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Volumn 423, Issue 5, 2012, Pages 736-751

The structure of human GALNS reveals the molecular basis for mucopolysaccharidosis IV A

Author keywords

cysteine modification; enzyme replacement therapy; lysosomal storage disease; sulfatase structure; X ray crystallography

Indexed keywords

CHONDROITIN 6 SULFATE; CYSTEINE; EFEPRISTIN; KERATAN SULFATE; N ACETYLGALACTOSAMINE 6 SULFATASE; NUCLEOPHILE;

EID: 84867583031     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.08.020     Document Type: Article
Times cited : (97)

References (66)
  • 1
    • 0038243196 scopus 로고    scopus 로고
    • POVScript+: A program for model and data visualization using persistence of vision ray-tracing
    • T.D. Fenn, D. Ringe, and G.A. Petsko POVScript+: a program for model and data visualization using persistence of vision ray-tracing J. Appl. Crystallogr. 36 2003 944 947
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 944-947
    • Fenn, T.D.1    Ringe, D.2    Petsko, G.A.3
  • 2
    • 0000869162 scopus 로고    scopus 로고
    • The mucopolysaccharidoses
    • C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle, 8th edit McGraw-Hill New York, NY
    • E.F. Neufeld, and J. Muenzer The mucopolysaccharidoses C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle, The Metabolic and Molecular Bases of Inherited Disease 8th edit 2001 McGraw-Hill New York, NY 3421 3452
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 3421-3452
    • Neufeld, E.F.1    Muenzer, J.2
  • 3
    • 0029935872 scopus 로고    scopus 로고
    • Mucopolysaccharidosis type IVA (Morquio syndrome): A clinical review
    • DOI 10.1007/BF01799267
    • H. Northover, R.A. Cowie, and J.E. Wraith Mucopolysaccharidosis type IVA (Morquio syndrome): a clinical review J. Inherited Metab. Dis. 19 1996 357 365 (Pubitemid 26185528)
    • (1996) Journal of Inherited Metabolic Disease , vol.19 , Issue.3 , pp. 357-365
    • Northover, H.1    Cowie, R.A.2    Wraith, J.E.3
  • 5
    • 83455186052 scopus 로고    scopus 로고
    • Biomarker analysis of Morquio syndrome: Identification of disease state and drug responsive markers
    • L. Martell, K. Lau, M. Mei, V. Burnett, C. Decker, and E.D. Foehr Biomarker analysis of Morquio syndrome: identification of disease state and drug responsive markers Orphanet J. Rare Dis. 6 2011 84
    • (2011) Orphanet J. Rare Dis. , vol.6 , pp. 84
    • Martell, L.1    Lau, K.2    Mei, M.3    Burnett, V.4    Decker, C.5    Foehr, E.D.6
  • 6
    • 0018765147 scopus 로고
    • Purification and properties of N-acetylgalactosamine 6-sulphate sulphatase from human placenta
    • J. Glössl, W. Truppe, and H. Kresse Purification and properties of N-acetylgalactosamine 6-sulphate sulphatase from human placenta Biochem. J. 181 1979 37 46 (Pubitemid 9236519)
    • (1979) Biochemical Journal , vol.181 , Issue.1 , pp. 37-46
    • Gloessl, J.1    Truppe, W.2    Kresse, H.3
  • 7
    • 0026052594 scopus 로고
    • Human liver N-acetylgalactosamine 6-sulphatase. Purification and characterization
    • J. Bielicki, and J.J. Hopwood Human liver N-acetylgalactosamine 6-sulphatase. Purification and characterization. Biochem. J. 279 1991 515 520
    • (1991) Biochem. J. , vol.279 , pp. 515-520
    • Bielicki, J.1    Hopwood, J.J.2
  • 8
    • 0006867618 scopus 로고
    • Different properties of residual N-acetylgalactosamine-6-sulfate sulfatase in fibroblasts from patients with mild and severe forms of Morquio disease type A
