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fluorescein-5-isothiocyanate and o(2',3')-(2,4,6-trinitrophenyl)-8-azidoadenosine triphosphate

fluorescein-5-isothiocyanate 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
Dupont, Y; McIntosh, DB; Miras, R; Moutin, MJ; Rapin, C; Vinçon, M1
Cavieres, JD; Ward, DG1

Other Studies

3 other study(ies) available for fluorescein-5-isothiocyanate 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
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
Affinity labeling of two nucleotide sites on Na,K-ATPase using 2'(3')-O-(2,4,6-trinitrophenyl)8-azidoadenosine 5'-[alpha-32P]diphosphate (TNP-8N3-[alpha-32P]ADP) as a photoactivatable probe. Label incorporation before and after blocking the high affinity
    The Journal of biological chemistry, 1998, Dec-11, Volume: 273, Issue:50

    Topics: Adenosine Triphosphate; Catalytic Domain; Fluorescein-5-isothiocyanate; Molecular Probes; Photoaffinity Labels; Sodium-Potassium-Exchanging ATPase; Substrate Specificity

1998