Evidence map›Paper›PMID 31728067›Full record

ArticleScientific reports2019

The first comprehensive phylogenetic and biochemical analysis of NADH diphosphatases reveals that the enzyme from Tuber melanosporum is highly active towards NAD

Antonio Ginés García-Saura, Rubén Zapata-Pérez, Ana Belén Martínez-Moñino, José Francisco Hidalgo, Asunción Morte, Manuela Pérez-Gilabert, Álvaro Sánchez-Ferrer

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 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact, top 93% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. 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

7 authors at 3 institutions in 2 countries.

Antonio Ginés García-SauraDepartment of Biochemistry and Molecular Biology-A, Faculty of Biology, Regional Campus of International Excellence "Campus Mare Nostrum", University of Murcia, Campus Espinardo, 30100, Murcia, Spain.
Rubén Zapata-PérezDepartment of Biochemistry and Molecular Biology-A, Faculty of Biology, Regional Campus of International Excellence "Campus Mare Nostrum", University of Murcia, Campus Espinardo, 30100, Murcia, Spain.
Ana Belén Martínez-MoñinoDepartment of Biochemistry and Molecular Biology-A, Faculty of Biology, Regional Campus of International Excellence "Campus Mare Nostrum", University of Murcia, Campus Espinardo, 30100, Murcia, Spain.
José Francisco HidalgoDepartment of Biochemistry and Molecular Biology-A, Faculty of Biology, Regional Campus of International Excellence "Campus Mare Nostrum", University of Murcia, Campus Espinardo, 30100, Murcia, Spain.
Asunción MorteDepartment of Plant Biology, Faculty of Biology, University of Murcia, Campus Espinardo, 30100, Murcia, Spain.ORCID http://orcid.org/0000-0002-6426-0202
Manuela Pérez-GilabertDepartment of Biochemistry and Molecular Biology-A, Faculty of Biology, Regional Campus of International Excellence "Campus Mare Nostrum", University of Murcia, Campus Espinardo, 30100, Murcia, Spain.
Álvaro Sánchez-FerrerDepartment of Biochemistry and Molecular Biology-A, Faculty of Biology, Regional Campus of International Excellence "Campus Mare Nostrum", University of Murcia, Campus Espinardo, 30100, Murcia, Spain. alvaro@um.es.ORCID http://orcid.org/0000-0001-7266-4402
Instituto Murciano de Investigación Biosanitaria · ESUniversidad de Murcia · ESAmsterdam UMC Location University of Amsterdam · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nudix (for nucleoside diphosphatases linked to other moieties, X) hydrolases are a diverse family of proteins capable of cleaving an enormous variety of substrates, ranging from nucleotide sugars to NAD

Indexed as

Computational BiologyComputer SimulationDatabases, ProteinEvolution, MolecularFungal ProteinsPhylogenyProtein DomainsPyrophosphatasesSaccharomycetalesSubstrate SpecificityFungal Proteinsnucleotide pyrophosphatasePyrophosphatases

Identifiers

PMID31728067
PMCPMC6856373
OpenAlexW2986900292

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.