Evidence map›Paper›PMID 22988139›Full record

ArticleThe Journal of physiology2012

TARP-associated AMPA receptors display an increased maximum channel conductance and multiple kinetically distinct open states.

Chris Shelley, Mark Farrant, Stuart G Cull-Candy

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed, 1 pooled it
1.7field-weighted citation impact, top 18% 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

33 citing papers in PubMed, 1 synthesis or guideline pooled it, 44 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. GluDs are ionotropic dopamine receptors tuned by G-proteins.bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
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  7. Temperature Sensitive Glutamate Gating of AMPA-subtype iGluRs.bioRxiv : the preprint server for biology · 2024
    Article
  8. Article
  9. Article
  10. Structural insights into function of ionotropic glutamate receptors.Biochemistry (Moscow) Supplement. Series A, Membrane and cell biology · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. CaThe Journal of physiology · 2021
    Article
  16. AMPA receptor structure and auxiliary subunits.The Journal of physiology · 2021
    Review
  17. Review
  18. Mechanism of modulation of AMPA receptors by TARP-γ8.The Journal of general physiology · 2020
    Article
  19. Article
  20. 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.

Chris ShelleyDepartment of Neuroscience, University College London, Gower Street, London WC1E 6BT, UK.
Mark Farrant
Stuart G Cull-Candy
University College London · GB

Funding

Medical Research Council MR/J002976/1Wellcome Trust
6 · The paper itself

Abstract

Fast excitatory synaptic transmission in the CNS is mediated mainly by AMPA-type glutamate receptors (AMPARs), whose biophysical properties are dramatically modulated by the presence of transmembrane AMPAR regulatory proteins (TARPs). To help construct a kinetic model that will realistically describe native AMPAR/TARP function, we have examined the single-channel properties of homomeric GluA1 AMPARs in combination with the TARPs, γ-2, γ-4 and γ-5. In a saturating concentration of agonist, each of these AMPAR/TARP combinations gave rise to single-channel currents with multiple conductance levels that appeared intrinsic to the receptor-channel complex, and showed long-lived subconductance states. The open time and burst length distributions of the receptor complexes displayed multiple dwell-time components. In the case of γ-2- and γ-4-associated receptors, these distributions included a long-lived component lasting tens of milliseconds that was absent from both GluA1 alone and γ-5-associated receptors. The open time distributions for each conductance level required two dwell-time components, indicating that at each conductance level the channel occupies a minimum of two kinetically distinct open states. We have explored how these data place novel constraints on possible kinetic models of TARP-associated AMPARs that may be used to define AMPAR-mediated synaptic transmission.

Indexed as

Ion Channel GatingAnimalsCalcium ChannelsCell LineHumansKineticsProtein MultimerizationRatsReceptors, AMPACacng2 protein, ratCacng4 protein, ratCacng5 protein, ratCalcium ChannelsReceptors, AMPA

Identifiers

PMID22988139
PMCPMC3528987
OpenAlexW1573414635

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.