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Volumn 580, Issue 1, 2006, Pages 87-92

Common antigenicity for two glycosidases

Author keywords

Antibody cross reactivity; Antigenicity; Enzyme replacement therapy; Epitope reactivity; Glycosidase; Lysosomal storage disorders

Indexed keywords

ALPHA GLUCOSIDASE; EPITOPE; GLYCOSAMINOGLYCAN; GLYCOSIDASE; LEVO IDURONIDASE; MONOCLONAL ANTIBODY; POLYCLONAL ANTIBODY;

EID: 29344467700     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.11.053     Document Type: Article
Times cited : (3)

References (28)
  • 1
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymic glycosyl transfer
    • M.L. Sinnott Catalytic mechanisms of enzymic glycosyl transfer Chem. Rev. 90 1990 1171 1202
    • (1990) Chem. Rev. , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 3
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • B. Henrissat, and A. Bairoch Updating the sequence-based classification of glycosyl hydrolases Biochem. J. 316 1996 695 696
    • (1996) Biochem. J. , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 4
    • 0030937787 scopus 로고    scopus 로고
    • Active site motifs of lysosomal acid hydrolases: Invariant features of clan GH-A glycosyl hydrolases deduced from hydrophobic cluster analysis
    • P. Durand, P. Lehn, I. Callebaut, S. Fabrega, B. Henrissat, and J.P. Mornon Active site motifs of lysosomal acid hydrolases: invariant features of clan GH-A glycosyl hydrolases deduced from hydrophobic cluster analysis Glycobiology 7 1997 277 284
    • (1997) Glycobiology , vol.7 , pp. 277-284
    • Durand, P.1    Lehn, P.2    Callebaut, I.3    Fabrega, S.4    Henrissat, B.5    Mornon, J.P.6
  • 5
    • 0034639932 scopus 로고    scopus 로고
    • Structural features of normal and mutant human lysosomal glycoside hydrolases deduced from bioinformatics analysis
    • P. Durand, S. Fabrega, B. Henrissat, J.P. Mornon, and P. Lehn Structural features of normal and mutant human lysosomal glycoside hydrolases deduced from bioinformatics analysis Hum. Mol. Genet. 9 2000 967 977
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 967-977
    • Durand, P.1    Fabrega, S.2    Henrissat, B.3    Mornon, J.P.4    Lehn, P.5
  • 6
    • 0028956984 scopus 로고
    • β-Glucosidase, β-galactosidase, family a cellulase, family F xylanases and two barley glycanases form a superfamily of enzymes with 8-fold β/α architecture and with two conserved glutamates near the carboxy-terminal ends of two β-strands four and seven
    • J. Jenkins, L. LoLeggio, G. Harris, and R. Pickersgill β-Glucosidase, β-galactosidase, family A cellulase, family F xylanases and two barley glycanases form a superfamily of enzymes with 8-fold β/α architecture and with two conserved glutamates near the carboxy-terminal ends of two β-strands four and seven FEBS Lett. 362 1995 281 285
    • (1995) FEBS Lett. , vol.362 , pp. 281-285
    • Jenkins, J.1    Loleggio, L.2    Harris, G.3    Pickersgill, R.4
  • 7
    • 0037125202 scopus 로고    scopus 로고
    • Iterative database searched demonstrate that glycoside hydrolase families 27, 31, 36 and 66 share a common evolutionary origin with family 13
    • D. Rigden Iterative database searched demonstrate that glycoside hydrolase families 27, 31, 36 and 66 share a common evolutionary origin with family 13 FEBS Lett. 523 2002 17 22
    • (2002) FEBS Lett. , vol.523 , pp. 17-22
    • Rigden, D.1
  • 9
    • 0035006850 scopus 로고    scopus 로고
    • Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of α-glucosidase from Schizosaccharomyces pombe
    • M. Okuyama, A. Okuno, N. Shimizu, H. Mori, A. Kimura, and S. Chiba Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of α-glucosidase from Schizosaccharomyces pombe Eur. J. Biochem. 268 2001 2270 2280
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2270-2280
    • Okuyama, M.1    Okuno, A.2    Shimizu, N.3    Mori, H.4    Kimura, A.5    Chiba, S.6
  • 10
    • 12544256784 scopus 로고    scopus 로고
    • Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate
    • A.L. Lovering, S.S. Lee, Y. Kim, S.G. Withers, and N.C. Strynadka Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate J. Biol. Chem. 280 2005 2105 2115
    • (2005) J. Biol. Chem. , vol.280 , pp. 2105-2115
    • Lovering, A.L.1    Lee, S.S.2    Kim, Y.3    Withers, S.G.4    Strynadka, N.C.5
  • 12
    • 0037709362 scopus 로고    scopus 로고
    • Family 39 α-l-iduronidases and β-d-xylosidases react through similar glycosyl-enzyme intermediates: Identification of the human iduronidase nucleophile
