ArticleThe journal of physical chemistry. B2011
Probing amyloid fibril growth by two-dimensional near-ultraviolet spectroscopy.
Article in The journal of physical chemistry. B, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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
6 citing papers in PubMed, 14 citations in OpenAlex.
- Machine learning recognition of protein secondary structures based on two-dimensional spectroscopic descriptors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Near-Ultraviolet Circular Dichroism and Two-Dimensional Spectroscopy of Polypeptides.Molecules (Basel, Switzerland) · 2021Article
- Disentangling Peptide Configurations via Two-Dimensional Electronic Spectroscopy: Ab Initio Simulations Beyond the Frenkel Exciton Hamiltonian.The journal of physical chemistry letters · 2014Article
- Two-dimensional stimulated resonance Raman spectroscopy study of the Trp-cage peptide folding.Physical chemistry chemical physics : PCCP · 2013Article
- Monitoring the folding of Trp-cage peptide by two-dimensional infrared (2DIR) spectroscopy.The journal of physical chemistry. B · 2013Article
- Distinguishing amyloid fibril structures in Alzheimer's disease (AD) by two-dimensional ultraviolet (2DUV) spectroscopy.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Keeping track of the aggregation kinetics of amyloid fibrils is essential for understanding their formation mechanism and eventually developing treatments for misfolded protein-related diseases. A simulation study of a series of Aβ(9-40) amyloid fibrils with different size shows that novel two-dimensional near-ultraviolet (2DNUV) spectra contain characteristic signatures of interactions between peptides. Chiral 2DNUV signals show a larger degree of exciton delocalization compared to their nonchiral counterparts. Intensities of specific peaks provide a direct measure of the number of peptides in a fibril. These signals could be used to monitor the fibril growth kinetics, one peptide at a time.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.