Evidence map›Paper›PMID 27398308›Full record

ArticleFEBS open bio2016

Characterization of the Nqo5 subunit of bacterial complex I in the isolated state.

Yuya Hanazono, Kazuki Takeda, Kunio Miki

Abstract read
In one paragraph

Article in FEBS open bio, 2016. 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
–field-weighted citation impact
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.

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

3 authors.

Yuya HanazonoDepartment of Chemistry Graduate School of Science Kyoto University Sakyo-ku Kyoto Japan.
Kazuki TakedaDepartment of Chemistry Graduate School of Science Kyoto University Sakyo-ku Kyoto Japan; RIKEN SPring-8 Center at Harima Institute Sayo Hyogo Japan.
Kunio MikiDepartment of Chemistry Graduate School of Science Kyoto University Sakyo-ku Kyoto Japan; RIKEN SPring-8 Center at Harima Institute Sayo Hyogo Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The subunits that comprise bacterial complex I (NADH:ubiquinone oxidoreductase) are also found in more complicated mitochondrial enzymes in eukaryotic organisms. Although the Nqo5 subunit is one of these conserved components and important for the formation of complex, it has been little studied. Here, we report structure analyses of isolated Nqo5 from Thermus thermophilus. Biochemical studies indicated that the C-terminal region following the 30-Kd subunit motif is disordered in the isolated state, while the remaining portion is already folded. Crystallographic studies of a trypsin-resistant fragment revealed detailed structural differences in the folded domain between the isolated and complexed states.

Indexed as

30‐Kd subunit motifcrystal structureNADH:ubiquinone oxidoreductase

Identifiers

PMID27398308
PMCPMC4932448

What OpenQuestion holds

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Registered trials

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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.