Evidence map›Paper›PMID 24385433›Full record

ArticleThe Journal of biological chemistry2014

Characterization of a novel β-L-arabinofuranosidase in Bifidobacterium longum: functional elucidation of a DUF1680 protein family member.

Kiyotaka Fujita, Yukari Takashi, Eriko Obuchi, Kanefumi Kitahara, Toshihiko Suganuma

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Observational
  2. Article
  3. Revealing AIEC Virulence Genes Behind the Mask of Antimicrobial Resistance.Cellular and molecular gastroenterology and hepatology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. β-l-ACS chemical biology · 2023
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Plant Glycan Metabolism by Bifidobacteria.Frontiers in microbiology · 2021
    Review
  16. Cracking the "Sugar Code": A Snapshot ofFrontiers in plant science · 2021
    Review
  17. Article
  18. Article
  19. Article
  20. Two Novel α-l-Arabinofuranosidases fromApplied and environmental microbiology · 2019
    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

5 authors.

Kiyotaka FujitaFrom the Faculty of Agriculture, Kagoshima University, Korimoto, Kagoshima 890-0065, Japan.
Yukari Takashi
Eriko Obuchi
Kanefumi Kitahara
Toshihiko Suganuma

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pfam DUF1680 (PF07944) is an uncharacterized protein family conserved in many species of bacteria, actinomycetes, fungi, and plants. Previously, we cloned and characterized the hypBA2 gene as a β-L-arabinobiosidase in Bifidobacterium longum JCM 1217. In this study, we cloned a DUF1680 family member, the hypBA1 gene, which constitutes a gene cluster with hypBA2. HypBA1 is a novel β-L-arabinofuranosidase that liberates L-arabinose from the L-arabinofuranose (Araf)-β1,2-Araf disaccharide. HypBA1 also transglycosylates 1-alkanols with retention of the anomeric configuration. Mutagenesis and azide rescue experiments indicated that Glu-338 is a critical residue for catalytic activity. This study provides the first characterization of a DUF1680 family member, which defines a new family of glycoside hydrolases, the glycoside hydrolase family 127.

Indexed as

Amino AcidsArabinoseBacterial ProteinsBifidobacteriumChromatography, High Pressure LiquidChromatography, Ion ExchangeChromatography, Thin LayerElectrophoresis, Polyacrylamide GelFermentationGlycoproteinsGlycoside HydrolasesGlycosylationHydrogen-Ion ConcentrationKineticsMagnetic Resonance SpectroscopyModels, BiologicalAmino AcidsarabinofuranoseArabinoseBacterial ProteinsGlycoproteinsGlycoside HydrolasesMutant ProteinsRecombinant ProteinsBacteriaCloningEnzyme CatalysisEnzyme KineticsGlycosidasesHydrolasesHydroxyprolineMutagenesisProtein Expression

Identifiers

PMID24385433
PMCPMC3931080

What OpenQuestion holds

Textmetadata
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.