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Edited by Scriver CR, Beaudet AL, Sly WS, Valle D. New York: McGraw-Hill
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Ballabio A, Shapiro LJ: STS deficiency and X-linked ichthyosis. In The Metabolic and Molecular Bases of Inherited Disease, edn 7. Edited by Scriver CR, Beaudet AL, Sly WS, Valle D. New York: McGraw-Hill; 1995:2999-3022.
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Ballabio, A.1
Shapiro, L.J.2
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2
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Metachromatic leukodystrophy and multiple sulfatase deficiency: Sulfatide lipidosis
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Edited by Scriver CR, Beaudet AL, Sly WS, Valle D. New York: McGraw-Hill
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Kolodny EH, Fluharty AL: Metachromatic leukodystrophy and multiple sulfatase deficiency: sulfatide lipidosis. In The Metabolic and Molecular Bases of Inherited Disease, edn 7. Edited by Scriver CR, Beaudet AL, Sly WS, Valle D. New York: McGraw-Hill; 1995:2693-2741.
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The Metabolic and Molecular Bases of Inherited Disease, Edn. 7
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Kolodny, E.H.1
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0000820862
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The mucopolysaccharidoses
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Edited by Scriver CR, Beaudet AL, Sly WS, Valle D. New York: McGraw-Hill
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Neufeld EF, Muenzer J: The mucopolysaccharidoses. In The Metabolic and Molecular Bases of Inherited Disease, edn 7. Edited by Scriver CR, Beaudet AL, Sly WS, Valle D. New York: McGraw-Hill; 1995:2645-2494.
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The Metabolic and Molecular Bases of Inherited Disease, Edn. 7
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Neufeld, E.F.1
Muenzer, J.2
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The mucopolysaccharidoses. Diagnosis, molecular genetics and treatment
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5
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0028924667
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A cluster of sulfatase genes on Xp22.3: Mutations in chondrodysplasia punctata (CDPX) and implications for Warfarin embryopathy
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Franco B, Meroni G, Parenti G, Levilliers J, Bernard L, Gebbia M, Cox L, Maroteaux P, Sheffield L, Rappold GA et al.: A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for Warfarin embryopathy. Cell 1995, 81:15-25. This paper describes the identification and cloning, together with [6•], of the new cluster of sulfatases in Xp22.3. Five missense mutations found in one of these sulfatases, ARSE, implicated this enzyme in the pathogenesis of CDPX. The ARSE product is inhibited by the coumarin derivative Warfarin, a teratogenic agent which interferes with bone and cartilage development. It is proposed that the teratogenic effects of Warfarin may be mediated by the inhibition of the ARSE product.
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Cell
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Franco, B.1
Meroni, G.2
Parenti, G.3
Levilliers, J.4
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Gebbia, M.6
Cox, L.7
Maroteaux, P.8
Sheffield, L.9
Rappold, G.A.10
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6
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0031172098
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Identification by shotgun sequencing, genomic organization, and functional analysis of a fourth arylsulphatase gene (ARSF) from the Xp22.3 region
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in press
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Puca A, Zollo M, Repetto M, Andolfi G, Guffanti A, Simon G, Ballabio A, Franco B: Identification by shotgun sequencing, genomic organization, and functional analysis of a fourth arylsulphatase gene (ARSF) from the Xp22.3 region. Genomics 1997, in press. This paper describes the cloning of the full-length cDNA of a new sulfatase gene, ARSF, already identified in the cluster of Xp22.3 sulfatases (see [5••]). The characterization of its genomic structure, reported in this paper, revealed conservation of the exon/intron junctions with the other Xp22.3 sulfatase genes. Moreover, enzymatic assays using ARSF cDNA transiently transfected in cos7 cells provide evidence that this new gene encodes a neutral arylsulfatase enzyme which is not inhibited by Warfarin.
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Genomics
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Puca, A.1
Zollo, M.2
Repetto, M.3
Andolfi, G.4
Guffanti, A.5
Simon, G.6
Ballabio, A.7
Franco, B.8
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7
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0029130352
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A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency
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Schmidt B, Seimer T, Ingendoh A, Von Figura K: A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell 1995, 82:271-278. This manuscript reports the identification of the molecular basis for multiple sulfatase deficiency. Chemical analysis revealed that Cys69 in the ARSA and Cys91 in the ARSB enzymes are modified either co- or post-translationally. The authors found that this modification is not achieved in fibroblasts from MSD patients, demonstrating that conversion of these cysteines to 2-amino-3-oxopropionic acid is required to produce a catalytically active sulfatase and that deficiency of this modification is the cause of MSD.
