Evidence map›Paper›PMID 38488017›Full record

ReviewNatural product reports2024

Structural, biochemical and bioinformatic analyses of nonribosomal peptide synthetase adenylation domains.

Stephanie C Heard, Jaclyn M Winter

Open access · hybridAbstract readReview
In one paragraph

Review in Natural product reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
12.5field-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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
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  8. Diversity of FAAL enzymes and prediction of their substrate specificity using FAALPred.Protein science : a publication of the Protein Society · 2026
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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 1 institution in 1 country.

Stephanie C HeardDepartment of Pharmacology and Toxicology, University of Utah, Salt Lake City, UT 84112, USA. sheard@uic.edu.ORCID 0000-0003-4312-5105
Jaclyn M WinterDepartment of Pharmacology and Toxicology, University of Utah, Salt Lake City, UT 84112, USA. sheard@uic.edu.ORCID 0000-0001-6273-5377
University of Utah · US

Funding

Genomics-Assisted Antibiotic Discovery from Unprecedented Microbes of the Great Salt LakeR01AI155694 · NIAID · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI WINTER, JACLYN MARIE · 2021 to 2025
$3.1M
NIAID NIH HHS R01 AI155694
6 · The paper itself

Abstract

Covering: 1997 to July 2023The adenylation reaction has been a subject of scientific intrigue since it was first recognized as essential to many biological processes, including the homeostasis and pathogenicity of some bacteria and the activation of amino acids for protein synthesis in mammals. Several foundational studies on adenylation (A) domains have facilitated an improved understanding of their molecular structures and biochemical properties, in particular work on nonribosomal peptide synthetases (NRPSs). In NRPS pathways, A domains activate their respective acyl substrates for incorporation into a growing peptidyl chain, and many nonribosomal peptides are bioactive. From a natural product drug discovery perspective, improving existing bioinformatics platforms to predict unique NRPS products more accurately from genomic data is desirable. Here, we summarize characterization efforts of A domains primarily from NRPS pathways from July 1997 up to July 2023, covering protein structure elucidation,

Indexed as

Computational BiologyPeptide SynthasesBiological ProductsMolecular StructureBiological Productsnon-ribosomal peptide synthasePeptide Synthases

Identifiers

PMID38488017
PMCPMC11253843
OpenAlexW4392872704

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.