Formation of Functional Heterodimers between the TASK-1 and TASK-3 Two-pore Domain Potassium Channel Subunits
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference44 articles.
1. TWIK-2, a New Weak Inward Rectifying Member of the Tandem Pore Domain Potassium Channel Family
2. A functional role for the two-pore domain potassium channel TASK-1 in cerebellar granule neurons
3. TASK-1, a Two–Pore Domain K+ Channel, Is Modulated by Multiple Neurotransmitters in Motoneurons
4. An oxygen‐, acid‐ and anaesthetic‐sensitive TASK‐like background potassium channel in rat arterial chemoreceptor cells
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1. Potassium channel TASK-5 forms functional heterodimers with TASK-1 and TASK-3 to break its silence;Nature Communications;2024-08-30
2. The Ubiquitin Ligase Adaptor NDFIP1 Interacts with TRESK and Negatively Regulates the Background K+ Current;International Journal of Molecular Sciences;2024-08-15
3. Structures of TASK-1 and TASK-3 K2P channels provide insight into their gating and dysfunction in disease;2024-08-06
4. Structure of the human K2P13.1(THIK-1) channel reveals a novel hydrophilic pore restriction and lipid cofactor site;2024-06-27
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