Evidence map›Paper›PMID 41662519›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2026

Structural and mechanistic diversity of glycogen phosphorylases from gut bacteria.

Keigo Shobu, Mayu Takai, Hiroki Tanino, Yohta Fukuda, Tsuyoshi Inoue

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 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

5 authors.

Keigo Shobu *Division of Advance Pharmaco-Science, School of Pharmaceutical Sciences, The University of Osaka, Suita, Osaka 565-0871, Japan.ORCID 0009-0006-3763-1115
Mayu Takai *Division of Advance Pharmaco-Science, School of Pharmaceutical Sciences, The University of Osaka, Suita, Osaka 565-0871, Japan.
Hiroki TaninoDivision of Advance Pharmaco-Science, School of Pharmaceutical Sciences, The University of Osaka, Suita, Osaka 565-0871, Japan.
Yohta FukudaDivision of Advance Pharmaco-Science, School of Pharmaceutical Sciences, The University of Osaka, Suita, Osaka 565-0871, Japan.ORCID 0000-0002-7386-8201
Tsuyoshi InoueDivision of Advance Pharmaco-Science, School of Pharmaceutical Sciences, The University of Osaka, Suita, Osaka 565-0871, Japan.

Funding

Japan Agency for Medical Research and Development (AMED) JP23ama121003 JP25ama121003 JP24ama121004MEXT | Japan Society for the Promotion of Science (JSPS) 22H02557MEXT | Japan Society for the Promotion of Science (JSPS) 22K05442MEXT | Japan Society for the Promotion of Science (JSPS) 25K02216MEXT | Japan Society for the Promotion of Science (JSPS) 25K08921
6 · The paper itself

Abstract

Glycogen phosphorylase (GP) plays a central role in glycogen metabolism. While the structure and regulation of mammalian GPs have been extensively studied, the corresponding mechanisms in gut bacterial GPs remain poorly understood. Here, we investigate GPs from

Indexed as

Gastrointestinal MicrobiomeGlycogen PhosphorylaseAdenosine MonophosphateCatalytic DomainCryoelectron MicroscopyCrystallography, X-RayEscherichia coliModels, MolecularAdenosine MonophosphateGlycogen PhosphorylaseCryo-EMglycogen phosphorylasegut bacteriaX-ray crystallography

Identifiers

PMID41662519
PMCPMC12912991

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.