guanidine has been researched along with congo red in 8 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (12.50) | 18.2507 |
| 2000's | 5 (62.50) | 29.6817 |
| 2010's | 2 (25.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Carlemalm, E; Eriksson, S; Janciauskiene, S | 1 |
| Du, HN; Hu, HY | 1 |
| DiGiammarino, EL; Galea, C; Jun, B; Kriwacki, RW; Lee, AS; Murti, G; Ribeiro, RC; Schultz, CP; Zambetti, G | 1 |
| Higurashi, T; Kawata, Y; Mizobata, T; Yagi, H | 1 |
| Chen, YH; Lee, HJ; Pon, YC; Yin, FY; Yu, CM | 1 |
| Dudzik, P; Kuciel, R; Mazurkiewicz, A | 1 |
| Li, W; Ma, B; Wei, L; Xie, J | 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 |
8 other study(ies) available for guanidine and congo red
| Article | Year |
|---|---|
In vitro amyloid fibril formation from alpha 1-antitrypsin.
Topics: alpha 1-Antitrypsin; Amyloid; Autoradiography; Blotting, Western; Circular Dichroism; Congo Red; Electrophoresis, Agar Gel; Guanidine; Guanidines; Hot Temperature; Humans; Lithocholic Acid; Microscopy, Electron; Neurofibrils; Protein Denaturation; Spectrometry, Fluorescence | 1995 |
Alpha-to-beta structural transformation of ovalbumin: heat and pH effects.
Topics: Animals; Circular Dichroism; Coloring Agents; Congo Red; Fluorescent Dyes; Guanidine; Hot Temperature; Hydrogen-Ion Concentration; Ovalbumin; Protein Folding; Protein Isoforms; Protein Structure, Secondary; Spectrometry, Fluorescence; Thermodynamics | 2000 |
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 |
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 |
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 |
Kinetic intermediates of unfolding of dimeric prostatic phosphatase.
Topics: Acid Phosphatase; Anilino Naphthalenesulfonates; Congo Red; Dimerization; Dithionitrobenzoic Acid; Enzyme Inhibitors; Guanidine; Humans; In Vitro Techniques; Kinetics; Male; Prostate; Protein Denaturation; Protein Folding; Protein Structure, Quaternary; Protein Tyrosine Phosphatases; Spectrometry, Fluorescence; Sulfhydryl Compounds | 2007 |
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 |
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 |