Evidence map›Paper›PMID 28754939›Full record

ArticleNature chemistry2017

Catalytic diversity in self-propagating peptide assemblies.

Tolulope O Omosun, Ming-Chien Hsieh, W Seth Childers, Dibyendu Das, Anil K Mehta, Neil R Anthony, Ting Pan, Martha A Grover, Keith M Berland, David G Lynn

Abstract read
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In one paragraph

Article in Nature chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

67 citing papers in PubMed, 238 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  6. Building Molecules by a Self-Replicator That Catalyzes Acyl Hydrazone Formation.Angewandte Chemie (International ed. in English) · 2026
    Article
  7. Emergent properties of supramolecular peptide assemblies.Chemical communications (Cambridge, England) · 2026
    Review
  8. Co-Assemblies Regulate the Catalytic Activity of Peptide Fibrils.Angewandte Chemie (International ed. in English) · 2026
    Article
  9. Regulating Promiscuous Catalysis via Substrate-Induced Transient Assembly.Angewandte Chemie (International ed. in English) · 2026
    Article
  10. Review
  11. Article
  12. The Ascent of Supramolecular Polymers and Gels in Asymmetric Catalysis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Site-selective peptide bond hydrolysis and ligation in water by short peptide-based assemblies.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article

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

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

10 authors at 2 institutions in 1 country.

Tolulope O OmosunDepartments of Chemistry and Biology, Emory University, Atlanta, Georgia 30322, USA.
Ming-Chien HsiehSchool of Chemical Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332, USA.
W Seth ChildersDepartments of Chemistry and Biology, Emory University, Atlanta, Georgia 30322, USA.
Dibyendu DasDepartments of Chemistry and Biology, Emory University, Atlanta, Georgia 30322, USA.
Anil K MehtaDepartments of Chemistry and Biology, Emory University, Atlanta, Georgia 30322, USA.ORCID 0000-0002-9867-151X
Neil R AnthonyDepartment of Physics, Emory University, Atlanta, Georgia 30322, USA.
Ting PanDepartments of Chemistry and Biology, Emory University, Atlanta, Georgia 30322, USA.
Martha A GroverSchool of Chemical Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332, USA.
Keith M BerlandDepartment of Physics, Emory University, Atlanta, Georgia 30322, USA.
David G LynnDepartments of Chemistry and Biology, Emory University, Atlanta, Georgia 30322, USA.
Emory University · USGeorgia Institute of Technology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein-only infectious agents known as prions exist within cellular matrices as populations of assembled polypeptide phases ranging from particles to amyloid fibres. These phases appear to undergo Darwinian-like selection and propagation, yet remarkably little is known about their accessible chemical and biological functions. Here we construct simple peptides that assemble into well-defined amyloid phases and define paracrystalline surfaces able to catalyse specific enantioselective chemical reactions. Structural adjustments of individual amino acid residues predictably control both the assembled crystalline order and their accessible catalytic repertoire. Notably, the density and proximity of the extended arrays of enantioselective catalytic sites achieve template-directed polymerization of new polymers. These diverse amyloid templates can now be extended as dynamic self-propagating templates for the construction of even more complex functional materials.

Indexed as

AldehydesAmyloidBinding SitesCatalysisNaphthalenesPeptidesProtein Conformation, beta-StrandProtein Multimerization6-methoxy-2-naphthaldehydeAldehydesAmyloidNaphthalenesPeptides

Identifiers

PMID28754939
OpenAlexW2594646845

What OpenQuestion holds

Textmetadata
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.