thioflavin t has been researched along with formazans in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 4 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Irie, K; Morimoto, A; Murakami, K; Nagao, M; Ohigashi, H; Shimizu, T; Shindo, M; Shirasawa, T | 1 |
| Baas, F; Chafekar, SM; Hoozemans, JJ; Scheper, W; Zwart, R | 1 |
| Dotti, CG; Esteras-Chopo, A; Kümmerer, N; López de la Paz, M; Pastor, MT; Schubert, V; Serrano, L | 1 |
| Battistin, L; Bellucci, A; Collo, G; Missale, C; Sarnico, I; Spano, P | 1 |
4 other study(ies) available for thioflavin t and formazans
| Article | Year |
|---|---|
Synthesis, aggregation, neurotoxicity, and secondary structure of various A beta 1-42 mutants of familial Alzheimer's disease at positions 21-23.
Topics: Alzheimer Disease; Amino Acid Sequence; Amyloid beta-Peptides; Animals; Benzothiazoles; Cerebral Amyloid Angiopathy; Chromatography, High Pressure Liquid; Formazans; Humans; Molecular Sequence Data; PC12 Cells; Peptide Fragments; Protein Conformation; Protein Structure, Secondary; Rats; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Structure-Activity Relationship; Thiazoles | 2002 |
Abeta 1-42 induces mild endoplasmic reticulum stress in an aggregation state-dependent manner.
Topics: Amyloid beta-Peptides; Benzothiazoles; Calnexin; Cell Differentiation; Cell Line; Cell Survival; Dimethyl Sulfoxide; Dose-Response Relationship, Drug; Endoplasmic Reticulum; Fluorescent Dyes; Formazans; Humans; In Situ Nick-End Labeling; Neuroblastoma; Peptide Fragments; Protein Conformation; Stress, Physiological; Temperature; Tetrazolium Salts; Thiazoles; Time Factors; Transfection; Tunicamycin | 2007 |
Amyloid toxicity is independent of polypeptide sequence, length and chirality.
Topics: Amino Acid Sequence; Amyloid beta-Peptides; Animals; Benzothiazoles; Cell Membrane; Cells, Cultured; Circular Dichroism; Cystatin C; Cystatins; Formazans; Hippocampus; Humans; Kinetics; Mass Spectrometry; Molecular Weight; Neurons; PC12 Cells; Peptide Fragments; Peptides; Prions; Protein Structure, Quaternary; Protein Structure, Secondary; Rats; Sonication; Synapses; tau Proteins; Tetrazolium Salts; Thiazoles | 2008 |
Alpha-synuclein aggregation and cell death triggered by energy deprivation and dopamine overload are counteracted by D2/D3 receptor activation.
Topics: alpha-Synuclein; Analysis of Variance; Animals; Benzothiazoles; Cell Death; Cells, Cultured; Dopamine; Dopamine Agents; Dopamine Plasma Membrane Transport Proteins; Embryo, Mammalian; Formazans; Gene Expression Regulation; Glucose; Mesencephalon; Mice; Mitochondria; Nerve Degeneration; Nerve Tissue Proteins; Neurons; Protein Transport; Receptors, Dopamine D2; Tetrazolium Salts; Thiazoles | 2008 |