Evidence map›Paper›PMID 34494356›Full record

ArticleAngewandte Chemie (International ed. in English)2021

Chiral Selectivity of Secondary Nucleation in Amyloid Fibril Propagation.

Mattias Törnquist, Sara Linse

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023
    Review
  4. Review
  5. Direct observation of secondary nucleation along the fibril surface of the amyloidProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Chemical science · 2023
    Article
  7. Article
  8. Chiral Selectivity of Secondary Nucleation in Amyloid Fibril Propagation.Angewandte Chemie (International ed. in English) · 2021
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Mattias TörnquistBiochemistry and Structural Biology, Lund University, Kemicentrum, Box 118, 22100, Lund, Sweden.ORCID 0000-0001-7513-7288
Sara LinseBiochemistry and Structural Biology, Lund University, Kemicentrum, Box 118, 22100, Lund, Sweden.ORCID 0000-0001-9629-7109

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chirality is a fundamental feature of asymmetric molecules and of critical importance for intermolecular interactions. The growth of amyloid fibrils displays a strong enantioselectivity, which is manifested as elongation through the addition of monomers of the same, but not opposite, chirality as the parent aggregate. Here we ask whether also secondary nucleation on the surface of amyloid fibrils, of relevance for toxicity, is governed by the chirality of the nucleating monomers. We use short amyloid peptides (Aβ20-34 and IAPP20-29) with all residues as L- or all D-enantiomer in self and cross-seeding experiments with low enough seed concentration that any acceleration of fibril formation is dominated by secondary nucleation. We find a strong enantio-specificity of this auto-catalytic process with secondary nucleation being observed in the self-seeding experiments only. The results highlight a role of secondary nucleation in strain propagation.

Indexed as

AmyloidHumansProtein ConformationAmyloidaggregationamyloid-beta peptidesautocatalysisenantioselectivitysecondary nucleation

Identifiers

PMID34494356
PMCPMC8596840

What OpenQuestion holds

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Registered trials

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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.