Evidence map›Paper›PMID 42757158›Full record

ArticleACS omega2026

Identification of Key Amino Acid Residues in the Adenylation Domains of Polymyxin Synthetase Responsible for l‑Threonine Adenylation in

Wataru Ando, Yuya Uemura, Mai Nemoto, Taichi Mano, Minjae Lee, Satoshi Yuzawa, Toshihisa Mizuno

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In one paragraph

Article in ACS omega, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

7 authors.

Wataru AndoDepartment of Life Science and Applied Chemistry, Graduate School of Engineering, Nagoya Institute of Technology, Gokiso-cho, Showa-ku, Nagoya, Aichi 466-8555, Japan.
Yuya UemuraDepartment of Life Science and Applied Chemistry, Graduate School of Engineering, Nagoya Institute of Technology, Gokiso-cho, Showa-ku, Nagoya, Aichi 466-8555, Japan.
Mai NemotoDepartment of Life Science and Applied Chemistry, Graduate School of Engineering, Nagoya Institute of Technology, Gokiso-cho, Showa-ku, Nagoya, Aichi 466-8555, Japan.
Taichi ManoDepartment of Life Science and Applied Chemistry, Graduate School of Engineering, Nagoya Institute of Technology, Gokiso-cho, Showa-ku, Nagoya, Aichi 466-8555, Japan.
Minjae LeeFaculty of Environment and Information Studies, Keio University, Fujisawa, Kanagawa 252-0882, Japan.
Satoshi YuzawaSystems Biology Program, Graduate School of Media and Governance, Keio University, Fujisawa, Kanagawa 252-0882, Japan.ORCID https://orcid.org/0000-0001-8358-2787
Toshihisa MizunoDepartment of Life Science and Applied Chemistry, Graduate School of Engineering, Nagoya Institute of Technology, Gokiso-cho, Showa-ku, Nagoya, Aichi 466-8555, Japan.ORCID https://orcid.org/0000-0002-6878-5911

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In nonribosomal peptide synthetase (NRPS) research, expanding our understanding of the relationship between active-site amino acid residues in adenylation (A) domains and their adenylation activity and substrate specificity remains essential, as detailed biochemical characterization is still limited. In this study, we investigated two l-threonine (l-Thr)-specific A domains, A2 and A10, from the NRPS responsible for polymyxin D biosynthesis in

Identifiers

PMID42757158
PMCPMC13584550

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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.