Compounds > fluorescein-5-isothiocyanate
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fluorescein-5-isothiocyanate and 1,5-i-aedans

fluorescein-5-isothiocyanate has been researched along with 1,5-i-aedans in 8 studies

Research

Studies (8)

TimeframeStudies, this research(%)All Research%
pre-19902 (25.00)18.7374
1990's5 (62.50)18.2507
2000's1 (12.50)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Bigelow, DJ; Garcia de Ancos, J; Inesi, G; Squier, TC1
Cittanova, N; Evrain, C; Jayle, MF; Rajkowski, KM1
Baker, KJ; East, JM; Lee, AG1
Ferreira, ST; Rietveld, AW1
Beltrán, C; Darszon, A; Ferreira, ST; Garzón-Rodríguez, W; Gómez-Puyou, A; Sepúlveda-Becerra, MA; Strasser, RJ1
Min, X; Yang, F; Zhang, X1
Bigelow, DJ; Chen, B; Jones, TE1
Bigelow, DJ; Chen, B; Squier, TC1

Other Studies

8 other study(ies) available for fluorescein-5-isothiocyanate and 1,5-i-aedans

ArticleYear
Localization of site-specific probes on the Ca-ATPase of sarcoplasmic reticulum using fluorescence energy transfer.
    The Journal of biological chemistry, 1987, Apr-05, Volume: 262, Issue:10

    Topics: Adenosine Monophosphate; Affinity Labels; Animals; Binding Sites; Calcium-Transporting ATPases; Energy Transfer; Fluorescein-5-isothiocyanate; Fluoresceins; In Vitro Techniques; Naphthalenesulfonates; Rabbits; Sarcoplasmic Reticulum; Spectrometry, Fluorescence; Sulfhydryl Compounds; Thiocyanates

1987
The preparation of three fluorescence-labeled derivatives of testosterone.
    Steroids, 1980, Volume: 35, Issue:6

    Topics: Chemical Phenomena; Chemistry; Cysteamine; Fluorescein-5-isothiocyanate; Fluoresceins; Fluorescent Antibody Technique; Iodoacetamide; Naphthalenesulfonates; Spectrophotometry, Ultraviolet; Testosterone; Thiocyanates

1980
Localization of the hinge region of the Ca(2+)-ATPase of sarcoplasmic reticulum using resonance energy transfer.
    Biochimica et biophysica acta, 1994, Jun-01, Volume: 1192, Issue:1

    Topics: Binding Sites; Calcium-Transporting ATPases; Energy Transfer; Fluorescein-5-isothiocyanate; Fluoresceins; Fluorescent Dyes; Muscles; Naphthalenesulfonates; Phospholipids; Protein Conformation; Sarcoplasmic Reticulum; Spectrometry, Fluorescence; Water

1994
Deterministic pressure dissociation and unfolding of triose phosphate isomerase: persistent heterogeneity of a protein dimer.
    Biochemistry, 1996, Jun-18, Volume: 35, Issue:24

    Topics: Animals; Fluorescein-5-isothiocyanate; Fluorescent Dyes; Guanidine; Guanidines; Kinetics; Macromolecular Substances; Muscle, Skeletal; Naphthalenesulfonates; Pressure; Protein Conformation; Protein Denaturation; Protein Folding; Rabbits; Spectrometry, Fluorescence; Thermodynamics; Triose-Phosphate Isomerase

1996
Refolding of triosephosphate isomerase in low-water media investigated by fluorescence resonance energy transfer.
    Biochemistry, 1996, Dec-10, Volume: 35, Issue:49

    Topics: Animals; Cetrimonium; Cetrimonium Compounds; Cysteine; Detergents; Fluorescein-5-isothiocyanate; Guanidine; Guanidines; Hexanols; Micelles; Muscle, Skeletal; Naphthalenesulfonates; Octanes; Protein Conformation; Protein Denaturation; Protein Folding; Rabbits; Spectrometry, Fluorescence; Triose-Phosphate Isomerase

1996
Conformational basis of the phospholipid requirement for the activity of SR Ca(2+)-ATPase.
    Chemistry and physics of lipids, 1998, Volume: 97, Issue:1

    Topics: Animals; Binding Sites; Calcium-Transporting ATPases; Fluorescein-5-isothiocyanate; Fluorescent Dyes; In Vitro Techniques; Naphthalenesulfonates; Phosphatidylcholines; Phosphatidylethanolamines; Phospholipids; Protein Conformation; Proteolipids; Rabbits; Sarcoplasmic Reticulum; Tryptophan

1998
The nucleotide-binding site of the sarcoplasmic reticulum Ca-ATPase is conformationally altered in aged skeletal muscle.
    Biochemistry, 1999, Nov-09, Volume: 38, Issue:45

    Topics: Aging; Animals; Binding Sites; Calcium-Transporting ATPases; Circular Dichroism; Energy Transfer; Fluorescein-5-isothiocyanate; Fluorescent Dyes; Models, Biological; Muscle, Skeletal; Naphthalenesulfonates; Nucleotides; Protein Conformation; Protein Structure, Secondary; Rats; Rats, Inbred F344; Sarcoplasmic Reticulum; Solvents; Spectrometry, Fluorescence

1999
Calcium activation of the Ca-ATPase enhances conformational heterogeneity between nucleotide binding and phosphorylation domains.
    Biochemistry, 2004, Apr-13, Volume: 43, Issue:14

    Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Binding Sites; Biological Transport; Calcium; Calcium-Transporting ATPases; Enzyme Activation; Enzyme Stability; Fluorescein-5-isothiocyanate; Fluorescence Polarization; Fluorescence Resonance Energy Transfer; Fluorescent Dyes; Naphthalenesulfonates; Phosphorylation; Protein Conformation; Protein Structure, Tertiary; Rabbits

2004