c(alpha)-formylglycine and serine

c(alpha)-formylglycine has been researched along with serine in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's4 (57.14)18.2507
2000's1 (14.29)29.6817
2010's2 (28.57)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Dierks, T; Miech, C; Schmidt, B; Selmer, T; von Figura, K1
Dierks, T; Recksiek, M; Schmidt, B; Selmer, T; von Figura, K1
Dierks, T; Hummerjohann, J; Kertesz, MA; Miech, C; Schmidt, B; von Figura, K1
Balleininger, M; Dierks, T; Miech, C; Schmidt, B; Szameit, C; von Figura, K1
Dierks, T; Fang, Q; Marquordt, C; Peng, J; von Figura, K; Will, E1
Benjdia, A; Berteau, O; Johnson, MK; Leprince, J; Subramanian, S; Vaudry, H1
Appel, MJ; Bertozzi, CR1

Reviews

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

ArticleYear
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

6 other study(ies) available for c(alpha)-formylglycine and serine

ArticleYear
Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine.
    The Journal of biological chemistry, 1998, Feb-27, Volume: 273, Issue:9

    Topics: Alanine; Amino Acid Sequence; Arylsulfatases; Glycine; Klebsiella pneumoniae; Molecular Sequence Data; Peptide Fragments; Prokaryotic Cells; Protein Processing, Post-Translational; Serine

1998
Sulfatases, trapping of the sulfated enzyme intermediate by substituting the active site formylglycine.
    The Journal of biological chemistry, 1998, Mar-13, Volume: 273, Issue:11

    Topics: Alanine; Alkaline Phosphatase; Binding Sites; Catechols; Cerebroside-Sulfatase; Chondro-4-Sulfatase; Galactose; Glycine; Humans; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; Serine; Sulfuric Acid Esters

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
The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase.
    The Journal of biological chemistry, 1999, May-28, Volume: 274, Issue:22

    Topics: Alanine; Bacterial Proteins; Borohydrides; Cloning, Molecular; Escherichia coli; Gene Expression Regulation, Bacterial; Glycine; Iron-Sulfur Proteins; Klebsiella pneumoniae; Molecular Sequence Data; Protein Processing, Post-Translational; Recombinant Proteins; Serine; Sulfatases; Transfection

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
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