Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation

Search Page

MyNCBI Filters
Text availability
Article attribute
Article type
Publication date

Search Results

59 results
Filters applied: . Clear all Results are displayed in a computed author sort order. Results by year timeline is unavailable
Page 1
Missense mutations in N-acetylglucosamine-1-phosphotransferase alpha/beta subunit gene in a patient with mucolipidosis III and a mild clinical phenotype.
Tiede S, Muschol N, Reutter G, Cantz M, Ullrich K, Braulke T. Tiede S, et al. Among authors: Muschol N. Am J Med Genet A. 2005 Sep 1;137A(3):235-40. doi: 10.1002/ajmg.a.30868. Am J Med Genet A. 2005. PMID: 16094673
Mucolipidosis type III (ML III, pseudo-Hurler polydystrophy), an autosomal recessive inherited disorder of lysosomal enzyme targeting is due to a defective N-acetylglucosamine 1-phosphotransferase (phosphotransferase) activity and leads to the impaired formation of mannose 6-phosphate markers in soluble lysosomal enzymes followed by their increased excretion into the serum. ...
Mucolipidosis type III (ML III, pseudo-Hurler polydystrophy), an autosomal recessive inherited disorder of lysosomal enzyme targeting is due …
Transport, enzymatic activity, and stability of mutant sulfamidase (SGSH) identified in patients with mucopolysaccharidosis type III A.
Muschol N, Storch S, Ballhausen D, Beesley C, Westermann JC, Gal A, Ullrich K, Hopwood JJ, Winchester B, Braulke T. Muschol N, et al. Hum Mutat. 2004 Jun;23(6):559-66. doi: 10.1002/humu.20037. Hum Mutat. 2004. PMID: 15146460
Mucopolysaccharidosis type IIIA (MPSIIIA) is an autosomal recessive lysosomal storage disease caused by mutations in the N-sulfoglucosamine sulfohydrolase gene (SGSH; encoding sulfamidase, also sulphamidase) leading to the lysosomal accumulation and urinary excretion of heparan sulfate. ...
Mucopolysaccharidosis type IIIA (MPSIIIA) is an autosomal recessive lysosomal storage disease caused by mutations in the N-sulfogluco …
A novel mutation in UDP-N-acetylglucosamine-1-phosphotransferase gamma subunit (GNPTAG) in two siblings with mucolipidosis type III alters a used glycosylation site.
Tiede S, Cantz M, Raas-Rothschild A, Muschol N, Bürger F, Ullrich K, Braulke T. Tiede S, et al. Among authors: Muschol N. Hum Mutat. 2004 Dec;24(6):535. doi: 10.1002/humu.9293. Hum Mutat. 2004. PMID: 15532026
The N-acetylglucosaminyl-1-phosphotransferase (termed phosphotransferase) catalyzes the initial step in the formation of mannose 6-phosphate (M6P) residues required for the efficient transport of soluble lysosomal enzymes. ...By direct sequencing a novel homozygous mutation, c.347_349delACA (p.Asn116del), was identified affecting a potential N-linked glycosylation site. ...
The N-acetylglucosaminyl-1-phosphotransferase (termed phosphotransferase) catalyzes the initial step in the formation of mannose 6-ph …
The mutation p.Ser298Pro in the sulphamidase gene (SGSH) is associated with a slowly progressive clinical phenotype in mucopolysaccharidosis type IIIA (Sanfilippo A syndrome).
Meyer A, Kossow K, Gal A, Steglich C, Mühlhausen C, Ullrich K, Braulke T, Muschol N. Meyer A, et al. Among authors: Muschol N. Hum Mutat. 2008 May;29(5):770. doi: 10.1002/humu.20738. Hum Mutat. 2008. PMID: 18407553
Mucopolysaccharidosis type IIIA (MPS IIIA, Sanfilippo A syndrome) is caused by mutations in the N-sulfoglucosamine sulfohydrolase (SGSH) gene and the resulting defective lysosomal degradation of the glycosaminoglycan heparan sulfate. ...
Mucopolysaccharidosis type IIIA (MPS IIIA, Sanfilippo A syndrome) is caused by mutations in the N-sulfoglucosamine sulfohydrolase (SG …
Loss of N-acetylglucosamine-1-phosphotransferase gamma subunit due to intronic mutation in GNPTG causes mucolipidosis type III gamma: Implications for molecular and cellular diagnostics.
Pohl S, Encarnacão M, Castrichini M, Müller-Loennies S, Muschol N, Braulke T. Pohl S, et al. Among authors: Muschol N. Am J Med Genet A. 2010 Jan;152A(1):124-32. doi: 10.1002/ajmg.a.33170. Am J Med Genet A. 2010. PMID: 20034096
Proteolytic processing of the gamma-subunit is associated with the failure to form GlcNAc-1-phosphotransferase complexes and mannose 6-phosphate residues on lysosomal enzymes in human macrophages.
Pohl S, Tiede S, Marschner K, Encarnação M, Castrichini M, Kollmann K, Muschol N, Ullrich K, Müller-Loennies S, Braulke T. Pohl S, et al. Among authors: Muschol N. J Biol Chem. 2010 Jul 30;285(31):23936-44. doi: 10.1074/jbc.M110.129684. Epub 2010 May 19. J Biol Chem. 2010. PMID: 20489197 Free PMC article.
Residual activity and proteasomal degradation of p.Ser298Pro sulfamidase identified in patients with a mild clinical phenotype of Sanfilippo A syndrome.
Muschol N, Pohl S, Meyer A, Gal A, Ullrich K, Braulke T. Muschol N, et al. Am J Med Genet A. 2011 Jul;155A(7):1634-9. doi: 10.1002/ajmg.a.34053. Epub 2011 Jun 10. Am J Med Genet A. 2011. PMID: 21671382
The gene underlying MPS IIIA, SGSH, encodes a lysosomal enzyme, N-sulfoglucosamine sulfohydrolase (sulfamidase). Mutational analysis of a large cohort of MPS IIIA patients showed a correlation of the missense mutation p.Ser298Pro and a slowly progressive course of the disease. ...
The gene underlying MPS IIIA, SGSH, encodes a lysosomal enzyme, N-sulfoglucosamine sulfohydrolase (sulfamidase). Mutational analysis …
59 results
Jump to page
Feedback