Evidence map›Paper›PMID 33763291›Full record

ArticleACS catalysis2021

Structure and Mechanism of

Karl A P Payne, Stephen A Marshall, Karl Fisher, Stephen E J Rigby, Matthew J Cliff, Reynard Spiess, Diego M Cannas, Igor Larrosa, Sam Hay, David Leys

Open access · hybridAbstract read
In one paragraph

Article in ACS catalysis, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

7 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. The Substrate Versatility of ΔMolecules (Basel, Switzerland) · 2026
    Article
  3. Review
  4. Enzymatic Conversion of COChemical reviews · 2023
    Review
  5. Article
  6. Article
  7. 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

10 authors at 1 institution in 1 country.

Karl A P PayneManchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom.
Stephen A MarshallManchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom.
Karl FisherManchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom.
Stephen E J RigbyManchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom.
Matthew J CliffManchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom.
Reynard SpiessManchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom.
Diego M CannasDepartment of Chemistry, University of Manchester, Chemistry Building, Oxford Road, Manchester M13 9PL, United Kingdom.
Igor LarrosaDepartment of Chemistry, University of Manchester, Chemistry Building, Oxford Road, Manchester M13 9PL, United Kingdom.
Sam HayManchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom.
David LeysManchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom.
University of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/P000622/1
6 · The paper itself

Abstract

The UbiD family of reversible (de)carboxylases depends on the recently discovered prenylated-FMN (prFMN) cofactor for activity. The model enzyme ferulic acid decarboxylase (Fdc1) decarboxylates unsaturated aliphatic acids via a reversible 1,3-cycloaddition process. Protein engineering has extended the Fdc1 substrate range to include (hetero)aromatic acids, although catalytic rates remain poor. This raises the question how efficient decarboxylation of (hetero)aromatic acids is achieved by other UbiD family members. Here, we show that the

Identifiers

PMID33763291
PMCPMC7976604
OpenAlexW3132022534

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.