Evidence map›Paper›PMID 34094654›Full record

ArticleACS catalysis2019

Minimalist

Liam R Marshall, Oleksii Zozulia, Zsofia Lengyel-Zhand, Ivan V Korendovych

Abstract read
In one paragraph

Article in ACS catalysis, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Structure-activity relationships in catalytic amyloids.Journal of inorganic biochemistry · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Supramolecular Peptide Nanostructures Regulate Catalytic Efficiency and Selectivity.Angewandte Chemie (International ed. in English) · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Synergistic Interactions Are Prevalent in Catalytic Amyloids.Chembiochem : a European journal of chemical biology · 2020
    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.

Liam R MarshallDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA.
Oleksii ZozuliaDepartment 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.
Ivan V KorendovychDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA.

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

The field of protein design has grown enormously in the past few decades. In this review we discuss the minimalist approach to design of artificial enzymes, in which protein sequences are created with the minimum number of elements for folding and function. This method relies on identifying starting points in catalytically inert scaffolds for active site installation. The progress of the field from the original helical assemblies of the 1980s to the more complex structures of the present day is discussed, highlighting the variety of catalytic reactions which have been achieved using these methods. We outline the strengths and weaknesses of the minimalist approaches, describe representative design cases and put it in the general context of the

Indexed as

catalysisdesign approachesenzymologyminimalismProtein design

Identifiers

PMID34094654
PMCPMC8174531

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.