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Neurophysiological studies in GM1, gangliosidosis
The Italian Journal of Neurological Sciences, 1982Neurophysiological studies (EEG, ERG, VEP) have been carried out on 8 children with proven GM1 gangliosidosis (3 of Type I and 5 of Type II). All the EEGs were abnormal showing an increasing amount of irregular slow activity as the disease progressed.
A, Harden, Z, Martinovic, G, Pampiglione
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Three cases of GM1-gangliosidosis
Clinica Chimica Acta, 1976A biochemical analysis was carried out on three cases of GM1-gangliosidosis which showed different clinical manifestations. These cases were classified in a previous study as Type 1, Type 2 (2B) and Type 2 (2A), an intermediate type between classical Type 1 and Type 2 (2B), by the determination of the chromatographic profile of the liver beta ...
T, Kudoh, T, Orii, T, Nakao, T, Sakagami
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Computed tomography of GM1 gangliosidosis
The Journal of Pediatrics, 1984REPORTS DESCRIBING THE VALUE of computed tomography in the identification of white matter abnormalities in the leukodystrophies and demyelinating diseases of children first appeared in 1977.1 Since then higher resolution scanners have resulted in CT descriptions of Canavan disease, 2 Alexander disease, 3 metachromatic leukodystrophy,4. 5 Krabbe disease,
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2007
The gangliosidoses are a group of lysosomal storage diseases characterized by the accumulation of these complex glycolipids in multiple organs of the body. They manifest a predominantly neurological phenotype, a fact that is probably related to their high prevalence in nervous tissues. The typical presentation is that of a progressive neurodegenerative
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The gangliosidoses are a group of lysosomal storage diseases characterized by the accumulation of these complex glycolipids in multiple organs of the body. They manifest a predominantly neurological phenotype, a fact that is probably related to their high prevalence in nervous tissues. The typical presentation is that of a progressive neurodegenerative
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GM1 ganglioside and Alzheimer’s disease
Glycoconjugate Journal, 2015Assembly and deposition of amyloid ß-protein (Aß) is an invariable and fundamental event in the pathological process of Alzheimer's disease (AD). To decipher the AD pathogenesis and also to develop disease-modifying drugs for AD, clarification of the molecular mechanism underlying the Aß assembly into amyloid fibrils in the brain has been a crucial ...
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