Evidence map›Paper›PMID 25324390›Full record

ArticleScience (New York, N.Y.)2014

Structure and selectivity in bestrophin ion channels.

Tingting Yang, Qun Liu, Brian Kloss, Renato Bruni, Ravi C Kalathur, Youzhong Guo, Edda Kloppmann, Burkhard Rost, Henry M Colecraft, Wayne A Hendrickson

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

91 citing papers in PubMed, 138 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Astrocytic BEST1 can serve as a target for functional recovery after ischemic stroke.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Article
  7. Electronic Polarizability Tunes the Function of the Human Bestrophin 1 ClJournal of chemical theory and computation · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Electronic Polarizability Tunes the Function of the Human Bestrophin 1 ClbioRxiv : the preprint server for biology · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

31 more citing papers are in PubMed but not listed here.

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 1 country.

Tingting YangDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Qun LiuNew York Structural Biology Center, Synchrotron Beamlines, Brookhaven National Laboratory, Upton, NY 11973, USA.
Brian KlossNew York Consortium on Membrane Protein Structure, New York Structural Biology Center, 89 Convent Avenue, New York, NY 10027, USA.
Renato BruniNew York Consortium on Membrane Protein Structure, New York Structural Biology Center, 89 Convent Avenue, New York, NY 10027, USA.
Ravi C KalathurNew York Consortium on Membrane Protein Structure, New York Structural Biology Center, 89 Convent Avenue, New York, NY 10027, USA.
Youzhong GuoDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Edda KloppmannNew York Consortium on Membrane Protein Structure, New York Structural Biology Center, 89 Convent Avenue, New York, NY 10027, USA. Department of Informatics, Bioinformatics and Computational Biology, TUM (Technische Universität München), Garching 85748, Germany.
Burkhard RostNew York Consortium on Membrane Protein Structure, New York Structural Biology Center, 89 Convent Avenue, New York, NY 10027, USA. Department of Informatics, Bioinformatics and Computational Biology, TUM (Technische Universität München), Garching 85748, Germany.
Henry M ColecraftDepartment of Physiology and Cellular Biophysics, Columbia University, New York, NY 10032, USA.
Wayne A HendricksonDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. New York Structural Biology Center, Synchrotron Beamlines, Brookhaven National Laboratory, Upton, NY 11973, USA. New York Consortium on Membrane Protein Structure, New York Structural Biology Center, 89 Convent Avenue, New York, NY 10027, USA. Department of Physiology and Cellular Biophysics, Columbia University, New York, NY 10032, USA. wayne@xtl.cumc.columbia.edu.
New York Structural Biology Center · USColumbia University · US

Funding

Sub 9 at AECMU54GM075026 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI GOUAUX, JAMES E · 2005 to 2009
$16.8M
Structural Genomics on Membrane ProteinsU54GM095315 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI ROST, BURKHARD · 2010 to 2014
$15.2M
Proposal for an Administrative Supplement for Equipment Purchases for NIGMS Awardees NOT-GM-18-022R01GM107462 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI HENDRICKSON, WAYNE A. · 2014 to 2021
$3.6M
Structure-function Analysis of BestrophinsR00EY025290 · NEI · UNIVERSITY OF ROCHESTER · PI YANG, TINGTING · 2016 to 2018
$747k
NEI NIH HHS R00 EY025290NIGMS NIH HHS GM095315NIGMS NIH HHS GM107462NIGMS NIH HHS R01 GM107462NIGMS NIH HHS U54 GM075026NIGMS NIH HHS U54 GM095315
6 · The paper itself

Abstract

Human bestrophin-1 (hBest1) is a calcium-activated chloride channel from the retinal pigment epithelium, where mutations are associated with vitelliform macular degeneration, or Best disease. We describe the structure of a bacterial homolog (KpBest) of hBest1 and functional characterizations of both channels. KpBest is a pentamer that forms a five-helix transmembrane pore, closed by three rings of conserved hydrophobic residues, and has a cytoplasmic cavern with a restricted exit. From electrophysiological analysis of structure-inspired mutations in KpBest and hBest1, we find a sensitive control of ion selectivity in the bestrophins, including reversal of anion/cation selectivity, and dramatic activation by mutations at the cytoplasmic exit. A homology model of hBest1 shows the locations of disease-causing mutations and suggests possible roles in regulation.

Indexed as

Klebsiella pneumoniaeBacterial ProteinsBestrophinsChloride ChannelsCrystallography, X-RayElectric ConductivityEye ProteinsHumansProtein ConformationStatic ElectricityBacterial ProteinsBEST1 protein, humanBestrophinsChloride ChannelsEye Proteins

Identifiers

PMID25324390
PMCPMC4341822
OpenAlexW2094310458

What OpenQuestion holds

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LicenceTDM
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.