Evidence map›Paper›PMID 30735358›Full record

ArticleAccounts of chemical research2019

Artificial Metalloenzymes Based on the Biotin-Streptavidin Technology: Enzymatic Cascades and Directed Evolution.

Alexandria Deliz Liang, Joan Serrano-Plana, Ryan L Peterson, Thomas R Ward

Open access · greenAbstract read
In one paragraph

Article in Accounts of chemical research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
11.8field-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

65 citing papers in PubMed, 191 citations in OpenAlex.

  1. Reprogramming NAD(P)Angewandte Chemie (International ed. in English) · 2026
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  5. Exploring PadR Proteins for Artificial Enzyme Design.Chembiochem : a European journal of chemical biology · 2026
    Article
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  7. Article
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  9. Journal of the American Chemical Society · 2025
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Designing Enzymatic Reactivity with an Expanded Palette.Chembiochem : a European journal of chemical biology · 2025
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

5 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

4 authors at 1 institution in 1 country.

Alexandria Deliz LiangDepartment of Chemistry , University of Basel , BPR1096, Mattenstrasse 24a , CH-4058 Basel , Switzerland.ORCID 0000-0002-9897-2822
Joan Serrano-PlanaDepartment of Chemistry , University of Basel , BPR1096, Mattenstrasse 24a , CH-4058 Basel , Switzerland.ORCID 0000-0003-2735-0943
Ryan L PetersonDepartment of Chemistry , University of Basel , BPR1096, Mattenstrasse 24a , CH-4058 Basel , Switzerland.
Thomas R WardDepartment of Chemistry , University of Basel , BPR1096, Mattenstrasse 24a , CH-4058 Basel , Switzerland.ORCID 0000-0001-8602-5468
University of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Artificial metalloenzymes (ArMs) result from anchoring a metal-containing moiety within a macromolecular scaffold (protein or oligonucleotide). The resulting hybrid catalyst combines attractive features of both homogeneous catalysts and enzymes. This strategy includes the possibility of optimizing the reaction by both chemical (catalyst design) and genetic means leading to achievement of a novel degree of (enantio)selectivity, broadening of the substrate scope, or increased activity, among others. In the past 20 years, the Ward group has exploited, among others, the biotin-(strept)avidin technology to localize a catalytic moiety within a well-defined protein environment. Streptavidin has proven versatile for the implementation of ArMs as it offers the following features: (i) it is an extremely robust protein scaffold, amenable to extensive genetic manipulation and mishandling, (ii) it can be expressed in E. coli to very high titers (up to >8 g·L

Indexed as

BiotinCatalysisCatalytic DomainDirected Molecular EvolutionEnzymesEscherichia coliHEK293 CellsHumansMetalloproteinsStreptavidinBiotinEnzymesMetalloproteinsStreptavidin

Identifiers

PMID30735358
PMCPMC6427477
OpenAlexW2912459103

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.