Evidence map›Paper›PMID 31925988›Full record

ArticleFEBS open bio2020

The N-terminal domains of the paralogous HycE and NuoCD govern assembly of the respective formate hydrogenlyase and NADH dehydrogenase complexes.

Philipp Skorupa, Ute Lindenstrauß, Sabrina Burschel, Christian Blumenscheit, Thorsten Friedrich, Constanze Pinske

Open access · goldAbstract read
In one paragraph

Article in FEBS open bio, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 62% 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

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

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

6 authors at 2 institutions in 2 countries.

Philipp SkorupaInstitute of Biology/Microbiology, Martin-Luther University Halle-Wittenberg, Germany.
Ute LindenstraußInstitute of Biology/Microbiology, Martin-Luther University Halle-Wittenberg, Germany.
Sabrina BurschelInstitute of Biochemistry/Molecular Bioenergetics, Albert-Ludwigs-University Freiburg, Germany.
Christian BlumenscheitInstitute of Biology/Microbiology, Martin-Luther University Halle-Wittenberg, Germany.ORCID 0000-0001-8987-2355
Thorsten FriedrichInstitute of Biochemistry/Molecular Bioenergetics, Albert-Ludwigs-University Freiburg, Germany.ORCID 0000-0002-0813-7883
Constanze PinskeInstitute of Biology/Microbiology, Martin-Luther University Halle-Wittenberg, Germany.ORCID 0000-0001-6248-2437
Martin Luther University Halle-Wittenberg · DEUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Formate hydrogenlyase (FHL) is the main hydrogen-producing enzyme complex in enterobacteria. It converts formate to CO

Indexed as

CatalysisElectron Transport Complex IEnterobacteriaceaeEscherichia coliEscherichia coli ProteinsFormate DehydrogenasesFormatesHydrogenaseMultienzyme ComplexesNADH DehydrogenaseOperonOxidation-ReductionProtonsElectron Transport Complex IEscherichia coli ProteinsFormate Dehydrogenasesformate hydrogenlyaseFormatesformic acidhycE protein, E coliHydrogenaseMultienzyme ComplexesNADH DehydrogenaseNuoCD protein, E coliProtonscomplex Iformate hydrogenlyasefusion proteinsHycENADH:ubiquinone oxidoreductaseNuoCD

Identifiers

PMID31925988
PMCPMC7050243
OpenAlexW2999552234

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.