Evidence map›Paper›PMID 22797911›Full record

ReviewJournal of cell science2012

Molecular force transduction by ion channels: diversity and unifying principles.

Sergei Sukharev, Frederick Sachs

Abstract readReview
In one paragraph

Review in Journal of cell science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed, 1 pooled it
–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

90 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. The energetics of rapid cellular mechanotransduction.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Article
  17. Review
  18. Capsaicin as an amphipathic modulator of NaChannels (Austin, Tex.) · 2022
    Article
  19. Article
  20. Review

30 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

2 authors.

Sergei SukharevDepartment of Biology, University of Maryland, College Park, MD 20742, USA. sukharev@umd.edu
Frederick Sachs

Funding

Roles of Hydration and Lipids in Mechanosensitive Channel GatingR01NS039314 · NINDS · UNIV OF MARYLAND, COLLEGE PARK · PI SUKHAREV, SERGEI I · 2000 to 2009
$2.3M
The bacterial mechanosentitive channel as a multimodal sensor deviceR01GM107652 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI ANISHKIN, ANDRIY, SINTIM, HERMAN O · 2013 to 2016
$1.1M
Functional Cycle of a Mechanosensitive ChannelR01GM075225 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI SUKHAREV, SERGEI I · 2006 to 2009
$1.1M
NIGMS NIH HHS GM075225NIGMS NIH HHS R01 GM075225NIGMS NIH HHS R01 GM107652NINDS NIH HHS NS039314NINDS NIH HHS R01 NS039314
6 · The paper itself

Abstract

Cells perceive force through a variety of molecular sensors, of which the mechanosensitive ion channels are the most efficient and act the fastest. These channels apparently evolved to prevent osmotic lysis of the cell as a result of metabolite accumulation and/or external changes in osmolarity. From this simple beginning, nature developed specific mechanosensitive enzymes that allow us to hear, maintain balance, feel touch and regulate many systemic variables, such as blood pressure. For a channel to be mechanosensitive it needs to respond to mechanical stresses by changing its shape between the closed and open states. In that way, forces within the lipid bilayer or within a protein link can do work on the channel and stabilize its state. Ion channels have the highest turnover rates of all enzymes, and they can act as both sensors and effectors, providing the necessary fluxes to relieve osmotic pressure, shift the membrane potential or initiate chemical signaling. In this Commentary, we focus on the common mechanisms by which mechanical forces and the local environment can regulate membrane protein structure, and more specifically, mechanosensitive ion channels.

Indexed as

Ion Channel GatingMechanotransduction, CellularAdaptation, PhysiologicalAnimalsBiomechanical PhenomenaCell ShapeEnergy MetabolismEscherichia coliEukaryotic CellsFocal AdhesionsHumansIon ChannelsMembrane ProteinsOsmotic PressureStress, MechanicalIon ChannelsMembrane Proteins

Identifiers

PMID22797911
PMCPMC3434843

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.