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Cell
, vol.82
, pp. 271-278
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Schmidt, B.1
Seimer, T.2
Ingendoh, A.3
Von Figura, K.4
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8
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0029898602
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The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri
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Selmer T, Hallmann A, Schmidt B, Sumper M, Von Figura K: The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri. Eur J Biochem 1996, 238:341-345. The authors report on the evolutionary conservation of a post-translational modification recently described in two human sulfatases [7••]. The authors have identified this modification in arylsulfatase from the green alga V. carteri. The evolutionary conservation of this novel protein modification between sulfatases of V. carteri and man lends further support to the assumption that this modification is required for the catalytic activity of sulfatases and may be present in all sulfatases of eukaryotic origin.
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Eur J Biochem
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Selmer, T.1
Hallmann, A.2
Schmidt, B.3
Sumper, M.4
Von Figura, K.5
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9
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0028920905
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Two site-directed mutations abrogate enzyme activity but have different effects on the conformation and cellular content of the N-acetylgalactosamine 4-sulphatase protein
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Brooks DA, Robertson DA, Bindloss C, Litjens T, Anson DS, Peters C, Morris CP, Hopwood JJ: Two site-directed mutations abrogate enzyme activity but have different effects on the conformation and cellular content of the N-acetylgalactosamine 4-sulphatase protein. Biochem J 1995, 307:457-463. In this paper, the authors describe mutagenesis experiments performed on ARSB. Two site-directed mutations were created, changing the cysteine at position 91 into either a serine residue or a tyrosine. The C91S mutation did not induce major structural changes in the ARSB polypeptide, whereas the C91T mutation resulted in the reduction of detectable enzyme. Both mutations destroy the catalytic activity, suggesting that the cysteine 91 may be a critical residue in the catalytic process.
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(1995)
Biochem J
, vol.307
, pp. 457-463
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Brooks, D.A.1
Robertson, D.A.2
Bindloss, C.3
Litjens, T.4
Anson, D.S.5
Peters, C.6
Morris, C.P.7
Hopwood, J.J.8
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10
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0031568850
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Structure of a human lysosomal sulfatase
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Bond CS, Clements PR, Ashby SJ, Collyer CA, Harrop SJ, Hopwood JJ, Guss JM: Structure of a human lysosomal sulfatase. Structure 1997, 5:277-289. The authors describe the structure of ARSB (N-acetylgalactosamine-4-sulfatase), a sulfatase deficient in Maroteaux-Lamy syndrome. The crystal structure of the purified protein has been investigated, showing that the protein has two domains, the larger of which contains the active site. The cysteine residue 91, which is post-translationally modified into 2-amino-3-oxopropanoic acid, and a metal ion are located at the base of the substrate-binding pocket. The mechanism involved in the hydrolysis of the sulfate ester bond by the enzyme is described, as well as the relationship between structure, targeting of the enzyme to the lysosomes, and glycosylation. Amino acid residues conserved among sulfatases are involved in stabilizing the metal ion and sulfate in the catalytic site. These data suggest that there are common mechanisms involved in the sulfate ester hydrolysis of sulfatases. Despite the lack of high sequence homology, the structure of ARSB resembles that of alkaline phosphatase.
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(1997)
Structure
, vol.5
, pp. 277-289
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Bond, C.S.1
Clements, P.R.2
Ashby, S.J.3
Collyer, C.A.4
Harrop, S.J.5
Hopwood, J.J.6
Guss, J.M.7
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11
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0028876076
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Cloning of the sulphamidase gene and identification of mutations in Sanfilippo A syndrome
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Scott HS, Blanch L, Guo X-H, Freeman C, Orsborn A, Baker E, Sutherland GR, Morris CP, Hopwood JJ: Cloning of the sulphamidase gene and identification of mutations in Sanfilippo A syndrome. Nat Genet 1995, 11:465-467. The authors report the isolation of cDNA encoding the enzyme sulfamidase, which is involved in the degradation pathway of heparan sulfate. The deficiency of this enzyme results in a neurological disorder (Sanfilippo A syndrome) as a result of the accumulation of heparan sulfate in the lysosomes. The finding of an 11 bp deletion present in sulfamidase cDNA from two unrelated Sanfilippo A patients clearly involves this gene in the pathogenesis of this disease. Although being a sulfamidase, this enzyme shares a high degree of amino acid sequence conservation with the sulfatases, probably revealing residues important for sulfate group recognition.
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(1995)
Nat Genet
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Scott, H.S.1
Blanch, L.2
Guo, X.-H.3
Freeman, C.4
Orsborn, A.5
Baker, E.6
Sutherland, G.R.7
Morris, C.P.8
Hopwood, J.J.9
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12
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85047693900
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cDNA cloning, nucleotide sequence and expression of the gene for arylsulfatase in the sea urchin (Hemiacentrotus pulcherrimus) embryo
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Sasaki H, Yamada K, Akasaka K, Kawasaki H, Suzuki K, Saito A, Sato M, Shimada H: cDNA cloning, nucleotide sequence and expression of the gene for arylsulfatase in the sea urchin (Hemiacentrotus pulcherrimus) embryo. Eur J Biochem 1988, 177:9-13.
