phenylalanine has been researched along with amyloid beta-peptides in 17 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 5 (29.41) | 29.6817 |
| 2010's | 12 (70.59) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Choe, H; Farzan, M; Leung, D; Schnitzler, CE; Vasilieva, N | 1 |
| Gordon, DJ; Meredith, SC | 1 |
| Schöneich, C; Williams, TD | 1 |
| Armirotti, A; Borghi, R; Damonte, G; Gelati, M; Ghetti, B; Giordano, R; Monaco, S; Noviello, C; Piccini, A; Russo, C; Russo, R; Tabaton, M; Zambenedetti, P; Zanusso, G | 1 |
| Meredith, SC; Orgel, JP; Sciarretta, KL; Tycko, R | 1 |
| Chen, YC; Chen, YR; Huang, HB; Lin, TH; Liu, HT; Lo, CJ; Shiao, MS; Su, CL; Wang, CC | 1 |
| Chang, P; Dai, X; Jiang, Z; Liu, W; Sun, Y; Xu, K; Zhu, S | 1 |
| Chen, R; Grinberg, I; Margel, S; Skaat, H | 1 |
| Chen, T; Liu, S; Lu, Y; Zhu, L; Zhu, S | 1 |
| Frölich, L; Hartmann, T; Hausner, L; Hentschel, F; Schmitt, HP; Tschäpe, JA | 1 |
| Falconer, IB; Hoatson, GL; Ostrovsky, D; Qiang, W; Vugmeyster, L | 1 |
| Adler, J; Huster, D; Korn, A; Krueger, M; Maiti, S; McLennan, S; Surendran, D | 1 |
| Huster, D; Korn, A; Krueger, M; Maiti, S; Surendran, D | 1 |
| Du, D; Elbassal, EA; Kent, TW; Lantz, R; Liu, H; Morris, C; Wojcikiewicz, EP | 1 |
| Fox, DM; Urbanc, B; Zhang, S | 1 |
| Carloni, P; Dong, X; Gräslund, A; Li, J; Liu, L; Liu, Y; Österlund, N | 1 |
| Luo, Y; Wei, G; Xie, L | 1 |
17 other study(ies) available for phenylalanine and amyloid beta-peptides
| Article | Year |
|---|---|
BACE2, a beta -secretase homolog, cleaves at the beta site and within the amyloid-beta region of the amyloid-beta precursor protein.
Topics: Alzheimer Disease; Amino Acid Sequence; Amino Acid Substitution; Amyloid beta-Peptides; Amyloid beta-Protein Precursor; Amyloid Precursor Protein Secretases; Arginine; Aspartic Acid Endopeptidases; Binding Sites; Cell Line; Cloning, Molecular; Endopeptidases; Gene Expression Profiling; Humans; Hydrogen-Ion Concentration; Molecular Sequence Data; Mutation, Missense; Nervous System; Netherlands; Peptide Fragments; Phenylalanine; Protein Processing, Post-Translational; Recombinant Fusion Proteins; RNA, Messenger; Sequence Homology, Amino Acid; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Substrate Specificity; Sweden | 2000 |
Probing the role of backbone hydrogen bonding in beta-amyloid fibrils with inhibitor peptides containing ester bonds at alternate positions.
Topics: Amino Acid Sequence; Amyloid beta-Peptides; Benzothiazoles; Congo Red; Cross-Linking Reagents; Diphenylhexatriene; Esters; Fluorescent Dyes; Humans; Hydrogen Bonding; Molecular Sequence Data; Peptide Fragments; Phenylalanine; Protein Binding; Protein Conformation; Spectrometry, Fluorescence; Spectrometry, Mass, Electrospray Ionization; Thiazoles; Ultracentrifugation | 2003 |
CU(II)-catalyzed oxidation of Alzheimer's disease beta-amyloid peptide and related sequences: remarkably different selectivities of neurotoxic betaAP1-40 and non-toxic betaAP40-1.
Topics: Amyloid beta-Peptides; Catalysis; Copper; Histidine; Humans; Models, Chemical; Molecular Structure; Oxidation-Reduction; Peptide Fragments; Phenylalanine; Spectrometry, Mass, Electrospray Ionization; Tyrosine | 2003 |
Association of a presenilin 1 S170F mutation with a novel Alzheimer disease molecular phenotype.
Topics: Adult; Alzheimer Disease; Amyloid beta-Peptides; Amyloid beta-Protein Precursor; Brain; DNA Mutational Analysis; Humans; Male; Mutation; Peptide Fragments; Phenotype; Phenylalanine; Presenilin-1; Serine | 2007 |
Evidence for novel beta-sheet structures in Iowa mutant beta-amyloid fibrils.
