Evidence map›Paper›PMID 36733774›Full record

ArticleFrontiers in microbiology2022

Conformational and mechanical stability of the isolated large subunit of membrane-bound [NiFe]-hydrogenase from

Jovan Dragelj, Chara Karafoulidi-Retsou, Sagie Katz, Oliver Lenz, Ingo Zebger, Giorgio Caserta, Sophie Sacquin-Mora, Maria Andrea Mroginski

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 72% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

8 authors at 1 institution in 2 countries.

Jovan DrageljInstitut für Chemie, Technische Universität Berlin, Berlin, Germany.
Chara Karafoulidi-RetsouInstitut für Chemie, Technische Universität Berlin, Berlin, Germany.
Sagie KatzInstitut für Chemie, Technische Universität Berlin, Berlin, Germany.
Oliver LenzInstitut für Chemie, Technische Universität Berlin, Berlin, Germany.
Ingo ZebgerInstitut für Chemie, Technische Universität Berlin, Berlin, Germany.
Giorgio CasertaInstitut für Chemie, Technische Universität Berlin, Berlin, Germany.
Sophie Sacquin-MoraInstitut für Chemie, Technische Universität Berlin, Berlin, Germany.
Maria Andrea MroginskiInstitut für Chemie, Technische Universität Berlin, Berlin, Germany.
Technische Universität Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Comprising at least a bipartite architecture, the large subunit of [NiFe]-hydrogenase harbors the catalytic nickel-iron site while the small subunit houses an array of electron-transferring Fe-S clusters. Recently, some [NiFe]-hydrogenase large subunits have been isolated showing an intact and redox active catalytic cofactor. In this computational study we have investigated one of these metalloproteins, namely the large subunit HoxG of the membrane-bound hydrogenase from

Indexed as

dipole momentelectrostatic potentialGaussian accelerated molecular dynamicshydrogenaseIR spectroscopymolecular modellingrigidity profilesize exclusion chromatography

Identifiers

PMID36733774
PMCPMC9886862
OpenAlexW4316669914

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.