Evidence map›Paper›PMID 38269041›Full record

ArticleACS catalysis2024

Broad Spectrum Enantioselective Amide Bond Synthetase from

Qingyun Tang, Mark Petchey, Benjamin Rowlinson, Thomas J Burden, Ian J S Fairlamb, Gideon Grogan

Open access · hybridAbstract read
In one paragraph

Article in ACS catalysis, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
3.5field-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

6 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. A tailored CoA ligase-Nature catalysis · 2026
    Article
  5. Genome Mining of Isoindolinone-Containing Peptide Natural Products.Journal of the American Chemical Society · 2025
    Article
  6. 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

6 authors at 1 institution in 1 country.

Qingyun TangDepartment of Chemistry, University of York, Heslington, York YO10 5DD, U.K.
Mark PetcheyDepartment of Chemistry, University of York, Heslington, York YO10 5DD, U.K.ORCID https://orcid.org/0000-0002-5196-4948
Benjamin RowlinsonDepartment of Chemistry, University of York, Heslington, York YO10 5DD, U.K.
Thomas J BurdenDepartment of Chemistry, University of York, Heslington, York YO10 5DD, U.K.ORCID https://orcid.org/0000-0001-9418-686X
Ian J S FairlambDepartment of Chemistry, University of York, Heslington, York YO10 5DD, U.K.ORCID https://orcid.org/0000-0002-7555-2761
Gideon GroganDepartment of Chemistry, University of York, Heslington, York YO10 5DD, U.K.ORCID https://orcid.org/0000-0003-1383-7056
University of York · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The synthesis of amide bonds is one of the most frequently performed reactions in pharmaceutical synthesis, but the requirement for stoichiometric quantities of coupling agents and activated substrates in established methods has prompted interest in biocatalytic alternatives. Amide Bond Synthetases (ABSs) actively catalyze both the ATP-dependent adenylation of carboxylic acid substrates and their subsequent amidation using an amine nucleophile, both within the active site of the enzyme, enabling the use of only a small excess of the amine partner. We have assessed the ability of an ABS from

Identifiers

PMID38269041
PMCPMC10804368
OpenAlexW4390636492

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.