Evidence map›Paper›PMID 40770053›Full record

ReviewThe Journal of antibiotics2025

Non-canonical thioesterases in bacterial non-ribosomal peptide biosynthesis.

Kenichi Matsuda

Abstract readReview
PubMed Publisher
In one paragraph

Review in The Journal of antibiotics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

1 author.

Kenichi MatsudaFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan. kematsuda@pharm.hokudai.ac.jp.ORCID 0000-0002-9269-688X

Funding

Japan Agency for Medical Research and Development (AMED) JP25gm1610007MEXT | Japan Science and Technology Agency (JST) ACT-X JPMJAX201FMEXT | Japan Science and Technology Agency (JST) FOREST JPMJFR233UMEXT | Japan Society for the Promotion of Science (JSPS) JP23K17410MEXT | Japan Society for the Promotion of Science (JSPS) JP24K01659
6 · The paper itself

Abstract

α/β hydrolase fold thioesterases (TEs) play fundamentally important roles in polyketide and non-ribosomal peptide biosynthesis. Type-I TEs, fused at the C-terminus of multi-modular enzymatic assembly lines, dictate the overall molecular shapes of assembly-line products, while standalone type-II TEs maintain assembly-line activity through proofreading functions. Beyond these established roles, recent studies have elucidated several distinct TE functions that expand the functional versatility of these enzymes. This review summarizes recently discovered non-canonical functions of TEs in bacterial non-ribosomal peptide biosynthesis.

Indexed as

BacteriaPeptide BiosynthesisPeptide Biosynthesis, Nucleic Acid-IndependentPeptidesThiolester HydrolasesPeptidesThiolester Hydrolases

Identifiers

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.