Evidence map›Paper›PMID 29556104›Full record

ArticleNature chemical biology2018

Structural basis for backbone N-methylation by an interrupted adenylation domain.

Shogo Mori, Allan H Pang, Taylor A Lundy, Atefeh Garzan, Oleg V Tsodikov, Sylvie Garneau-Tsodikova

Abstract read
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In one paragraph

Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
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  6. Article
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  11. Structural Studies of Modular Nonribosomal Peptide Synthetases.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  12. (mLife · 2022
    Article
  13. Review
  14. Article
  15. Article
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  19. Biosynthesis of depsipeptides, or Depsi: The peptides with varied generations.Protein science : a publication of the Protein Society · 2020
    Review
  20. 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.

Shogo MoriDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY, USA.
Allan H PangDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY, USA.
Taylor A LundyDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY, USA.
Atefeh GarzanDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY, USA.
Oleg V TsodikovDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY, USA. oleg.tsodikov@uky.edu.
Sylvie Garneau-TsodikovaDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY, USA. sylviegtsodikova@uky.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interrupted adenylation domains are enigmatic fusions, in which one enzyme is inserted into another to form a highly unusual bifunctional enzyme. We present the first crystal structure of an interrupted adenylation domain that reveals a unique embedded methyltransferase. The structure and functional data provide insight into how these enzymes N-methylate amino acid precursors en route to nonribosomal peptides.

Indexed as

MethylationAdenosine MonophosphateAmino AcidsCatalysisCatalytic DomainCrystallography, X-RayEnzymesEscherichia coliIminesKineticsPeptidesPeptide SynthasesProtein DomainsSubstrate SpecificityTime FactorsAdenosine MonophosphateAmino AcidsEnzymesIminesPeptidesPeptide Synthases

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Registered trials

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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.