Evidence map›Paper›PMID 35013184›Full record

ArticleNature communications2022

Aminoacyl chain translocation catalysed by a type II thioesterase domain in an unusual non-ribosomal peptide synthetase.

Shan Wang, William D G Brittain, Qian Zhang, Zhou Lu, Ming Him Tong, Kewen Wu, Kwaku Kyeremeh, Matthew Jenner, Yi Yu, Steven L Cobb and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
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  4. Review
  5. Article
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  7. Article
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  9. Review
  10. Article
  11. Review
  12. Article
  13. Thiamyxins: Structure and Biosynthesis of Myxobacterial RNA-Virus Inhibitors.Angewandte Chemie (International ed. in English) · 2022
    Article
  14. 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

11 authors.

Shan Wang *Department of Chemistry, University of Aberdeen, Aberdeen, AB24 3UE, UK.ORCID http://orcid.org/0000-0002-9573-7579
William D G Brittain *Department of Chemistry, Durham University, Science Site, Durham, DH1 3LE, UK.ORCID http://orcid.org/0000-0002-2876-5895
Qian Zhang *Key Laboratory of Combinatorial Biosynthesis and Drug Discovery (MOE) and Hubei Province Engineering and Technology Research Centre for Fluorinated Pharmaceuticals, School of Pharmaceutical Sciences, Wuhan University, Wuhan, 430071, China.
Zhou LuDepartment of Chemistry, University of Aberdeen, Aberdeen, AB24 3UE, UK.
Ming Him TongDepartment of Chemistry, University of Aberdeen, Aberdeen, AB24 3UE, UK.
Kewen WuDepartment of Chemistry, University of Aberdeen, Aberdeen, AB24 3UE, UK.
Kwaku KyeremehDepartment of Chemistry, University of Ghana, P.O. Box LG56, Legon-Accra, Ghana.ORCID http://orcid.org/0000-0002-3644-9497
Matthew JennerDepartment of Chemistry, University of Warwick, Coventry, CV4 7AL, UK. M.Jenner@warwick.ac.uk.ORCID http://orcid.org/0000-0003-2317-3011
Yi YuKey Laboratory of Combinatorial Biosynthesis and Drug Discovery (MOE) and Hubei Province Engineering and Technology Research Centre for Fluorinated Pharmaceuticals, School of Pharmaceutical Sciences, Wuhan University, Wuhan, 430071, China. yu_yi@whu.edu.cn.ORCID http://orcid.org/0000-0001-8590-0574
Steven L CobbDepartment of Chemistry, Durham University, Science Site, Durham, DH1 3LE, UK. s.l.cobb@durham.ac.uk.ORCID http://orcid.org/0000-0002-3790-7023
Hai DengDepartment of Chemistry, University of Aberdeen, Aberdeen, AB24 3UE, UK. h.deng@abdn.ac.uk.ORCID http://orcid.org/0000-0002-0047-0622

Funding

Biotechnology and Biological Sciences Research Council BB/M017982/1Biotechnology and Biological Sciences Research Council BB/P003656/1Biotechnology and Biological Sciences Research Council BB/R00479X/1Biotechnology and Biological Sciences Research Council BB/R01212/1Biotechnology and Biological Sciences Research Council BB/R012121/1Medical Research Council MR/S00520X/1
6 · The paper itself

Abstract

Non-Ribosomal Peptide Synthetases (NRPSs) assemble a diverse range of natural products with important applications in both medicine and agriculture. They consist of several multienzyme subunits that must interact with each other in a highly controlled manner to facilitate efficient chain transfer, thus ensuring biosynthetic fidelity. Several mechanisms for chain transfer are known for NRPSs, promoting structural diversity. Herein, we report the first biochemically characterized example of a type II thioesterase (TE

Indexed as

CatalysisEscherichia coliFatty Acid SynthasesMetabolic EngineeringPeptide SynthasesProtein DomainsThiolester HydrolasesFatty Acid Synthasesnon-ribosomal peptide synthasePeptide Synthasesthioesterase IIThiolester Hydrolases

Identifiers

PMID35013184
PMCPMC8748450

What OpenQuestion holds

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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.