ArticleScience advances2022
Cryo-electron microscopy unveils unique structural features of the human Kir2.1 channel.
Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 39 citations in OpenAlex.
- Molecular mechanisms of Kir channel gating.Biochemical Society transactions · 2026Review
- Structural and functional studies of inward rectifier Kir7.1 and its regulation by the Melanocortin-4 receptor.Nature communications · 2026Article
- Potassium channels in vascular smooth muscle cells.Physiological reviews · 2026Review
- Cryo-EM structures of heteromeric Kir4.1/5.1 channel suggest mechanisms of inward rectification and channel blockage.Nature communications · 2026Article
- Bioactive lipid-mediated structural and functional regulation of the essential human potassium channel Kir7.1.Nature communications · 2026Article
- Inwardly rectifying potassium channels: Critical insights for insect species and Apis mellifera.Channels (Austin, Tex.) · 2025Review
- PIP2-driven cytoplasmic domain motions are coupled to Kir2 channel gating.The Journal of general physiology · 2025Article
- The citrus tristeza virus p33 protein functions as a viroporin.PLoS pathogens · 2025Article
- High-yield production and characterization of functional Kir2.1 ion channel usingSynthetic and systems biotechnology · 2025Article
- Review
- Atomic-level investigation of KCNJ2 mutations associated with ventricular arrhythmic syndrome phenotypes.Scientific reports · 2025Article
- Extended Sampling of Macromolecular Conformations from Uniformly Distributed Points on Multidimensional Normal Mode Hyperspheres.Journal of chemical theory and computation · 2024Article
- Kir2.1 mutations differentially increase the risk of flecainide proarrhythmia in Andersen Tawil Syndrome.medRxiv : the preprint server for health sciences · 2024Article
- The network of cardiac KNaunyn-Schmiedeberg's archives of pharmacology · 2024Review
- Structure of the Ion Channel Kir7.1 and Implications for its Function in Normal and Pathophysiologic States.bioRxiv : the preprint server for biology · 2024Article
- Extracellular Kir2.1Circulation research · 2024Article
- Electro-metabolic signaling.The Journal of general physiology · 2024Article
- Endocannabinoid regulation of inward rectifier potassium (Kir) channels.Frontiers in pharmacology · 2024Article
- Human Kir2.1 Potassium Channel: Protocols for Cryo-EM Data Processing and Molecular Dynamics Simulations.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We present the first structure of the human Kir2.1 channel containing both transmembrane domain (TMD) and cytoplasmic domain (CTD). Kir2.1 channels are strongly inward-rectifying potassium channels that play a key role in maintaining resting membrane potential. Their gating is modulated by phosphatidylinositol 4,5-bisphosphate (PIP
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.