Evidence map›Paper›PMID 25950970›Full record

ReviewMethods in enzymology2015

EPR Studies of Gating Mechanisms in Ion Channels.

Sudha Chakrapani

Open access · greenAbstract readReview
In one paragraph

Review in Methods in enzymology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.6field-weighted citation impact, top 4% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

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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

1 author at 1 institution in 1 country.

Sudha ChakrapaniDepartment of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, Ohio, USA. Electronic address: sudha.chakrapani@case.edu.
Case Western Reserve University · US

Funding

MOLECULAR MECHANISMS OF DESENSITIZATION AND DRUG MODULATION IN LIGAND-GATED ION CHANNELSR01GM108921 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI CHAKRAPANI, SUDHA · 2014 to 2018
$1.9M
NIGMS NIH HHS 1R01GM108921NIGMS NIH HHS R01 GM108921
6 · The paper itself

Abstract

Ion channels open and close in response to diverse stimuli, and the molecular events underlying these processes are extensively modulated by ligands of both endogenous and exogenous origin. In the past decade, high-resolution structures of several channel types have been solved, providing unprecedented details of the molecular architecture of these membrane proteins. Intrinsic conformational flexibility of ion channels critically governs their functions. However, the dynamics underlying gating mechanisms and modulations are obscured in the information from crystal structures. While nuclear magnetic resonance spectroscopic methods allow direct measurements of protein dynamics, they are limited by the large size of these membrane protein assemblies in detergent micelles or lipid membranes. Electron paramagnetic resonance (EPR) spectroscopy has emerged as a key biophysical tool to characterize structural dynamics of ion channels and to determine stimulus-driven conformational transition between functional states in a physiological environment. This review will provide an overview of the recent advances in the field of voltage- and ligand-gated channels and highlight some of the challenges and controversies surrounding the structural information available. It will discuss general methods used in site-directed spin labeling and EPR spectroscopy and illustrate how findings from these studies have narrowed the gap between high-resolution structures and gating mechanisms in membranes, and have thereby helped reconcile seemingly disparate models of ion channel function.

Indexed as

Ion Channel GatingAnimalsElectron Spin Resonance SpectroscopyHumansLigand-Gated Ion ChannelsModels, MolecularPotassium Channels, Voltage-GatedProtein ConformationVoltage-Gated Sodium ChannelsLigand-Gated Ion ChannelsPotassium Channels, Voltage-GatedVoltage-Gated Sodium ChannelsEPR spectroscopyGatingIon channelsMembrane reconstitutionProtein dynamics

Identifiers

PMID25950970
PMCPMC4503332
OpenAlexW258056059

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.