alanine has been researched along with thioflavin t in 10 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 7 (70.00) | 29.6817 |
| 2010's | 2 (20.00) | 24.3611 |
| 2020's | 1 (10.00) | 2.80 |
| Authors | Studies |
|---|---|
| Conway, KA; Harper, JD; Lansbury, PT | 1 |
| Du, HN; Hu, HY; Hu, J; Li, HT; Luo, XY; Tang, L; Zhou, JW | 1 |
| Keasling, JD; Muller, SJ; Wang, K | 1 |
| He, Y; Luo, Y; Tang, H; Zhou, H | 1 |
| Dikov, D; Otzen, DE; Pedersen, JS | 1 |
| Gupta, R; Marek, P; Raleigh, DP | 1 |
| Chung, RS; Howells, C; Karafin, A; Palumaa, P; Tõugu, V; West, AK; Zovo, K | 1 |
| Aucoin, D; Hoos, MD; Kotarba, AE; Smith, SO; Van Nostrand, WE | 1 |
| Bottomley, SP; Ellisdon, AM; Hughes, VA; Lupton, CJ; Steer, DL; Wintrode, PL | 1 |
| Fujii, N; Hachiya, N; Magami, K; Morikawa, K; Takata, T | 1 |
10 other study(ies) available for alanine and thioflavin t
| Article | Year |
|---|---|
Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid.
Topics: Alanine; alpha-Synuclein; Amino Acid Sequence; Amyloid; Benzothiazoles; Binding Sites; Brain; Circular Dichroism; Congo Red; Endopeptidases; Humans; Hydrolysis; Immunohistochemistry; Lewy Bodies; Microscopy, Atomic Force; Microscopy, Polarization; Molecular Sequence Data; Mutation, Missense; Nerve Tissue Proteins; Parkinson Disease; Postmortem Changes; Proline; Protein Structure, Secondary; Recombinant Proteins; Spectrometry, Fluorescence; Spectroscopy, Fourier Transform Infrared; Synucleins; Thiazoles; Threonine | 2000 |
A peptide motif consisting of glycine, alanine, and valine is required for the fibrillization and cytotoxicity of human alpha-synuclein.
Topics: Alanine; alpha-Synuclein; Amino Acid Motifs; Benzothiazoles; Circular Dichroism; Escherichia coli; Glycine; Humans; Microscopy, Atomic Force; Mutagenesis, Site-Directed; Mutation; Nerve Tissue Proteins; Peptides; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Synucleins; Thiazoles; Time Factors; Valine | 2003 |
Effects of the sequence and size of non-polar residues on self-assembly of amphiphilic peptides.
Topics: Alanine; Amino Acid Motifs; Amyloid; Benzothiazoles; Circular Dichroism; Congo Red; Gene Library; Glycine; Hydrogel, Polyethylene Glycol Dimethacrylate; Isoleucine; Leucine; Macromolecular Substances; Microscopy, Electron, Scanning; Microscopy, Electron, Transmission; Models, Molecular; Peptides; Phenylalanine; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Secondary; Temperature; Thiazoles; Ultraviolet Rays; Valine; X-Ray Diffraction | 2005 |
Deficiency of disulfide bonds facilitating fibrillogenesis of endostatin.
Topics: Alanine; Alzheimer Disease; Animals; Benzothiazoles; Cell Survival; Circular Dichroism; Disulfides; Endostatins; Escherichia coli; Fibril-Associated Collagens; Fluorescent Dyes; Glutathione; Hydrogen-Ion Concentration; Light; Microscopy, Atomic Force; Neovascularization, Pathologic; PC12 Cells; Protein Conformation; Protein Structure, Tertiary; Rats; Scattering, Radiation; Spectroscopy, Fourier Transform Infrared; Temperature; Tetrazolium Salts; Thiazoles; Time Factors; Tryptophan; Ultraviolet Rays | 2006 |
N- and C-terminal hydrophobic patches are involved in fibrillation of glucagon.
Topics: Acids; Alanine; Alkalies; Benzothiazoles; Glucagon; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Kinetics; Mutation; Spectrometry, Fluorescence; Thiazoles | 2006 |
The fluorescent amino acid p-cyanophenylalanine provides an intrinsic probe of amyloid formation.
Topics: Alanine; Amino Acid Sequence; Amyloid; Benzothiazoles; Diabetes Mellitus, Type 2; Fluorescence; Fluorescent Dyes; Humans; Islet Amyloid Polypeptide; Kinetics; Molecular Sequence Data; Nitriles; Phenylalanine; Point Mutation; Protein Binding; Thiazoles; Time Factors | 2008 |
Zn(II)- and Cu(II)-induced non-fibrillar aggregates of amyloid-beta (1-42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators.
Topics: Alanine; Amyloid; Amyloid beta-Peptides; Animals; Benzothiazoles; Cells, Cultured; Cerebral Cortex; Chelating Agents; Copper; Dose-Response Relationship, Drug; Histidine; Metallothionein 3; Microscopy, Electron, Transmission; Mutation; Nerve Tissue Proteins; Neurons; Peptide Fragments; Rats; Thiazoles; Time Factors; Zinc | 2009 |
Fine mapping of the amyloid β-protein binding site on myelin basic protein.
Topics: Alanine; Amyloid beta-Peptides; Benzothiazoles; Binding Sites; Humans; Magnetic Resonance Spectroscopy; Microscopy, Electron, Transmission; Mutagenesis, Site-Directed; Myelin Basic Protein; Peptide Fragments; Thiazoles | 2013 |
Enhanced molecular mobility of ordinarily structured regions drives polyglutamine disease.
Topics: Alanine; Allosteric Site; Amyloidogenic Proteins; Ataxin-3; Benzothiazoles; Catalytic Domain; Chromatography, High Pressure Liquid; Disease Progression; Escherichia coli; Genetic Variation; Humans; Machado-Joseph Disease; Microscopy, Electron, Transmission; Mutagenesis; Peptide Mapping; Peptides; Protein Binding; Protein Folding; Protein Structure, Secondary; Tandem Mass Spectrometry; Thiazoles | 2015 |
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 |