Evidence map›Paper›PMID 17893367›Full record

ArticleProtein science : a publication of the Protein Society2007

WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases.

Jannette Carey, Jiri Brynda, Julie Wolfová, Rita Grandori, Tobias Gustavsson, Rüdiger Ettrich, Ivana Kutá Smatanová

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

19 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Effects of the Quinone Oxidoreductase WrbA onAntioxidants (Basel, Switzerland) · 2021
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  14. Molecular tracing of the emergence, diversification, and transmission of S. aureus sequence type 8 in a New York community.Proceedings of the National Academy of Sciences of the United States of America · 2014
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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

7 authors at 6 institutions in 4 countries.

Jannette CareyChemistry Department, Princeton University, Princeton, New Jersey 08544-1009, USA. jcarey@princeton.edu
Jiri Brynda
Julie Wolfová
Rita Grandori
Tobias Gustavsson
Rüdiger Ettrich
Ivana Kutá Smatanová
University of South Bohemia in České Budějovice · CZCzech Academy of Sciences · CZCzech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZLund University · SEPrinceton University · USUniversity of Milano-Bicocca · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The crystal structure of the flavodoxin-like protein WrbA with oxidized FMN bound reveals a close relationship to mammalian NAD(P)H:quinone oxidoreductase, Nqo1. Structural comparison of WrbA, flavodoxin, and Nqo1 indicates how the twisted open-sheet fold of flavodoxins is elaborated to form multimers that extend catalytic function from one-electron transfer between protein partners using FMN to two-electron reduction of xenobiotics using FAD. The structure suggests a novel physiological role for WrbA and Nqo1.

Indexed as

Binding SitesDNA-Binding ProteinsEscherichia coli ProteinsFlavodoxinModels, MolecularNAD(P)H Dehydrogenase (Quinone)Protein FoldingRepressor ProteinsDNA-Binding ProteinsEscherichia coli ProteinsFlavodoxinNAD(P)H Dehydrogenase (Quinone)Repressor ProteinsWrbA protein, E coli

Identifiers

PMID17893367
PMCPMC2204128
OpenAlexW1976652162

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.