Evidence map›Paper›PMID 32329215›Full record

ArticleChembiochem : a European journal of chemical biology2020

Synergistic Interactions Are Prevalent in Catalytic Amyloids.

Liam R Marshall, Megha Jayachandran, Zsofia Lengyel-Zhand, Caroline M Rufo, Austin Kriews, Min-Chul Kim, Ivan V Korendovych

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2020. 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. Structure-activity relationships in catalytic amyloids.Journal of inorganic biochemistry · 2026
    Article
  3. Article
  4. Article
  5. Catalytic amyloids: Is misfolding folding?Current opinion in chemical biology · 2021
    Review
  6. Review
  7. Catalytic Amyloids as Novel Synthetic Hydrolases.International journal of molecular sciences · 2021
    Review
  8. 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

7 authors.

Liam R MarshallDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.ORCID 0000-0002-5698-4841
Megha JayachandranDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Zsofia Lengyel-ZhandDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Caroline M RufoDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Austin KriewsDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Min-Chul KimDepartment 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.ORCID 0000-0001-8144-783X

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

Interactions between multiple functional groups are key to catalysis. Previously, we reported synergistic interactions in catalytic amyloids formed by mixtures of heptameric peptides that lead to significant improvements in esterase activity. Herein, we describe the in-depth investigation of synergistic interactions within a family of amyloid fibrils, exploring the results of functional group interactions, the effects of chirality and the use of mixed enantiomers within fibrils. Remarkably, we find that synergistic interactions (either positive or negative) are found in the vast majority of binary mixtures of catalytic amyloid-forming peptides. The productive arrangements of functionalities rapidly identified by mixing different peptides will undoubtedly lead to the development of more active catalysts for a variety of different transformations.

Indexed as

AmyloidCatalysisPeptidesAmyloidPeptidesamyloidscatalysispeptidesself-assemblysynergistic interactions

Identifiers

PMID32329215
PMCPMC7605102

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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.