c(alpha)-formylglycine has been researched along with Sphingolipid Storage Diseases in 3 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 3 (100.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Baenziger, JU | 1 |
Borissenko, LV; Dierks, T; Mariappan, M; Peng, J; Preusser, A; Schmidt, B; von Figura, K | 1 |
Dickmanns, A; Dierks, T; Ficner, R; Mariappan, M; Preusser-Kunze, A; Rudolph, MG; Schmidt, B; von Figura, K | 1 |
1 review(s) available for c(alpha)-formylglycine and Sphingolipid Storage Diseases
Article | Year |
---|---|
A major step on the road to understanding a unique posttranslational modification and its role in a genetic disease.
Topics: Alanine; Animals; Catalytic Domain; Gene Expression Regulation, Enzymologic; Glycine; Humans; Mutation; Protein Processing, Post-Translational; Sphingolipidoses; Sulfatases | 2003 |
2 other study(ies) available for c(alpha)-formylglycine and Sphingolipid Storage Diseases
Article | Year |
---|---|
Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme.
Topics: Alanine; Amino Acid Sequence; Animals; Base Sequence; Biological Assay; Cattle; CHO Cells; Chromosomes, Human, Pair 3; Cricetinae; DNA, Complementary; Endoplasmic Reticulum; Enzymes; Gene Expression Regulation, Enzymologic; Genetic Vectors; Glycine; Humans; Mice; Molecular Sequence Data; Mutation; Protein Structure, Tertiary; Sphingolipidoses; Sulfatases; Transduction, Genetic | 2003 |
Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme.
Topics: Alanine; Amino Acid Sequence; Binding Sites; Calcium; Catalytic Domain; Crystallography, X-Ray; Cysteine; Glycine; Humans; Models, Molecular; Molecular Conformation; Molecular Sequence Data; Mutation, Missense; Oxidation-Reduction; Oxidoreductases Acting on Sulfur Group Donors; Oxygen; Protein Structure, Secondary; Sequence Homology, Amino Acid; Sphingolipidoses; Sulfatases; Tumor Cells, Cultured | 2005 |