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Presynaptic potassium channels

Current Opinion in Neurobiology, 1996
The past year has witnessed some significant improvements in our understanding of the molecular diversity, subunit composition, and functional properties of K+ channels in heterologous expression systems. Immunocytochemical studies have yielded important information on the localization of K+ channel proteins to synaptic terminals in mammalian brain ...
J, Roeper, O, Pongs
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INWARD RECTIFIER POTASSIUM CHANNELS

Annual Review of Physiology, 1997
▪ Abstract  The past three years have seen remarkable progress in research on the molecular basis of inward rectification, with significant implications for basic understanding and pharmacological manipulation of cellular excitability. Expression cloning of the first inward rectifier K channel (Kir) genes provided the necessary breakthrough that has ...
C G, Nichols, A N, Lopatin
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Potassium channels and epilepsy

Acta Neurologica Scandinavica, 2022
With the development and application of next-generation sequencing technology, the aetiological diagnosis of genetic epilepsy is rapidly becoming easier and less expensive. Additionally, there is a growing body of research into precision therapy based on genetic diagnosis.
Kai, Gao   +3 more
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Potassium Channel Ontogeny

Annual Review of Physiology, 2002
▪ Abstract  Potassium channels are multi-subunit complexes, often composed of several polytopic membrane proteins and cytosolic proteins. The formation of these oligomeric structures, including both biogenesis and trafficking, is the subject of this review.
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Potassium channel structures

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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Potassium channel toxins

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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Potassium Channels in Cancer

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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Trafficking of potassium channels

Current Opinion in Neurobiology, 2005
Recent 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

1997
Publisher 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, 2005
ATP-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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