Compounds > cysteine

cysteine and n-(4-(7-(diethylamino)-4-methylcoumarin-3-yl))maleimide

cysteine has been researched along with n-(4-(7-(diethylamino)-4-methylcoumarin-3-yl))maleimide in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's4 (100.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Aggeler, R; Capaldi, RA1
Colvert, KK; Mills, DA; Richter, ML1
Capaldi, RA; Turina, P2

Other Studies

4 other study(ies) available for cysteine and n-(4-(7-(diethylamino)-4-methylcoumarin-3-yl))maleimide

ArticleYear
Cross-linking of the gamma subunit of the Escherichia coli ATPase (ECF1) via cysteines introduced by site-directed mutagenesis.
    The Journal of biological chemistry, 1992, Oct-25, Volume: 267, Issue:30

    Topics: Adenosine Triphosphatases; Base Sequence; Blotting, Western; Coumarins; Cross-Linking Reagents; Cysteine; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Fluorescent Dyes; Maleimides; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Plasmids

1992
Structural mapping of cysteine-63 of the chloroplast ATP synthase beta subunit.
    Biochemistry, 1992, Apr-28, Volume: 31, Issue:16

    Topics: Amino Acid Sequence; Binding Sites; Chloroplasts; Coumarins; Cysteine; Energy Transfer; Fluorescein; Fluoresceins; Fluorescence Polarization; Fluorescent Dyes; Kinetics; Maleimides; Molecular Sequence Data; Plants; Protein Conformation; Proton-Translocating ATPases; Spectrometry, Fluorescence

1992
ATP binding causes a conformational change in the gamma subunit of the Escherichia coli F1ATPase which is reversed on bond cleavage.
    Biochemistry, 1994, Nov-29, Volume: 33, Issue:47

    Topics: Adenosine Triphosphate; Adenylyl Imidodiphosphate; Binding Sites; Coumarins; Cysteine; Escherichia coli; Fluorescent Dyes; Hydrolysis; Kinetics; Maleimides; Mutagenesis, Site-Directed; Protein Conformation; Proton-Translocating ATPases; Spectrometry, Fluorescence

1994
ATP hydrolysis-driven structural changes in the gamma-subunit of Escherichia coli ATPase monitored by fluorescence from probes bound at introduced cysteine residues.
    The Journal of biological chemistry, 1994, May-06, Volume: 269, Issue:18

    Topics: Adenosine Triphosphate; Coumarins; Cysteine; Escherichia coli; Fluorescence Polarization; Fluorescent Dyes; Hydrolysis; Kinetics; Maleimides; Mutation; Nucleotides; Protein Conformation; Proton-Translocating ATPases

1994