet]. Seattle (WA): University of Washington, Seattle; 1993-2013.
    • TM
    • Tsilou, E.1    MacDonald, I.M.2
  • 41
    • 80052927249 scopus 로고    scopus 로고
    • Genetic and functional linkage between ADAMTS superfamily proteins and fibrillin-1: A novel mechanism influencing microfibril assembly and function
    • Hubmacher D, Apte SS. Genetic and functional linkage between ADAMTS superfamily proteins and fibrillin-1: a novel mechanism influencing microfibril assembly and function. Cell Mol Life Sci 2011;68(19):3137-3148.
    • (2011) Cell Mol Life Sci , vol.68 , Issue.19 , pp. 3137-3148
    • Hubmacher, D.1    Apte, S.S.2
  • 42
    • 57149101542 scopus 로고    scopus 로고
    • Functional analysis of an ADAMTS10 signal peptide mutation in Weill-Marchesani syndrome demonstrates a long-range effect on secretion of the full-length enzyme
    • Kutz WE, Wang LW, Dagoneau N, et al. Functional analysis of an ADAMTS10 signal peptide mutation in Weill-Marchesani syndrome demonstrates a long-range effect on secretion of the full-length enzyme. Hum Mutat 2008;29(12):1425-1434.
    • (2008) Hum Mutat , vol.29 , Issue.12 , pp. 1425-1434
    • Kutz, W.E.1    Wang, L.W.2    Dagoneau, N.3
  • 43
    • 0033387766 scopus 로고    scopus 로고
    • Weill-Marchesani syndrome in three generations
    • Evereklioglu C, Hepsen IF, Er H. Weill-Marchesani syndrome in three generations. Eye (Lond) 1999;13(Pt 6): 773-777.
    • (1999) Eye (Lond) , vol.13 , Issue.PART 6 , pp. 773-777
    • Evereklioglu, C.1    Hepsen, I.F.2    Er, H.3
  • 44
    • 0029795618 scopus 로고    scopus 로고
    • Weill-Marchesani syndrome: Possible linkage of the autosomal dominant form to 15q21.1
    • Wirtz MK, Samples JR, Kramer PL, et al. Weill-Marchesani syndrome: possible linkage of the autosomal dominant form to 15q21.1. Am J Med Genet 1996;65(1):68-75.
    • (1996) Am J Med Genet , vol.65 , Issue.1 , pp. 68-75
    • Wirtz, M.K.1    Samples, J.R.2    Kramer, P.L.3
  • 45
    • 0000662416 scopus 로고
    • Possible genetic carriers in the spherophakia-brachymorphia syndrome
    • Kloepfer HW, Rosenthal JW. Possible genetic carriers in the spherophakia-brachymorphia syndrome. American Journal of Human Genetics 1955;7(4):398-425.
    • (1955) American Journal of Human Genetics , vol.7 , Issue.4 , pp. 398-425
    • Kloepfer, H.W.1    Rosenthal, J.W.2
  • 46
    • 0036556307 scopus 로고    scopus 로고
    • Homozygosity mapping of a Weill-Marchesani syndrome locus to chromosome 19p13.3-p13.2
    • Faivre L, Megarbane A, Alswaid A, et al. Homozygosity mapping of a Weill-Marchesani syndrome locus to chromosome 19p13.3-p13.2. Hum Genet 2002; 110(4):366-370.
    • (2002) Hum Genet , vol.110 , Issue.4 , pp. 366-370
    • Faivre, L.1    Megarbane, A.2    Alswaid, A.3
  • 47
    • 0037238770 scopus 로고    scopus 로고
    • In frame fibrillin-1 gene deletion in autosomal dominant Weill-Marchesani syndrome
    • Faivre L, Gorlin RJ, Wirtz MK, et al. In frame fibrillin-1 gene deletion in autosomal dominant Weill-Marchesani syndrome. J Med Genet 2003;40(1):34-36.
    • (2003) J Med Genet , vol.40 , Issue.1 , pp. 34-36
    • Faivre, L.1    Gorlin, R.J.2    Wirtz, M.K.3
  • 48
    • 71849096809 scopus 로고    scopus 로고
    • Homozygous mutations in ADAMTS10 and ADAMTS17 cause lenticular myopia, ectopia lentis, glaucoma, spherophakia, and short stature
    • Morales J, Al-Sharif L, Khalil DS, et al. Homozygous mutations in ADAMTS10 and ADAMTS17 cause lenticular myopia, ectopia lentis, glaucoma, spherophakia, and short stature. American Journal of Human Genetics 2009; 85(5):558-568.
