Evidence map›Paper›PMID 10390219›Full record

ArticleAntimicrobial agents and chemotherapy1999

Nonactin biosynthesis: the product of nonS catalyzes the formation of the furan ring of nonactic acid.

A J Woo, W R Strohl, N D Priestley

Open access · bronzeAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 1999. 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
0.6field-weighted citation impact, top 34% of its field
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, 57 citations in OpenAlex.

  1. Article
  2. Natural products targeting cancer cell dependency.The Journal of antibiotics · 2021
    Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Enzymology of Pyran Ring A Formation in Salinomycin Biosynthesis.Angewandte Chemie (International ed. in English) · 2015
    Article
  8. Enzymology of Pyran Ring A Formation in Salinomycin Biosynthesis.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2015
    Article
  9. Enantiomeric natural products: occurrence and biogenesis.Angewandte Chemie (International ed. in English) · 2012
    Review
  10. Article
  11. Article
  12. Article
  13. A polyketide synthase-peptide synthetase gene cluster from an uncultured bacterial symbiont of Paederus beetles.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  14. 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 at 1 institution in 1 country.

A J WooDepartment of Microbiology, The Ohio State University, Columbus, Ohio 43210, USA.
W R Strohl
N D Priestley
The Ohio State University · US

Funding

BIO-ENGINEERING OF COMPOUNDS ACTIVE AGAINST MDR CANCERR01CA077347 · NCI · UNIVERSITY OF MONTANA · PI PRIESTLEY, NIGEL D · 2003 to 2006
$1.3M
BIO-ENGINEERING OF COMPOUNDS ACTIVE AGAINST MDR CANCERR29CA077347 · NCI · UNIVERSITY OF MONTANA · PI PRIESTLEY, NIGEL D · 1998 to 2002
$267k
NCI NIH HHS CA77347NCI NIH HHS R01 CA077347NCI NIH HHS R29 CA077347
6 · The paper itself

Abstract

Nonactin is the parent compound of a group of ionophore antibiotics, known as the macrotetrolides, produced by Streptomyces griseus subsp. griseus ETH A7796. Nonactin is a significant compound because of its inhibitory effects on the P170 glycoprotein-mediated efflux of chemotherapeutic agents in multiple-drug-resistant cancer cells. Nonactin is also significant in that it is a highly atypical polyketide. Very little is presently known about the genes of the nonactin biosynthesis cluster. In this paper we describe our efforts to establish a connection between the product of a gene from the nonactin biosynthesis cluster and a known biochemical transformation in nonactin biosynthesis. Nonactate synthase is the enzyme which catalyzes the formation of nonactic acid from an acyclic precursor in nonactin biosynthesis. We have synthesized the substrate for this enzyme and have detected the in vitro cyclization activity of the substrate in cell-free preparations of S. griseus subsp. griseus ETH A7796. Previous studies by R. Plater and J. A. Robinson (Gene 112:117-122, 1992) had suggested, based on sequence homology, that the product of a partial open reading frame found close to the tetranactin resistance gene of S. griseus could be the nonactate synthase. We have therefore cloned, sequenced, and heterologously expressed this full gene (nonS), and we have shown that the gene product, NonS, does indeed catalyze the formation of the furan ring of nonactic acid as hypothesized.

Indexed as

Genes, BacterialAmino Acid SequenceAnti-Bacterial AgentsBase SequenceCloning, MolecularFuransMacrolidesMolecular Sequence DataMultigene FamilyStreptomyces griseusAnti-Bacterial AgentsFuransMacrolidesnonactin

Identifiers

PMID10390219
PMCPMC89340
OpenAlexW2158328214

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.