thioflavin t has been researched along with guanidine in 16 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 9 (56.25) | 29.6817 |
| 2010's | 7 (43.75) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| DiGiammarino, EL; Galea, C; Jun, B; Kriwacki, RW; Lee, AS; Murti, G; Ribeiro, RC; Schultz, CP; Zambetti, G | 1 |
| Dimitry, JM; Frazier, WA; McDonald, JF | 1 |
| Ahmad, A; Doniach, S; Fink, AL; Millett, IS; Uversky, VN | 1 |
| Berry, Y; Carver, JA; Dobson, CM; Luisi, B; MacPhee, CE; Meehan, S | 1 |
| Higurashi, T; Kawata, Y; Mizobata, T; Yagi, H | 1 |
| Chatani, E; Goto, Y; Kato, M; Kawai, T; Naiki, H | 1 |
| Chen, YH; Lee, HJ; Pon, YC; Yin, FY; Yu, CM | 1 |
| Lewandowska, A; Liberek, K; Matuszewska, M | 1 |
| Artemov, AV; Kuznetsova, IM; Mikhaĭlova, EV; Nevzgliadova, OV; Soĭdla, TR; Turoverov, KK | 1 |
| Bienkiewicz, EA; Bullard, RL; Kumar, A; Morgan, SE; Paslay, LC; Patel, P; Rangachari, V; Singh, D | 1 |
| Iram, A; Naeem, A | 1 |
| Li, W; Ma, B; Wei, L; Xie, J | 1 |
| Guan, Y; Wang, Y; Zhang, H | 1 |
| Alagón, A; Castellanos-Mendoza, A; Castro-Acosta, RM; García-Hernández, E; Mendoza-Vera, M; Olvera, A; Trujillo-Roldán, MA; Valdez-Cruz, NA; Zavala, G | 1 |
| Adachi, M; Akazawa-Ogawa, Y; Goto, Y; Hagihara, Y; Kardos, J; Noda, S; So, M | 1 |
| DeGrado, WF; Elkins, MR; Hong, M; Jo, H; Lemmin, T; Nick, M; Prusiner, SB; Stöhr, J; Wang, T | 1 |
16 other study(ies) available for thioflavin t and guanidine
| Article | Year |
|---|---|
Reversible amyloid formation by the p53 tetramerization domain and a cancer-associated mutant.
Topics: Amyloid; Benzothiazoles; Circular Dichroism; Coloring Agents; Congo Red; Dose-Response Relationship, Drug; Guanidine; Hot Temperature; Humans; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Microscopy, Electron; Mutation; Neoplasms; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrophotometry; Spectroscopy, Fourier Transform Infrared; Temperature; Thiazoles; Time Factors; Tumor Suppressor Protein p53 | 2003 |
An amyloid-like C-terminal domain of thrombospondin-1 displays CD47 agonist activity requiring both VVM motifs.
Topics: Amino Acid Motifs; Amino Acid Sequence; Amyloid; Antigens, CD; Benzothiazoles; Carrier Proteins; CD47 Antigen; Cell Adhesion; Circular Dichroism; GTP-Binding Proteins; Guanidine; Heparin; Humans; Melanoma; Models, Biological; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Peptide Fragments; Pertussis Toxin; Protein Binding; Protein Conformation; Protein Denaturation; Protein Structure, Tertiary; Signal Transduction; Thiazoles; Thrombospondin 1; Tumor Cells, Cultured; Vitronectin | 2003 |
Partially folded intermediates in insulin fibrillation.
Topics: Acetic Acid; Acrylamide; Benzothiazoles; Chromatography, Gel; Circular Dichroism; Dimerization; Guanidine; Humans; Hydrogen-Ion Concentration; Insulin; Kinetics; Microscopy, Electron; Protein Conformation; Protein Denaturation; Protein Folding; Scattering, Radiation; Spectrometry, Fluorescence; Thiazoles; X-Rays | 2003 |
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 |
Amyloid-like fibril formation of co-chaperonin GroES: nucleation and extension prefer different degrees of molecular compactness.
Topics: Amyloid; Benzothiazoles; Carrier Proteins; Chaperonin 10; Circular Dichroism; Coloring Agents; Congo Red; Dose-Response Relationship, Drug; Escherichia coli; Guanidine; Hydrogen-Ion Concentration; Light; Mass Spectrometry; Microscopy, Atomic Force; Microscopy, Electron, Transmission; Microscopy, Fluorescence; Molecular Conformation; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Secondary; Scattering, Radiation; Thiazoles; Time Factors | 2005 |
Main-chain dominated amyloid structures demonstrated by the effect of high pressure.