    • J. Glössl, P. Maroteaux, P. Di Natale, and H. Kresse Different properties of residual N-acetylgalactosamine-6-sulfate sulfatase in fibroblasts from patients with mild and severe forms of Morquio disease type A Pediatr. Res. 15 1981 976 978
    • (1981) Pediatr. Res. , vol.15 , pp. 976-978
    • Glössl, J.1    Maroteaux, P.2    Di Natale, P.3    Kresse, H.4
  • 9
    • 0019972227 scopus 로고
    • Impaired degradation of keratan sulphate by Morquio A fibroblasts
    • J. Glössl, and H. Kresse Impaired degradation of keratan sulphate by Morquio A fibroblasts Biochem. J. 203 1982 335 338 (Pubitemid 12076053)
    • (1982) Biochemical Journal , vol.203 , Issue.1 , pp. 335-338
    • Glossl, J.1    Kresse, H.2
  • 10
    • 77957870094 scopus 로고    scopus 로고
    • Enzyme replacement in a human model of mucopolysaccharidosis IVA in vitro and its biodistribution in the cartilage of wild type mice
    • M. Dvorak-Ewell, D. Wendt, C. Hague, T. Christianson, V. Koppaka, and D. Crippen Enzyme replacement in a human model of mucopolysaccharidosis IVA in vitro and its biodistribution in the cartilage of wild type mice PLoS One 5 2010 e12194
    • (2010) PLoS One , vol.5 , pp. 12194
    • Dvorak-Ewell, M.1    Wendt, D.2    Hague, C.3    Christianson, T.4    Koppaka, V.5    Crippen, D.6
  • 12
    • 0032539976 scopus 로고    scopus 로고
    • Crystal structure of human arylsulfatase A: The aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis
    • DOI 10.1021/bi9714924
    • G. Lukatela, N. Krauss, K. Theis, T. Selmer, V. Gieselmann, K. von Figura, and W. Saenger Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis Biochemistry 37 1998 3654 3664 (Pubitemid 28162920)
    • (1998) Biochemistry , vol.37 , Issue.11 , pp. 3654-3664
    • Lukatela, G.1    Krauss, N.2    Theis, K.3    Selmer, T.4    Gieseimann, V.5    Von Figura, K.6    Saenger, W.7
  • 14
    • 0037509873 scopus 로고    scopus 로고
    • The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases
    • DOI 10.1016/S0092-8674(03)00348-9
    • M.P. Cosma, S. Pepe, I. Annunziata, R.F. Newbold, M. Grompe, G. Parenti, and A. Ballabio The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases Cell 113 2003 445 456 (Pubitemid 36588748)
    • (2003) Cell , vol.113 , Issue.4 , pp. 445-456
    • Cosma, M.P.1    Pepe, S.2    Annunziata, I.3    Newbold, R.F.4    Grompe, M.5    Parenti, G.6    Ballabio, A.7
  • 16
    • 62949163223 scopus 로고    scopus 로고
    • Molecular basis of multiple sulfatase deficiency, mucolipidosis II/III and Niemann-Pick C1 disease - Lysosomal storage disorders caused by defects of non-lysosomal proteins
    • T. Dierks, L. Schlotawa, M.A. Frese, K. Radhakrishnan, K. von Figura, and B. Schmidt Molecular basis of multiple sulfatase deficiency, mucolipidosis II/III and Niemann-Pick C1 disease - lysosomal storage disorders caused by defects of non-lysosomal proteins Biochim. Biophys. Acta 1793 2009 710 725
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 710-725
    • Dierks, T.1    Schlotawa, L.2    Frese, M.A.3    Radhakrishnan, K.4    Von Figura, K.5    Schmidt, B.6
  • 17
    • 53849125403 scopus 로고    scopus 로고
    • Sulfotransferases, sulfatases and formylglycine-generating enzymes: A sulfation fascination
    • P. Bojarova, and S.J. Williams Sulfotransferases, sulfatases and formylglycine-generating enzymes: a sulfation fascination Curr. Opin. Chem. Biol. 12 2008 573 581
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 573-581
    • Bojarova, P.1    Williams, S.J.2
  • 18
    • 51949117979 scopus 로고    scopus 로고
    • New aldehyde tag sequences identified by screening formylglycine generating enzymes in vitro and in vivo