    • (2009) American Journal of Human Genetics , vol.85 , Issue.5 , pp. 558-568
    • Morales, J.1    Al-Sharif, L.2    Khalil, D.S.3
  • 49
    • 79955753992 scopus 로고    scopus 로고
    • ADAMTS10 protein 780 interacts with fibrillin-1 and promotes its deposition in extracellular matrix of cultured fibroblasts
    • Kutz WE, Wang LW, Bader HL, et al. ADAMTS10 protein 780 interacts with fibrillin-1 and promotes its deposition in extracellular matrix of cultured fibroblasts. J Biol Chem 2011;286(19):17156-17167.
    • (2011) J Biol Chem , vol.286 , Issue.19 , pp. 17156-17167
    • Kutz, W.E.1    Wang, L.W.2    Bader, H.L.3
  • 50
    • 50449084307 scopus 로고    scopus 로고
    • ADAMTSL2 mutations in geleophysic dysplasia demonstrate a role for ADAMTS-like proteins in TGF-beta bioavailability regulation
    • Le Goff C, Morice-Picard F, Dagoneau N, et al. ADAMTSL2 mutations in geleophysic dysplasia demonstrate a role for ADAMTS-like proteins in TGF-beta bioavailability regulation. Nat Genet 2008;40(9):1119-1123.
    • (2008) Nat Genet , vol.40 , Issue.9 , pp. 1119-1123
    • Le Goff, C.1    Morice-Picard, F.2    Dagoneau, N.3
  • 51
    • 11344280403 scopus 로고    scopus 로고
    • The molecular basis of classic Ehlers-Danlos syndrome: A comprehensive study of biochemical and molecular findings in 48 unrelated patients
    • Malfait F, Coucke P, Symoens S, et al. The molecular basis of classic Ehlers-Danlos syndrome: a comprehensive study of biochemical and molecular findings in 48 unrelated patients. Hum Mutat 2005;25(1):28-37.
    • (2005) Hum Mutat , vol.25 , Issue.1 , pp. 28-37
    • Malfait, F.1    Coucke, P.2    Symoens, S.3
  • 52
    • 0035909658 scopus 로고    scopus 로고
    • A recessive form of the Ehlers-Danlos syndrome caused by tenascin-X deficiency
    • Schalkwijk J, Zweers MC, Steijlen PM, et al. A recessive form of the Ehlers-Danlos syndrome caused by tenascin-X deficiency. N Engl J Med 2001;345(16):1167-1175.
    • (2001) N Engl J Med , vol.345 , Issue.16 , pp. 1167-1175
    • Schalkwijk, J.1    Zweers, M.C.2    Steijlen, P.M.3
  • 53
    • 2342638980 scopus 로고    scopus 로고
    • Rare auto-somal recessive cardiac valvular form of Ehlers-Danlos syndrome results from mutations in the COL1A2 gene that activate the nonsense-mediated RNA decay pathway
    • Schwarze U, Hata R, McKusick VA, et al. Rare auto-somal recessive cardiac valvular form of Ehlers-Danlos syndrome results from mutations in the COL1A2 gene that activate the nonsense-mediated RNA decay pathway. American Journal of Human Genetics 2004;74(5): 917-930.
    • (2004) American Journal of Human Genetics , vol.74 , Issue.5 , pp. 917-930
    • Schwarze, U.1    Hata, R.2    McKusick, V.A.3
  • 54
    • 33646593224 scopus 로고    scopus 로고
    • Molecular mechanism of alpha 1(I)-osteogenesis imperfecta/Ehlers-Danlos syndrome: Unfolding of an N-anchor domain at the N-terminal end of the type i collagen triple helix
    • Makareeva E, Cabral WA, Marini JC, Leikin S. Molecular mechanism of alpha 1(I)-osteogenesis imperfecta/Ehlers-Danlos syndrome: unfolding of an N-anchor domain at the N-terminal end of the type I collagen triple helix. J Biol Chem 2006;281(10):6463-6470.
