Page last updated: 2024-08-17

adenosine diphosphate and thioflavin t

adenosine diphosphate has been researched along with thioflavin t in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	2 (100.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Arita-Morioka, K; Mizunoe, Y; Ogura, T; Sugimoto, S; Yamanaka, K	1
Diaz-Espinoza, R; Monasterio, O; Nova, E	1

Other Studies

2 other study(ies) available for adenosine diphosphate and thioflavin t

Article	Year
Thioflavin T as a fluorescence probe for monitoring RNA metabolism at molecular and cellular levels. Nucleic acids research, 2015, Aug-18, Volume: 43, Issue:14 Topics: Adenosine Diphosphate; Benzothiazoles; Fluorescent Dyes; Polyribonucleotide Nucleotidyltransferase; RNA; RNA, Bacterial; Single-Cell Analysis; Thiazoles	2015
Development of a novel catalytic amyloid displaying a metal-dependent ATPase-like activity. Biochemical and biophysical research communications, 2017, Jan-22, Volume: 482, Issue:4 Topics: Adenosine Diphosphate; Adenosine Monophosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Amyloid; Amyloidogenic Proteins; Benzothiazoles; Catalysis; Catalytic Domain; Computer Simulation; Humans; Hydrogen-Ion Concentration; Hydrolysis; Ions; Magnesium; Manganese; Metals; Peptides; Thiazoles	2017

Article

Year

Thioflavin T as a fluorescence probe for monitoring RNA metabolism at molecular and cellular levels.

Nucleic acids research, 2015, Aug-18, Volume: 43, Issue:14

Topics: Adenosine Diphosphate; Benzothiazoles; Fluorescent Dyes; Polyribonucleotide Nucleotidyltransferase; RNA; RNA, Bacterial; Single-Cell Analysis; Thiazoles

2015

Development of a novel catalytic amyloid displaying a metal-dependent ATPase-like activity.

Biochemical and biophysical research communications, 2017, Jan-22, Volume: 482, Issue:4

Topics: Adenosine Diphosphate; Adenosine Monophosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Amyloid; Amyloidogenic Proteins; Benzothiazoles; Catalysis; Catalytic Domain; Computer Simulation; Humans; Hydrogen-Ion Concentration; Hydrolysis; Ions; Magnesium; Manganese; Metals; Peptides; Thiazoles

2017