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Eur J Biochem
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Kawasaki, H.4
Suzuki, K.5
Saito, A.6
Sato, M.7
Shimada, H.8
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13
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0028272939
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An inducible arylsulfatase of Volvox carteri with properties suitable reporter-gene system. Purification, characterization and molecular cloning
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Hallmann A, Sumper M: An inducible arylsulfatase of Volvox carteri with properties suitable reporter-gene system. Purification, characterization and molecular cloning. Eur J Biochem 1994, 221:143-150.
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Eur J Biochem
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Hallmann, A.1
Sumper, M.2
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0023662270
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Cloning and expression of steroid sulfatase cDNA and the frequent occurrence of deletions in STS deficiency: Implication for X-Y interchange
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Yen PH, Allen E, Marsh B, Mohandas T, Wang N, Taggart RT, Shapiro U: Cloning and expression of steroid sulfatase cDNA and the frequent occurrence of deletions in STS deficiency: implication for X-Y interchange. Cell 1987, 49:443-454.
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Cell
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Yen, P.H.1
Allen, E.2
Marsh, B.3
Mohandas, T.4
Wang, N.5
Taggart, R.T.6
Shapiro, U.7
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15
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0027437257
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The pseudoautosomal regions of the human sex chromosomes
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Rappold GA: The pseudoautosomal regions of the human sex chromosomes. Hum Genet 1993, 92:315-324.
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Hum Genet
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Rappold, G.A.1
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0030137347
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Cloning and expression of the mouse pseudoautosomal steroid sulphatase gene (Sts)
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Salido EC, Li XM, Yen PH, Martin N, Mohandas TK, Shapiro LJ: Cloning and expression of the mouse pseudoautosomal steroid sulphatase gene (Sts). Nat Genet 1996, 13:83-86. After repeated attempts to clone the murine homolog of genes located in the distal part of the short arm of the X chromosome, Salido et al. succeeded in the cloning of mouse steroid sulfatase. They used a degenerate-primer RT-PCR approach to clone first the rat and then the mouse homolog of STS. The cloning confirmed the divergence between these homologs.
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Nat Genet
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Salido, E.C.1
Li, X.M.2
Yen, P.H.3
Martin, N.4
Mohandas, T.K.5
Shapiro, L.J.6
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17
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0029987932
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Characterization of a cluster of sulfatase genes on Xp22.3 suggests gene duplications in an ancestral pseudoautosomal region
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Meroni G, Franco B, Archidiacono N, Messali S, Andolfi G, Rocchi M, Ballabio A: Characterization of a cluster of sulfatase genes on Xp22.3 suggests gene duplications in an ancestral pseudoautosomal region. Hum Mol Genet 1996, 5:423-431. This manuscript reports on the genomic characterization of a new cluster of sulfatase genes in Xp22.3 and the identification, mapping assignment, and partial sequence of their Y-homologs. These data suggest that possible duplication events, leading to the generation of this family of genes, occurred in an ancestral pseudoautosomal region.
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Hum Mol Genet
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Meroni, G.1
Franco, B.2
Archidiacono, N.3
Messali, S.4
Andolfi, G.5
Rocchi, M.6
Ballabio, A.7
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18
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0024208474
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The human X-linked steroid sulfatase gene and a Y-encoded pseudogene: Evidence for an inversion of the Y chromosome during primate evolution
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Yen PH, Marsh B, Allen E, Tsai SP, Ellison J, Connolly L, Neiswanger K, Shapiro LJ: The human X-linked steroid sulfatase gene and a Y-encoded pseudogene: evidence for an inversion of the Y chromosome during primate evolution. Cell 1988, 55:1123-1135.
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Cell
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Yen, P.H.1
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Tsai, S.P.4
Ellison, J.5
Connolly, L.6
Neiswanger, K.7
Shapiro, L.J.8
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19
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0027254236
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Sequence of the human iduronate 2-sulfatase (IDS) gene
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Wilson PJ, Meaney CA, Hopwood JJ, Morris CP: Sequence of the human iduronate 2-sulfatase (IDS) gene. Genomics 1993, 17:773-775.