    • J.S. Rush, and C.R. Bertozzi New aldehyde tag sequences identified by screening formylglycine generating enzymes in vitro and in vivo J. Am. Chem. Soc. 130 2008 12240 12241
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12240-12241
    • Rush, J.S.1    Bertozzi, C.R.2
  • 19
    • 84861034877 scopus 로고    scopus 로고
    • Site-specific chemical protein conjugation using genetically encoded aldehyde tags
    • D. Rabuka, J.S. Rush, G.W. Dehart, P. Wu, and C.R. Bertozzi Site-specific chemical protein conjugation using genetically encoded aldehyde tags Nat. Protoc. 7 2012 1052 1067
    • (2012) Nat. Protoc. , vol.7 , pp. 1052-1067
    • Rabuka, D.1    Rush, J.S.2    Dehart, G.W.3    Wu, P.4    Bertozzi, C.R.5
  • 21
    • 0032104543 scopus 로고    scopus 로고
    • A novel protein modification generating an aldehyde group in sulfatases: Its role in catalysis and disease
    • K. von Figura, B. Schmidt, T. Selmer, and T. Dierks A novel protein modification generating an aldehyde group in sulfatases: its role in catalysis and disease BioEssays 20 1998 505 510 (Pubitemid 28320613)
    • (1998) BioEssays , vol.20 , Issue.6 , pp. 505-510
    • Von Figura, K.1    Schmidt, B.2    Selmer, T.3    Dierks, T.4
  • 22
    • 34447618279 scopus 로고    scopus 로고
    • Human sulfatases: A structural perspective to catalysis
    • DOI 10.1007/s00018-007-7175-y
    • D. Ghosh Human sulfatases: a structural perspective to catalysis Cell. Mol. Life Sci. 64 2007 2013 2022 (Pubitemid 47094434)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.15 , pp. 2013-2022
    • Ghosh, D.1
  • 23
    • 8844275956 scopus 로고    scopus 로고
    • Sulfatases: Structure, mechanism, biological activity, inhibition, and synthetic utility
    • S.R. Hanson, M.D. Best, and C.H. Wong Sulfatases: structure, mechanism, biological activity, inhibition, and synthetic utility Angew. Chem., Int. Ed. Engl. 43 2004 5736 5763
    • (2004) Angew. Chem., Int. Ed. Engl. , vol.43 , pp. 5736-5763
    • Hanson, S.R.1    Best, M.D.2    Wong, C.H.3
  • 24
    • 0034987576 scopus 로고    scopus 로고
    • 1.3 Å structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family
    • DOI 10.1016/S0969-2126(01)00609-8, PII S0969212601006098
    • I. Boltes, H. Czapinska, A. Kahnert, R. von Bulow, T. Dierks, and B. Schmidt 1.3 Å structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family Structure 9 2001 483 491 (Pubitemid 32575346)
    • (2001) Structure , vol.9 , Issue.6 , pp. 483-491
    • Boltes, I.1    Czapinska, H.2    Kahnert, A.3    Von Bulow, R.4    Dierks, T.5    Schmidt, B.6    Von Figura, K.7    Kertesz, M.A.8    Uson, I.9
  • 26
    • 0000497407 scopus 로고    scopus 로고
    • Metachromatic leukodystrophy
    • C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle, 8th edit McGraw-Hill New York, NY
    • K. von Figura, V. Gieselmann, and J. Jaeken Metachromatic leukodystrophy C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle, The Metabolic and Molecular Bases of Inherited Disease 8th edit 2001 McGraw-Hill New York, NY 3695 3724
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 3695-3724
    • Von Figura, K.1    Gieselmann, V.2    Jaeken, J.3
  • 27
    • 0038265006 scopus 로고    scopus 로고
    • Structure of human estrone sulfatase suggests functional roles of membrane association
    • DOI 10.1074/jbc.M211497200
    • F.G. Hernandez-Guzman, T. Higashiyama, W. Pangborn, Y. Osawa, and D. Ghosh Structure of human estrone sulfatase suggests functional roles of membrane association J. Biol. Chem. 278 2003 22989 22997 (Pubitemid 36830364)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.25 , pp. 22989-22997
