ArticleProtein science : a publication of the Protein Society2020
β-amyloid model core peptides: Effects of hydrophobes and disulfides.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- Elucidating the Oligomerization and Cellular Interactions of a Trimer Derived from Aβ through Fluorescence and Mass Spectrometric Studies.ACS chemical neuroscience · 2022Article
- Synthesis and study of macrocyclic β-hairpin peptides for investigating amyloid oligomers.Methods in enzymology · 2021Article
- β-amyloid model core peptides: Effects of hydrophobes and disulfides.Protein science : a publication of the Protein Society · 2020Article
- Intein-mediated recombinant expression of monomeric B22Asp desB30 insulin.BMC biotechnology · 2020Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The mechanism by which a disordered peptide nucleates and forms amyloid is incompletely understood. A central domain of β-amyloid (Aβ21-30) has been proposed to have intrinsic structural propensities that guide the limited formation of structure in the process of fibrillization. In order to test this hypothesis, we examine several internal fragments of Aβ, and variants of these either cyclized or with an N-terminal Cys. While Aβ21-30 and variants were always monomeric and unstructured (circular dichroism (CD) and nuclear magnetic resonance spectroscopy (NMRS)), we found that the addition of flanking hydrophobic residues in Aβ16-34 led to formation of typical amyloid fibrils. NMR showed no long-range nuclear overhauser effect (nOes) in Aβ21-30, Aβ16-34, or their variants, however. Serial
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Registered trials
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