Evidence map›Paper›PMID 41204437›Full record

ArticleFEBS letters2026

Structural insights into lacto-N-biose I recognition by a family 32 carbohydrate-binding module from Bifidobacterium bifidum.

Xinzhe Zhang, Naoki Sunagawa, Toma Kashima, Kiyohiko Igarashi, Akimasa Miyanaga, Shinya Fushinobu

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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

6 authors.

Xinzhe ZhangDepartment of Biotechnology, The University of Tokyo, Japan.
Naoki SunagawaDepartment of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Japan.
Toma KashimaDepartment of Biotechnology, The University of Tokyo, Japan.
Kiyohiko IgarashiDepartment of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Japan.
Akimasa MiyanagaDepartment of Biotechnology, The University of Tokyo, Japan.ORCID 0000-0003-2219-6051
Shinya FushinobuDepartment of Biotechnology, The University of Tokyo, Japan.ORCID 0000-0003-1346-6435

Funding

AMED JP22ama121001Japan Society for the Promotion of Science 23H00322
6 · The paper itself

Abstract

Bifidobacterium bifidum, a predominant colonizer of the infant gut, utilizes lacto-N-biose I (LNB), a prominent component of human milk oligosaccharides (HMOs), through a dedicated metabolic pathway. Among a diverse set of extracellular glycosidases involved in HMO degradation, lacto-N-biosidase (LnbB) plays a pivotal role by releasing LNB. We investigated the structure and function of the carbohydrate-binding module family 32 (CBM32) domain located at the C-terminus of the glycoside hydrolase family 20 catalytic domain in LnbB. Isothermal titration calorimetry showed that CBM32 binds LNB with a dissociation constant (K

Indexed as

Bacterial ProteinsBifidobacterium bifidumGlycoside HydrolasesAcetylglucosamineCatalytic DomainCrystallography, X-RayHumansMilk, HumanModels, MolecularOligosaccharidesProtein BindingAcetylglucosamineBacterial Proteinsgalactosyl-1,3-N-acetylglucosamineGlycoside HydrolasesOligosaccharidesBifidobacterium bifidumcarbohydrate‐binding module family 32crystal structureglycoside hydrolase family 20lacto‐N‐biosidasesugar binding domain

Identifiers

PMID41204437
PMCPMC12926856

What OpenQuestion holds

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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.