Evidence map›Paper›PMID 37192161›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

The membrane electric field regulates the PIP

Venkata Shiva Mandala, Roderick MacKinnon

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
10.2field-weighted citation impact, top 1% 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

45 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. PIPNature communications · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Chemical tuning reveals a cation-π gating bridge between the voltage-sensor and pore domains in the KProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. Mapping the Functional Landscape ofmedRxiv : the preprint server for health sciences · 2025
    Article
  12. Article
  13. KCNQ1 and PIPCell research · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
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

2 authors at 1 institution in 1 country.

Venkata Shiva MandalaLaboratory of Molecular Neurobiology and Biophysics, The Rockefeller University, New York, NY 10065.
Roderick MacKinnonLaboratory of Molecular Neurobiology and Biophysics, The Rockefeller University, New York, NY 10065.
Rockefeller University · US

Funding

Howard Hughes Medical Institute (HHMI) HHMI
6 · The paper itself

Abstract

Voltage-dependent ion channels underlie the propagation of action potentials and other forms of electrical activity in cells. In these proteins, voltage sensor domains (VSDs) regulate opening and closing of the pore through the displacement of their positive-charged S4 helix in response to the membrane voltage. The movement of S4 at hyperpolarizing membrane voltages in some channels is thought to directly clamp the pore shut through the S4-S5 linker helix. The KCNQ1 channel (also known as K

Indexed as

KCNQ1 Potassium ChannelLipidsAction PotentialsBinding SitesHumansProtein DomainsKCNQ1 Potassium ChannelKCNQ1 protein, humanLipidscryo-EMKCNQ1 channelKv7.1 channelmembrane potentialvoltage sensor

Identifiers

PMID37192161
PMCPMC10214144
OpenAlexW4376872640

What Socratic 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 Socratic graph.