glutamine has been researched along with congo red in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (20.00) | 18.2507 |
| 2000's | 2 (40.00) | 29.6817 |
| 2010's | 1 (20.00) | 24.3611 |
| 2020's | 1 (20.00) | 2.80 |
| Authors | Studies |
|---|---|
| Agianian, B; Becker, PB; Bonte, E; Leonard, K; Tucker, PA; Van der Zandt, H | 1 |
| Akagi, T; Hashikawa, T; Morishima, I; Nukina, N; Tanaka, M | 1 |
| Bairati, A; Fusi, P; Pozzuolo, S; Secundo, F; Shehi, E; Tortora, P | 1 |
| Cao, Z; Chen, Y; Dai, H; Li, H; Lin, Y; Pang, L; Wu, R; Yao, J; You, K | 1 |
| Cuéllar-Cruz, M; López-Romero, E; Ortiz-Ramírez, JA | 1 |
1 review(s) available for glutamine and congo red
| Article | Year |
|---|---|
Cell compensatory responses of fungi to damage of the cell wall induced by Calcofluor White and Congo Red with emphasis on
Topics: Animals; Antifungal Agents; Benzenesulfonates; beta-Glucans; Cell Wall; Cellulose; Chitin; Congo Red; Glutamine; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing); Hexosamines; Humans; Mammals; Polymers; Sporothrix; Sugars; Uridine Diphosphate | 2022 |
4 other study(ies) available for glutamine and congo red
| Article | Year |
|---|---|
The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling.
Topics: Amyloid; Animals; Benzothiazoles; Binding Sites; Birefringence; Chromatin; Congo Red; DNA-Binding Proteins; Drosophila melanogaster; Drosophila Proteins; Fluorescent Dyes; Glutamine; Homeodomain Proteins; Mutagenesis; Protein Structure, Secondary; Recombinant Fusion Proteins; Structure-Activity Relationship; Thiazoles; Trans-Activators; Transcription Factors | 1999 |
Intra- and intermolecular beta-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases.
Topics: Amino Acid Sequence; Animals; Antibodies, Monoclonal; Circular Dichroism; Congo Red; Dose-Response Relationship, Drug; Escherichia coli; Glutamine; Immunoblotting; Magnetic Resonance Spectroscopy; Microscopy, Electron; Models, Molecular; Molecular Sequence Data; Mutation; Myoglobin; Neurodegenerative Diseases; Peptides; Plasmids; Protein Conformation; Protein Folding; Protein Structure, Secondary; Sequence Homology, Amino Acid; Spectrophotometry, Infrared; Time Factors; Trinucleotide Repeat Expansion; Ultraviolet Rays; Whales | 2001 |
Temperature-dependent, irreversible formation of amyloid fibrils by a soluble human ataxin-3 carrying a moderately expanded polyglutamine stretch (Q36).
Topics: Amyloid; Animals; Ataxin-3; Chemical Precipitation; Circular Dichroism; Coloring Agents; Congo Red; Endopeptidases; Glutamine; Glutathione Transferase; Hot Temperature; Humans; Hydrolysis; Mice; Molecular Sequence Data; Nerve Tissue Proteins; Nuclear Proteins; Peptides; Protein Conformation; Protein Structure, Secondary; Recombinant Fusion Proteins; Repressor Proteins; Solubility; Spectrophotometry; Temperature; Transcription Factors | 2003 |
Hippocampal neurochemical changes in senescent mice induced with chronic injection of D-galactose and NaNO₂: an in vitro high-resolution NMR spectroscopy study at 9.4T.
Topics: Amyloid; Animals; Apoptosis; Aspartic Acid; Behavior, Animal; Cell Proliferation; Congo Red; Disease Progression; Galactose; Glutamine; Hippocampus; Inositol; Magnetic Resonance Spectroscopy; Male; Maze Learning; Mice; Neurofibrillary Tangles; Neuroglia; Neurons; Sodium Nitrite; Time Factors | 2014 |