c(alpha)-formylglycine and Sphingolipid Storage Diseases

c(alpha)-formylglycine has been researched along with Sphingolipid Storage Diseases in 3 studies

Research

Studies (3)

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

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

Reviews

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. Cell, 2003, May-16, Volume: 113, Issue:4 Topics: Alanine; Animals; Catalytic Domain; Gene Expression Regulation, Enzymologic; Glycine; Humans; Mutation; Protein Processing, Post-Translational; Sphingolipidoses; Sulfatases	2003

Other Studies

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. Cell, 2003, May-16, Volume: 113, Issue:4 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. Cell, 2005, May-20, Volume: 121, Issue:4 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

Article

Year

Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme.

Cell, 2003, May-16, Volume: 113, Issue:4

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.

Cell, 2005, May-20, Volume: 121, Issue:4

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