    • (2006) J Biol Chem , vol.281 , Issue.10 , pp. 6463-6470
    • Makareeva, E.1    Cabral, W.A.2    Marini, J.C.3    Leikin, S.4
  • 55
    • 4644297498 scopus 로고    scopus 로고
    • Novel types of mutation responsible for the dermatosparactic type of Ehlers-Danlos syndrome (Type VIIC) and common polymorphisms in the ADAMTS2 gene
    • Colige A, Nuytinck L, Hausser I, et al. Novel types of mutation responsible for the dermatosparactic type of Ehlers-Danlos syndrome (Type VIIC) and common polymorphisms in the ADAMTS2 gene. J Invest Dermatol 2004; 123(4):656-663.
    • (2004) J Invest Dermatol , vol.123 , Issue.4 , pp. 656-663
    • Colige, A.1    Nuytinck, L.2    Hausser, I.3
  • 56
    • 0000912036 scopus 로고
    • Hyperlysinemia
    • Woody NC. Hyperlysinemia. Am J Dis Child 1964;108: 543-553.
    • (1964) Am J Dis Child , vol.108 , pp. 543-553
    • Woody, N.C.1
  • 58
    • 0014559754 scopus 로고
    • Familial hyperlysinemia with lysine-ketoglutarate reductase insufficiency
    • Dancis J, Hutzler J, Cox RP, Woody NC. Familial hyperlysinemia with lysine-ketoglutarate reductase insufficiency. J Clin Invest 1969;48(8):1447- 1452.
    • (1969) J Clin Invest , vol.48 , Issue.8 , pp. 1447-1452
    • Dancis, J.1    Hutzler, J.2    Cox, R.P.3    Woody, N.C.4
  • 59
    • 0021906426 scopus 로고
    • Alpha-Aminoadipate pathway for the biosynthesis of lysine in lower eukaryotes
    • Bhattacharjee JK. alpha-Aminoadipate pathway for the biosynthesis of lysine in lower eukaryotes. Crit Rev Microbiol 1985;12(2):131-151.
    • (1985) Crit Rev Microbiol , vol.12 , Issue.2 , pp. 131-151
    • Bhattacharjee, J.K.1
  • 60
    • 0033941102 scopus 로고    scopus 로고
    • Identification of the alpha-aminoadipic semialdehyde synthase gene, which is defective in familial hyperlysinemia
    • Sacksteder KA, Biery BJ, Morrell JC, et al. Identification of the alpha-aminoadipic semialdehyde synthase gene, which is defective in familial hyperlysinemia. American Journal of Human Genetics 2000;66(6):1736-1743.
    • (2000) American Journal of Human Genetics , vol.66 , Issue.6 , pp. 1736-1743
    • Sacksteder, K.A.1    Biery, B.J.2    Morrell, J.C.3
  • 61
    • 0014214685 scopus 로고
    • Sulfite oxidase deficiency in man: Demonstration of the enzymatic defect
    • Mudd SH, Irreverre F, Laster L. Sulfite oxidase deficiency in man: demonstration of the enzymatic defect. Science 1967;156(3782):1599-1602.
    • (1967) Science , vol.156 , Issue.3782 , pp. 1599-1602
    • Mudd, S.H.1    Irreverre, F.2    Laster, L.3
  • 62
    • 33644625000 scopus 로고    scopus 로고
    • Isolated sulfite oxidase deficiency: A case report with a novel mutation and review of the literature
    • Tan WH, Eichler FS, Hoda S, et al. Isolated sulfite oxidase deficiency: a case report with a novel mutation and review of the literature. Pediatrics 2005;116(3):757-766.
    • (2005) Pediatrics , vol.116 , Issue.3 , pp. 757-766
    • Tan, W.H.1    Eichler, F.S.2    Hoda, S.3
  • 64
    • 1842486041 scopus 로고    scopus 로고
    • Isolated sulphite oxidase deficiency: Clinical and biochemical features in an Italian patient
    • Schiaffino MC, Fantasia AR, Minniti G, et al. Isolated sulphite oxidase deficiency: clinical and biochemical features in an Italian patient. J Inherit Metab Dis 2004; 27(1):101-102.
    • (2004) J Inherit Metab Dis , vol.27 , Issue.1 , pp. 101-102
    • Schiaffino, M.C.1    Fantasia, A.R.2    Minniti, G.3
  • 65
    • 0347985324 scopus 로고    scopus 로고
    • Isolated ectopia lentis: Potential role of matrix metallopro-teinases in fibrillin degradation
    • Sachdev NH, Coroneo MT, Wakefield D, Hennessy MP. Isolated ectopia lentis: potential role of matrix metallopro-teinases in fibrillin degradation. Arch Ophthalmol 2004; 122(1):111-114.
