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KcsA protein, Streptomyces coelicolor

 
National Institutes of Health

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2 relations

Broader (2)

Bacterial ProteinsVoltage-Gated Potassium Channel

Papers overview

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2015
2015
Visualizing KcsA Conformational Changes upon Ion Binding by Infrared Spectroscopy and Atomistic Modeling
The effect of ion binding in the selectivity filter of the potassium channel KcsA is investigated by combining amide I Fourier… Expand
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Highly Cited
2012
Highly Cited
2012
Protonation state of E71 in KcsA and its role for channel collapse and inactivation
The prototypical prokaryotic potassium channel KcsA alters its pore depending on the ambient potassium; at high potassium, it… Expand
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2012
2012
Contribution of ion binding affinity to ion selectivity and permeation in KcsA, a model potassium channel.
Ion permeation and selectivity, key features in ion channel function, are believed to arise from a complex ensemble of energetic… Expand
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2011
2011
Do Small Headgroups of Phosphatidylethanolamine and Phosphatidic Acid Lead to a Similar Folding Pattern of the K+ Channel?
Phospholipid headgroups act as major determinants in proper folding of oligomeric membrane proteins. The K+-channel KcsA is the… Expand
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2009
2009
Dissimilarity in the channel intrinsic stability among the bacterial KcsA and the inwardly rectifying potassium channel ROMK1.
In this study, we compared the channel intrinsic stability of the bacterial K(+)-channel KcsA and the inwardly rectifying… Expand
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2009
2009
Mutations in the K+-Channel KcsA Toward Kir Channels Alter Salt-Induced Clusterization and Blockade by Quaternary Alkylammonium Ions
Protein aggregation is a result of malfunction in protein folding, assembly, and transport, caused by protein mutation and/or… Expand
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Highly Cited
2009
Highly Cited
2009
Pulsed electron-electron double-resonance determination of spin-label distances and orientations on the tetrameric potassium ion channel KcsA.
Pulsed electron-electron double-resonance (PELDOR) measurements are presented from the potassium ion channel KcsA both… Expand
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2003
2003
The peptaibol antiamoebin as a model ion channel: similarities to bacterial potassium channels.
Antiamoebin (AAM) is a polypeptide antibiotic that is capable of forming ion channels in phospholipid membranes: planar bilayer… Expand
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