ArticleScientific reports2017
Using chirality to probe the conformational dynamics and assembly of intrinsically disordered amyloid proteins.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 46 citations in OpenAlex.
- AI-directed gene fusing prolongs the evolutionary half-life of synthetic gene circuits.Science advances · 2025Article
- A methodology for calculating the rarity of diverse proteins based on functional specificity and thermodynamic stability.PloS one · 2025Article
- Uncovering supramolecular chirality codes for the design of tunable biomaterials.Nature communications · 2024Article
- Insights and Perspectives on the Role of Proteostasis and Heat Shock Proteins in Fungal Infections.Microorganisms · 2023Review
- Impact of Non-Covalent Interactions of Chiral Linked Systems in Solution on Photoinduced Electron Transfer Efficiency.International journal of molecular sciences · 2023Article
- Photoinduced Processes in Lysine-Tryptophan-Lysine Tripeptide with L and D Tryptophan.International journal of molecular sciences · 2023Article
- Monitoring α-synuclein aggregation.Neurobiology of disease · 2023Review
- Stereoselectivity of Interaction of Nonsteroidal Anti-Inflammatory Drug S-Ketoprofen with L/D-Tryptophan in Phospholipid Membranes.Membranes · 2022Article
- Arrow of Time, Entropy, and Protein Folding: Holistic View on Biochirality.International journal of molecular sciences · 2022Review
- Chiral Linked Systems as a Model for Understanding D-Amino Acids Influence on the Structure and Properties of Amyloid Peptides.International journal of molecular sciences · 2022Review
- Optical Configuration Effect on the Structure and Reactivity of Diastereomers Revealed by Spin Effects and Molecular Dynamics Calculations.International journal of molecular sciences · 2021Article
- Understanding and controlling amyloid aggregation with chirality.Current opinion in chemical biology · 2021Review
- Role of Chiral Configuration in the Photoinduced Interaction of D- and L-Tryptophan with Optical Isomers of Ketoprofen in Linked Systems.International journal of molecular sciences · 2021Article
- Racemization in Post-Translational Modifications Relevance to Protein Aging, Aggregation and Neurodegeneration: Tip of the Iceberg.Symmetry · 2021Article
- Assessing Reproducibility in Amyloid β Research: Impact of Aβ Sources on Experimental Outcomes.Chembiochem : a European journal of chemical biology · 2020Article
- Stereoselectivity of Electron and Energy Transfer in the Quenching of (International journal of molecular sciences · 2020Article
- A DFT-Assisted Topological Analysis of Four Polymorphic, S-Shaped Aβ42 Fibril Structures.Chembiochem : a European journal of chemical biology · 2019Article
- Article
- Mapping the energy landscapes of supramolecular assembly by thermal hysteresis.Nature communications · 2018Article
- Shear-Induced Amyloid Formation in the Brain: III. The Roles of Shear Energy and Seeding in a Proposed Shear Model.Journal of Alzheimer's disease : JAD · 2018Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intrinsically disordered protein (IDP) conformers occupy large regions of conformational space and display relatively flat energy surfaces. Amyloid-forming IDPs, unlike natively folded proteins, have folding trajectories that frequently involve movements up shallow energy gradients prior to the "downhill" folding leading to fibril formation. We suggest that structural perturbations caused by chiral inversions of amino acid side-chains may be especially valuable in elucidating these pathways of IDP folding. Chiral inversions are subtle in that they do not change side-chain size, flexibility, hydropathy, charge, or polarizability. They allow focus to be placed solely on the question of how changes in amino acid side-chain orientation, and the resultant alterations in peptide backbone structure, affect a peptide's conformational landscape (Ramachandran space). If specific inversions affect folding and assembly, then the sites involved likely are important in mediating these processes. We suggest here a "focused chiral mutant library" approach for the unbiased study of amyloid-forming IDPs.
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