Evidence map›Paper›PMID 39055018›Full record

ArticleChemical science2024

Delineation of the complete reaction cycle of a natural Diels-Alderase.

Laurence Maschio, Catherine R Back, Jawaher Alnawah, James I Bowen, Samuel T Johns, Sbusisiwe Z Mbatha, Li-Chen Han, Nicholas R Lees, Katja Zorn, James E M Stach and 6 more

Abstract read
In one paragraph

Article in Chemical science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

16 authors.

Laurence MaschioSchool of Biochemistry, University Walk, University of Bristol BS8 1TD UK.
Catherine R BackSchool of Biochemistry, University Walk, University of Bristol BS8 1TD UK.
Jawaher AlnawahSchool of Chemistry, University of Bristol Cantock's Close BS8 1TS UK Chris.Willis@bristol.ac.uk.ORCID https://orcid.org/0009-0002-8617-9445
James I BowenSchool of Chemistry, University of Bristol Cantock's Close BS8 1TS UK Chris.Willis@bristol.ac.uk.ORCID https://orcid.org/0000-0002-1596-4174
Samuel T JohnsSchool of Biochemistry, University Walk, University of Bristol BS8 1TD UK.
Sbusisiwe Z MbathaSchool of Chemistry, University of Bristol Cantock's Close BS8 1TS UK Chris.Willis@bristol.ac.uk.
Li-Chen HanSchool of Chemistry, University of Bristol Cantock's Close BS8 1TS UK Chris.Willis@bristol.ac.uk.
Nicholas R LeesSchool of Chemistry, University of Bristol Cantock's Close BS8 1TS UK Chris.Willis@bristol.ac.uk.
Katja ZornDiscovery Sciences, Biopharmaceuticals R&D, AstraZeneca Pepparedsleden 1 431 83 Mölndal Sweden.
James E M StachSchool of Natural and Environmental Sciences, Newcastle University NE1 7RU UK paul.race1@newcastle.ac.uk.ORCID https://orcid.org/0000-0001-8787-2407
Martin A HayesDiscovery Sciences, Biopharmaceuticals R&D, AstraZeneca Pepparedsleden 1 431 83 Mölndal Sweden.ORCID https://orcid.org/0000-0002-2640-8464
Marc W van der KampSchool of Biochemistry, University Walk, University of Bristol BS8 1TD UK.ORCID https://orcid.org/0000-0002-8060-3359
Christopher R PudneyDepartment of Biology and Biochemistry, University of Bath Claverton Down BA2 7AY UK.
Steven G BurstonSchool of Biochemistry, University Walk, University of Bristol BS8 1TD UK.ORCID https://orcid.org/0000-0003-1848-1853
Christine L WillisSchool of Chemistry, University of Bristol Cantock's Close BS8 1TS UK Chris.Willis@bristol.ac.uk.ORCID https://orcid.org/0000-0002-3919-3642
Paul R RaceSchool of Natural and Environmental Sciences, Newcastle University NE1 7RU UK paul.race1@newcastle.ac.uk.ORCID https://orcid.org/0000-0003-0184-5630

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Diels-Alder reaction is one of the most effective methods for the synthesis of substituted cyclohexenes. The development of protein catalysts for this reaction remains a major priority, affording new sustainable routes to high value target molecules. Whilst a small number of natural enzymes have been shown capable of catalysing [4 + 2] cycloadditions, there is a need for significant mechanistic understanding of how these prospective Diels-Alderases promote catalysis to underpin their development as biocatalysts for use in synthesis. Here we present a molecular description of the complete reaction cycle of the

Identifiers

PMID39055018
PMCPMC11268479

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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.