Bei Xie
University of Toronto
6 Papers
100 Citations
Bei Xie is an academic researcher from University of Toronto. The author has contributed to research in topics: G(M2) Activator Protein & Activator (genetics). The author has an hindex of 5, co-authored 6 publications.
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Papers
Characterization of the affinity of the GM2 activator protein for glycolipids by a fluorescence dequenching assay
TL;DR: It is shown that various glycolipids inhibit the transport between liposomes of a self-quenching fluorescent lipid probe, octadecylrhodamine, by the activator protein, and the data suggest that the C-terminus of the Activator is required to produce a functional hydrophobic binding pocket.
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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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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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Refined Mapping of the GM2 Activator Protein (GM2A) Locus to 5q31.3-q33.1, Distal to the Spinal Muscular Atrophy Locus
TL;DR: It is demonstrated that the PCR primers used preferentially amplified a processed pseudogene (GM2AP) that was mapped to chromosome 3 and that GM2A was located on chromosome 5 and that it is not a candidate gene for SMA.
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Biochemical characterization of the Cys138Arg substitution associated with the AB variant form of GM2 gangliosidosis: evidence that Cys138 is required for the recognition of the GM2 activator/GM2 ganglioside complex by beta-hexosaminidase A.
TL;DR: It is demonstrated that the heat stability of the GM2 activator protein at 60 degrees C is reduced 14-fold, suggesting some localized change in tertiary structure, and that the Cys138 Arg substitution has no effect on these functions.
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