Evidence map›Paper›PMID 31366978›Full record

ArticleScientific reports2019

Structural basis for broad substrate specificity of UDP-glucose 4-epimerase in the human milk oligosaccharide catabolic pathway of Bifidobacterium longum.

Young-Woo Nam, Mamoru Nishimoto, Takatoshi Arakawa, Motomitsu Kitaoka, Shinya Fushinobu

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 15% of its field
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

12 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  6. Biological Function of Prophage-Related Gene Cluster ΔInternational journal of molecular sciences · 2024
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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 at 4 institutions in 2 countries.

Young-Woo NamDepartment of Biotechnology, The University of Tokyo, Tokyo, 113-8657, Japan.
Mamoru NishimotoFood Research Institute, National Agriculture and Food Research Organization, Tsukuba, Ibaraki, 305-8642, Japan.
Takatoshi ArakawaDepartment of Biotechnology, The University of Tokyo, Tokyo, 113-8657, Japan.ORCID http://orcid.org/0000-0001-6496-5440
Motomitsu KitaokaFood Research Institute, National Agriculture and Food Research Organization, Tsukuba, Ibaraki, 305-8642, Japan.ORCID http://orcid.org/0000-0002-0083-1838
Shinya FushinobuDepartment of Biotechnology, The University of Tokyo, Tokyo, 113-8657, Japan. asfushi@mail.ecc.u-tokyo.ac.jp.ORCID http://orcid.org/0000-0003-1346-6435
National Agriculture and Food Research Organization · JPChapman University · USInnovative Research (United States) · USThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Infant gut-associated bifidobacteria has a metabolic pathway that specifically utilizes lacto-N-biose I (Gal-β1,3-GlcNAc) and galacto-N-biose (Gal-β1,3-GalNAc) from human milk and mucin glycans. UDP-glucose 4-epimerase (GalE) from Bifidobacterium longum (bGalE) catalyzes epimerization reactions of UDP-Gal into UDP-Glc and UDP-GalNAc into UDP-GlcNAc with the same level of activity that is required to send galacto-hexoses into glycolysis. Here, we determined the crystal structures of bGalE in three ternary complex forms: NAD

Indexed as

Amino Acid SequenceBifidobacterium longumCatalytic DomainEscherichia coliHumansMilk, HumanModels, MolecularOligosaccharidesSequence AlignmentSignal TransductionSubstrate SpecificityUDPglucose 4-EpimeraseOligosaccharidesUDPglucose 4-Epimerase

Identifiers

PMID31366978
PMCPMC6668579
OpenAlexW2965953501

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.