    • Hernandez-Guzman, F.G.1    Higashiyama, T.2    Pangborn, W.3    Osawa, Y.4    Ghosh, D.5
  • 28
    • 73849117658 scopus 로고    scopus 로고
    • Recent developments in the methods and applications of the bond valence model
    • I.D. Brown Recent developments in the methods and applications of the bond valence model Chem. Rev. 109 2009 6858 6919
    • (2009) Chem. Rev. , vol.109 , pp. 6858-6919
    • Brown, I.D.1
  • 30
    • 0029952519 scopus 로고    scopus 로고
    • Structural basis of lectin-carbohydrate recognition
    • W.I. Weis, and K. Drickamer Structural basis of lectin-carbohydrate recognition Annu. Rev. Biochem. 65 1996 441 473 (Pubitemid 26250616)
    • (1996) Annual Review of Biochemistry , vol.65 , pp. 441-473
    • Weis, W.I.1    Drickamer, K.2
  • 31
    • 0030666313 scopus 로고    scopus 로고
    • Lectin-carbohydrate interactions: Different folds, common recognition principles
    • DOI 10.1016/S0968-0004(97)01146-8, PII S0968000497011468
    • S. Elgavish, and B. Shaanan Lectin-carbohydrate interactions: different folds, common recognition principles Trends Biochem. Sci. 22 1997 462 467 (Pubitemid 27515911)
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.12 , pp. 462-467
    • Elgavish, S.1    Shaanan, B.2
  • 33
    • 0029094174 scopus 로고
    • Expression, purification and characterization of recombinant human N-acetylgalactosamine-6-sulphatase
    • J. Bielicki, M. Fuller, X.H. Guo, C.P. Morris, J.J. Hopewood, and D.S. Anson Expression, purification and characterization of recombinant human N-acetylgalactosamine-6-sulphatase Biochem. J. 311 1995 333 339
    • (1995) Biochem. J. , vol.311 , pp. 333-339
    • Bielicki, J.1    Fuller, M.2    Guo, X.H.3    Morris, C.P.4    Hopewood, J.J.5    Anson, D.S.6
  • 35
    • 30344475839 scopus 로고    scopus 로고
    • Three-dimensional structures of sulfatases
    • DOI 10.1016/S0076-6879(05)00016-9, PII S0076687905000169, 16, Phase II Conjugation Enzymes and Transport Systems
    • D. Ghosh Three-dimensional structures of sulfatases Methods Enzymol. 400 2005 273 293 (Pubitemid 43054903)
    • (2005) Methods in Enzymology , vol.400 , pp. 273-293
    • Ghosh, D.1
  • 36
    • 6044259013 scopus 로고    scopus 로고
    • Mucopolysaccharidosis IVA (Morquio A): Identification of novel common mutations in the N-acetylgalactosamine-6-sulfate sulfatase (GALNS) gene in Italian patients
    • S. Tomatsu, M. Filocamo, K.O. Orii, W.S. Sly, M.A. Gutierrez, and T. Nishioka Mucopolysaccharidosis IVA (Morquio A): identification of novel common mutations in the N-acetylgalactosamine-6-sulfate sulfatase (GALNS) gene in Italian patients Hum. Mutat. 24 2004 187 188
    • (2004) Hum. Mutat. , vol.24 , pp. 187-188
    • Tomatsu, S.1    Filocamo, M.2    Orii, K.O.3    Sly, W.S.4    Gutierrez, M.A.5    Nishioka, T.6
  • 37
    • 77957581737 scopus 로고    scopus 로고
    • Mucopolysaccharidosis IVA mutations in Chinese patients: 16 novel mutations
    • Z. Wang, W. Zhang, Y. Wang, Y. Meng, L. Su, H. Shi, and S. Huang Mucopolysaccharidosis IVA mutations in Chinese patients: 16 novel mutations J. Hum. Genet. 55 2010 534 540
    • (2010) J. Hum. Genet. , vol.55 , pp. 534-540
    • Wang, Z.1    Zhang, W.2    Wang, Y.3    Meng, Y.4    Su, L.5    Shi, H.6    Huang, S.7
  • 38
  • 39
    • 0028928337 scopus 로고
    • Mucopolysaccharidosis IVA: Screening and identification of mutations of the N-acetylgalactosamine-6-sulfate sulfatase gene
