Evidence map›Paper›PMID 24440354›Full record

ArticleFEBS letters2014

A simple method for the determination of reduction potentials in heme proteins.

Igor Efimov, Gary Parkin, Elizabeth S Millett, Jennifer Glenday, Cheuk K Chan, Holly Weedon, Harpreet Randhawa, Jaswir Basran, Emma L Raven

Open access · hybridAbstract read
In one paragraph

Article in FEBS letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

34 citing papers in PubMed, 56 citations in OpenAlex.

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  7. Identification of Potent and Selective Inhibitors ofJournal of medicinal chemistry · 2024
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  12. Competition between intra-protein charge recombination and electron transfer outside photosystem I complexes used for photovoltaic applications.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022
    Article
  13. Article
  14. Article
  15. Ferric heme as a CO/NO sensor in the nuclear receptor Rev-Erbß by coupling gas binding to electron transfer.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Article
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  18. Article
  19. Heme binding to human CLOCK affects interactions with the E-box.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. 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 1 institution in 1 country.

Igor EfimovDepartment of Chemistry, Henry Wellcome Building, University of Leicester, University Road, Leicester LE1 7RH, United Kingdom.
Gary ParkinDepartment of Chemistry, Henry Wellcome Building, University of Leicester, University Road, Leicester LE1 7RH, United Kingdom.
Elizabeth S MillettDepartment of Chemistry, Henry Wellcome Building, University of Leicester, University Road, Leicester LE1 7RH, United Kingdom.
Jennifer GlendayDepartment of Chemistry, Henry Wellcome Building, University of Leicester, University Road, Leicester LE1 7RH, United Kingdom.
Cheuk K ChanDepartment of Chemistry, Henry Wellcome Building, University of Leicester, University Road, Leicester LE1 7RH, United Kingdom.
Holly WeedonDepartment of Chemistry, Henry Wellcome Building, University of Leicester, University Road, Leicester LE1 7RH, United Kingdom.
Harpreet RandhawaDepartment of Chemistry, Henry Wellcome Building, University of Leicester, University Road, Leicester LE1 7RH, United Kingdom.
Jaswir BasranDepartment of Biochemistry, Henry Wellcome Building, University of Leicester, University Road, Leicester LE1 9HN, United Kingdom.
Emma L RavenDepartment of Chemistry, Henry Wellcome Building, University of Leicester, University Road, Leicester LE1 7RH, United Kingdom. Electronic address: emma.raven@le.ac.uk.
University of Leicester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/C00602X/1Wellcome Trust 083636
6 · The paper itself

Abstract

We describe a simple method for the determination of heme protein reduction potentials. We use the method to determine the reduction potentials for the PAS-A domains of the regulatory heme proteins human NPAS2 (Em=-115 mV ± 2 mV, pH 7.0) and human CLOCK (Em=-111 mV ± 2 mV, pH 7.0). We suggest that the method can be easily and routinely applied to the determination of reduction potentials across the family of heme proteins.

Indexed as

Basic Helix-Loop-Helix ProteinsCLOCK ProteinsFluorescent DyesHemeHemeproteinsHumansNerve Tissue ProteinsOxazinesOxidation-ReductionSpectrum AnalysisBasic Helix-Loop-Helix ProteinsCLOCK protein, humanCLOCK ProteinsFluorescent DyesHemeHemeproteinsNerve Tissue ProteinsNile BlueNPAS2 protein, humanOxazinesHemeHeme proteinRedoxReduction potential

Identifiers

PMID24440354
PMCPMC3999514
OpenAlexW2128385833

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.