mscS Antibody

1. inactivation process of wild-type MscS was strongly affected by voltage. The wild-type MscS inactivated at +60 to +80 mV but not at -60 to +40 mV. PMID: 28101504
2. Mutations in a conserved domain of E. coli MscS to the most conserved superfamily residue leads to kinetic changes. PMID: 26340270
3. Molecular dynamics and biophysical analyses show that the volume of the pockets and thus the number of lipid acyl chains within them decreases upon channel opening. PMID: 26551077
4. Data show that trifluoroethanol (TFE) affects mechanosensitive channel of small conductance (MscS) channel gating kinetics in spheroplasts and liposomes. PMID: 26116700
5. Data indicate that mechanosensitive channel of small conductance (MscS) protein opens in response to a relief of intrinsic lipid bilayer pressure. PMID: 25450806
6. We report here crystal structures of MscS from E. coli and Helicobacter pylori solubilized in the detergent beta-dodecylmaltoside at resolutions of 4.4 and 4.2 A, respectively. PMID: 23339071
7. Article reviews the science that led to the isolation and identification of MscS. structure-function relationship of the channel, in particular the structural and biochemical approaches to understanding channel gating. [Review] PMID: 22404681
8. Data show that the MscL/MscS threshold ratio dramatically decreased in thinner compared with thicker bilayers. PMID: 22586095
9. Tension dependencies of both inactivation and recovery rates suggest the spatial scale of the inactivating transition, which guides the modeling of the inactivated state of MscS. PMID: 21670207
10. Both F68S and L111S in MscS substitutions produced severe loss-of-function phenotypes in vivo by increasing the inactivation rate and promoting unusual 'silent' inactivation from the resting state PMID: 20208543
11. the crystal structure of MscS does not represent an open state; MscS gate involves a vapor-lock mechanism where limited changes of geometry or surface polarity can locally switch the regime between water-filled (conducting)& empty (nonconducting) states PMID: 15111405
12. The crystal structure of MscS reveals a homoheptamer with three transmembrane segments and a large cytoplasmic domain PMID: 17500538
13. Analysis of the fluorescence properties of purified mutant MscS proteins containing single Trp residues revealed that W16 and W251 are relatively inaccessible, whereas W240 is accessible to quenching agents. PMID: 17718516
14. Transition to this unique mechanosensitive channel state is discussed in terms of existing data. PMID: 18065458
15. study presents a 3.45 angstrom-resolution structure for the MscS channel in an open conformation; structure suggests a molecular mechanism that underlies MscS gating and its decay of conductivity during prolonged activation PMID: 18755969
16. determination of structural rearrangements associated with MscS activation in membranes; transition from closed to open state is accompanied by downward tilting of the transmembrane TM1-TM2 hairpin & by expansion, tilt & rotation of the TM3 helices PMID: 18755978
17. MscL and MscS are tangible models for studying conformational transitions in membrane proteins driven directly by membrane tension. PMID: 19383606

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KEGG: ecj:JW2891

STRING: 316385.ECDH10B_3099