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Volumn 377, Issue 4, 2008, Pages 1168-1172

Structural basis of aspartylglucosaminuria

Author keywords

Aspartylglucosaminidase; Aspartylglucosaminuria; Gene mutation; Protein structure

Indexed keywords

ENZYME; N4 (BETA N ACETYLGLUCOSAMINYL)ASPARAGINASE;

EID: 56349106482     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.10.142     Document Type: Article
Times cited : (13)

References (15)
  • 4
    • 0025733719 scopus 로고
    • Genome structure of human lysosomal glycoasparaginase
    • Park H., Fisher K.J., and Aronson Jr. N.N. Genome structure of human lysosomal glycoasparaginase. FEBS Lett. 288 (1991) 168-172
    • (1991) FEBS Lett. , vol.288 , pp. 168-172
    • Park, H.1    Fisher, K.J.2    Aronson Jr., N.N.3
  • 5
    • 0026089364 scopus 로고
    • Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease
    • Ikonen E., Baumann M., Grön K., Syvänen A.-C., Enomaa N., Halila R., Aula P., and Peltonen L. Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease. EMBO J. 10 (1991) 51-58
    • (1991) EMBO J. , vol.10 , pp. 51-58
    • Ikonen, E.1    Baumann, M.2    Grön, K.3    Syvänen, A.-C.4    Enomaa, N.5    Halila, R.6    Aula, P.7    Peltonen, L.8
  • 8
    • 0029998354 scopus 로고    scopus 로고
    • Ser72Pro active-site disease mutation in human lysosomal aspartylglucosaminidase: abnormal intracellular processing and evidence for extracellular activation
    • Peltola M., Tikkanen R., Peltonen L., and Jalanko A. Ser72Pro active-site disease mutation in human lysosomal aspartylglucosaminidase: abnormal intracellular processing and evidence for extracellular activation. Hum. Mol. Genet. 5 (1996) 737-743
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 737-743
    • Peltola, M.1    Tikkanen, R.2    Peltonen, L.3    Jalanko, A.4
  • 9
    • 0030887772 scopus 로고    scopus 로고
    • Two novel mutations in a Canadian family with aspartylglucosaminuria and early outcome post-bone marrow transplantation
    • Laitinen A., Hietala M., Haworth J.C., Schroeder M.L., Seargeant L.E., Greenberg C.R., and Aula P P. Two novel mutations in a Canadian family with aspartylglucosaminuria and early outcome post-bone marrow transplantation. Clin. Genet. 51 (1997) 174-178
    • (1997) Clin. Genet. , vol.51 , pp. 174-178
    • Laitinen, A.1    Hietala, M.2    Haworth, J.C.3    Schroeder, M.L.4    Seargeant, L.E.5    Greenberg, C.R.6    Aula P, P.7
  • 11
    • 0028786346 scopus 로고
    • Three-dimensional structure of human lysosomal aspartylglucosaminidase
    • Oinonen C., Tikkanen R., Rouvinen J., and Peltonen L. Three-dimensional structure of human lysosomal aspartylglucosaminidase. Nat. Struct. Biol. 2 (1995) 1102-1108
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1102-1108
    • Oinonen, C.1    Tikkanen, R.2    Rouvinen, J.3    Peltonen, L.4
  • 12
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface area and their gradient for macromolecules
    • Fraczkiewicz R., and Braun W. Exact and efficient analytical calculation of the accessible surface area and their gradient for macromolecules. J. Comput. Chem. 19 (1998) 319-333
    • (1998) J. Comput. Chem. , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 13
    • 43449095983 scopus 로고    scopus 로고
    • Structural study on mutant alpha-l-iduronidases: insight into mucopolysaccharidosis type I
    • Sugawara K., Saito S., Ohno K., Okuyama T., and Sakuraba H. Structural study on mutant alpha-l-iduronidases: insight into mucopolysaccharidosis type I. J. Hum. Genet. 53 (2008) 467-474
    • (2008) J. Hum. Genet. , vol.53 , pp. 467-474
    • Sugawara, K.1    Saito, S.2    Ohno, K.3    Okuyama, T.4    Sakuraba, H.5
  • 14
    • 84986533794 scopus 로고
    • Algorithms for calculating excluded volume and its derivatives as a function of molecular conformation and their use in energy minimization
    • Kundrot C.E., Ponder J.W., and Richards F.M. Algorithms for calculating excluded volume and its derivatives as a function of molecular conformation and their use in energy minimization. J. Comput. Chem. 12 (1991) 402-409
    • (1991) J. Comput. Chem. , vol.12 , pp. 402-409
    • Kundrot, C.E.1    Ponder, J.W.2    Richards, F.M.3
  • 15
    • 12944249776 scopus 로고
    • A discussion of the solution for the best rotation to relate two sets of vectors
    • Kabsch W. A discussion of the solution for the best rotation to relate two sets of vectors. Acta Cryst. A34 (1978) 922-923
    • (1978) Acta Cryst. , vol.A34 , pp. 922-923
    • Kabsch, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.