Significance of two point mutations present in each HEXB allele of patients with adult GM2 gangliosidosis (Sandhoff disease) Homozygosity for the Ile207 → Val substitution is not associated with a clinical or biochemical phenotype
- 15 November 1996
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
- Vol. 1317 (2) , 127-133
- https://doi.org/10.1016/s0925-4439(96)00044-0
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- A common ? hexosaminidase gene mutation in adult Sandhoff disease patientsHuman Genetics, 1995
- Molecular basis of an adult form of Sandhoff disease: Substitution of glutamine for arginine at position 505 of the β-chain of β-hexosaminidase results in a labile enzymeBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 1993
- An unusual splicing mutation in the HEXB gene is associated with dramatically different phenotypes in patients from different racial backgrounds.Journal of Clinical Investigation, 1992
- Quantitative correlation between the residual activity of β-hexosaminidase A and arylsulfatase A and the severity of the resulting lysosomal storage diseaseHuman Genetics, 1992
- Molecular basis of an adult form of β-hexosaminidase B deficiency with motor neuron diseaseBiochemical and Biophysical Research Communications, 1991
- The biochemistry of HEXA and HEXB gene mutations causing GM2 gangliosidosisBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 1991
- Structure and distribution of an Alu-type deletion mutation in Sandhoff disease.Journal of Clinical Investigation, 1990
- Genetic cause of a Juvenile Form of Sandhoff DiseaseJournal of Biological Chemistry, 1989
- A routine method for the establishment of permanent growing lymphoblastoid cell linesHuman Genetics, 1986
- Validity of Lymphoid Cell Line for Enzymatic Studies of GM2-Gangliosidosis Variant 0 (Sandhoff Disease)Enzyme, 1985