    • T. Ogawa, S. Tomatsu, S. Fukuda, A. Yamagishi, G.M. Rezvi, and K. Sukegawa Mucopolysaccharidosis IVA: screening and identification of mutations of the N-acetylgalactosamine-6-sulfate sulfatase gene Hum. Mol. Genet. 4 1995 341 349
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 341-349
    • Ogawa, T.1    Tomatsu, S.2    Fukuda, S.3    Yamagishi, A.4    Rezvi, G.M.5    Sukegawa, K.6
  • 41
    • 6844251004 scopus 로고    scopus 로고
    • Molecular heterogeneity in mucopolysaccharidosis IVA in Australia and Northern Ireland: Nine novel mutations including T312S, a common allele that confers a mild phenotype
    • DOI 10.1002/(SICI)1098-1004(1998)11:3<202::AID-HUMU4>3.0.CO;2-J
    • N. Yamada, S. Fukuda, S. Tomatsu, V. Muller, J.J. Hopwood, and J. Nelson Molecular heterogeneity in mucopolysaccharidosis IVA in Australia and Northern Ireland: nine novel mutations including T312S, a common allele that confers a mild phenotype Hum. Mutat. 11 1998 202 208 (Pubitemid 28132876)
    • (1998) Human Mutation , vol.11 , Issue.3 , pp. 202-208
    • Yamada, N.1    Fukuda, S.2    Tomatsu, S.3    Muller, V.4    Hopwood, J.J.5    Nelson, J.6    Kato, Z.7    Yamagishi, A.8    Sukegawa, K.9    Kondo, N.10    Orii, T.11
  • 46
    • 0036885012 scopus 로고    scopus 로고
    • Molecular analysis of Turkish mucopolysaccharidosis IVA (Morquio A) patients: Identification of novel mutations in the N-acetylgalactosamine-6- sulfate sulfatase (GALNS) gene
    • M. Terzioglu, A. Tokatli, T. Coskun, and S. Emre Molecular analysis of Turkish mucopolysaccharidosis IVA (Morquio A) patients: identification of novel mutations in the N-acetylgalactosamine-6-sulfate sulfatase (GALNS) gene Hum. Mutat. 20 2002 477 478
    • (2002) Hum. Mutat. , vol.20 , pp. 477-478
    • Terzioglu, M.1    Tokatli, A.2    Coskun, T.3    Emre, S.4
  • 47
    • 0026733483 scopus 로고
    • Mucopolysaccharidosis type IVA. N-acetylgalactosamine-6-sulfate sulfatase exonic point mutations in classical Morquio and mild cases
    • S. Fukuda, S. Tomatsu, M. Masue, K. Sukegawa, H. Iwata, and T. Ogawa Mucopolysaccharidosis type IVA. N-acetylgalactosamine-6-sulfate sulfatase exonic point mutations in classical Morquio and mild cases J. Clin. Invest. 90 1992 1049 1053
    • (1992) J. Clin. Invest. , vol.90 , pp. 1049-1053
    • Fukuda, S.1    Tomatsu, S.2    Masue, M.3    Sukegawa, K.4    Iwata, H.5    Ogawa, T.6
  • 48
    • 0028914368 scopus 로고
    • Mucopolysaccharidosis type IVA: Identification of six novel mutations among non-Japanese patients
    • S. Tomatsu, S. Fukuda, A. Cooper, J.E. Wraith, G.M. Rezvi, and A. Yamagishi Mucopolysaccharidosis type IVA: identification of six novel mutations among non-Japanese patients Hum. Mol. Genet. 4 1995 741 743
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 741-743
    • Tomatsu, S.1    Fukuda, S.2    Cooper, A.3    Wraith, J.E.4    Rezvi, G.M.5    Yamagishi, A.6
  • 51
    • 0029131527 scopus 로고
    • Two new mutations, Q473X and N487S, in a Caucasian patient with mucopolysaccharidosis IVA (Morquio disease)
    • S. Tomatsu, S. Fukuda, A. Cooper, J.E. Wraith, N. Yamada, and K. Isogai Two new mutations, Q473X and N487S, in a Caucasian patient with mucopolysaccharidosis IVA (Morquio disease) Hum. Mutat. 6 1995 195 196
    • (1995) Hum. Mutat. , vol.6 , pp. 195-196
    • Tomatsu, S.1    Fukuda, S.2    Cooper, A.3    Wraith, J.E.4    Yamada, N.5    Isogai, K.6
  • 52
    • 0030013161 scopus 로고    scopus 로고
    • Heteroallelic missense mutations of the galactosamine-6-sulfate sulfatase (GALNS) gene in a mild form of Morquio disease (MPS IVA)
