Evidence map›Paper›PMID 10828243›Full record

ArticleThe Journal of general physiology2000

Interactions of cyclic nucleotide-gated channel subunits and protein tyrosine kinase probed with genistein.

E Molokanova, A Savchenko, R H Kramer

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

11 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  5. Effects of the protein tyrosine kinase inhibitor genistein and taurine on retinal function in isolated superfused retina.Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie · 2007
    Article
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  11. Developmental expression of retinal cone cGMP-gated channels: evidence for rapid turnover and trophic regulation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001
    Article
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

3 authors at 1 institution in 1 country.

E MolokanovaDepartment of Molecular and Cellular Pharmacology, University of Miami School of Medicine, FL 33101, USA.
A Savchenko
R H Kramer
University of Miami · US

Funding

Detection/Dysplastic Epithelium/Gastrointestinal TractR33CA094304 · NCI · UNIVERSITY HOSPITALS OF CLEVELAND · PI SIVAK, MICHAEL V · 2002 to 2004
$1.5M
NCI NIH HHS R33 CA094304
6 · The paper itself

Abstract

The cGMP sensitivity of cyclic nucleotide-gated (CNG) channels can be modulated by changes in phosphorylation catalyzed by protein tyrosine kinases (PTKs) and protein tyrosine phosphatases. Previously, we used genistein, a PTK inhibitor, to probe the interaction between PTKs and homomeric channels comprised of alpha subunits (RETalpha) of rod photoreceptor CNG channels expressed in Xenopus oocytes. We showed that in addition to inhibiting phosphorylation, genistein triggers a noncatalytic interaction between PTKs and homomeric RETalpha channels that allosterically inhibits channel gating. Here, we show that native CNG channels from rods, cones, and olfactory receptor neurons also exhibit noncatalytic inhibition induced by genistein, suggesting that in each of these sensory cells, CNG channels are part of a regulatory complex that contains PTKs. Native CNG channels are heteromers, containing beta as well as alpha subunits. To determine the contributions of alpha and beta subunits to genistein inhibition, we compared the effect of genistein on native, homomeric (RETalpha and OLFalpha), and heteromeric (RETalpha+beta, OLFalpha+beta, and OLFalpha+RETbeta) CNG channels. We found that genistein only inhibits channels that contain either the RETalpha or the OLFbeta subunits. This finding, along with other observations about the maximal effect of genistein and the Hill coefficient of genistein inhibition, suggests that the RETalpha and OLFbeta subunits contain binding sites for the PTK, whereas RETbeta and OLFalpha subunits do not.

Indexed as

AmbystomaAnimalsCyclic GMPCyclic Nucleotide-Gated Cation ChannelsDose-Response Relationship, DrugElectrophysiologyEnzyme InhibitorsFemaleGenisteinIon Channel GatingIon ChannelsMembrane PotentialsOlfactory Receptor NeuronsOocytesProtein Structure, TertiaryProtein-Tyrosine KinasesCyclic GMPCyclic Nucleotide-Gated Cation ChannelsEnzyme InhibitorsGenisteinIon ChannelsProtein-Tyrosine Kinases

Identifiers

PMID10828243
PMCPMC2232887
OpenAlexW2125759176

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.