Evidence map›Paper›PMID 9138564›Full record

ArticleBiophysical journal1997

Single-channel properties of ionic channels gated by cyclic nucleotides.

G Bucossi, M Nizzari, V Torre

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.3field-weighted citation impact, top 11% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Gating in CNGA1 channels.Pflugers Archiv : European journal of physiology · 2010
    Review
  8. Article
  9. Article
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  15. Article
  16. Molecular basis of an inherited form of incomplete achromatopsia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004
    Article
  17. Article
  18. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

G BucossiINFM, Genova, Italy.
M Nizzari
V Torre
Istituto Nazionale di Fisica Nucleare, Sezione di Genova · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This paper presents an extensive analysis of single-channel properties of cyclic nucleotide gated (CNG) channels, obtained by injecting into Xenopus laevis oocytes the mRNA encoding for the alpha and beta subunits from bovine rods. When the alpha and beta subunits of the CNG channel are coexpressed, at least three types of channels with different properties are observed. One type of channel has well-resolved, multiple conductive levels at negative voltages, but not at positive voltages. The other two types of channel are characterized by flickering openings, but are distinguished because they have a low and a high conductance. The alpha subunit of CNG channels has a well-defined conductance of about 28 pS, but multiple conductive levels are observed in mutant channels E363D and T364M. The conductance of these open states is modulated by protons and the membrane voltage, and has an activation energy around 44 kJ/mol. The relative probability of occupying any of these open states is independent of the cGMP concentration, but depends on extracellular protons. The open probability in the presence of saturating cGMP was 0.78, 0.47, 0.5, and 0.007 in the w.t. and mutants E363D, T364M, and E363G, and its dependence on temperature indicates that the thermodynamics of the transition between the closed and open state is also affected by mutations in the pore region. These results suggest that CNG channels have different conductive levels, leading to the existence of multiple open states in homomeric channels and to the flickering behavior in heteromeric channels, and that the pore is an essential part of the gating of CNG channels.

Indexed as

Ion Channel GatingAmino Acid SequenceAnimalsCattleCyclic GMPCyclic Nucleotide-Gated Cation ChannelsDiltiazemFemaleHumansIon ChannelsMacromolecular SubstancesMembrane PotentialsMolecular Sequence DataOocytesPoint MutationProbabilityCyclic GMPCyclic Nucleotide-Gated Cation ChannelsDiltiazemIon ChannelsMacromolecular SubstancesRecombinant ProteinsRNA, Messenger

Identifiers

PMID9138564
PMCPMC1184501
OpenAlexW2008303351

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.