Evidence map›Paper›PMID 23063010›Full record

ArticleStructure (London, England : 1993)2012

Nano-positioning system for structural analysis of functional homomeric proteins in multiple conformations.

H Clark Hyde, Walter Sandtner, Ernesto Vargas, Alper T Dagcan, Janice L Robertson, Benoit Roux, Ana M Correa, Francisco Bezanilla

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. A Historical Outline of Fluorescence Spectroscopy in Ion Channel Research.Advances in experimental medicine and biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Mapping of voltage sensor positions in resting and inactivated mammalian sodium channels by LRET.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  7. Article
  8. β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  9. 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

8 authors.

H Clark HydeDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA. fbezanilla@uchicago.edu
Walter Sandtner
Ernesto Vargas
Alper T Dagcan
Janice L Robertson
Benoit Roux
Ana M Correa
Francisco Bezanilla

Funding

Synthetic Antigen Binder CoreU54GM087519 · NIGMS · UNIVERSITY OF CHICAGO · PI PEROZO, EDUARDO A · 2010 to 2017
$31.9M
The Electrophysiological Studies of Voltage Gated ChannelsR01GM030376 · NIGMS · UNIVERSITY OF CHICAGO · PI BEZANILLA, FRANCISCO J · 1985 to 2025
$9.1M
Computational Studies of Ion Channels - Resubmission 01R01GM062342 · NIGMS · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI ROUX, BENOIT · 2001 to 2022
$8.7M
Graduate Program in Biophysical Sciences at the University of Chicago - Renewal 0T32EB009412 · NIBIB · UNIVERSITY OF CHICAGO · PI ENGEL, GREGORY S, SOSNICK, TOBIN R · 2009 to 2023
$4.9M
ELECTROPHYSIOLOGICAL STUDIES OF VOLTAGE GATED CHANNELSR37GM030376 · NIGMS · UNIVERSITY OF CHICAGO · PI BEZANILLA, FRANCISCO J · 1999 to 2008
$3.7M
Voltage-Gating in Bacterial Ion ChannelsR01GM068044 · NIGMS · UNIVERSITY OF CHICAGO · PI CORREA, ANA M · 2004 to 2010
$1.8M
NIBIB NIH HHS T32 EB009412NIGMS NIH HHS R01 GM030376NIGMS NIH HHS R01 GM062342NIGMS NIH HHS R01 GM068044NIGMS NIH HHS R37 GM030376NIGMS NIH HHS U54 GM087519
6 · The paper itself

Abstract

Proteins may undergo multiple conformational changes required for their function. One strategy used to estimate target-site positions in unknown structural conformations involves single-pair resonance energy transfer (RET) distance measurements. However, interpretation of inter-residue distances is difficult when applied to three-dimensional structural rearrangements, especially in homomeric systems. We developed a positioning method using inverse trilateration/triangulation to map target sites within a homomeric protein in all defined states, with simultaneous functional recordings. The procedure accounts for probe diffusion to accurately determine the three-dimensional position and confidence region of lanthanide LRET donors attached to a target site (one per subunit), relative to a single fluorescent acceptor placed in a static site. As first application, the method is used to determine the position of a functional voltage-gated potassium channel's voltage sensor. Our results verify the crystal structure relaxed conformation and report on the resting and active conformations for which crystal structures are not available.

Indexed as

Molecular Dynamics SimulationAlgorithmsAnimalsCells, CulturedCoordination ComplexesFluorescence Resonance Energy TransferProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryShaker Superfamily of Potassium ChannelsSoftwareTerbiumXenopus laevisCoordination ComplexesShaker Superfamily of Potassium ChannelsTerbium

Identifiers

PMID23063010
PMCPMC3633233

What OpenQuestion holds

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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.