Compounds > c(alpha)-formylglycine

c(alpha)-formylglycine and cysteine

c(alpha)-formylglycine has been researched along with cysteine in 10 studies

Research

Studies (10)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	4 (40.00)	18.2507
2000's	2 (20.00)	29.6817
2010's	4 (40.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Dierks, T; Schmidt, B; von Figura, K	1
Dierks, T; Lecca, MR; Schmidt, B; von Figura, K	1
Dierks, T; Hummerjohann, J; Kertesz, MA; Miech, C; Schmidt, B; von Figura, K	1
Dierks, T; Lecca, MR; Schlotterhose, P; Schmidt, B; von Figura, K	1
Dierks, T; Fang, Q; Marquordt, C; Peng, J; von Figura, K; Will, E	1
Dickmanns, A; Dierks, T; Ficner, R; Mariappan, M; Preusser-Kunze, A; Rudolph, MG; Schmidt, B; von Figura, K	1
Benjdia, A; Berteau, O; Johnson, MK; Leprince, J; Subramanian, S; Vaudry, H	1
Bertozzi, CR; deHart, GW; Rabuka, D; Rush, JS; Wu, P	1
Appel, MJ; Bertozzi, CR	1
Alam, S; Dierks, T; Mariappan, M; May, C; Peng, J; Radhakrishnan, K; Rudolph, MG; Schmidt, B; von Figura, K	1

Reviews

1 review(s) available for c(alpha)-formylglycine and cysteine

Article	Year
Formylglycine, a post-translationally generated residue with unique catalytic capabilities and biotechnology applications. ACS chemical biology, 2015, Jan-16, Volume: 10, Issue:1 Topics: Alanine; Animals; Binding Sites; Biotechnology; Catalysis; Catalytic Domain; Cysteine; Glycine; Humans; Models, Molecular; Protein Processing, Post-Translational; Serine; Sulfotransferases	2015

Other Studies

9 other study(ies) available for c(alpha)-formylglycine and cysteine

Article	Year
Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum. Proceedings of the National Academy of Sciences of the United States of America, 1997, Oct-28, Volume: 94, Issue:22 Topics: Alanine; Amino Acid Sequence; Binding Sites; Biological Transport; Cerebroside-Sulfatase; Cysteine; Endoplasmic Reticulum; Glycine; Humans; Lysosomal Storage Diseases; Molecular Sequence Data; Protein Biosynthesis; Protein Processing, Post-Translational	1997
Conversion of cysteine to formylglycine in eukaryotic sulfatases occurs by a common mechanism in the endoplasmic reticulum. FEBS letters, 1998, Feb-13, Volume: 423, Issue:1 Topics: Alanine; Animals; Cell Line; Cerebroside-Sulfatase; Chondro-4-Sulfatase; Cricetinae; Cysteine; Endoplasmic Reticulum; Eukaryotic Cells; Glycine; Humans; Protein Processing, Post-Translational; Time Factors	1998
Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine. The Journal of biological chemistry, 1998, Oct-02, Volume: 273, Issue:40 Topics: Alanine; Arylsulfatases; Bacterial Proteins; Binding Sites; Borohydrides; Cysteine; Glycine; Klebsiella pneumoniae; Mutagenesis, Site-Directed; Peptide Fragments; Prokaryotic Cells; Protein Processing, Post-Translational; Pseudomonas aeruginosa; Recombinant Proteins; Sequence Analysis; Serine; Sulfates; Trypsin	1998
Sequence determinants directing conversion of cysteine to formylglycine in eukaryotic sulfatases. The EMBO journal, 1999, Apr-15, Volume: 18, Issue:8 Topics: Alanine; Amino Acid Sequence; Base Sequence; Catalytic Domain; Cerebroside-Sulfatase; Cysteine; DNA Primers; Glycine; Molecular Sequence Data; Mutagenesis, Site-Directed; Sequence Homology, Amino Acid	1999
Posttranslational modification of serine to formylglycine in bacterial sulfatases. Recognition of the modification motif by the iron-sulfur protein AtsB. The Journal of biological chemistry, 2003, Jan-24, Volume: 278, Issue:4 Topics: Alanine; Amino Acid Motifs; Amino Acid Sequence; Arylsulfatases; beta-Galactosidase; Blotting, Western; Cysteine; Cytosol; Dose-Response Relationship, Drug; Escherichia coli; Glutathione Transferase; Glycine; Iron-Sulfur Proteins; Klebsiella pneumoniae; Models, Chemical; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptides; Protein Binding; Protein Processing, Post-Translational; Protein Sorting Signals; Serine; Subcellular Fractions; Sulfatases; Two-Hybrid System Techniques	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
Anaerobic sulfatase-maturating enzyme--a mechanistic link with glycyl radical-activating enzymes? The FEBS journal, 2010, Volume: 277, Issue:8 Topics: Alanine; Anaerobiosis; Binding Sites; Catalysis; Cysteine; Electron Spin Resonance Spectroscopy; Eukaryota; Glycine; Iron-Sulfur Proteins; Oxidation-Reduction; S-Adenosylmethionine; Serine; Substrate Specificity; Sulfatases	2010
Site-specific chemical protein conjugation using genetically encoded aldehyde tags. Nature protocols, 2012, May-10, Volume: 7, Issue:6 Topics: Alanine; Aldehydes; Animals; CHO Cells; Chromatography, High Pressure Liquid; Cricetinae; Cysteine; Escherichia coli; Glycine; Mass Spectrometry; Oxidoreductases Acting on Sulfur Group Donors; Proteins; Recombinant Proteins; Sulfatases	2012
Eukaryotic formylglycine-generating enzyme catalyses a monooxygenase type of reaction. The FEBS journal, 2015, Volume: 282, Issue:17 Topics: Alanine; Animals; Baculoviridae; Biocatalysis; Catalytic Domain; Cysteine; Disulfides; Dithiothreitol; Enzyme Assays; Gene Expression; Glycine; Humans; Kinetics; Mixed Function Oxygenases; Oxidation-Reduction; Oxidoreductases Acting on Sulfur Group Donors; Oxygen; Recombinant Proteins; Sf9 Cells; Spodoptera; Sulfatases	2015