ArticleProceedings of the National Academy of Sciences of the United States of America1999
Cytoplasmic amino and carboxyl domains form a wide intracellular vestibule in an inwardly rectifying potassium channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed.
- Redox Regulation of KAntioxidants & redox signaling · 2024Review
- The network of cardiac KNaunyn-Schmiedeberg's archives of pharmacology · 2024Review
- Mechanism for attenuated outward conductance induced by mutations in the cytoplasmic pore of Kir2.1 channels.Scientific reports · 2015Article
- In vivo expression of a light-activatable potassium channel using unnatural amino acids.Neuron · 2013Article
- Phosphatidylinositol-4,5-bisphosphate (PIP2) regulation of strong inward rectifier Kir2.1 channels: multilevel positive cooperativity.The Journal of physiology · 2008Article
- Localization of the pH gate in Kir1.1 channels.Biophysical journal · 2006Article
- Ring of negative charge in BK channels facilitates block by intracellular Mg2+ and polyamines through electrostatics.The Journal of general physiology · 2006Article
- Electrostatics in the cytoplasmic pore produce intrinsic inward rectification in kir2.1 channels.The Journal of general physiology · 2005Article
- Functional architecture of the inner pore of a voltage-gated Ca2+ channel.The Journal of general physiology · 2005Article
- Cysteine accessibility in ClC-0 supports conservation of the ClC intracellular vestibule.The Journal of general physiology · 2005Article
- A ring of negative charges in the intracellular vestibule of Kir2.1 channel modulates K+ permeation.Biophysical journal · 2005Article
- Molecular basis of inward rectification: polyamine interaction sites located by combined channel and ligand mutagenesis.The Journal of general physiology · 2004Article
- Probing the pore of ClC-0 by substituted cysteine accessibility method using methane thiosulfonate reagents.The Journal of general physiology · 2003Article
- Inward rectification by polyamines in mouse Kir2.1 channels: synergy between blocking components.The Journal of physiology · 2003Article
- Contribution of cytosolic cysteine residues to the gating properties of the Kir2.1 inward rectifier.Biophysical journal · 2003Article
- Spermine block of the strong inward rectifier potassium channel Kir2.1: dual roles of surface charge screening and pore block.The Journal of general physiology · 2002Article
- Structural and functional determinants of conserved lipid interaction domains of inward rectifying Kir6.2 channels.The Journal of general physiology · 2002Article
- Mechanism of Kir6.2 channel inhibition by sulfhydryl modification: pore block or allosteric gating?The Journal of physiology · 2002Article
- Control of rectification and permeation by two distinct sites after the second transmembrane region in Kir2.1 K+ channel.The Journal of physiology · 2001Article
- Structural determinants of PIP(2) regulation of inward rectifier K(ATP) channels.The Journal of general physiology · 2000Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
We have studied the structural components and architecture of the intracellular vestibule of a strongly rectifying channel (Kir2.1) expressed in Xenopus oocytes. Putative vestibule-lining residues were identified by systematically examining covalent modification by sulfhydryl-specific reagents of cysteine residues engineered into two cytoplasmic regions. In a stretch of 33 amino acids in the amino terminus (from C54 to V86) and 22 amino acids in the carboxyl terminus (from R213 to S234), 15 and 11 residues, respectively, were found to be accessible to methanethiosulfonate ethylammonium (MTSEA) or methanethiosulfonate ethyltrimethylammonium (MTSET) and presumably project into the aqueous intracellular vestibule. The pattern of accessibility suggests that both stretches may adopt an extended loop structure. To explore the physical dimension of the intracellular vestibule, we covalently linked a constrained number (one to four) of positively charged moieties of different sizes to the E224 position and found that this vestibule region is sufficiently wide to accommodate four modifying groups with dimensions of 12 A x 10 A x 6 A. These results suggest that regions in both the amino and carboxyl domains of Kir2.1 channel form a long and wide intracellular vestibule that protrudes beyond the membrane into the cytoplasm.
Indexed as
Identifiers
What OpenQuestion holds
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.