ReviewPflugers Archiv : European journal of physiology2010
Gating in CNGA1 channels.
Review in Pflugers Archiv : European journal of physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed.
- P-Loop Channels: Experimental Structures, and Physics-Based and Neural Networks-Based Models.Membranes · 2022Review
- CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021Review
- An iris diaphragm mechanism to gate a cyclic nucleotide-gated ion channel.Nature communications · 2018Article
- Insights into the molecular mechanism for hyperpolarization-dependent activation of HCN channels.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- New views on phototransduction from atomic force microscopy and single molecule force spectroscopy on native rods.Scientific reports · 2017Article
- Structural Heterogeneity of CNGA1 Channels Revealed by Electrophysiology and Single-Molecule Force Spectroscopy.ACS omega · 2016Article
- A Cyclic GMP-Dependent K+ Channel in the Blastocladiomycete Fungus Blastocladiella emersonii.Eukaryotic cell · 2015Article
- A structural, functional, and computational analysis suggests pore flexibility as the base for the poor selectivity of CNG channels.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Conformational rearrangements in the transmembrane domain of CNGA1 channels revealed by single-molecule force spectroscopy.Nature communications · 2015Article
- Proton transfer unlocks inactivation in cyclic nucleotide-gated A1 channels.The Journal of physiology · 2015Article
- Structure, dynamics and implied gating mechanism of a human cyclic nucleotide-gated channel.PLoS computational biology · 2014Article
- Central role of soluble adenylyl cyclase and cAMP in sperm physiology.Biochimica et biophysica acta · 2014Review
- The Concise Guide to PHARMACOLOGY 2013/14: ion channels.British journal of pharmacology · 2013Article
- Genome-wide Membrane Protein Structure Prediction.Current genomics · 2013Article
- A ring of threonines in the inner vestibule of the pore of CNGA1 channels constitutes a binding site for permeating ions.The Journal of physiology · 2012Article
- Gating of cyclic nucleotide-gated channels is voltage dependent.Nature communications · 2012Article
- Sodium selectivity of semicircular canal duct epithelial cells.BMC research notes · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aminoacid sequences of CNG and K(+) channels share a significant sequence identity, and it has been suggested that these channels have a common ancestral 3D architecture. However, K(+) and CNG channels have profoundly different physiological properties: indeed, K(+) channels have a high ionic selectivity, their gating strongly depends on membrane voltage and when opened by a steady depolarizing voltage several K(+) channels inactivate, whereas CNG channels have a low ion selectivity, their gating is poorly voltage dependent, and they do not desensitize in the presence of a steady concentration of cyclic nucleotides that cause their opening. The purpose of the present review is to summarize and recapitulate functional and structural differences between K(+) and CNG channels with the aim to understand the gating mechanisms of CNG channels.
Indexed as
Identifiers
19898862What 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.