ReviewJournal of bioenergetics and biomembranes1996
Molecular mechanisms of cyclic nucleotide-gated channels.
Review in Journal of bioenergetics and biomembranes, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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
5 citing papers in PubMed, 14 citations in OpenAlex.
- Calcium-dependent gating of MthK, a prokaryotic potassium channel.The Journal of general physiology · 2006Article
- HCN-encoded pacemaker channels: from physiology and biophysics to bioengineering.The Journal of membrane biology · 2006Review
- Movement of the C-helix during the gating of cyclic nucleotide-gated channels.Biophysical journal · 2002Article
- The interaction of Na(+) and K(+) in the pore of cyclic nucleotide-gated channels.Biophysical journal · 2000Article
- The alphabet of intrinsic disorder: II. Various roles of glutamic acid in ordered and intrinsically disordered proteins.Intrinsically disordered proteinsReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Cyclic nucleotide-gated (CNG) channels are highly specialized to carry out their unique role in cell signalling. Significant progress has been made in the last several years determining the molecular mechanisms for these specializations. The activation of the channels begins with the binding of cyclic nucleotide to a domain in the carboxyl terminal region. This binding, in turn, produces an induced fit of the protein that involves a movement of the C-helix portion of the binding domain. The induced fit of the binding domain is coupled to an allosteric conformational change that opens the channel pore. The pore is formed primarily from the sequence between the S5 and S6 segments. A single glutamic acid in the pore represents the binding site for multiple monovalent cations, the blocking site for external divalent cations, and the site for the effect of protons on permeation.
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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.