Beth McInnes
Montreal Neurological Institute and Hospital
5 Papers
118 Citations
Beth McInnes is an academic researcher from Montreal Neurological Institute and Hospital. The author has contributed to research in topics: HEXB & Sandhoff disease. The author has an hindex of 5, co-authored 5 publications.
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Papers
A Pro504 → Ser Substitution in the β-Subunit of β-Hexosaminidase A Inhibits α-Subunit Hydrolysis of GM2Ganglioside, Resulting in Chronic Sandhoff Disease
TL;DR: It is concluded that the β-Pro504 → Ser mutation directly affects the ability of Hex A to hydrolyze its natural substrate but not its artificial substrates.
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Isolation and expression of a full-length cDNA encoding the human GM2 activator protein.
TL;DR: The construction of a cDNA clone encoding a functional GM2-activator protein was reported, and the ability of purified hexosaminidase A to hydrolyse labeled GM2 ganglioside was enhanced 10-fold more by the addition in the assay mix of lysate from transfected COS-1 cells.
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Characterization of two HEXB gene mutations in Argentinean patients with Sandhoff disease.
TL;DR: Two novel PCR-based assays were developed to detect mutations in the HEXB gene encoded beta-subunit and it is suggested that one of these assays could be modified and used as a rapid screening procedure for 5' donor splice site defects in other genes.
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Two small deletion mutations of the HEXB gene are present in DNA from a patient with infantile Sandhoff disease.
TL;DR: The characterization of two rare HEXB mutations present in genomic DNA from a single fibroblast cell line, GM203, taken from a patient with the infantile form of Sandhoff disease are reported, consistent with the idea that the severe infantiles form of Tay-Sachs or Sandhoff Disease is associated with a total lack of residual hexosaminidase A activity.
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Identification of a processed pseudogene related to the functional gene encoding the GM2 activator protein: localization of the pseudogene to human chromosome 3 and the functional gene to human chromosome 5.
TL;DR: It is demonstrated here that conflicts were caused by the presence of a previously unidentified processed activator-pseudogene on chromosome 3, and a previous ELISA-based localization of the functional activator gene to chromosome 5 is confirmed.
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