Evidence map›Paper›PMID 28522606›Full record

ArticleThe Journal of biological chemistry2017

Structural analysis of the dual-function thioesterase SAV606 unravels the mechanism of Michael addition of glycine to an α,β-unsaturated thioester.

Taichi Chisuga, Akimasa Miyanaga, Fumitaka Kudo, Tadashi Eguchi

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Biosynthesis of isonitrile lipopeptides.Current opinion in chemical biology · 2024
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Thioesterase enzyme families: Functions, structures, and mechanisms.Protein science : a publication of the Protein Society · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Isonitrile Formation by a Non-Heme Iron(II)-Dependent Oxidase/Decarboxylase.Angewandte Chemie (International ed. in English) · 2018
    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

4 authors.

Taichi ChisugaFrom the Department of Chemistry and Materials Science and.
Akimasa MiyanagaDepartment of Chemistry, Tokyo Institute of Technology, O-okayama, Meguro-ku, Tokyo 152-8551, Japan.ORCID 0000-0003-2219-6051
Fumitaka KudoDepartment of Chemistry, Tokyo Institute of Technology, O-okayama, Meguro-ku, Tokyo 152-8551, Japan.
Tadashi EguchiFrom the Department of Chemistry and Materials Science and eguchi@chem.titech.ac.jp.ORCID 0000-0002-7830-7104

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thioesterases catalyze hydrolysis of acyl thioesters to release carboxylic acid or macrocyclization to produce the corresponding macrocycle in the biosynthesis of fatty acids, polyketides, or nonribosomal peptides. Recently, we reported that the thioesterase CmiS1 from

Indexed as

Bacterial ProteinsCatalysisGlycineMutagenesis, Site-DirectedProtein Structure, SecondaryStreptomycesSulfidesThiolester HydrolasesBacterial ProteinsGlycineSulfidesThiolester Hydrolasesenzyme mechanismenzyme structurehotdog foldhydrolaseMichael additionsecondary metabolismthioesteraseX-ray crystallographyβ-amino acid

Identifiers

PMID28522606
PMCPMC5491777

What OpenQuestion holds

Textmetadata
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.