Evidence map›Paper›PMID 21559285›Full record

ArticlePloS one2011

Functional K(v)10.1 channels localize to the inner nuclear membrane.

Ye Chen, Araceli Sánchez, María E Rubio, Tobias Kohl, Luis A Pardo, Walter Stühmer

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

39 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The Kv10.1 Channel: A Promising Target in Cancer.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Targeting Ion Channels for Cancer Treatment: Current Progress and Future Challenges.Reviews of physiology, biochemistry and pharmacology · 2022
    Review
  8. Article
  9. Therapeutic Antibodies Targeting Potassium Ion Channels.Handbook of experimental pharmacology · 2021
    Article
  10. Ion Channel Dysregulation in Head and Neck Cancers: Perspectives for Clinical Application.Reviews of physiology, biochemistry and pharmacology · 2021
    Review
  11. Review
  12. Article
  13. Eag1 KOxidative medicine and cellular longevity · 2017
    Review
  14. Review
  15. Kv10.1 K(+) channel: from physiology to cancer.Pflugers Archiv : European journal of physiology · 2016
    Review
  16. Article
  17. Review
  18. The Role of KV7.3 in Regulating Osteoblast Maturation and Mineralization.International journal of molecular sciences · 2016
    Article
  19. Article
  20. Astemizole-based anticancer therapy for hepatocellular carcinoma (HCC), and Eag1 channels as potential early-stage markers of HCC.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    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

6 authors at 1 institution in 2 countries.

Ye ChenDepartment of Molecular Biology of Neuronal Signals, Max-Planck-Institute of Experimental Medicine, Göttingen, Germany.
Araceli Sánchez
María E Rubio
Tobias Kohl
Luis A Pardo
Walter Stühmer
Max Planck Institute of Experimental Medicine · DE

Funding

Molecular neuroanatomy of the cochlear nucleus in deafnessR01DC006881 · NIDCD · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI RUBIO-VALERO, MARIA-EULALIA · 2006 to 2010
$1.4M
NIDCD NIH HHS R01 DC006881
6 · The paper itself

Abstract

Ectopically expressed human K(V)10.1 channels are relevant players in tumor biology. However, their function as ion channels at the plasma membrane does not totally explain their crucial role in tumors. Both in native and heterologous systems, it has been observed that a majority of K(V)10.1 channels remain at intracellular locations. In this study we investigated the localization and possible roles of perinuclear K(V)10.1. We show that K(V)10.1 is expressed at the inner nuclear membrane in both human and rat models; it co-purifies with established inner nuclear membrane markers, shows resistance to detergent extraction and restricted mobility, all of them typical features of proteins at the inner nuclear membrane. K(V)10.1 channels at the inner nuclear membrane are not all transported directly from the ER but rather have been exposed to the extracellular milieu. Patch clamp experiments on nuclei devoid of external nuclear membrane reveal the existence of channel activity compatible with K(V)10.1. We hypothesize that K(V)10.1 channels at the nuclear envelope might participate in the homeostasis of nuclear K(+), or indirectly interact with heterochromatin, both factors known to affect gene expression.

Indexed as

AnimalsCell NucleusCell ProliferationCHO CellsCricetinaeCricetulusEther-A-Go-Go Potassium ChannelsGolgi ApparatusHumansIon ChannelsMiceNIH 3T3 CellsNuclear EnvelopePatch-Clamp TechniquesEther-A-Go-Go Potassium ChannelsIon ChannelsKCNH1 protein, humanKcnh1 protein, mouse

Identifiers

PMID21559285
PMCPMC3086910
OpenAlexW2086648262

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.