    • (2004) Arch Ophthalmol , vol.122 , Issue.1 , pp. 111-114
    • Sachdev, N.H.1    Coroneo, M.T.2    Wakefield, D.3    Hennessy, M.P.4
  • 66
    • 0034615550 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Evolution, structure and function
    • Brew K, Dinakarpandian D, Nagase H. Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochim Biophys Acta 2000;1477(1-2):267-283.
    • (2000) Biochim Biophys Acta , vol.1477 , Issue.1-2 , pp. 267-283
    • Brew, K.1    Dinakarpandian, D.2    Nagase, H.3
  • 67
    • 0036694940 scopus 로고    scopus 로고
    • A novel mutation in neonatal isolated sulphite oxidase deficiency
    • Lee HF, Mak BS, Chi CS, et al. A novel mutation in neonatal isolated sulphite oxidase deficiency. Neuropediatrics 2002;33(4):174-179.
    • (2002) Neuropediatrics , vol.33 , Issue.4 , pp. 174-179
    • Lee, H.F.1    Mak, B.S.2    Chi, C.S.3
  • 68
    • 0036116835 scopus 로고    scopus 로고
    • Isolated sulfite oxidase deficiency: Mutation analysis and DNA-based prenatal diagnosis
    • Johnson JL, Rajagopalan KV, Renier WO, et al. Isolated sulfite oxidase deficiency: mutation analysis and DNA-based prenatal diagnosis. Prenatal Diagnosis 2002; 22(5):433-436.
    • (2002) Prenatal Diagnosis , vol.22 , Issue.5 , pp. 433-436
    • Johnson, J.L.1    Rajagopalan, K.V.2    Renier, W.O.3
  • 69
    • 12644251085 scopus 로고    scopus 로고
    • Isolated sulfite oxidase deficiency
    • Rupar CA, Gillett J, Gordon BA, et al. Isolated sulfite oxidase deficiency. Neuropediatrics 1996;27(6):299-304.
    • (1996) Neuropediatrics , vol.27 , Issue.6 , pp. 299-304
    • Rupar, C.A.1    Gillett, J.2    Gordon, B.A.3
  • 70
    • 84907112514 scopus 로고
    • Autosomal recessive ectopia lentis in two Arab family pedigrees
    • Al-Salem M. Autosomal recessive ectopia lentis in two Arab family pedigrees. Ophthalmic Paediatr Genet 1990; 11(2):123-127.
    • (1990) Ophthalmic Paediatr Genet , vol.11 , Issue.2 , pp. 123-127
    • Al-Salem, M.1
  • 71
    • 0023785999 scopus 로고
    • Clinical manifestations of ectopia lentis et pupillae in 16 patients
    • Goldberg MF. Clinical manifestations of ectopia lentis et pupillae in 16 patients. Ophthalmology 1988;95(8): 1080-1087.
    • (1988) Ophthalmology , vol.95 , Issue.8 , pp. 1080-1087
    • Goldberg, M.F.1
  • 72
    • 0017645654 scopus 로고
    • Iris transillu-mination and variable expression in ectopia lentis et pupillae
    • Luebbers JA, Goldberg MF, Herbst R, et al. Iris transillu-mination and variable expression in ectopia lentis et pupillae. Am J Ophthalmol 1977;83(5):647-656.
    • (1977) Am J Ophthalmol , vol.83 , Issue.5 , pp. 647-656
    • Luebbers, J.A.1    Goldberg, M.F.2    Herbst, R.3
  • 73
    • 0028335388 scopus 로고
    • Mutations in the fibrillin gene responsible for dominant ectopia lentis and neonatal Marfan syndrome
    • Kainulainen K, Karttunen L, Puhakka L, et al. Mutations in the fibrillin gene responsible for dominant ectopia lentis and neonatal Marfan syndrome. Nat Genet 1994;6(1):64-69.
    • (1994) Nat Genet , vol.6 , Issue.1 , pp. 64-69
    • Kainulainen, K.1    Karttunen, L.2    Puhakka, L.3
  • 74
    • 0028345635 scopus 로고
    • A novel mutation of the fibrillin gene causing ectopia lentis
    • Lonnqvist L, Child A, Kainulainen K, et al. A novel mutation of the fibrillin gene causing ectopia lentis. Genomics 1994;19(3):573-576.
    • (1994) Genomics , vol.19 , Issue.3 , pp. 573-576
    • Lonnqvist, L.1    Child, A.2    Kainulainen, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.