Compounds > cysteine

cysteine and n-(4-azido-2,3,5,6-tetrafluorobenzyl)-3-maleimidopropionamide

cysteine has been researched along with n-(4-azido-2,3,5,6-tetrafluorobenzyl)-3-maleimidopropionamide in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (33.33)18.2507
2000's2 (66.67)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Aggeler, R; Cai, SX; Capaldi, RA; Chicas-Cruz, K; Keana, JF1
Beal, PA; Spanggord, RJ1
Jiang, P; Ninfa, AJ; Pioszak, AA1

Other Studies

3 other study(ies) available for cysteine and n-(4-azido-2,3,5,6-tetrafluorobenzyl)-3-maleimidopropionamide

ArticleYear
Introduction of reactive cysteine residues in the epsilon subunit of Escherichia coli F1 ATPase, modification of these sites with tetrafluorophenyl azide-maleimides, and examination of changes in the binding of the epsilon subunit when different nucleotid
    Biochemistry, 1992, Mar-24, Volume: 31, Issue:11

    Topics: Adenosine Triphosphate; Azides; Base Sequence; Binding Sites; Cross-Linking Reagents; Cysteine; Edetic Acid; Escherichia coli; Ethylmaleimide; Fluorobenzenes; Magnesium; Maleimides; Molecular Sequence Data; Mutagenesis, Site-Directed; Photolysis; Proton-Translocating ATPases

1992
Site-specific modification and RNA crosslinking of the RNA-binding domain of PKR.
    Nucleic acids research, 2000, May-01, Volume: 28, Issue:9

    Topics: Base Sequence; Binding Sites; Binding, Competitive; Cross-Linking Reagents; Cysteine; eIF-2 Kinase; Fluorobenzenes; Maleimides; Molecular Sequence Data; Mutation; Protein Binding; Protein Structure, Tertiary; RNA; RNA-Binding Proteins; Sulfides

2000
The Escherichia coli PII signal transduction protein regulates the activities of the two-component system transmitter protein NRII by direct interaction with the kinase domain of the transmitter module.
    Biochemistry, 2000, Nov-07, Volume: 39, Issue:44

    Topics: Bacterial Proteins; Chromatography, Gel; Cross-Linking Reagents; Cysteine; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Escherichia coli; Fluorobenzenes; Maleimides; Mutagenesis, Site-Directed; Peptide Fragments; Peptide Mapping; Phosphoprotein Phosphatases; Phosphorylation; PII Nitrogen Regulatory Proteins; Protein Kinases; Protein Structure, Tertiary; Serine; Signal Transduction

2000