Evidence map›Paper›PMID 35524737›Full record

ReviewAngewandte Chemie (International ed. in English)2022

Unlocking New Reactivities in Enzymes by Iminium Catalysis.

Guangcai Xu, Gerrit J Poelarends

Open access · hybridAbstract readReview
In one paragraph

Review in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

15 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Enzymatic 1,4-addition of 2-hydroxy-3-keto-glucal for β-selective aryl-Chemical communications (Cambridge, England) · 2026
    Article
  3. Building Molecules by a Self-Replicator That Catalyzes Acyl Hydrazone Formation.Angewandte Chemie (International ed. in English) · 2026
    Article
  4. Article
  5. Designing Enzymatic Reactivity with an Expanded Palette.Chembiochem : a European journal of chemical biology · 2025
    Review
  6. Review
  7. Transitioning enzyme catalysis towards photocatalysis.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2025
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. AsymmetricJournal of the American Chemical Society · 2023
    Article
  13. Article
  14. Article
  15. Unlocking New Reactivities in Enzymes by Iminium Catalysis.Angewandte Chemie (International ed. in English) · 2022
    Review
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

2 authors at 1 institution in 1 country.

Guangcai XuDepartment of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713, AV Groningen, The Netherlands.
Gerrit J PoelarendsDepartment of Chemical and Pharmaceutical Biology, Groningen Research Institute of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713, AV Groningen, The Netherlands.ORCID 0000-0002-6917-6368
University of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The application of biocatalysis in conquering challenging synthesis requires the constant input of new enzymes. Developing novel biocatalysts by absorbing catalysis modes from synthetic chemistry has yielded fruitful new-to-nature enzymes. Organocatalysis was originally bio-inspired and has become the third pillar of asymmetric catalysis. Transferring organocatalytic reactions back to enzyme platforms is a promising approach for biocatalyst creation. Herein, we summarize recent developments in the design of novel biocatalysts that adopt iminium catalysis, a fundamental branch in organocatalysis. By repurposing existing enzymes or constructing artificial enzymes, various biocatalysts for iminium catalysis have been created and optimized via protein engineering to promote valuable abiological transformations. Recent advances in iminium biocatalysis illustrate the power of combining chemomimetic biocatalyst design and directed evolution to generate useful new-to-nature enzymes.

Indexed as

Directed Molecular EvolutionProtein EngineeringBiocatalysisCatalysisEnzymesEnzymesBiocatalysisChemomimetic CatalysisIminium IonsOrganocatalysis

Identifiers

PMID35524737
PMCPMC9400869
OpenAlexW4229036473

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.