    • D.E. Cole, S. Fukuda, B.A. Gordon, J.W. Rip, A.N. LeCouteur, and C.A. Rupar Heteroallelic missense mutations of the galactosamine-6-sulfate sulfatase (GALNS) gene in a mild form of Morquio disease (MPS IVA) Am. J. Med. Genet. 63 1996 558 565
    • (1996) Am. J. Med. Genet. , vol.63 , pp. 558-565
    • Cole, D.E.1    Fukuda, S.2    Gordon, B.A.3    Rip, J.W.4    Lecouteur, A.N.5    Rupar, C.A.6
  • 53
    • 0029103415 scopus 로고
    • Mucopolysaccharidosis IVA: Identification of a common missense mutation I113F in the N-acetylgalactosamine-6-sulfate sulfatase gene
    • S. Tomatsu, S. Fukuda, A. Cooper, J.E. Wraith, G.M. Rezvi, and A. Yamagishi Mucopolysaccharidosis IVA: identification of a common missense mutation I113F in the N-acetylgalactosamine-6-sulfate sulfatase gene Am. J. Hum. Genet. 57 1995 556 563
    • (1995) Am. J. Hum. Genet. , vol.57 , pp. 556-563
    • Tomatsu, S.1    Fukuda, S.2    Cooper, A.3    Wraith, J.E.4    Rezvi, G.M.5    Yamagishi, A.6
  • 55
    • 0035224941 scopus 로고    scopus 로고
    • Lysosomal multienzyme complex: Biochemistry, genetics, and molecular pathophysiology
    • A.V. Pshezhetsky, and M. Ashmarina Lysosomal multienzyme complex: biochemistry, genetics, and molecular pathophysiology Prog. Nucleic Acid Res. Mol. Biol. 69 2001 81 114
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.69 , pp. 81-114
    • Pshezhetsky, A.V.1    Ashmarina, M.2
  • 56
    • 0029904847 scopus 로고    scopus 로고
    • Association of N-acetylgalactosamine-6-sulfate sulfatase with the multienzyme lysosomal complex of β-galactosidase, cathepsin A, and neuraminidase: Possible implication for intralysosomal catabolism of keratan sulfate
    • DOI 10.1074/jbc.271.45.28359
    • A.V. Pshezhetsky, and M. Potier Association of N-acetylgalactosamine-6- sulfate sulfatase with the multienzyme lysosomal complex of β- galactosidase, cathepsin A, and neuraminidase. Possible implication for intralysosomal catabolism of keratan sulfate J. Biol. Chem. 271 1996 28359 28365 (Pubitemid 26374653)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.45 , pp. 28359-28365
    • Pshezhetsky, A.V.1    Potier, M.2
  • 57
    • 77953140333 scopus 로고    scopus 로고
    • Enhancement of drug delivery: Enzyme-replacement therapy for murine Morquio A syndrome
    • S. Tomatsu, A.M. Montano, V.C. Dung, A. Ohashi, H. Oikawa, and T. Oguma Enhancement of drug delivery: enzyme-replacement therapy for murine Morquio A syndrome Mol. Ther. 18 2010 1094 1102
    • (2010) Mol. Ther. , vol.18 , pp. 1094-1102
    • Tomatsu, S.1    Montano, A.M.2    Dung, V.C.3    Ohashi, A.4    Oikawa, H.5    Oguma, T.6
  • 58
    • 0026314681 scopus 로고
    • N-Acetylgalactosamine-6-sulfate sulfatase in human placenta: Purification and characteristics
    • M. Masue, K. Sukegawa, T. Orii, and T. Hashimoto N-Acetylgalactosamine-6- sulfate sulfatase in human placenta: purification and characteristics J. Biochem. 110 1991 965 970
    • (1991) J. Biochem. , vol.110 , pp. 965-970
    • Masue, M.1    Sukegawa, K.2    Orii, T.3    Hashimoto, T.4
  • 59
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode C.W. Carter, R.M. Sweet, Methods in Enzymology: Macromolecular Crystallography, Part A Vol. 276 1997 Academic Press New York, NY 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 60
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 63
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680 (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


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