Evidence map›Paper›PMID 31378315›Full record

ArticleBiophysical journal2019

Voltage-Dependent Profile Structures of a Kv-Channel via Time-Resolved Neutron Interferometry.

Andrey Y Tronin, Lina J Maciunas, Kimberly C Grasty, Patrick J Loll, Haile A Ambaye, Andre A Parizzi, Valeria Lauter, Andrew D Geragotelis, J Alfredo Freites, Douglas J Tobias and 1 more

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Review
  3. Voltage-dependent structural models of the human Hv1 proton channel from long-timescale molecular dynamics simulations.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

11 authors at 4 institutions in 1 country.

Andrey Y TroninDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania.
Lina J MaciunasDepartment of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania.
Kimberly C GrastyDepartment of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania.
Patrick J LollDepartment of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania.
Haile A AmbayeNeutron Scattering Division, Neutron Sciences Directorate, Oak Ridge National Laboratory, Oak Ridge, Tennessee.
Andre A ParizziNeutron Scattering Division, Neutron Sciences Directorate, Oak Ridge National Laboratory, Oak Ridge, Tennessee.
Valeria LauterNeutron Scattering Division, Neutron Sciences Directorate, Oak Ridge National Laboratory, Oak Ridge, Tennessee.
Andrew D GeragotelisDepartment of Chemistry, University of California Irvine, Irvine, California.
J Alfredo FreitesDepartment of Chemistry, University of California Irvine, Irvine, California.
Douglas J TobiasDepartment of Chemistry, University of California Irvine, Irvine, California.
J Kent BlasieDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania. Electronic address: jkblasie@sas.upenn.edu.
Drexel University · USOak Ridge National Laboratory · USUniversity of California, Irvine · USUniversity of Pennsylvania · US

Funding

X-ray and Neutron Interferometry Studies of Anesthetic Interactions with VoltageP01GM055876 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI LOLL, PATRICK J · 1997 to 2017
$22.4M
NIGMS NIH HHS P01 GM055876
6 · The paper itself

Abstract

Available experimental techniques cannot determine high-resolution three-dimensional structures of membrane proteins under a transmembrane voltage. Hence, the mechanism by which voltage-gated cation channels couple conformational changes within the four voltage sensor domains, in response to either depolarizing or polarizing transmembrane voltages, to opening or closing of the pore domain's ion channel remains unresolved. Single-membrane specimens, composed of a phospholipid bilayer containing a vectorially oriented voltage-gated K

Indexed as

Ion Channel GatingInterferometryLipid BilayersMembrane PotentialsMolecular Dynamics SimulationNeutronsPotassium Channels, Voltage-GatedProtein DomainsLipid BilayersPotassium Channels, Voltage-Gated

Identifiers

PMID31378315
PMCPMC6712512
OpenAlexW2959633472

What OpenQuestion holds

Textmetadata
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.