Evidence map›Paper›PMID 21723817›Full record

ArticleBiophysical journal2011

Cytoplasmic domain filter function in the mechanosensitive channel of small conductance.

Ramya Gamini, Marcos Sotomayor, Christophe Chipot, Klaus Schulten

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.2field-weighted citation impact, top 9% 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

16 citing papers in PubMed, 30 citations in OpenAlex.

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  13. Structure and molecular mechanism of an anion-selective mechanosensitive channel of small conductance.Proceedings of the National Academy of Sciences of the United States of America · 2012
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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

4 authors at 3 institutions in 2 countries.

Ramya GaminiBeckman Institute, University of Illinois at Urbana-Champaign, Champaign, Illinois, USA.
Marcos Sotomayor
Christophe Chipot
Klaus Schulten
University of Illinois Urbana-Champaign · USCentre National de la Recherche Scientifique · FRHarvard University · US

Funding

System-Level Simulation of a Bioenergetic MembraneR01GM067887 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2003 to 2018
$4.0M
Howard Hughes Medical InstituteNIGMS NIH HHS 1 R01-GM067887NIGMS NIH HHS R01 GM067887
6 · The paper itself

Abstract

Mechanosensitive channels, inner membrane proteins of bacteria, open and close in response to mechanical stimuli such as changes in membrane tension during osmotic stress. In bacteria, these channels act as safety valves preventing cell lysis upon hypoosmotic cell swelling: the channels open under membrane tension to release osmolytes along with water. The mechanosensitive channel of small conductance, MscS, consists, in addition to the transmembrane channel, of a large cytoplasmic domain (CD) that features a balloon-like, water filled chamber opening to the cytoplasm through seven side pores and a small distal pore. The CD is apparently a molecular sieve covering the channel that optimizes loss of osmolytes during osmoadaptation. We employ diffusion theory and molecular dynamics simulations to explore the transport kinetics of Glu(-) and K(+) as representative osmolytes. We suggest that the CD indeed acts as a filter that actually balances passage of Glu(-) and K(+), and possibly other positive and negative osmolytes, to yield a largely neutral efflux and, thereby, reduce cell depolarization in the open state and conserve to a large degree the essential metabolite Glu(-).

Indexed as

Ion Channel GatingMechanotransduction, CellularBiological TransportCell MembraneCytoplasmDiffusionEscherichia coliEscherichia coli ProteinsGlutamic AcidIon ChannelsModels, MolecularPotassiumProtein Structure, TertiaryStatic ElectricityStructure-Activity RelationshipThermodynamicsEscherichia coli ProteinsGlutamic AcidIon ChannelsMscS protein, E coliPotassium

Identifiers

PMID21723817
PMCPMC3127185
OpenAlexW2045454598

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.