Evidence map›Paper›PMID 9502797›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1998

dSLo interacting protein 1, a novel protein that interacts with large-conductance calcium-activated potassium channels.

X m Xia, B Hirschberg, S Smolik, M Forte, J P Adelman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 68 citations in OpenAlex.

  1. HRPU-2, a Homolog of Mammalian hnRNP U, Regulates Synaptic Transmission by Controlling the Expression of SLO-2 Potassium Channel inThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  2. Article
  3. Review
  4. A novel auxiliary subunit critical to BK channel function in Caenorhabditis elegans.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010
    Article
  5. Article
  6. Impaired function of coronary BK(Ca) channels in metabolic syndrome.American journal of physiology. Heart and circulatory physiology · 2009
    Article
  7. Article
  8. Regulation of colonic apical potassium (BK) channels by cAMP and somatostatin.American journal of physiology. Gastrointestinal and liver physiology · 2009
    Article
  9. Article
  10. Article
  11. Article
  12. MaxiK channel partners: physiological impact.The Journal of physiology · 2006
    Review
  13. Article
  14. Article
  15. Article
  16. Association of beta-catenin with the alpha-subunit of neuronal large-conductance Ca2+-activated K+ channels.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  17. Article
  18. Article
  19. Article
  20. Modulation of Drosophila slowpoke calcium-dependent potassium channel activity by bound protein kinase a catalytic subunit.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002
    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

5 authors at 2 institutions in 1 country.

X m XiaVollum Institute, Oregon Health Sciences University, Portland, Oregon 97201, USA.
B Hirschberg
S Smolik
M Forte
J P Adelman
Vollum Institute · USOregon Health & Science University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Large-conductance calcium-activated potassium channels (BK channels) are activated by depolarized membrane potential and elevated levels of intracellular calcium. BK channel activity underlies the fast afterhyperpolarization that follows an action potential and attenuates neurotransmitter and hormone secretion. Using a modified two-hybrid approach, the interaction trap, we have identified a novel protein from Drosophila, dSLIP1 (dSLo interacting protein), which specifically interacts with Drosophila and human BK channels and has partial homology to the PDZ domain of alpha1 syntrophin. The dSLIP1 and dSlo mRNAs are expressed coincidently throughout the Drosophila nervous system, the two proteins interact in vitro, and they may be coimmunoprecipitated from transfected cells. Coexpression of dSLIP1 with dSlo or hSlo BK channels in Xenopus oocytes results in reduced currents as compared with expression of BK channels alone; current amplitudes may be rescued by coexpression with the channel domain that interacts with dSLIP1. Single-channel recordings and immunostaining of transfected tissue culture cells suggest that dSLIP1 selectively reduces Slo BK currents by reducing the number of BK channels in the plasma membrane.

Indexed as

Drosophila ProteinsPotassium Channels, Calcium-ActivatedAmino Acid SequenceAnimalsAntibody SpecificityCalciumCOS CellsDrosophilaGene ExpressionLarge-Conductance Calcium-Activated Potassium ChannelsMembrane PotentialsMolecular ChaperonesMolecular Sequence DataPatch-Clamp TechniquesPotassium ChannelsPrecipitin TestsCalciumDrosophila ProteinsLarge-Conductance Calcium-Activated Potassium ChannelsMolecular ChaperonesPotassium ChannelsPotassium Channels, Calcium-ActivatedRNA, MessengerSlip1 protein, Drosophilaslo protein, Drosophila

Identifiers

PMID9502797
PMCPMC6793097
OpenAlexW2146405466

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.