thioflavin t has been researched along with Cataract in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 1 (33.33) | 29.6817 |
| 2010's | 1 (33.33) | 24.3611 |
| 2020's | 1 (33.33) | 2.80 |
| Authors | Studies |
|---|---|
| Fujii, N; Hachiya, N; Magami, K; Morikawa, K; Takata, T | 1 |
| Hemmateenejad, B; Khoshaman, K; Masoudi, R; Yousefi, R; Zm, SZ | 1 |
| Berry, Y; Carver, JA; Dobson, CM; Luisi, B; MacPhee, CE; Meehan, S | 1 |
3 other study(ies) available for thioflavin t and Cataract
| Article | Year |
|---|---|
Isomerization of Asp is essential for assembly of amyloid-like fibrils of αA-crystallin-derived peptide.
Topics: Aging; Alanine; alpha-Crystallin A Chain; Amino Acid Sequence; Amino Acid Substitution; Amyloid; Aspartic Acid; Benzothiazoles; Cataract; Fluorescent Dyes; Humans; Hydrophobic and Hydrophilic Interactions; Isoaspartic Acid; Isomerism; Lens, Crystalline; Microscopy, Electron; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein D-Aspartate-L-Isoaspartate Methyltransferase; Protein Processing, Post-Translational; Static Electricity | 2021 |
The structural alteration and aggregation propensity of glycated lens crystallins in the presence of calcium: Importance of lens calcium homeostasis in development of diabetic cataracts.
Topics: Animals; Benzothiazoles; Calcium; Cataract; Cattle; Chymotrypsin; Circular Dichroism; Cross-Linking Reagents; Crystallins; Diabetes Mellitus; Dynamic Light Scattering; Fluorescence; Glycosylation; Homeostasis; Ions; Kinetics; Lens, Crystalline; Molecular Weight; Protein Aggregates; Protein Conformation; Protein Stability; Proteolysis; Thiazoles; Tryptophan | 2017 |
Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation.
Topics: Aging; alpha-Crystallins; Amyloid; Animals; Benzothiazoles; beta-Crystallins; Cataract; Cattle; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; gamma-Crystallins; Guanidine; Hydrogen-Ion Concentration; Lens, Crystalline; Microscopy, Electron; Protein Folding; Protein Processing, Post-Translational; Temperature; Thiazoles; X-Ray Diffraction | 2004 |