Evidence map›Paper›PMID 26831698›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2016

Structural Biology of Nonribosomal Peptide Synthetases.

Bradley R Miller, Andrew M Gulick

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
32.3field-weighted citation impact, top 1% 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

83 citing papers in PubMed, 156 citations in OpenAlex.

  1. Article
  2. Bioactive Peptides From theFood science & nutrition · 2026
    Review
  3. Article
  4. Iron acquisition strategies of the rock-inhabiting fungusApplied and environmental microbiology · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. A chlorinated diketopiperazine antibiotic targetsAntimicrobial agents and chemotherapy · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. mSystems · 2024
    Article
  19. Review
  20. Article

23 more citing papers are in PubMed but not listed here.

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.

Bradley R MillerHauptman-Woodward Medical Research Institute, 700 Ellicott St, Buffalo, NY, 14203-1102, USA.
Andrew M GulickHauptman-Woodward Medical Research Institute, 700 Ellicott St, Buffalo, NY, 14203-1102, USA. gulick@hwi.buffalo.edu.
Hauptman-Woodward Medical Research Institute · USUniversity at Buffalo, State University of New York · US

Funding

Structures of Peptide Synthetases and Related EnzymesR01GM068440 · NIGMS · HAUPTMAN-WOODWARD MEDICAL RESEARCH INST · PI GULICK, ANDREW M · 2004 to 2013
$3.1M
NIGMS NIH HHS GM-068440NIGMS NIH HHS R01 GM068440
6 · The paper itself

Abstract

The nonribosomal peptide synthetases are modular enzymes that catalyze synthesis of important peptide products from a variety of standard and non-proteinogenic amino acid substrates. Within a single module are multiple catalytic domains that are responsible for incorporation of a single residue. After the amino acid is activated and covalently attached to an integrated carrier protein domain, the substrates and intermediates are delivered to neighboring catalytic domains for peptide bond formation or, in some modules, chemical modification. In the final module, the peptide is delivered to a terminal thioesterase domain that catalyzes release of the peptide product. This multi-domain modular architecture raises questions about the structural features that enable this assembly line synthesis in an efficient manner. The structures of the core component domains have been determined and demonstrate insights into the catalytic activity. More recently, multi-domain structures have been determined and are providing clues to the features of these enzyme systems that govern the functional interaction between multiple domains. This chapter describes the structures of NRPS proteins and the strategies that are being used to assist structural studies of these dynamic proteins, including careful consideration of domain boundaries for generation of truncated proteins and the use of mechanism-based inhibitors that trap interactions between the catalytic and carrier protein domains.

Indexed as

AnimalsBacteriaCatalytic DomainCrystallizationCrystallography, X-RayHumansModels, MolecularNuclear Magnetic Resonance, BiomolecularPeptide SynthasesProtein ConformationProtein Structure, Tertiarynon-ribosomal peptide synthasePeptide SynthasesEnzymologyMetabolic pathwaysModular enzymesNonribosomal peptide synthetasePeptidesSiderophoresStructural biology

Identifiers

PMID26831698
PMCPMC4760355
OpenAlexW2260987152

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.