Evidence map›Paper›PMID 25290819›Full record

ArticleNature communications2014

Proof of dual-topology architecture of Fluc F- channels with monobody blockers.

Randy B Stockbridge, Akiko Koide, Christopher Miller, Shohei Koide

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

35 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
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  5. Review
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  9. Review
  10. Article
  11. Article
  12. Membrane Exporters of Fluoride Ion.Annual review of biochemistry · 2021
    Review
  13. Article
  14. Article
  15. Article
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  19. Review
  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

4 authors at 3 institutions in 1 country.

Randy B StockbridgeDepartment of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA.
Akiko KoideDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois 60637, USA.
Christopher MillerDepartment of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454, USA.
Shohei KoideDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois 60637, USA.
University of Chicago · USBrandeis University · USHoward Hughes Medical Institute · US

Funding

Synthetic Antigen Binder CoreU54GM087519 · NIGMS · UNIVERSITY OF CHICAGO · PI ZHOU, MING · 2010 to 2017
$31.9M
Re-Engineering Translational Research at the University of ChicagoUL1TR000430 · NCATS · UNIVERSITY OF CHICAGO · PI SOLWAY, JULIAN · 2012 to 2016
$20.2M
Mechanisms of Biological Fluoride Resistance ExportersR01GM107023 · NIGMS · BRANDEIS UNIVERSITY · PI MILLER, CHRISTOPHER · 2014 to 2017
$1.1M
The structure, function, and biological role of a microbial fluoride channelK99GM111767 · NIGMS · BRANDEIS UNIVERSITY · PI STOCKBRIDGE, RANDY B. · 2014 to 2015
$128k
NCATS NIH HHS UL1 TR000430NIGMS NIH HHS K99 GM111767NIGMS NIH HHS R01 GM107023NIGMS NIH HHS R01-GM107023NIGMS NIH HHS U54 GM087519NIGMS NIH HHS U54-GM087519
6 · The paper itself

Abstract

Fluc-type F(-) channels--used by microorganisms for resisting fluoride toxicity--are unusual in their quaternary architecture: they are thought to associate as dimers with the two subunits in antiparallel transmembrane orientation. Here, we subject this unusual structural feature to a direct test. Single purified Fluc channels recorded in planar lipid bilayers are constitutively open, with rare, short-lived closings. Using combinatorial libraries, we generated synthetic binding proteins, 'monobodies,' that specifically bind to Fluc homologues with nanomolar affinity. Reversible binding of monobodies to two different Fluc channel homologues is seen in single-channel recordings as long-lived nonconducting events that follow bimolecular kinetics. By applying monobodies sequentially to the two sides of the bilayer in a double-sided perfusion manoeuvre, we show that Fluc channels present monobody-binding epitopes to both sides of the membrane. The result establishes that Fluc subunits are arranged in dimeric antiparallel orientation.

Indexed as

FluoridesIon ChannelsLipid BilayersProtein Structure, QuaternaryFluoridesIon ChannelsLipid Bilayers

Identifiers

PMID25290819
PMCPMC4265568
OpenAlexW2031664044

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.