Evidence map›Paper›PMID 30188553›Full record

ReviewNatural product reports2018

Protein-protein interactions in "cis-AT" polyketide synthases.

Greg J Dodge, Finn P Maloney, Janet L Smith

Abstract readReview
In one paragraph

Review in Natural product reports, 2018. 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
  2. Article
  3. Article
  4. Review
  5. Structure of a modular polyketide synthase reducing region.Structure (London, England : 1993) · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Docking domain-mediated subunit interactions in natural product megasynth(et)ases.Journal of industrial microbiology & biotechnology · 2021
    Review
  11. Article
  12. Review
  13. Review
  14. Review
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.

Greg J DodgeLife Sciences Institute, University of Michigan, Ann Arbor, Michigan, USA 48109. JanetSmith@umich.edu.
Finn P Maloney
Janet L Smith

Funding

STRUCTURE AND FUNCTION OF A PURINE BIOSYNTHETIC ENZYMER01DK042303 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SMITH, JANET L. · 1990 to 2024
$6.6M
GLUTAMINE AMIDOTRANSFERASES AND PARTNER ENZYMESR37DK042303 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SMITH, JANET L. · 1998 to 2007
$2.4M
NIDDK NIH HHS R01 DK042303NIDDK NIH HHS R37 DK042303
6 · The paper itself

Abstract

Covering: up to the end of 2018 Polyketides are a valuable source of bioactive and clinically important molecules. The biosynthesis of these chemically complex molecules has led to the discovery of equally complex polyketide synthase (PKS) pathways. Crystallography has yielded snapshots of individual catalytic domains, di-domains, and multi-domains from a variety of PKS megasynthases, and cryo-EM studies have provided initial views of a PKS module in a series of defined biochemical states. Here, we review the structural and biochemical results that shed light on the protein-protein interactions critical to catalysis by PKS systems with an embedded acyltransferase. Interactions include those that occur both within and between PKS modules, as well as with accessory enzymes.

Indexed as

Protein Interaction Domains and MotifsAcyltransferasesCatalytic DomainPolyketide SynthasesProtein MultimerizationAcyltransferasesPolyketide Synthases

Identifiers

PMID30188553
PMCPMC6207950

What OpenQuestion holds

Textmetadata
LicenceTDM
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.