Evidence map›Paper›PMID 7690146›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1993

Zn2+ potentiates excitatory action of ATP on mammalian neurons.

C Li, R W Peoples, Z Li, F F Weight

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

19 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. Review
  3. Orthosteric and allosteric binding sites of P2X receptors.European biophysics journal : EBJ · 2009
    Review
  4. Opposite effects of zinc on human and rat P2X2 receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008
    Article
  5. Pharmacology of P2X channels.Pflugers Archiv : European journal of physiology · 2006
    Review
  6. On the contribution of the first transmembrane domain to whole-cell current through an ATP-gated ionotropic P2X receptor.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. A domain contributing to the ion channel of ATP-gated P2X2 receptors identified by the substituted cysteine accessibility method.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998
    Article
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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.

C LiLaboratory of Molecular and Cellular Neurobiology, National Institute on Alcohol Abuse and Alcoholism, National Institutes of Health, Rockville, MD 20852.
R W Peoples
Z Li
F F Weight
National Institute on Alcohol Abuse and Alcoholism · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite the increasing recognition that ATP is an important extracellular excitatory mediator in the nervous system, the regulation of ATP receptors is poorly understood. Because the extracellular Zn2+ concentration is regulated in a variety of biological tissues, we studied modulation of the ATP-gated cation channel by Zn2+ in mammalian neurons using the whole-cell patch-clamp technique. In approximately 73% of cells tested, the amplitude of ATP-activated membrane ion current increased up to 5-fold in the presence of micromolar concentrations of Zn2+. The characteristics of this action suggest that Zn2+ increases the apparent affinity of the receptor for ATP. In addition, Zn2+ increased membrane depolarization and action potential firing elicited by ATP. These observations suggest that Zn2+ may play a physiological role in regulating the excitatory action of ATP on mammalian neurons.

Indexed as

Adenosine TriphosphateAnimalsDose-Response Relationship, DrugDrug SynergismGanglia, SympatheticIn Vitro TechniquesIon ChannelsMaleMembrane PotentialsNeuronsRatsRats, Sprague-DawleyZincAdenosine TriphosphateIon ChannelsZinc

Identifiers

PMID7690146
PMCPMC47329
OpenAlexW2077224751

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.