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Results: 1 to 20 of 127

Similar articles for PubMed (Select 18992224)

1.

Structural basis of aspartylglucosaminuria.

Saito S, Ohno K, Sugawara K, Suzuki T, Togawa T, Sakuraba H.

Biochem Biophys Res Commun. 2008 Dec 26;377(4):1168-72. doi: 10.1016/j.bbrc.2008.10.142. Epub 2008 Nov 4.

PMID:
18992224
2.

Structural basis of neuronal ceroid lipofuscinosis 1.

Ohno K, Saito S, Sugawara K, Suzuki T, Togawa T, Sakuraba H.

Brain Dev. 2010 Aug;32(7):524-30. doi: 10.1016/j.braindev.2009.08.010. Epub 2009 Sep 29.

PMID:
19793631
3.

A novel aspartylglucosaminuria mutation affects translocation of aspartylglucosaminidase.

Saarela J, von Schantz C, Peltonen L, Jalanko A.

Hum Mutat. 2004 Oct;24(4):350-1.

PMID:
15365992
4.

Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations.

Saarela J, Laine M, Oinonen C, von Schantz C, Jalanko A, Rouvinen J, Peltonen L.

Hum Mol Genet. 2001 Apr 15;10(9):983-95.

5.

Structural characterization of mutant alpha-galactosidases causing Fabry disease.

Sugawara K, Ohno K, Saito S, Sakuraba H.

J Hum Genet. 2008;53(9):812-24. doi: 10.1007/s10038-008-0316-9. Epub 2008 Jul 17.

PMID:
18633574
6.

Adenovirus-mediated gene transfer results in decreased lysosomal storage in brain and total correction in liver of aspartylglucosaminuria (AGU) mouse.

Peltola M, Kyttälä A, Heinonen O, Rapola J, Paunio T, Revah F, Peltonen L, Jalanko A.

Gene Ther. 1998 Oct;5(10):1314-21.

7.

Structural study on mutant alpha-L-iduronidases: insight into mucopolysaccharidosis type I.

Sugawara K, Saito S, Ohno K, Okuyama T, Sakuraba H.

J Hum Genet. 2008;53(5):467-74. doi: 10.1007/s10038-008-0272-4. Epub 2008 Mar 14.

PMID:
18340403
8.

Dissection of the molecular consequences of a double mutation causing a human lysosomal disease.

Riikonen A, Ikonen E, Sormunen R, Lehto VP, Peltonen L, Jalanko A.

DNA Cell Biol. 1994 Mar;13(3):257-64.

PMID:
8172656
9.

Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease.

Ikonen E, Baumann M, Grön K, Syvänen AC, Enomaa N, Halila R, Aula P, Peltonen L.

EMBO J. 1991 Jan;10(1):51-8.

11.

Characterization of three alleles causing aspartylglycosaminuria: two from a British family and one from an American patient.

Park H, Vettese MB, Fensom AH, Fisher KJ, Aronson NN Jr.

Biochem J. 1993 Mar 15;290 ( Pt 3):735-41.

12.

In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation.

Ikonen E, Enomaa N, Ulmanen I, Peltonen L.

Genomics. 1991 Sep;11(1):206-11.

PMID:
1765378
13.

Assignment of the aspartylglucosaminidase gene (AGA) to 4q33----q35 based on decreased activity in a girl with a 46,XX,del(4)(q33) karyotype.

Engelen J, Hamers A, Schrander-Stumpel C, Mulder H, Poorthuis B.

Cytogenet Cell Genet. 1992;60(3-4):208-9.

PMID:
1505217
14.

Structural modeling of mutant alpha-glucosidases resulting in a processing/transport defect in Pompe disease.

Sugawara K, Saito S, Sekijima M, Ohno K, Tajima Y, Kroos MA, Reuser AJ, Sakuraba H.

J Hum Genet. 2009 Jun;54(6):324-30. doi: 10.1038/jhg.2009.32. Epub 2009 Apr 3.

PMID:
19343043
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Autoproteolytic activation of human aspartylglucosaminidase.

Saarela J, Oinonen C, Jalanko A, Rouvinen J, Peltonen L.

Biochem J. 2004 Mar 1;378(Pt 2):363-71.

19.

Human aspartylglucosaminidase. A biochemical and immunocytochemical characterization of the enzyme in normal and aspartylglucosaminuria fibroblasts.

Enomaa N, Heiskanen T, Halila R, Sormunen R, Seppälä R, Vihinen M, Peltonen L.

Biochem J. 1992 Sep 1;286 ( Pt 2):613-8.

20.

Spectrum of mutations in aspartylglucosaminuria.

Ikonen E, Aula P, Grön K, Tollersrud O, Halila R, Manninen T, Syvänen AC, Peltonen L.

Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11222-6.

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