Evidence map›Paper›PMID 39056119›Full record

ArticleChemical communications (Cambridge, England)2024

Modular polyketide synthase ketosynthases collaborate with upstream dehydratases to install double bonds.

Katherine A Ray, Nisha Saif, Adrian T Keatinge-Clay

Abstract read
In one paragraph

Article in Chemical communications (Cambridge, England), 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
–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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. 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

3 authors.

Katherine A RayDepartment of Molecular Biosciences, The University of Texas at Austin, 100 E. 24th St., Austin, TX 78712, USA. adriankc@utexas.edu.ORCID 0009-0003-1408-9771
Nisha SaifDepartment of Molecular Biosciences, The University of Texas at Austin, 100 E. 24th St., Austin, TX 78712, USA. adriankc@utexas.edu.ORCID 0000-0002-2868-0584
Adrian T Keatinge-ClayDepartment of Molecular Biosciences, The University of Texas at Austin, 100 E. 24th St., Austin, TX 78712, USA. adriankc@utexas.edu.ORCID 0000-0002-4358-7628

Funding

Determining the Architectures and Activities of Polyketide Synthase ModulesR01GM106112 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI KEATINGE-CLAY, ADRIAN TRISTAN · 2013 to 2025
$3.9M
NIGMS NIH HHS R01 GM106112
6 · The paper itself

Abstract

A VMYH motif was determined to help ketosynthases in polyketide assembly lines select α,β-unsaturated intermediates from an equilibrium mediated by an upstream dehydratase. Alterations of this motif decreased ketosynthase selectivity within a model tetraketide synthase, most significantly when replaced by the TNGQ motif of ketosynthases that accept D-β-hydroxy intermediates.

Indexed as

Hydro-LyasesPolyketide SynthasesHydro-LyasesPolyketide Synthases

Identifiers

PMID39056119
PMCPMC11321453

What OpenQuestion holds

Textmetadata
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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.