tryptophan has been researched along with amyloid beta-peptides in 8 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 2 (25.00) | 29.6817 |
| 2010's | 6 (75.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Berthoumieu, O; Derreumaux, P; Doig, AJ; Faller, P; Nguyen, PH; Tarus, B | 1 |
| Akagi, T; Takashima, A; Yoshiike, Y | 1 |
| Ding, H; Gafni, A; Lee, EL; Schauerte, JA; Steel, DG; Wisser, KC; Wong, PT | 1 |
| Ajit, D; Gallazzi, F; Nichols, MR; Touchette, JC; Williams, LL | 1 |
| Gallazzi, F; McDonough, RT; Nichols, MR; Paranjape, G | 1 |
| Chen, S; Dudzik, CG; Grant, GP; Hao, Y; Jiang, D; Millhauser, GL; Patel, S; Zhang, L; Zhou, F | 1 |
| Caflisch, A; Convertino, M; Gazit, E; Pellarin, R; Scherzer-Attali, R; Segal, D | 1 |
| Luo, Y; Wei, G; Xie, L | 1 |
8 other study(ies) available for tryptophan and amyloid beta-peptides
| Article | Year |
|---|---|
Molecular structure of the NQTrp inhibitor with the Alzheimer Aβ1-28 monomer.
Topics: Amyloid beta-Peptides; Humans; Kinetics; Molecular Dynamics Simulation; Naphthoquinones; Peptide Fragments; Protein Binding; Protein Folding; Protein Multimerization; Protein Structure, Secondary; Thermodynamics; Tryptophan | 2015 |
Surface structure of amyloid-beta fibrils contributes to cytotoxicity.
Topics: Acetylation; Amyloid beta-Peptides; Animals; Benzothiazoles; Carrier Proteins; Cattle; Cell Survival; Cells, Cultured; Fluorescence; Humans; Kidney; Maltose-Binding Proteins; Microscopy, Electron, Transmission; Peptide Fragments; Plaque, Amyloid; Thiazoles; Tryptophan | 2007 |
Amyloid-beta membrane binding and permeabilization are distinct processes influenced separately by membrane charge and fluidity.
Topics: Amyloid beta-Peptides; Binding Sites; Cell Membrane Permeability; Circular Dichroism; Fluorescence Resonance Energy Transfer; Humans; Lipid Bilayers; Liposomes; Molecular Weight; Peptide Fragments; Tryptophan | 2009 |
Probing the amyloid-beta(1-40) fibril environment with substituted tryptophan residues.
Topics: Amino Acid Sequence; Amino Acid Substitution; Amyloid beta-Peptides; Benzothiazoles; Hydrophobic and Hydrophilic Interactions; Molecular Sequence Data; Peptide Fragments; Protein Structure, Secondary; Spectrometry, Fluorescence; Thiazoles; Tryptophan | 2010 |
Substituted tryptophans at amyloid-β(1-40) residues 19 and 20 experience different environments after fibril formation.
Topics: Alzheimer Disease; Amyloid beta-Peptides; Fluorescence; Humans; Hydrophobic and Hydrophilic Interactions; Peptide Fragments; Protein Conformation; Tryptophan | 2011 |
The elevated copper binding strength of amyloid-β aggregates allows the sequestration of copper from albumin: a pathway to accumulation of copper in senile plaques.
Topics: Amino Acid Substitution; Amyloid beta-Peptides; Chromatography, Gel; Copper; Electron Spin Resonance Spectroscopy; Histidine; Humans; Kinetics; Microscopy, Atomic Force; Models, Molecular; Molecular Weight; Mutant Proteins; Peptide Fragments; Plaque, Amyloid; Protein Denaturation; Serum Albumin; Serum Albumin, Human; Spectrometry, Fluorescence; Tryptophan | 2013 |
Methylations of tryptophan-modified naphthoquinone affect its inhibitory potential toward Aβ aggregation.
Topics: Alzheimer Disease; Amyloid beta-Peptides; Fluorescence Polarization; Humans; Hydrogen Bonding; Molecular Dynamics Simulation; Naphthoquinones; Peptide Fragments; Structure-Activity Relationship; Tryptophan | 2013 |
Aβ(16-22) peptides can assemble into ordered β-barrels and bilayer β-sheets, while substitution of phenylalanine 19 by tryptophan increases the population of disordered aggregates.
Topics: Amino Acid Substitution; Amyloid beta-Peptides; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Molecular Dynamics Simulation; Peptide Fragments; Phenylalanine; Protein Structure, Secondary; Temperature; Thermodynamics; Tryptophan | 2013 |