Evidence map›Paper›PMID 42529406›Full record

ArticleJACS Au2026

Isotopic Editing Unveils Ergosterol-Dependent Sugar Orientation Constraints That Stabilize Amphotericin B Channel Assemblies and May Contribute to Their Clustering.

Tomoya Yamamoto, Mayank Dixit, Yuichi Umegawa, Masaki Yamagami, Shinya Hanashima, Hiroshi Tsuchikawa, Nobuaki Matsumori, Wataru Shinoda, Michio Murata

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in JACS Au, 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

9 authors.

Tomoya YamamotoDepartment of Chemistry, Graduate School of Science, The University of Osaka, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.ORCID https://orcid.org/0000-0002-3284-5388
Mayank DixitDepartment of Materials Chemistry, Nagoya University, Nagoya 464-8603, Japan.ORCID https://orcid.org/0000-0003-2956-6756
Yuichi UmegawaDepartment of Chemistry, Graduate School of Science, The University of Osaka, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.ORCID https://orcid.org/0000-0002-1057-8119
Masaki YamagamiDepartment of Chemistry, Graduate School of Science, The University of Osaka, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.
Shinya HanashimaDepartment of Chemistry, Graduate School of Science, The University of Osaka, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.ORCID https://orcid.org/0000-0003-3102-7890
Hiroshi TsuchikawaDepartment of Chemistry, Graduate School of Science, The University of Osaka, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.
Nobuaki MatsumoriDepartment of Chemistry, Graduate School of Science, The University of Osaka, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.ORCID https://orcid.org/0000-0003-0495-2044
Wataru ShinodaDepartment of Materials Chemistry, Nagoya University, Nagoya 464-8603, Japan.ORCID https://orcid.org/0000-0002-3388-9227
Michio MurataDepartment of Chemistry, Graduate School of Science, The University of Osaka, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.ORCID https://orcid.org/0000-0002-1600-145X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amphotericin B (AmB) is the drug of choice for treating systemic fungal infections. Its selective toxicity is thought to arise from preferential binding to ergosterol in fungal membranes, which enables stable ion-permeable pores. The amino sugar mycosamine, attached to the AmB macrolide ring, has been proposed to mediate specific interactions with ergosterol; however, its orientation in membranes remains elusive, mainly because glycosidic-linkage conformations are difficult to analyze in lipid bilayers. Here we apply an isotopic editing strategylate-stage glycosylation combined with site-selective isotopic editing (

Indexed as

amphotericin Bconformationglycosidic linkagemolecular dynamics simulation, rotational echo double resonancemultilamellar vesicles

Identifiers

PMID42529406
PMCPMC13417286

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Registered trials

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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.