Evidence map›Paper›PMID 30217823›Full record

ArticleThe Journal of biological chemistry2018

InhA, the enoyl-thioester reductase from

Bastian Vögeli, Raoul G Rosenthal, Gabriele M M Stoffel, Tristan Wagner, Patrick Kiefer, Niña Socorro Cortina, Seigo Shima, Tobias J Erb

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Review
  2. Article
  3. MedComm · 2023
    Review
  4. Article
  5. Enzymatic Conversion of COChemical reviews · 2023
    Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Four amino acids define the COProceedings of the National Academy of Sciences of the United States of America · 2019
    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

8 authors.

Bastian VögeliFrom the Departments of Biochemistry and Synthetic Metabolism and.ORCID 0000-0001-7870-7311
Raoul G RosenthalFrom the Departments of Biochemistry and Synthetic Metabolism and.
Gabriele M M StoffelFrom the Departments of Biochemistry and Synthetic Metabolism and.
Tristan WagnerMicrobial Protein Structure, Max-Planck-Institute for Terrestrial Microbiology, 35043 Marburg, Germany and.
Patrick Kieferthe Institute of Microbiology, ETH Zürich, 8093 Zürich, Switzerland.
Niña Socorro CortinaFrom the Departments of Biochemistry and Synthetic Metabolism and.
Seigo ShimaMicrobial Protein Structure, Max-Planck-Institute for Terrestrial Microbiology, 35043 Marburg, Germany and.
Tobias J ErbFrom the Departments of Biochemistry and Synthetic Metabolism and toerb@mpi-marburg.mpg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The enoyl-thioester reductase InhA catalyzes an essential step in fatty acid biosynthesis of

Indexed as

Amino Acid MotifsBacterial ProteinsBiocatalysisCatalytic DomainModels, MolecularMycobacterium tuberculosisOxidoreductasesProtein ConformationBacterial ProteinsInhA protein, MycobacteriumOxidoreductasesenoyl-CoA reductaseenzyme catalysisenzyme kineticsenzyme mechanismenzyme structureInhAMycobacterium tuberculosispericyclic reactionreductaseshort-chain dehydrogenase/reductase

Identifiers

PMID30217823
PMCPMC6222099

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.