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Nature Reviews Neuroscience, 2002
The molecular basis of K+ channel function is universally conserved. K+ channels allow K+ flux and are essential for the generation of electric current across excitable membranes. K+ channels are also the targets of various intracellular control mechanisms, such that the suboptimal regulation of channel function might be related to pathological ...
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The molecular basis of K+ channel function is universally conserved. K+ channels allow K+ flux and are essential for the generation of electric current across excitable membranes. K+ channels are also the targets of various intracellular control mechanisms, such that the suboptimal regulation of channel function might be related to pathological ...
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Pharmacology & Therapeutics, 1990
Many venom toxins interfere with ion channel function. Toxins, as specific, high affinity ligands, have played an important part in purifying and characterizing many ion channel proteins. Our knowledge of potassium ion channel structure is meager because until recently, no specific potassium channel toxins were known, or identified as such. This review
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Many venom toxins interfere with ion channel function. Toxins, as specific, high affinity ligands, have played an important part in purifying and characterizing many ion channel proteins. Our knowledge of potassium ion channel structure is meager because until recently, no specific potassium channel toxins were known, or identified as such. This review
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2021
Neoplastic transformation is reportedly associated with alterations of the potassium transport across plasma and intracellular membranes. These alterations have been identified as crucial elements of the tumourigenic reprogramming of cells. Potassium channels may contribute to cancer initiation, malignant progression and therapy resistance of tumour ...
Katrin, Ganser +5 more
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Neoplastic transformation is reportedly associated with alterations of the potassium transport across plasma and intracellular membranes. These alterations have been identified as crucial elements of the tumourigenic reprogramming of cells. Potassium channels may contribute to cancer initiation, malignant progression and therapy resistance of tumour ...
Katrin, Ganser +5 more
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Trafficking of potassium channels
Current Opinion in Neurobiology, 2005Recent progress in our understanding of the trafficking of potassium channels can be seen in particular when considering the Kv-type channels. To date, we have discovered that folding of the Kv1.3 T1 domain begins in the ribosomal exit tunnel, and that the cell surface expression of Kv4 channels is enhanced by the presence of two recently identified ...
Heusser, Katja, Schwappach, Blanche
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Pharmacology of Potassium Channels
1997Publisher Summary Potassium channels represent the largest and most diverse family of ion channels. K+ channels can be divided into two groups, voltage-gated and ligand-gated channels, depending on the stimulus that triggers the conformational changes leading to channel opening. K+ channels share in common the feature of having high selectivity for K+
M L, Garcia +6 more
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ATP-Sensitive Potassium Channels
Current Pharmaceutical Design, 2005ATP-sensitive potassium (K(ATP)) channels link membrane excitability to metabolism. They are regulated by intracellular nucleotides and by other factors including membrane phospholipids, protein kinases and phosphatases. K(ATP) channels comprise octamers of four Kir6 pore-forming subunits associated with four sulphonylurea receptor subunits.
Rodrigo, GC, Standen, NB
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Trends in Pharmacological Sciences, 1997
The last session of the conference focused on studies which showed the formation of a channel complex consisting of KvLQT1 (a classical K+ channel protein with six transmembrane regions with one pore structure) and another component, termed minK or IsK (a small protein with a single transmembrane domain) resulting in heteromeric channel with new ...
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The last session of the conference focused on studies which showed the formation of a channel complex consisting of KvLQT1 (a classical K+ channel protein with six transmembrane regions with one pore structure) and another component, termed minK or IsK (a small protein with a single transmembrane domain) resulting in heteromeric channel with new ...
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The structure of the potassium channel: molecular basis of K+ conduction and selectivity.
Science, 1998D. Doyle +7 more
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It's “juxta” potassium channel!
Journal of Neuroscience Research, 2004AbstractNeuronal excitability depends on the appropriate expression and localization of ion channels. Juxtaparanodal Kv1 channels have been used as a model to study the role of neuroglial interactions in regulating the expression and localization of channels in myelinated axons.
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The value of LGI1, Caspr2 and voltage-gated potassium channel antibodies in encephalitis
Nature Reviews Neurology, 2017A. Sonderen +3 more
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