Evidence map›Paper›PMID 9625863›Full record

ArticleThe Journal of physiology1998

Modulation of ATP-gated non-selective cation channel (P2X1 receptor) activation and desensitization by the actin cytoskeleton.

K E Parker

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

10 citing papers in PubMed, 32 citations in OpenAlex.

  1. Microglia proliferation is controlled by P2X7 receptors in a Pannexin-1-independent manner during early embryonic spinal cord invasion.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article
  2. Article
  3. Article
  4. Interaction of P2 purinergic receptors with cellular macromolecules.Naunyn-Schmiedeberg's archives of pharmacology · 2008
    Review
  5. ATP modulation of excitatory synapses onto interneurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. 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

1 author at 1 institution in 1 country.

K E ParkerDepartment of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH, USA. kep5@po.cwru.edu
Case Western Reserve University · US

Funding

VASOACTIVE HORMONES: RECEPTORS AND SIGNALING MECHANISMSP01HL041618 · NHLBI · CASE WESTERN RESERVE UNIVERSITY · PI HOPFER, ULRICH · 1989 to 2004
$6.7M
NHLBI NIH HHS HL 41618NHLBI NIH HHS P01 HL041618
6 · The paper itself

Abstract

1. ATP-gated non-selective cation channels from the rat vas deferens (P2X1 receptors) were stably expressed in HEK 293 cells, assayed by patch clamp on the first day after passage of the culture, and found to have whole-cell current kinetics markedly faster in both activation and desensitization than those found in the native vas deferens tissue, in agreement with previous reports. 2. By the second day after passage of the culture, however, the whole-cell current kinetics of the expressed receptors shifted, slowing in both activation and desensitization. The kinetic change correlated with a change in phenotype of the host cells from round to flat, and the slower kinetics were similar to native P2X1 currents recorded from dissociated rat vas deferens smooth muscle cells. Two point mutations in a pore-like domain near or within the second transmembrane domain of the P2X1 receptor appeared to confer on the receptor the inability to effect this change in kinetics over time. 3. Treatment of cells on day 3 after passage with cytochalasins B or D caused a reversion to the rapid kinetics phenotype, implicating the actin cytoskeleton in the development of the native kinetics. P2X1 receptors may therefore require interaction with an intact actin cytoskeleton for native kinetics, and the mutants may be defective either in interaction with the actin skeleton or in coupling the interaction to gating.

Indexed as

ActinsAdenosine TriphosphateAnimalsCell LineCytochalasin BCytochalasin DCytoskeletonElectrophysiologyHumansKineticsMaleMutationPatch-Clamp TechniquesPhenotypeRatsReceptors, Purinergic P2ActinsAdenosine TriphosphateCytochalasin BCytochalasin DReceptors, Purinergic P2

Identifiers

PMID9625863
PMCPMC2231021
OpenAlexW1970885763

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.