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Wilson, P.J.1
Meaney, C.A.2
Hopwood, J.J.3
Morris, C.P.4
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20
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0029165961
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130kb of DNA sequence reveals two new genes and a regional duplication distal to the human iduronate-2-sulfate sulfatase locus
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Timms KM, Lu F, Shen Y, Pierson CA, Muzny DM, Gu Y, Nelson DL, Gibbs RA: 130kb of DNA sequence reveals two new genes and a regional duplication distal to the human iduronate-2-sulfate sulfatase locus. Genome Res 1995, 5:71-78. See annotation [21•].
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Genome Res
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Timms, K.M.1
Lu, F.2
Shen, Y.3
Pierson, C.A.4
Muzny, D.M.5
Gu, Y.6
Nelson, D.L.7
Gibbs, R.A.8
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21
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0029161632
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Presence of an IDS-related locus (IDS2) in Xq28 complicates the mutational analysis of Hunter syndrome
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Bondeson M-L, Malmgren H, Dahl N, Carlberg B-M, Pettersson U: Presence of an IDS-related locus (IDS2) in Xq28 complicates the mutational analysis of Hunter syndrome. Eur J Hum Genet 1995, 3:219-227. This manuscript, together with [20•], describes the identification of IDS-related sequences in Xq28.
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Eur J Hum Genet
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Bondeson, M.-L.1
Malmgren, H.2
Dahl, N.3
Carlberg, B.-M.4
Pettersson, U.5
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22
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0028866985
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X-linked ichthyosis without STS deficiency: Clinical, genetical, and molecular studies
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Robledo R, Melis P, Schillinger E, Casciano I, Balazs I, Rinaldi A, Siniscalco M, Filippi G: X-linked ichthyosis without STS deficiency: clinical, genetical, and molecular studies. Am J Med Genet 1995, 59:143-148. This report is a description of a Sardinian pedigree showing X-linked ichthyosis associated with a normal level of steroid sulfatase and a normal molecular pattern of the STS gene. Although it is X-linked, the authors found that this form of ichthyosis segregates independently of genetic markers from the Xp22.3 region, suggesting that a different locus, other than STS, may be involved in the disease.
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Am J Med Genet
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Robledo, R.1
Melis, P.2
Schillinger, E.3
Casciano, I.4
Balazs, I.5
Rinaldi, A.6
Siniscalco, M.7
Filippi, G.8
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0018916729
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Maternal and fetal sequelae of anticoagulation during pregnancy
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0029738625
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Targeted disruption of the arylsulfatase B gene results in mice resembling the phenotype of mucopolysaccharidosis VI
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Evers M, Saftig P, Schmidt P, Hafner A, McLoghlin DB, Schmahl W, Hess B, Von Figura K, Peters C: Targeted disruption of the arylsulfatase B gene results in mice resembling the phenotype of mucopolysaccharidosis VI. Proc Natl Acad Sci USA 1996, 93:8214-8219. The authors report the generation of an MPS VI mouse model by targeted disruption of ARSB. These mice develop symptoms resembling those of MPS VI in humans and may represent a model to evaluate therapeutical approaches for Maroteaux-Lamy syndrome and other lysosomal storage diseases.
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Proc Natl Acad Sci USA
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Schmahl, W.6
Hess, B.7
Von Figura, K.8
Peters, C.9
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25
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15844392149
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Enzyme replacement therapy in a feline model of Maroteaux-Lamy syndrome
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Crawley AC, Brooks DA, Muller VJ, Petersen BA, Isaac EL, Bielicki J, King BM, Boulter CD, Moore AJ, Fazzalari NL et al.: Enzyme replacement therapy in a feline model of Maroteaux-Lamy syndrome. J Clin Invest 1996, 97:1864-1873. A feline model of Maroteaux-Lamy syndrome has been used to evaluate the clinical efficacy of enzyme-replacement therapy. The tissue distribution and efficacy of three forms of recombinant human enzyme have been studied. After intravenous administration, the enzyme was rapidly cleared from circulation and distributed to liver and other tissues where the half-life was 2-4 days. The treated cats showed reduction of storage vacuoles in Kupfer cells and connective tissues. No reduction of vacuolization was seen in chondrocytes. Vertebral bone mineral volume increased in two cats in which therapy was started early, before skeletal maturity. One cat showed improved mobility in response to therapy. These data support the feasibility of enzyme replacement in the treatment of mucopolysaccharidoses.
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Treatment of late infantile metachromatic leukodystrophy by bone marrow transplantation
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Bone marrow transplantation in Hunter syndrome (mucopolysaccharidosis type II): Two-year follow-up of the first Italian patient and review of the literature
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Correction of steroid sulfatase deficiency by gene transfer into basal cells of tissue cultured epidermis from patients with recessive X-linked ichthyosis
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Arylsulfatase B activities and glycosaminoglycan levels in retrovirally transduced mucopolysaccharidosis type VI cells. Prospects for gene therapy
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