arginine has been researched along with g(m2) ganglioside in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 4 (100.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| dos Santos, MR; Maia, M; Ribeiro, MG; sá Miranda, MC; Suzuki, K; Tanaka, A | 1 |
| Kaback, MM; Moskowitz, SM; Neufeld, EF; Paw, BH; Uhrhammer, N; Wright, N | 1 |
| Fontes, A; Palmeira, MM; Pinto, E; Pinto, RA; Ribeiro, H; Ribeiro, MG; Sá Miranda, MC; Sonin, T | 1 |
| Deng, H; Mahuran, D; Rigat, B; Smiljanic-Georgijev, N; Xie, B | 1 |
4 other study(ies) available for arginine and g(m2) ganglioside
| Article | Year |
|---|---|
GM2-gangliosidosis B1 variant: analysis of beta-hexosaminidase alpha gene mutations in 11 patients from a defined region in Portugal.
Topics: Adolescent; Arginine; beta-N-Acetylhexosaminidases; Blotting, Southern; Cell Line, Transformed; Child; Child, Preschool; Female; G(M2) Ganglioside; Humans; Male; Mutation; Oligonucleotides; Polymerase Chain Reaction; Portugal; Tay-Sachs Disease | 1991 |
Juvenile GM2 gangliosidosis caused by substitution of histidine for arginine at position 499 or 504 of the alpha-subunit of beta-hexosaminidase.
Topics: Arginine; Base Sequence; beta-N-Acetylhexosaminidases; Cells, Cultured; Child; Child, Preschool; DNA; Female; Fibroblasts; G(M2) Ganglioside; Gangliosidoses; Histidine; Homozygote; Humans; Lysosomes; Macromolecular Substances; Male; Molecular Sequence Data; Mutation; Nucleic Acid Hybridization; Polymerase Chain Reaction; Transcription, Genetic | 1990 |
Clinical, enzymatic, and molecular characterisation of a Portuguese family with a chronic form of GM2-gangliosidosis B1 variant.
Topics: Adult; Alleles; Amino Acid Sequence; Arginine; beta-N-Acetylhexosaminidases; DNA Mutational Analysis; G(M2) Ganglioside; Gangliosidoses; Hexosaminidase A; Histidine; Humans; Molecular Sequence Data; Pedigree; Phenotype; Polymerase Chain Reaction; Polymorphism, Single-Stranded Conformational; Portugal | 1996 |
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.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Arginine; beta-N-Acetylhexosaminidases; CHO Cells; Cricetinae; Cysteine; Disulfides; Escherichia coli; G(M2) Activator Protein; G(M2) Ganglioside; Gangliosidoses; Genetic Variation; Molecular Sequence Data; Oligopeptides; Peptides; Protein Folding; Proteins; Recombinant Fusion Proteins | 1998 |