A novel exonic mutation in the aspartylglucosaminidase gene causes exon skipping

Journal of Inherited Metabolic Disease

Volumn 22, Issue 5, 1999, Pages 682-683

  Coulter Mackie, M B ^a,b  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^b BC CHILDREN S HOSPITAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; MESSENGER RNA; N4 (BETA N ACETYLGLUCOSAMINYL)ASPARAGINASE;

ARTICLE; BASE MISPAIRING; CANADA; CASE REPORT; CLINICAL FEATURE; CONTROLLED STUDY; DNA SEQUENCE; EXON; GENE MUTATION; HETEROZYGOSITY; HOMOZYGOSITY; HUMAN; INTRON; MISSENSE MUTATION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RNA SPLICING; SIBLING;

ASPARTIC ACID; ASPARTYLGLUCOSYLAMINASE; EXONS; GLYCINE; HUMANS; MUTATION, MISSENSE; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION;

EID: 0033067889     PISSN: 01418955     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005563004678     Document Type: Article

References (3)

1. Cooper TA, Mattox W (1997) The regulation of splice-site selection and its role in human disease. Am J Hum Genet 61: 259-266.
2. Gordon BA, Rupar CA, Rip JW, et al (1998) Aspartylglucosaminuria in a Canadian family. Clin Invest Med 21: 114-123.
3. Oinonen C, Tikkanen R, Rouvinen J, Peltonen L (1995) Three-dimensional structure of human lysosomal aspartylglucosaminidase. Nature Structural Biology 2: 1102-1108.