tryptophan has been researched along with Protein Aggregation, Pathological 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 | 0 (0.00) | 29.6817 |
| 2010's | 8 (80.00) | 24.3611 |
| 2020's | 2 (20.00) | 2.80 |
| Authors | Studies |
|---|---|
| Butts, CT; Freites, JA; Prytkova, V; Tobias, DJ; Wong, EK | 1 |
| Ayers, JI; Borchelt, DR; Brown, H; Cashman, NR; Crown, A; Fagerli, E; Galaleldeen, A; McAlary, L; Yerbury, JJ | 1 |
| Abu-Hussien, M; Gazit, E; Haj, E; Paul, A; Segal, D; Viswanathan, GK | 1 |
| Dyson, HJ; Sun, X; Wright, PE | 1 |
| Gazit, E; KrishnaKumar, VG; Paul, A; Segal, D | 1 |
| Crick, SL; Diamond, MI; Harmon, TS; Li, A; Pappu, RV; Posey, AE; Ruff, KM | 1 |
| Bosco, DA; Brown, RH; Hetz, C; Martínez Traub, F; Medinas, DB; Rozas, P; Woehlbier, U | 1 |
| Cashman, NR; Farrawell, NE; McAlary, L; Pokrishevsky, E; Sher, M; Yerbury, JJ; Zhao, B | 1 |
| Augusto, O; Coelho, FR; Cuccovia, IM; Iqbal, A; Lima, FS; Linares, E; Silva, DF | 1 |
| Anbarasu, A; Kumar, CV; Ramaiah, S; Swetha, RG | 1 |
10 other study(ies) available for tryptophan and Protein Aggregation, Pathological
| Article | Year |
|---|---|
Molecular Mechanism of Aggregation of the Cataract-Related γD-Crystallin W42R Variant from Multiscale Atomistic Simulations.
Topics: Amino Acid Substitution; Arginine; Cataract; gamma-Crystallins; Humans; Hydrophobic and Hydrophilic Interactions; Lens, Crystalline; Models, Molecular; Molecular Dynamics Simulation; Mutant Proteins; Protein Aggregates; Protein Aggregation, Pathological; Protein Conformation; Protein Denaturation; Protein Folding; Protein Multimerization; Tryptophan | 2019 |
Tryptophan residue 32 in human Cu-Zn superoxide dismutase modulates prion-like propagation and strain selection.
Topics: Amino Acid Substitution; Amyotrophic Lateral Sclerosis; Animals; Animals, Newborn; Disease Models, Animal; Female; Humans; Male; Mice; Mice, Transgenic; Mutagenesis, Site-Directed; Prions; Protein Aggregation, Pathological; Recombinant Fusion Proteins; Superoxide Dismutase-1; Tryptophan | 2020 |
An amyloidogenic hexapeptide from the cataract-associated γD-crystallin is a model for the full-length protein and is inhibited by naphthoquinone-tryptophan hybrids.
Topics: Amino Acid Sequence; Amyloid; Cataract; Dose-Response Relationship, Drug; gamma-Crystallins; Humans; Models, Molecular; Molecular Conformation; Naphthalenes; Oligopeptides; Protein Aggregates; Protein Aggregation, Pathological; Recombinant Proteins; Structure-Activity Relationship; Tryptophan | 2020 |
Fluorotryptophan Incorporation Modulates the Structure and Stability of Transthyretin in a Site-Specific Manner.
Topics: Amino Acid Substitution; Dimerization; Fluorescent Dyes; Kinetics; Models, Molecular; Mutation; Nuclear Magnetic Resonance, Biomolecular; Prealbumin; Protein Aggregation, Pathological; Protein Conformation; Protein Denaturation; Protein Interaction Domains and Motifs; Protein Multimerization; Protein Stability; Protein Unfolding; Recombinant Proteins; Tryptophan; Urea | 2017 |
Mechanistic insights into remodeled Tau-derived PHF6 peptide fibrils by Naphthoquinone-Tryptophan hybrids.
Topics: Alzheimer Disease; Amino Acid Sequence; Amyloid; Circular Dichroism; Humans; Models, Molecular; Molecular Structure; Naphthalenes; Peptide Fragments; Protein Aggregates; Protein Aggregation, Pathological; Protein Binding; Protein Conformation; Protein Interaction Domains and Motifs; Protein Multimerization; tau Proteins; Tryptophan | 2018 |
Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers.
Topics: Amino Acid Substitution; Binding Sites; Fluorescence; Humans; Huntingtin Protein; Image Processing, Computer-Assisted; Ligands; Microscopy, Electron, Transmission; Models, Molecular; Mutation; Negative Staining; Peptide Fragments; Polyglutamic Acid; Profilins; Proline-Rich Protein Domains; Protein Aggregation, Pathological; Protein Stability; Recombinant Proteins; Scattering, Small Angle; Solubility; Thermodynamics; Tryptophan | 2018 |
Endoplasmic reticulum stress leads to accumulation of wild-type SOD1 aggregates associated with sporadic amyotrophic lateral sclerosis.
Topics: Adult; Aged; Aged, 80 and over; Aging; Amyotrophic Lateral Sclerosis; Animals; Astrocytes; Brain; Cell Line; Disease Models, Animal; Endoplasmic Reticulum Stress; Female; Humans; Male; Mice; Mice, Inbred C57BL; Mice, Transgenic; Middle Aged; Motor Neurons; Mutation; Oxidation-Reduction; Protein Aggregation, Pathological; Protein Folding; Proteostasis; Spinal Cord; Superoxide Dismutase-1; Tryptophan; Tunicamycin; Unfolded Protein Response | 2018 |
Tryptophan 32-mediated SOD1 aggregation is attenuated by pyrimidine-like compounds in living cells.
Topics: Amino Acid Substitution; Flow Cytometry; HEK293 Cells; Humans; Mass Spectrometry; Mutant Proteins; Protein Aggregation, Pathological; Protein Stability; Pyrimidines; Superoxide Dismutase-1; Tryptophan | 2018 |
Oxidation of the tryptophan 32 residue of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity triggers the non-amyloid aggregation of the enzyme.
Topics: Amino Acid Sequence; Amino Acid Substitution; Bicarbonates; Humans; Molecular Sequence Data; Oxidation-Reduction; Protein Aggregation, Pathological; Protein Carbonylation; Protein Multimerization; Superoxide Dismutase; Superoxide Dismutase-1; Tryptophan | 2014 |
Tryptophan to Glycine mutation in the position 116 leads to protein aggregation and decreases the stability of the LITAF protein.
Topics: Codon; Genetic Predisposition to Disease; Glycine; Humans; Hydrogen Bonding; Models, Molecular; Molecular Dynamics Simulation; Mutation; Nuclear Proteins; Polymorphism, Single Nucleotide; Protein Aggregation, Pathological; Protein Conformation; Protein Stability; Reproducibility of Results; Structure-Activity Relationship; Transcription Factors; Tryptophan | 2015 |