Evidence map›Paper›PMID 31366732›Full record

ArticleThe Journal of biological chemistry2019

Functional analyses of ancestral thioredoxins provide insights into their evolutionary history.

Silvia Napolitano, Robin J Reber, Marina Rubini, Rudi Glockshuber

Open access · hybridAbstract readHistorical Article
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

10 citing papers in PubMed, 20 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

4 authors at 3 institutions in 2 countries.

Silvia NapolitanoInstitute of Molecular Biology and Biophysics, Department of Biology, Swiss Federal Institute of Technology Zurich, Otto-Stern-Weg 5, CH-8093 Zurich, Switzerland.ORCID 0000-0001-9020-0767
Robin J ReberInstitute of Molecular Biology and Biophysics, Department of Biology, Swiss Federal Institute of Technology Zurich, Otto-Stern-Weg 5, CH-8093 Zurich, Switzerland.
Marina RubiniSchool of Chemistry, University College Dublin, Belfield, Dublin 4, Ireland.ORCID 0000-0002-3102-2558
Rudi GlockshuberInstitute of Molecular Biology and Biophysics, Department of Biology, Swiss Federal Institute of Technology Zurich, Otto-Stern-Weg 5, CH-8093 Zurich, Switzerland rudi@mol.biol.ethz.ch.ORCID 0000-0003-3320-3843
École Polytechnique Fédérale de Lausanne · CHETH Zurich · CHUniversity College Dublin · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thioredoxin (Trx) is a conserved, cytosolic reductase in all known organisms. The enzyme receives two electrons from NADPH via thioredoxin reductase (TrxR) and passes them on to multiple cellular reductases via disulfide exchange. Despite the ubiquity of thioredoxins in all taxa, little is known about the functions of resurrected ancestral thioredoxins in the context of a modern mesophilic organism. Here, we report on functional

Indexed as

CytoplasmCytosolDisulfidesEscherichia coliEvolution, MolecularHistory, AncientKineticsNADPOxidantsOxidation-ReductionStructure-Activity RelationshipThioredoxin-Disulfide ReductaseThioredoxinsDisulfidesNADPOxidantsThioredoxin-Disulfide ReductaseThioredoxinselectron transfermethionine sulfoxide reductasemolecular evolutionoxidative stressphylogenetic reconstructionredox biologyredox homeostasisthioredoxinthioredoxin reductase

Identifiers

PMID31366732
PMCPMC6755812
OpenAlexW2965557027

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.