The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Inwardly Rectifying Potassium Channels: Their Structure, Function, and Physiological Roles
Abstract
Inwardly rectifying K+(Kir) channels allow K+to move more easily into rather than out of the cell. They have diverse physiological functions depending on their type and their location. There are seven Kir channel subfamilies that can be classified into four functional groups: classical Kir channels (Kir2.x) are constitutively active, G protein-gated Kir channels (Kir3.x) are regulated by G protein-coupled receptors, ATP-sensitive K+channels (Kir6.x) are tightly linked to cellular metabolism, and K+transport channels (Kir1.x, Kir4.x, Kir5.x, and Kir7.x). Inward rectification results from pore block by intracellular substances such as Mg 2+and polyamines. Kir channel activity can be modulated by ions, phospholipids, and binding proteins. The basic building block of a Kir channel is made up of two transmembrane helices with cytoplasmic NH 2 and COOH termini and an extracellular loop which folds back to form the pore-lining ion selectivity filter. In vivo, functional Kir channels are composed of four such subunits which are either homo- or heterotetramers. Gene targeting and genetic analysis have linked Kir channel dysfunction to diverse pathologies. The crystal structure of different Kir channels is opening the way to understanding the structure-function relationships of this simple but diverse ion channel family.
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Cited by
Verkhratsky, A., & Nedergaard, M. (2018) · Physiological Reviews · doi:10.1152/physrev.00042.2016 · Cited by 1,678
Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men
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Nitric oxide and redox mechanisms in the immune response
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Equalizing excitation-inhibition ratios across visual cortical neurons
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Astroglial Kir4.1 in the lateral habenula drives neuronal bursts in depression
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Metadata
- Authors
- Hibino, H., Inanobe, A., Furutani, K., Murakami, S., Findlay, I., & Kurachi, Y.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2010-01
- Volume
- 90
- Issue
- 1
- Pages
- 291-366
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2161227647
- Cited by
- 1,539
- References
- 19
- FWCI
- 4.96
- Type
- journal article
- Language
- en
- Open access
- closed
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