Page last updated: 2024-08-25

5-aminofluorescein and fluorescein-5-isothiocyanate

5-aminofluorescein has been researched along with fluorescein-5-isothiocyanate in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Gribbon, P; Hardingham, TE; Heng, BC	1
Anselmetti, D; Güntherodt, HJ; Honegger, A; Jermutus, L; Pluckthun, A; Ros, R; Schwesinger, F; Strunz, T; Tiefenauer, L	1

Other Studies

2 other study(ies) available for 5-aminofluorescein and fluorescein-5-isothiocyanate

Article	Year
The molecular basis of the solution properties of hyaluronan investigated by confocal fluorescence recovery after photobleaching. Biophysical journal, 1999, Volume: 77, Issue:4 Topics: Animals; Dextrans; Diffusion; Dose-Response Relationship, Drug; Electrolytes; Fluorescein-5-isothiocyanate; Fluoresceins; Fluorescence; Hyaluronic Acid; Hydrogen Bonding; Hydrogen-Ion Concentration; Microscopy, Confocal; Models, Chemical; Molecular Weight; Osmolar Concentration; Polyelectrolytes; Polymers; Sodium Chloride; Sodium Hydroxide; Solutions; Static Electricity	1999
Unbinding forces of single antibody-antigen complexes correlate with their thermal dissociation rates. Proceedings of the National Academy of Sciences of the United States of America, 2000, Aug-29, Volume: 97, Issue:18 Topics: Amino Acid Substitution; Antigen-Antibody Complex; Binding Sites, Antibody; Fluorescein-5-isothiocyanate; Fluoresceins; Fluorescent Dyes; Immunoglobulin Fragments; Kinetics; Microscopy, Atomic Force; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Proteins; Spectrometry, Fluorescence; Thermodynamics	2000

Article

Year

The molecular basis of the solution properties of hyaluronan investigated by confocal fluorescence recovery after photobleaching.

Biophysical journal, 1999, Volume: 77, Issue:4

Topics: Animals; Dextrans; Diffusion; Dose-Response Relationship, Drug; Electrolytes; Fluorescein-5-isothiocyanate; Fluoresceins; Fluorescence; Hyaluronic Acid; Hydrogen Bonding; Hydrogen-Ion Concentration; Microscopy, Confocal; Models, Chemical; Molecular Weight; Osmolar Concentration; Polyelectrolytes; Polymers; Sodium Chloride; Sodium Hydroxide; Solutions; Static Electricity

1999

Unbinding forces of single antibody-antigen complexes correlate with their thermal dissociation rates.

Proceedings of the National Academy of Sciences of the United States of America, 2000, Aug-29, Volume: 97, Issue:18

Topics: Amino Acid Substitution; Antigen-Antibody Complex; Binding Sites, Antibody; Fluorescein-5-isothiocyanate; Fluoresceins; Fluorescent Dyes; Immunoglobulin Fragments; Kinetics; Microscopy, Atomic Force; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Proteins; Spectrometry, Fluorescence; Thermodynamics

2000