Evidence map›Paper›PMID 27958724›Full record

ArticleJournal of the American Chemical Society2016

Engineering an Artificial Flavoprotein Magnetosensor.

Chris Bialas, Lauren E Jarocha, Kevin B Henbest, Tilo M Zollitsch, Goutham Kodali, Christiane R Timmel, Stuart R Mackenzie, P Leslie Dutton, Christopher C Moser, P J Hore

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

10 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
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  7. The ascent of man(made oxidoreductases).Current opinion in structural biology · 2018
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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

10 authors at 2 institutions in 2 countries.

Chris BialasJohnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.
Lauren E JarochaDepartment of Chemistry, University of Oxford , Physical and Theoretical Chemistry Laboratory, Oxford OX1 3QZ, United Kingdom.
Kevin B HenbestDepartment of Chemistry, University of Oxford , Inorganic Chemistry Laboratory, Oxford OX1 3QR, United Kingdom.
Tilo M ZollitschDepartment of Chemistry, University of Oxford , Physical and Theoretical Chemistry Laboratory, Oxford OX1 3QZ, United Kingdom.
Goutham KodaliJohnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.ORCID 0000-0001-6356-9016
Christiane R TimmelDepartment of Chemistry, University of Oxford , Inorganic Chemistry Laboratory, Oxford OX1 3QR, United Kingdom.
Stuart R MackenzieDepartment of Chemistry, University of Oxford , Physical and Theoretical Chemistry Laboratory, Oxford OX1 3QZ, United Kingdom.ORCID 0000-0002-3166-8631
P Leslie DuttonJohnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.
Christopher C MoserJohnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.
P J HoreDepartment of Chemistry, University of Oxford , Physical and Theoretical Chemistry Laboratory, Oxford OX1 3QZ, United Kingdom.ORCID 0000-0002-8863-570X
University of Oxford · GBJohnson Foundation · US

Funding

STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
European Research Council 340451NIGMS NIH HHS T32 GM008275
6 · The paper itself

Abstract

Migratory birds use the Earth's magnetic field as a source of navigational information. This light-dependent magnetic compass is thought to be mediated by cryptochrome proteins in the retina. Upon light activation, electron transfer between the flavin adenine dinucleotide cofactor and tryptophan residues leads to the formation of a spin-correlated radical pair, whose subsequent fate is sensitive to external magnetic fields. To learn more about the functional requirements of this complex chemical compass, we have created a family of simplified, adaptable proteins-maquettes-that contain a single tryptophan residue at different distances from a covalently bound flavin. Despite the complete absence of structural resemblance to the native cryptochrome fold or sequence, the maquettes exhibit a strong magnetic field effect that rivals those observed in the natural proteins in vitro. These novel maquette designs offer unprecedented flexibility to explore the basic requirements for magnetic sensing in a protein environment.

Indexed as

Magnetic FieldsProtein EngineeringFlavoproteinsProtein Conformation, alpha-HelicalFlavoproteins

Identifiers

PMID27958724
PMCPMC5711731
OpenAlexW2567233592

What OpenQuestion holds

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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.