Topics: Amyloid; Amyloid beta-Peptides; Amyloid Neuropathies, Familial; Aspartic Acid; Benzothiazoles; Glutamic Acid; Humans; Kinetics; Leucine; Lysine; Microscopy, Electron, Transmission; Models, Molecular; Mutation, Missense; Nuclear Magnetic Resonance, Biomolecular; Peptide Fragments; Phenylalanine; Protein Structure, Secondary; Spectrometry, Fluorescence; Thiazoles; X-Ray Diffraction | 2009 |
Aβ40(L17A/F19A) mutant diminishes the aggregation and neurotoxicity of Aβ40.
Topics: Alanine; Alzheimer Disease; Amino Acid Substitution; Amyloid beta-Peptides; Animals; Cell Survival; Humans; Leucine; Mutation; Neurons; Nuclear Magnetic Resonance, Biomolecular; PC12 Cells; Peptide Fragments; Phenylalanine; Protein Conformation; Rats; Urea | 2011 |
Aβ-40 Y10F increases βfibrils formation but attenuates the neurotoxicity of amyloid-β peptide.
Topics: Alzheimer Disease; Amino Acid Substitution; Amyloid beta-Peptides; Animals; Cells, Cultured; Humans; Hydrogen Peroxide; Neurons; Peptide Fragments; Phenylalanine; Protein Aggregation, Pathological; Protein Folding; Protein Structure, Secondary; Rats, Sprague-Dawley; Tyrosine | 2012 |
Engineered polymer nanoparticles containing hydrophobic dipeptide for inhibition of amyloid-β fibrillation.
Topics: Amino Acids; Amyloid beta-Peptides; Biocompatible Materials; Cell Line, Tumor; Cell Survival; Dipeptides; Esters; Humans; Hydrophobic and Hydrophilic Interactions; Kinetics; Magnetic Resonance Spectroscopy; Nanoparticles; Particle Size; Peptide Fragments; Peptides; Phenylalanine; Polymers; Protein Structure, Secondary; Spectroscopy, Fourier Transform Infrared | 2012 |
Two nitrogen-containing ligands as inhibitors of metal-induced amyloid β-peptide aggregation.
Topics: Amyloid beta-Peptides; Aza Compounds; Boron Compounds; Chelating Agents; Copper; Dose-Response Relationship, Drug; Humans; Metals; Microscopy, Atomic Force; Peptide Fragments; Phenylalanine; Piperidines; Protein Conformation; Spectrometry, Fluorescence; Zinc | 2014 |
Clinical characterization of a presenilin 1 mutation (F177S) in a family with very early-onset Alzheimer's disease in the third decade of life.
Topics: Adult; Age of Onset; Aged; Alzheimer Disease; Amyloid beta-Peptides; Brain; Brain Waves; Cognition Disorders; Electroencephalography; Family Health; Female; Genetic Predisposition to Disease; Humans; Male; Mental Status Schedule; Middle Aged; Mutation; Peptide Fragments; Phenylalanine; Positron-Emission Tomography; Presenilin-1; Radiography; Serine | 2014 |
Solvent-Driven Dynamical Crossover in the Phenylalanine Side-Chain from the Hydrophobic Core of Amyloid Fibrils Detected by
Topics: Amino Acid Sequence; Amyloid; Amyloid beta-Peptides; Hydrophobic and Hydrophilic Interactions; Models, Molecular; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Peptide Fragments; Phenylalanine; Solvents; Temperature | 2017 |
Amyloid β (1-40) Toxicity Depends on the Molecular Contact between Phenylalanine 19 and Leucine 34.
Topics: Amyloid; Amyloid beta-Peptides; Kinetics; Leucine; Peptide Fragments; Phenylalanine; Protein Structure, Secondary | 2018 |
Ring structure modifications of phenylalanine 19 increase fibrillation kinetics and reduce toxicity of amyloid β (1-40).
Topics: Amyloid beta-Peptides; Animals; Cell Line; Cell Survival; Kinetics; Molecular Structure; Peptide Fragments; Phenylalanine; Rats | 2018 |
Residue-Specific Dynamics and Local Environmental Changes in Aβ40 Oligomer and Fibril Formation.
Topics: Amyloid; Amyloid beta-Peptides; Fluorescent Dyes; Hydrophobic and Hydrophilic Interactions; Kinetics; Mutagenesis; Peptide Fragments; Phenylalanine; Protein Aggregates; Spectrometry, Fluorescence | 2018 |
Elucidating the Role of Hydroxylated Phenylalanine in the Formation and Structure of Cross-Linked Aβ Oligomers.
Topics: Amino Acid Sequence; Amyloid beta-Peptides; Hydrogen Bonding; Molecular Dynamics Simulation; Peptide Fragments; Phenylalanine; Protein Aggregates; Protein Conformation; Protein Multimerization | 2019 |
Role of hydrophobic residues for the gaseous formation of helical motifs.
Topics: Amino Acid Sequence; Amyloid beta-Peptides; Gases; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Molecular Dynamics Simulation; Peptide Fragments; Phenylalanine; Protein Conformation, alpha-Helical | 2019 |
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 |