Page last updated: 2024-08-17

lysine and o(2',3')-(2,4,6-trinitrophenyl)-8-azidoadenosine triphosphate

lysine has been researched along with o(2',3')-(2,4,6-trinitrophenyl)-8-azidoadenosine triphosphate in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (100.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Berman, MC; McIntosh, DB; Woolley, DG1
McIntosh, DB; Woolley, DG1
Dupont, Y; McIntosh, DB; Miras, R; Moutin, MJ; Rapin, C; Vinçon, M1

Other Studies

3 other study(ies) available for lysine and o(2',3')-(2,4,6-trinitrophenyl)-8-azidoadenosine triphosphate

ArticleYear
2',3'-O-(2,4,6-trinitrophenyl)-8-azido-AMP and -ATP photolabel Lys-492 at the active site of sarcoplasmic reticulum Ca(2+)-ATPase.
    The Journal of biological chemistry, 1992, Mar-15, Volume: 267, Issue:8

    Topics: Adenosine Monophosphate; Adenosine Triphosphate; Affinity Labels; Amino Acid Sequence; Animals; Azides; Binding Sites; Calcium-Transporting ATPases; Chromatography, High Pressure Liquid; Fluorescein-5-isothiocyanate; Humans; Kinetics; Lysine; Molecular Sequence Data; Muscles; Peptide Fragments; Rabbits; Sarcoplasmic Reticulum; Sequence Homology, Nucleic Acid; Spectrometry, Fluorescence; Thermolysin

1992
Catalysis of an ATP analogue untethered and tethered to lysine 492 of sarcoplasmic reticulum Ca(2+)-ATPase.
    The Journal of biological chemistry, 1994, Aug-26, Volume: 269, Issue:34

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Affinity Labels; Biological Transport; Borohydrides; Calcium; Calcium-Transporting ATPases; Cross-Linking Reagents; Enzyme Stability; Hydrogen-Ion Concentration; Hydrolysis; Light; Lysine; Phosphorylation; Sarcoplasmic Reticulum

1994
Autonomous folding of the recombinant large cytoplasmic loop of sarcoplasmic reticulum Ca2+-ATPase probed by affinity labeling and trypsin digestion.
    European journal of biochemistry, 1998, Feb-01, Volume: 251, Issue:3

    Topics: Adenosine Triphosphate; Affinity Labels; Animals; Calcium-Transporting ATPases; Cross-Linking Reagents; Cytoplasm; Ethylmaleimide; Fluorescein-5-isothiocyanate; Glutaral; Hydrogen-Ion Concentration; Kinetics; Lysine; Models, Molecular; Muscle, Skeletal; Peptide Fragments; Protein Conformation; Protein Folding; Rabbits; Recombinant Proteins; Sarcoplasmic Reticulum; Trypsin

1998