Evidence map›Paper›PMID 24560608›Full record

ArticleChemistry & biology2014

Mechanisms of self-resistance in the platensimycin- and platencin-producing Streptomyces platensis MA7327 and MA7339 strains.

Ryan M Peterson, Tingting Huang, Jeffrey D Rudolf, Michael J Smanski, Ben Shen

Abstract read
In one paragraph

Article in Chemistry & biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Novel Targets for Antimicrobials.Turkish journal of pharmaceutical sciences · 2020
    Review
  13. Review
  14. Review
  15. Discovery of a Cryptic Intermediate in Late Steps of Mithramycin Biosynthesis.Angewandte Chemie (International ed. in English) · 2020
    Article
  16. Targeting Bacterial Genomes for Natural Product Discovery.Trends in pharmacological sciences · 2020
    Review
  17. Crossroads of Antibiotic Resistance and Biosynthesis.Journal of molecular biology · 2019
    Review
  18. Review
  19. Review
  20. 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

5 authors.

Ryan M Peterson *Division of Pharmaceutical Sciences, University of Wisconsin-Madison, Madison, Wisconsin 53705, USA.
Tingting Huang *Department of Chemistry, The Scripps Research Institute, Jupiter, Florida, 33458, USA.
Jeffrey D RudolfDepartment of Chemistry, The Scripps Research Institute, Jupiter, Florida, 33458, USA.
Michael J SmanskiMicrobiology Doctoral Training Program, University of Wisconsin-Madison, Madison, Wisconsin 53705, USA.
Ben ShenDepartment of Chemistry, The Scripps Research Institute, Jupiter, Florida, 33458, USA.

Funding

Chemistry-Biology Interface Training ProgramT32GM008505 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BLACKWELL, HELEN E. · 1993 to 2023
$9.8M
Platnesimycin and platencin biosynthesis and engineering in antibacterial drugsR56AI079070 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI SHEN, BEN · 2010 to 2010
$363k
NIAID NIH HHS AI079070NIAID NIH HHS R56 AI079070NIGMS NIH HHS GM08505NIGMS NIH HHS T32 GM008505
6 · The paper itself

Abstract

Platensimycin (PTM) and platencin (PTN) are potent inhibitors of bacterial fatty acid synthases and have emerged as promising antibacterial drug leads. We previously characterized the PTM and PTN biosynthetic machineries in the Streptomyces platensis producers. We now identify two mechanisms for PTM and PTN resistance in the S. platensis producers-the ptmP3 or ptnP3 gene within the PTM-PTN or PTN biosynthetic cluster and the fabF gene within the fatty acid synthase locus. PtmP3/PtnP3 and FabF confer PTM and PTN resistance by target replacement and target modification, respectively. PtmP3/PtnP3 also represents an unprecedented mechanism for fatty acid biosynthesis in which FabH and FabF are functionally replaced by a single condensing enzyme. These findings challenge the current paradigm for fatty acid biosynthesis and should be considered in future development of effective therapeutics targeting fatty acid synthase.

Indexed as

AdamantaneAmino Acid SubstitutionAminobenzoatesAminophenolsAnilidesAnti-Bacterial AgentsBacterial ProteinsBase SequenceDrug Resistance, BacterialFatty Acid Synthase, Type IIMicrobial Sensitivity TestsMolecular Sequence DataMultigene FamilyPolycyclic CompoundsStreptomycesAdamantaneAminobenzoatesAminophenolsAnilidesAnti-Bacterial AgentsBacterial ProteinsFatty Acid Synthase, Type IIplatencinplatensimycinPolycyclic Compounds

Identifiers

PMID24560608
PMCPMC3966621

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.