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Presynaptic potassium channels
Current Opinion in Neurobiology, 1996The 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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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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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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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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▪ 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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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 as a Target for Cancer Therapy: Current Perspectives
OncoTargets and Therapy, 2022Wendy Gonzalez +2 more
exaly
Flavonoids as Modulators of Potassium Channels
International Journal of Molecular Sciences, 2023Agata Wawrzkiewicz-Jałowiecka +2 more
exaly
Peptide toxins and potassium channels
1990After the first detailed description of the delayed outward potassium current in squid axon by Hodgkin and Huxley (1952) it took electrophysiologists more than 20 years to realize that in addition to it several types of K+ currents can exist in the same cell and that they have a number of functions including modulation of cell excitability and ...
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