Topics: Amyloid; Benzothiazoles; beta 2-Microglobulin; Dialysis; Guanidine; Humans; Hydrostatic Pressure; Protein Conformation; Protein Denaturation; Protein Folding; Thiazoles; Tryptophan | 2005 |
Kinetic refolding barrier of guanidinium chloride denatured goose delta-crystallin leads to regular aggregate formation.
Topics: Animals; Benzothiazoles; Birds; Chromatography, Gel; Circular Dichroism; Congo Red; delta-Crystallins; Dimerization; Electrophoresis, Polyacrylamide Gel; Guanidine; Kinetics; Microscopy, Electron, Transmission; Models, Molecular; Mutation; Protein Conformation; Protein Denaturation; Protein Folding; Protein Subunits; Thiazoles; Tryptophan | 2007 |
Conformational properties of aggregated polypeptides determine ClpB-dependence in the disaggregation process.
Topics: Benzothiazoles; Circular Dichroism; Endopeptidase Clp; Escherichia coli; Escherichia coli Proteins; Guanidine; Heat-Shock Proteins; Luciferases; Peptides; Protein Denaturation; Protein Structure, Quaternary; Protein Structure, Secondary; Thiazoles | 2007 |
[Estimating of changes in the amyloid and prion content of yeast cells].
Topics: Amyloid; Benzothiazoles; Crosses, Genetic; Guanidine; Peptide Termination Factors; Prions; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Staining and Labeling; Thiazoles | 2008 |
Non-esterified fatty acids generate distinct low-molecular weight amyloid-β (Aβ42) oligomers along pathway different from fibril formation.
Topics: Amyloid beta-Peptides; Benzothiazoles; Blotting, Western; Circular Dichroism; Fatty Acids, Nonesterified; Fluorescence; Guanidine; Micelles; Models, Biological; Molecular Weight; Protein Denaturation; Protein Structure, Quaternary; Protein Structure, Secondary; Thermodynamics; Thiazoles | 2011 |
Existence of different structural intermediates and aggregates on the folding pathway of ovalbumin.
Topics: Anilino Naphthalenesulfonates; Animals; Benzothiazoles; Dose-Response Relationship, Drug; Glucose; Glycation End Products, Advanced; Guanidine; Ovalbumin; Protein Denaturation; Protein Folding; Spectrum Analysis; Thiazoles; Time Factors | 2012 |
Macromolecular crowding modulates the kinetics and morphology of amyloid self-assembly by β-lactoglobulin.
Topics: Amyloid; Animals; Benzothiazoles; Cattle; Congo Red; Fluorescent Dyes; Guanidine; Hydrogen-Ion Concentration; Kinetics; Lactoglobulins; Microscopy, Electron, Transmission; Protein Multimerization; Protein Structure, Quaternary; Thiazoles | 2013 |
New insight into the binding interaction of hydroxylated carbon nanotubes with bovine serum albumin.
Topics: Animals; Benzothiazoles; Cattle; Circular Dichroism; Guanidine; Hydrogen-Ion Concentration; Hydroxylation; Kinetics; Molecular Docking Simulation; Nanotubes, Carbon; Protein Aggregates; Protein Binding; Protein Denaturation; Protein Structure, Secondary; Serum Albumin, Bovine; Spectrometry, Fluorescence; Thiazoles | 2014 |
Influence of pH control in the formation of inclusion bodies during production of recombinant sphingomyelinase-D in Escherichia coli.
Topics: Animals; Benzothiazoles; Biomass; Congo Red; Endopeptidase K; Escherichia coli; Guanidine; Hydrogen-Ion Concentration; Inclusion Bodies; Kinetics; Phosphoric Diester Hydrolases; Recombinant Proteins; Solubility; Spectrometry, Fluorescence; Thiazoles; Ticks | 2014 |
Thioflavin T-Silent Denaturation Intermediates Support the Main-Chain-Dominated Architecture of Amyloid Fibrils.
Topics: Amyloid; Animals; Benzothiazoles; beta 2-Microglobulin; Cell Survival; Guanidine; Humans; Insulin; PC12 Cells; Protein Aggregates; Protein Denaturation; Protein Structure, Secondary; Rats; Thiazoles; Ultrasonic Waves | 2016 |
Structural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study.
Topics: Amyloid beta-Peptides; Benzothiazoles; Binding Sites; Guanidine; Humans; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Mutation; Peptides; Phenotype; Protein Conformation; Temperature; Thiazoles | 2016 |