Evidence map›Paper›PMID 30046790›Full record

ReviewNatural product reports2018

Trapping interactions between catalytic domains and carrier proteins of modular biosynthetic enzymes with chemical probes.

Andrew M Gulick, Courtney C Aldrich

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 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

27 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Structural Studies of Modular Nonribosomal Peptide Synthetases.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Interfacial plasticity facilitates high reaction rate ofProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. 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

2 authors at 2 institutions in 1 country.

Andrew M GulickUniversity at Buffalo, Department of Structural Biology, Jacobs School of Medicine and Biomedical Sciences, 955 Main St, Buffalo, NY 14203, USA. amgulick@buffalo.edu.
Courtney C Aldrich
Jacobs (United States) · USUniversity of Minnesota · US

Funding

The Structural Basis for Modular Nonribosomal Peptide SynthesisR01GM116957 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI GULICK, ANDREW M · 2016 to 2019
$1.5M
NIGMS NIH HHS R01 GM116957
6 · The paper itself

Abstract

Covering: up to early 2018 The Nonribosomal Peptide Synthetases (NRPSs) and Polyketide Synthases (PKSs) are families of modular enzymes that produce a tremendous diversity of natural products, with antibacterial, antifungal, immunosuppressive, and anticancer activities. Both enzymes utilize a fascinating modular architecture in which the synthetic intermediates are covalently attached to a peptidyl- or acyl-carrier protein that is delivered to catalytic domains for natural product elongation, modification, and termination. An investigation of the structural mechanism therefore requires trapping the often transient interactions between the carrier and catalytic domains. Many novel chemical probes have been produced to enable the structural and functional investigation of multidomain NRPS and PKS structures. This review will describe the design and implementation of the chemical tools that have proven to be useful in biochemical and biophysical studies of these natural product biosynthetic enzymes.

Indexed as

AcetamidesBiochemistryBiological ProductsCarrier ProteinsCatalytic DomainCrystallography, X-RayEnzymesMolecular ProbesPeptide SynthasesPolyketide SynthasesProtein DomainsProtein Interaction MapsProteomicsAcetamidesBiological ProductsCarrier ProteinschloroacetamideEnzymesMolecular Probesnon-ribosomal peptide synthasePeptide SynthasesPolyketide Synthases

Identifiers

PMID30046790
PMCPMC6235721
OpenAlexW2883597714

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.