Evidence map›Paper›PMID 31914410›Full record

ArticleThe Journal of biological chemistry2020

Characterization of l-2-keto-3-deoxyfuconate aldolases in a nonphosphorylating l-fucose metabolism pathway in anaerobic bacteria.

Seiya Watanabe

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.4field-weighted citation impact, top 45% 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

9 citing papers in PubMed, 13 citations in OpenAlex.

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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

1 author at 1 institution in 1 country.

Seiya WatanabeDepartment of Bioscience, Graduate School of Agriculture, Ehime University, Matsuyama, Ehime 790-8566, Japan Faculty of Agriculture, Ehime University, Matsuyama, Ehime 790-8566, Japan Center for Marine Environmental Studies, Ehime University, Matsuyama, Ehime 790-8577, Japan irab@agr.ehime-u.ac.jp.ORCID 0000-0002-6530-9047
Ehime University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The genetic context in bacterial genomes and screening for potential substrates can help identify the biochemical functions of bacterial enzymes. The Gram-negative, strictly anaerobic bacterium

Indexed as

Aldehyde-LyasesAldehydesAmino Acid SequenceBinding SitesCampylobacter jejuniCatalytic DomainDeoxy SugarsEvolution, MolecularFucoseHydro-LyasesKineticsModels, MolecularMultigene FamilyMutagenesis, Site-DirectedMutationOxo-Acid-Lyases3-hydroxybutanal4-hydroxy-tetrahydrodipicolinate synthaseAldehyde-LyasesAldehydesDeoxy SugarsFucoseHydro-LyasesN-acetylneuraminate lyaseOxo-Acid-Lyases2-keto-3-deoxysugar acidaldolaseenzyme catalysisenzyme mechanismgene clusterL-fucose metabolismmolecular evolutionstereoselectivitysubstrate specificityVeillonella ratti

Identifiers

PMID31914410
PMCPMC6996899
OpenAlexW2996878602

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.