Evidence map›Paper›PMID 10557223›Full record

ArticlePlant physiology1999

Cloning and first functional characterization of a plant cyclic nucleotide-gated cation channel.

Q Leng, R W Mercier, W Yao, G A Berkowitz

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

96 citing papers in PubMed, 275 citations in OpenAlex.

  1. Review
  2. Article
  3. Frontiers in plant science · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. The Complex Story of Plant Cyclic Nucleotide-Gated Channels.International journal of molecular sciences · 2021
    Review
  15. Article
  16. Review
  17. Article
  18. Cyclic AMP: A Polyhedral Signalling Molecule in Plants.International journal of molecular sciences · 2020
    Review
  19. Article
  20. MgInternational journal of molecular sciences · 2020
    Article

36 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Q LengDepartment of Plant Science U-67, 1376 Storrs Road, University of Connecticut, Storrs, Connecticut 06269-4067, USA.
R W Mercier
W Yao
G A Berkowitz
University of Connecticut · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclic nucleotide-gated (cng) non-selective cation channels have been cloned from a number of animal systems. These channels are characterized by direct gating upon cAMP or cGMP binding to the intracellular portion of the channel protein, which leads to an increase in channel conductance. Animal cng channels are involved in signal transduction systems; they translate stimulus-induced changes in cytosolic cyclic nucleotide into altered cell membrane potential and/or cation flux as part of a signal cascade pathway. Putative plant homologs of animal cng channels have been identified. However, functional characterization (i.e. demonstration of cyclic-nucleotide-dependent ion currents) of a plant cng channel has not yet been accomplished. We report the cloning and first functional characterization of a plant member of this family of ion channels. The Arabidopsis cDNA AtCNGC2 encodes a polypeptide with deduced homology to the alpha-subunit of animal channels, and facilitates cyclic nucleotide-dependent cation currents upon expression in a number of heterologous systems. AtCNGC2 expression in a yeast mutant lacking a low-affinity K(+) uptake system complements growth inhibition only when lipophilic cyclic nucleotides are present in the culture medium. Voltage clamp analysis indicates that Xenopus laevis oocytes injected with AtCNGC2 cRNA demonstrate cyclic-nucleotide-dependent, inward-rectifying K(+) currents. Human embryonic kidney cells (HEK293) transfected with AtCNGC2 cDNA demonstrate increased permeability to Ca(2+) only in the presence of lipophilic cyclic nucleotides. The evidence presented here supports the functional classification of AtCNGC2 as a cyclic-nucleotide-gated cation channel, and presents the first direct evidence (to our knowledge) identifying a plant member of this ion channel family.

Indexed as

Amino Acid SequenceAnimalsArabidopsisCell MembraneCloning, MolecularCyclic AMPCyclic GMPCyclic Nucleotide-Gated Cation ChannelsFemaleHumansIon ChannelsMolecular Sequence DataOocytesPlant ProteinsRecombinant ProteinsSequence AlignmentCyclic AMPCyclic GMPCyclic Nucleotide-Gated Cation ChannelsIon ChannelsPlant ProteinsRecombinant Proteins

Identifiers

PMID10557223
PMCPMC59437
OpenAlexW2112027893

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.