Evidence map›Paper›PMID 25005105›Full record

ArticleActa crystallographica. Section F, Structural biology communications2014

Crystallization and preliminary analysis of the NqrA and NqrC subunits of the Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae.

Georg Vohl, Ruslan Nedielkov, Björn Claussen, Marco S Casutt, Thomas Vorburger, Kay Diederichs, Heiko M Möller, Julia Steuber, Günter Fritz

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

Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.3field-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

7 citing papers in PubMed, 7 citations in OpenAlex.

  1. Molecular dynamics modeling of the Vibrio cholera NaMolecular and cellular biochemistry · 2022
    Article
  2. Article
  3. Article
  4. Frontiers in microbiology · 2018
    Article
  5. Article
  6. Article
  7. 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

9 authors at 3 institutions in 1 country.

Georg VohlInstitute for Neuropathology, University of Freiburg, Breisacher Strasse 64, 79106 Freiburg, Germany.
Ruslan NedielkovDepartment of Chemistry and Research School Chemical Biology, University of Konstanz, Universitätsstrasse 10, Konstanz, 78457, Germany.
Björn ClaussenHermann-Staudinger-Graduate School, University of Freiburg, Hebelstrasse 27, 79104 Freiburg, Germany.
Marco S CasuttInstitute for Neuropathology, University of Freiburg, Breisacher Strasse 64, 79106 Freiburg, Germany.
Thomas VorburgerDepartment of Microbiology, University of Hohenheim, 70599 Garbenstrasse 30, Stuttgart, Germany.
Kay DiederichsDepartment of Chemistry and Research School Chemical Biology, University of Konstanz, Universitätsstrasse 10, Konstanz, 78457, Germany.
Heiko M MöllerDepartment of Chemistry and Research School Chemical Biology, University of Konstanz, Universitätsstrasse 10, Konstanz, 78457, Germany.
Julia SteuberDepartment of Microbiology, University of Hohenheim, 70599 Garbenstrasse 30, Stuttgart, Germany.
Günter FritzInstitute for Neuropathology, University of Freiburg, Breisacher Strasse 64, 79106 Freiburg, Germany.
University of Freiburg · DEUniversity of Konstanz · DEUniversity of Hohenheim · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Na+-translocating NADH:ubiquinone oxidoreductase (Na+-NQR) from Vibrio cholerae is a membrane protein complex consisting of six different subunits NqrA-NqrF. The major domains of the NqrA and NqrC subunits were heterologously expressed in Escherichia coli and crystallized. The structure of NqrA1-377 was solved in space groups C222₁ and P2₁ by SAD phasing and molecular replacement at 1.9 and 2.1 Å resolution, respectively. NqrC devoid of the transmembrane helix was co-expressed with ApbE to insert the flavin mononucleotide group covalently attached to Thr225. The structure was determined by molecular replacement using apo-NqrC of Parabacteroides distasonis as search model at 1.8 Å resolution.

Indexed as

Bacterial ProteinsCloning, MolecularCrystallizationCrystallography, X-RayEscherichia coliFlavin MononucleotideGene ExpressionMembrane ProteinsProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsQuinone ReductasesRecombinant ProteinsStructural Homology, ProteinVibrio choleraeBacterial ProteinsFlavin MononucleotideMembrane ProteinsProtein SubunitsQuinone ReductasesRecombinant Proteinssodium-translocating NADH-quinone reductasecovalently bound FMNNa+-translocating NQRVibrio cholerae

Identifiers

PMID25005105
PMCPMC4089548
OpenAlexW2056512879

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.