Evidence map›Paper›PMID 25080832›Full record

ArticleJournal of the American Chemical Society2014

Probing the phosphopantetheine arm conformations of acyl carrier proteins using vibrational spectroscopy.

Matthew N R Johnson, Casey H Londergan, Louise K Charkoudian

Erratum issuedAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. RSC chemical biology · 2026
    Article
  2. bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Structural Characterization of an ACP fromInternational journal of molecular sciences · 2020
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Simple method to introduce an ester infrared probe into proteins.Protein science : a publication of the Protein Society · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Using modern tools to probe the structure-function relationship of fatty acid synthases.Chembiochem : a European journal of chemical biology · 2015
    Review
  19. Visualizing the chain-flipping mechanism in fatty-acid biosynthesis.Angewandte Chemie (International ed. in English) · 2014
    Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Matthew N R JohnsonDepartment of Chemistry, Haverford College , Haverford, Pennsylvania 19041-1392, United States.
Casey H Londergan
Louise K Charkoudian
Haverford College · US

Funding

Cyanylated cysteine as vibrational probe of binding-induced structural transitionR15GM088749 · NIGMS · HAVERFORD COLLEGE · PI LONDERGAN, CASEY H · 2009 to 2012
$505k
NIGMS NIH HHS GM088749-02NIGMS NIH HHS R15 GM088749
6 · The paper itself

Abstract

Acyl carrier proteins (ACPs) are universal and highly conserved domains central to both fatty acid and polyketide biosynthesis. These proteins tether reactive acyl intermediates with a swinging 4'-phosphopantetheine (Ppant) arm and interact with a suite of catalytic partners during chain transport and elongation while stabilizing the growing chain throughout the biosynthetic pathway. The flexible nature of the Ppant arm and the transient nature of ACP-enzyme interactions impose a major obstacle to obtaining structural information relevant to understanding polyketide and fatty acid biosynthesis. To overcome this challenge, we installed a thiocyanate vibrational spectroscopic probe on the terminal thiol of the ACP Ppant arm. This site-specific probe successfully reported on the local environment of the Ppant arm of two ACPs previously characterized by solution NMR, and was used to determine the solution exposure of the Ppant arm of an ACP from 6-deoxyerythronolide B synthase (DEBS). Given the sensitivity of the probe's CN stretching band to conformational distributions resolved on the picosecond time scale, this work lays a foundation for observing the dynamic action-related structural changes of ACPs using vibrational spectroscopy.

Indexed as

Acyl Carrier ProteinCatalysisFatty AcidsGeobacterMagnetic Resonance SpectroscopyModels, MolecularPolyketidesPolyketide SynthasesProtein Structure, TertiaryReproducibility of ResultsSpectrophotometryStreptomyces coelicolorTime FactorsAcyl Carrier ProteinFatty AcidsPolyketidesPolyketide Synthases

Identifiers

PMID25080832
PMCPMC4140477
OpenAlexW2034504850

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.