ArticleBiophysical journal2006
New roles for a key glycine and its neighboring residue in potassium channel gating.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed.
- Cryo-EM structures of Drosophila OR67d-Orco complexes reveal insect pheromone sensing mechanism.Cell research · 2026Article
- Structure and Gating Behavior of the Human Integral Membrane Protein VDAC1 in a Lipid Bilayer.Journal of the American Chemical Society · 2022Article
- Inferring functional units in ion channel pores via relative entropy.European biophysics journal : EBJ · 2021Article
- Conduction through a narrow inward-rectifier KThe Journal of general physiology · 2019Article
- Article
- Conservation analysis of residues in the S4-S5 linker and the terminal part of the S5-P-S6 pore modulus in Kv and HCN channels: flexible determinants for the electromechanical coupling.Pflugers Archiv : European journal of physiology · 2015Article
- Channel Gating Dependence on Pore Lining Helix Glycine Residues in Skeletal Muscle Ryanodine Receptor.The Journal of biological chemistry · 2015Article
- Aromatic-aromatic interactions between residues in KCa3.1 pore helix and S5 transmembrane segment control the channel gating process.The Journal of general physiology · 2014Article
- Cholesterol binding to ion channels.Frontiers in physiology · 2014Review
- Identification of novel cholesterol-binding regions in Kir2 channels.The Journal of biological chemistry · 2013Article
- Q/R site interactions with the M3 helix in GluK2 kainate receptor channels revealed by thermodynamic mutant cycles.The Journal of general physiology · 2013Article
- A conserved mechanism for gating in an ionotropic glutamate receptor.The Journal of biological chemistry · 2013Article
- A Kir6.2 pore mutation causes inactivation of ATP-sensitive potassium channels by disrupting PIP2-dependent gating.PloS one · 2013Article
- Distant cytosolic residues mediate a two-way molecular switch that controls the modulation of inwardly rectifying potassium (Kir) channels by cholesterol and phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)).The Journal of biological chemistry · 2012Article
- Being flexible: the voltage-controllable activation gate of kv channels.Frontiers in pharmacology · 2012Article
- A molecular switch between the outer and the inner vestibules of the voltage-gated Na+ channel.The Journal of biological chemistry · 2010Article
- The RCK2 domain uses a coordination site present in Kir channels to confer sodium sensitivity to Slo2.2 channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Characterization and functional restoration of a potassium channel Kir6.2 pore mutation identified in congenital hyperinsulinism.The Journal of biological chemistry · 2010Article
- PIP(2)-binding site in Kir channels: definition by multiscale biomolecular simulations.Biochemistry · 2009Article
- Non-equivalent role of TM2 gating hinges in heteromeric Kir4.1/Kir5.1 potassium channels.European biophysics journal : EBJ · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Potassium channel activation regulates cellular excitability in cells such as neurons and heart. Ion channel activity relies on a switching mechanism between two conformations, the open and closed states, known as gating. It has been suggested that potassium channels are gated via a pivoted mechanism of the pore-lining helix. Our analysis suggests that hinging occurs at the residue immediately preceding the central glycine of the inner helix. Furthermore, we show that the highly conserved central glycine is necessary to prevent constraining interactions with critical residues in its vicinity, including those located in the selectivity filter. We show that such interactions can impair channel function, and that upon their removal channel activity can be restored.
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.