Evidence map›Paper›PMID 24651196›Full record

ArticleNature chemistry2014

Short peptides self-assemble to produce catalytic amyloids.

Caroline M Rufo, Yurii S Moroz, Olesia V Moroz, Jan Stöhr, Tyler A Smith, Xiaozhen Hu, William F DeGrado, Ivan V Korendovych

Open access · greenAbstract read
In one paragraph

Article in Nature chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 205 papers.

0numbers the graph read from it
0cells of the map it votes in
205citing papers in PubMed
21.2field-weighted citation impact, top 1% of its field
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

205 citing papers in PubMed, 647 citations in OpenAlex.

  1. Article
  2. Review
  3. Peptides adopt stable omega-loop structures in concentrated sulfuric acid.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Reverse-engineering amyloid strains with generative protein design.bioRxiv : the preprint server for biology · 2026
    Article
  8. Article
  9. Article
  10. COACS applied materials & interfaces · 2026
    Article
  11. Article
  12. Article
  13. Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  14. Structure-activity relationships in catalytic amyloids.Journal of inorganic biochemistry · 2026
    Article
  15. Article
  16. Co-Assemblies Regulate the Catalytic Activity of Peptide Fibrils.Angewandte Chemie (International ed. in English) · 2026
    Article
  17. Article
  18. Review
  19. The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  20. Article

145 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Caroline M Rufo1] Department of Chemistry, Syracuse University, Syracuse, New York 13244, USA [2].
Yurii S Moroz1] Department of Chemistry, Syracuse University, Syracuse, New York 13244, USA [2].
Olesia V Moroz1] Department of Chemistry, Syracuse University, Syracuse, New York 13244, USA [2].
Jan StöhrInstitute for Neurodegenerative Diseases and Department of Neurology, University of California - San Francisco, San Francisco, California 94143, USA.
Tyler A SmithDepartment of Chemistry, Syracuse University, Syracuse, New York 13244, USA.
Xiaozhen HuDepartment of Pharmaceutical Chemistry, University of California - San Francisco, Francisco, California 94158, USA.
William F DeGradoDepartment of Pharmaceutical Chemistry, University of California - San Francisco, Francisco, California 94158, USA.
Ivan V KorendovychDepartment of Chemistry, Syracuse University, Syracuse, New York 13244, USA.
Syracuse University · US

Funding

De novo design of alpha-helical bundlesR37GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2004 to 2013
$3.6M
DE NOVO DESIGN OF ALPHA HELICAL BUNDLESR01GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1996 to 2016
$2.4M
NIGMS NIH HHS GM54616NIGMS NIH HHS R01 GM054616NIGMS NIH HHS R37 GM054616
6 · The paper itself

Abstract

Enzymes fold into unique three-dimensional structures, which underlie their remarkable catalytic properties. The requirement to adopt a stable, folded conformation is likely to contribute to their relatively large size (>10,000 Da). However, much shorter peptides can achieve well-defined conformations through the formation of amyloid fibrils. To test whether short amyloid-forming peptides might in fact be capable of enzyme-like catalysis, we designed a series of seven-residue peptides that act as Zn(2+)-dependent esterases. Zn(2+) helps stabilize the fibril formation, while also acting as a cofactor to catalyse acyl ester hydrolysis. These results indicate that prion-like fibrils are able to not only catalyse their own formation, but they can also catalyse chemical reactions. Thus, they might have served as intermediates in the evolution of modern-day enzymes. These results also have implications for the design of self-assembling nanostructured catalysts including ones containing a variety of biological and non-biological metal ions.

Indexed as

AmyloidCarbonic AnhydrasesCatalysisHumansHydrolysisMicroscopy, Electron, TransmissionPeptidesProtein ConformationZincAmyloidCarbonic AnhydrasesPeptidesZinc

Identifiers

PMID24651196
PMCPMC3996680
OpenAlexW1971948710

What OpenQuestion holds

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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.