    • C.E. Nieman, A.W. Wong, S. He, L. Clarke, J.J. Hopwood, and S.G. Withers Family 39 α-l-iduronidases and β-d-xylosidases react through similar glycosyl-enzyme intermediates: identification of the human iduronidase nucleophile Biochemistry 42 2003 8054 8065
    • (2003) Biochemistry , vol.42 , pp. 8054-8065
    • Nieman, C.E.1    Wong, A.W.2    He, S.3    Clarke, L.4    Hopwood, J.J.5    Withers, S.G.6
  • 13
    • 0000869162 scopus 로고    scopus 로고
    • The Mucopolysaccharidosis
    • C.R. Scriver A. Beaudet W.S. Sly D. Valle 8th edn. McGraw-Hill New York
    • E.F. Neufeld, and J. Muenzer The Mucopolysaccharidosis C.R. Scriver A. Beaudet W.S. Sly D. Valle The Metabollic and Molecular Basis of Inherited Diseases 8th edn. 2001 McGraw-Hill New York 3421 3452
    • (2001) The Metabollic and Molecular Basis of Inherited Diseases , pp. 3421-3452
    • Neufeld, E.F.1    Muenzer, J.2
  • 14
    • 73649187940 scopus 로고
    • Alpha-glucosidase deficiency in generalised glycogen-storage disease
    • H.G. Hers Alpha-glucosidase deficiency in generalised glycogen-storage disease Biochem. J. 86 1963 11
    • (1963) Biochem. J. , vol.86 , pp. 11
    • Hers, H.G.1
  • 16
    • 2342666229 scopus 로고    scopus 로고
    • Enzyme replacement therapy for mucopolysaccharidosis I: A randomized, double-blinded, placebo-controlled, multinational study of recombinant human α-l-iduronidase (laronidase)
    • J.E. Wraith, L.A. Clarke, M. Beck, E.H. Kolodny, G.M. Pastores, J. Muenzer, D.M. Rapoport, K.I. Berger, S.J. Swiedler, and E.D. Kakkis Enzyme replacement therapy for mucopolysaccharidosis I: a randomized, double-blinded, placebo-controlled, multinational study of recombinant human α-l-iduronidase (laronidase) J. Pediatr. 144 2004 581 588
    • (2004) J. Pediatr. , vol.144 , pp. 581-588
    • Wraith, J.E.1    Clarke, L.A.2    Beck, M.3    Kolodny, E.H.4    Pastores, G.M.5    Muenzer, J.6    Rapoport, D.M.7    Berger, K.I.8    Swiedler, S.J.9    Kakkis, E.D.10
  • 21
    • 15044345490 scopus 로고    scopus 로고
    • Safety and efficacy of recombinant acid alpha-glucosidase (rhGAA) in patients with classical infantile Pompe disease: Results of a phase II clinical trial
    • L. Klinge, V. Straub, U. Neudorf, J. Schaper, T. Bosbach, K. Gorlinger, M. Wallot, S. Richards, and T. Voit Safety and efficacy of recombinant acid alpha-glucosidase (rhGAA) in patients with classical infantile Pompe disease: results of a phase II clinical trial Neuromuscul. Disord. 15 2005 24 31
    • (2005) Neuromuscul. Disord. , vol.15 , pp. 24-31
    • Klinge, L.1    Straub, V.2    Neudorf, U.3    Schaper, J.4    Bosbach, T.5    Gorlinger, K.6    Wallot, M.7    Richards, S.8    Voit, T.9
  • 22
    • 0346059410 scopus 로고    scopus 로고
    • Iduronate-2-sulphatase protein detection in plasma from mucopolysaccharidosis type II patients
    • E.J. Parkinson, V. Muller, J.J. Hopwood, and D.A. Brooks Iduronate-2-sulphatase protein detection in plasma from mucopolysaccharidosis type II patients Mol. Genet. Metab. 81 2004 58 64
    • (2004) Mol. Genet. Metab. , vol.81 , pp. 58-64
    • Parkinson, E.J.1    Muller, V.2    Hopwood, J.J.3    Brooks, D.A.4
  • 23
    • 0037906571 scopus 로고    scopus 로고
    • Immune tolerance after long-term enzyme-replacement therapy among patients who have mucopolysaccharidosis I
    • R. Kakavanos, C.T. Turner, J.J. Hopwood, E.D. Kakkis, and D.A. Brooks Immune tolerance after long-term enzyme-replacement therapy among patients who have mucopolysaccharidosis I Lancet 361 2003 1608 1613
    • (2003) Lancet , vol.361 , pp. 1608-1613
    • Kakavanos, R.1    Turner, C.T.2    Hopwood, J.J.3    Kakkis, E.D.4    Brooks, D.A.5
  • 24
    • 0000951677 scopus 로고
    • Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid
    • H.M. Geysen, R.H. Meloen, and S.J. Barteling Use of peptide synthesis to probe viral antigens for epitopes to a resolution of a single amino acid Proc. Natl. Acad. Sci. USA 81 1984 3998 4002
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3998-4002
    • Geysen, H.M.1    Meloen, R.H.2    Barteling, S.J.3
  • 27
    • 0036396627 scopus 로고    scopus 로고
    • Immune response to enzyme replacement therapy: Single epitope control of antigen distribution from circulation
    • E.N. Glaros, C.T. Turner, E.J. Parkinson, J.J. Hopwood, and D.A. Brooks Immune response to enzyme replacement therapy: single epitope control of antigen distribution from circulation Mol. Genet. Metab. 77 2002 127 135
    • (2002) Mol. Genet. Metab. , vol.77 , pp. 127-135
    • Glaros, E.N.1    Turner, C.T.2    Parkinson, E.J.3    Hopwood, J.J.4    Brooks, D.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.