Evidence map›Paper›PMID 28584265›Full record

ArticleScientific reports2017

X-ray structures of fructosyl peptide oxidases revealing residues responsible for gating oxygen access in the oxidative half reaction.

Tomohisa Shimasaki, Hiromi Yoshida, Shigehiro Kamitori, Koji Sode

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

4 citing papers in PubMed, 19 citations in OpenAlex.

  1. Targeting Fructosamine Oxidase (Amadoriase II) inCurrent medicinal chemistry · 2026
    Article
  2. In Silico Engineering of Enzyme Access Tunnels.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  3. Review
  4. Article
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

4 authors at 2 institutions in 1 country.

Tomohisa ShimasakiDepartment of Biotechnology and Life Science, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16, Nakamachi, Koganei, Tokyo, 184-8588, Japan.
Hiromi YoshidaLife Science Research Center and Faculty of Medicine, Kagawa University, Ikenobe, Miki-cho, Kita-gun, Kagawa, Japan.
Shigehiro KamitoriLife Science Research Center and Faculty of Medicine, Kagawa University, Ikenobe, Miki-cho, Kita-gun, Kagawa, Japan.
Koji SodeDepartment of Biotechnology and Life Science, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16, Nakamachi, Koganei, Tokyo, 184-8588, Japan. sode@cc.tuat.ac.jp.
Kagawa University · JPTokyo University of Agriculture and Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Current enzymatic systems for quantifying glycated hemoglobin are based on the FAD-containing enzyme fructosyl peptide oxidase (FPOX). FPOX has substrate specificity for fructosyl-

Indexed as

Oxidation-ReductionAmino Acid OxidoreductasesAmino AcidsAmino Acid SubstitutionBinding SitesCrystallography, X-RayFlavin-Adenine DinucleotideGlycated HemoglobinModels, MolecularMutagenesis, Site-DirectedOxygenProtein ConformationStructure-Activity RelationshipAmino Acid OxidoreductasesAmino AcidsFlavin-Adenine Dinucleotidefructosyl-peptide oxidaseGlycated HemoglobinOxygen

Identifiers

PMID28584265
PMCPMC5459902
OpenAlexW2619879835

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.