ArticleChannels (Austin, Tex.)2014
Selectivity mechanisms in MscS-like channels: From structure to function.
Article in Channels (Austin, Tex.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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.
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Who cites it
5 citing papers in PubMed.
- Article
- Nonpolar residues in the presumptive pore-lining helix of mechanosensitive channel MSL10 influence channel behavior and establish a nonconducting function.Plant direct · 2018Article
- Patch clamp characterization of the effect of cardiolipin on MscS of E. coli.European biophysics journal : EBJ · 2015Article
- The evolutionary 'tinkering' of MscS-like channels: generation of structural and functional diversity.Pflugers Archiv : European journal of physiology · 2015Review
- Energetics of gating MscS by membrane tension in azolectin liposomes and giant spheroplasts.Channels (Austin, Tex.) · 2014Article
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The E. coli mechanosensitive (MS) channel of small conductance (EcMscS) is the prototype of a diverse family of channels present in all domains of life. While EcMscS has been extensively studied, recent developments show that MscS may display some characteristics not widely conserved in this protein subfamily. With numerous members now electrophysiologically characterized, this subfamily of channels displays a breadth of ion selectivity with both anion and cation selective members. The selectivity of these channels may be relatively weak in comparison to voltage-gated channels but their selectivity mechanisms represent great novelty. Recent studies have identified unexpected residues important for selectivity in these homologs revealing different selectivity mechanisms than those employed by voltage gated K(+), Na(+), Ca(2+) and Cl(-) channels whose selectivity filters are housed within their transmembrane pores. This commentary looks at what is currently known about MscS subfamily selectivity and begins to unravel the potential physiological relevance of these differences.
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