Evidence map›Paper›PMID 34425319›Full record

ReviewCurrent opinion in chemical biology2021

Catalytic amyloids: Is misfolding folding?

Liam R Marshall, Ivan V Korendovych

Abstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  3. Structure-activity relationships in catalytic amyloids.Journal of inorganic biochemistry · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Stopped-flow measurement of COMethods in enzymology · 2024
    Article
  10. Chemical catalysis by biological amyloids.Biochemical Society transactions · 2023
    Article
  11. Review
  12. Article
  13. EMBER multidimensional spectral microscopy enables quantitative determination of disease- and cell-specific amyloid strains.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Article
  15. Review
  16. Review
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.

Liam R MarshallDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA.
Ivan V KorendovychDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA. Electronic address: ikorendo@syr.edu.

Funding

Understanding Evolution of Protein Function Through Design.R35GM119634 · NIGMS · SYRACUSE UNIVERSITY · PI KORENDOVYCH, IVAN V · 2016 to 2025
$4.3M
NIGMS NIH HHS R35 GM119634
6 · The paper itself

Abstract

Originally regarded as a disease symptom, amyloids have shown a rich diversity of functions, including biologically beneficial ones. As such, the traditional view of polypeptide aggregation into amyloid-like structures being 'misfolding' should rather be viewed as 'alternative folding.' Various amyloid folds have been recently used to create highly efficient catalysts with specific catalytic efficiencies rivaling those of enzymes. Here we summarize recent developments and applications of catalytic amyloids, derived from both de novo and bioinspired designs, and discuss how progress in the last 2 years reflects on the field as a whole.

Indexed as

AmyloidPeptidesCatalysisProtein FoldingAmyloidPeptidesAmyloidCatalysisPeptideSelf-assembly

Identifiers

PMID34425319
PMCPMC8585703

What OpenQuestion holds

Textmetadata
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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.