An Intracellular Allosteric Modulator Binding Pocket in SK2 Ion Channels Is Shared by Multiple Chemotypes. [electronic resource]
Producer: 20190111Description: 533-544.e3 p. digitalISSN:- 1878-4186
- Allosteric Regulation
- Amino Acid Motifs
- Anticonvulsants -- chemistry
- Binding Sites
- Calmodulin -- chemistry
- Cloning, Molecular
- Crystallography, X-Ray
- Escherichia coli -- genetics
- Gene Expression
- Genetic Vectors -- chemistry
- HEK293 Cells
- Humans
- Indoles -- chemistry
- Models, Molecular
- Oximes -- chemistry
- Protein Binding
- Protein Conformation, alpha-Helical
- Protein Interaction Domains and Motifs
- Pyrazoles -- chemistry
- Pyrimidines -- chemistry
- Recombinant Proteins -- chemistry
- Riluzole -- chemistry
- Small-Conductance Calcium-Activated Potassium Channels -- chemistry
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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