Evidence map›Paper›PMID 36906667›Full record

ArticleScientific reports2023

Cryo-EM structure of a catalytic amyloid fibril.

Thomas Heerde, Akanksha Bansal, Matthias Schmidt, Marcus Fändrich

Full text read
In one paragraph

Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  2. Structure-activity relationships in catalytic amyloids.Journal of inorganic biochemistry · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023
    Review
  9. 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

4 authors.

Thomas HeerdeInstitute of Protein Biochemistry, Ulm University, 89081, Ulm, Germany. thomas.heerde@uni-ulm.de.
Akanksha BansalInstitute of Protein Biochemistry, Ulm University, 89081, Ulm, Germany.
Matthias SchmidtInstitute of Protein Biochemistry, Ulm University, 89081, Ulm, Germany.
Marcus FändrichInstitute of Protein Biochemistry, Ulm University, 89081, Ulm, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Catalytic amyloid fibrils are novel types of bioinspired, functional materials that combine the chemical and mechanical robustness of amyloids with the ability to catalyze a certain chemical reaction. In this study we used cryo-electron microcopy to analyze the amyloid fibril structure and the catalytic center of amyloid fibrils that hydrolyze ester bonds. Our findings show that catalytic amyloid fibrils are polymorphic and consist of similarly structured, zipper-like building blocks that consist of mated cross-β sheets. These building blocks define the fibril core, which is decorated by a peripheral leaflet of peptide molecules. The observed structural arrangement differs from previously described catalytic amyloid fibrils and yielded a new model of the catalytic center.

Indexed as

AmyloidAmyloid beta-PeptidesCryoelectron MicroscopyProtein Conformation, beta-StrandAmyloidAmyloid beta-Peptides

Identifiers

PMID36906667
PMCPMC10008563

What OpenQuestion holds

Textfull text, public
LicenceCC BY
measurements read18
Read underepoch 390

Registered trials

None linked

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.