Evidence map›Paper›PMID 28768808›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Transmembrane allosteric energetics characterization for strong coupling between proton and potassium ion binding in the KcsA channel.

Yunyao Xu, Manasi P Bhate, Ann E McDermott

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Structures of Gating Intermediates in a KJournal of molecular biology · 2021
    Article
  9. Article
  10. Article
  11. NMR studies of lipid regulation of the KBiochimica et biophysica acta. Biomembranes · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Modulation of Function, Structure and Clustering of KInternational journal of molecular sciences · 2020
    Review
  16. Probing allosteric coupling in a constitutively open mutant of the ion channel KcsA using solid-state NMR.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Conformational changes upon gating of KirBac1.1 into an open-activated state revealed by solid-state NMR and functional assays.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. TmDOTP: An NMR-based thermometer for magic angle spinning NMR experiments.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019
    Article
  19. Queueing arrival and release mechanism for KThe journal of physiological sciences : JPS · 2019
    Article
  20. Identifying coupled clusters of allostery participants through chemical shift perturbations.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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.

Yunyao XuDepartment of Chemistry, Columbia University, New York, NY 10027.
Manasi P BhateDepartment of Chemistry, Columbia University, New York, NY 10027.
Ann E McDermottDepartment of Chemistry, Columbia University, New York, NY 10027 aem5@columbia.edu.ORCID 0000-0002-9249-1649
Columbia University · US

Funding

Structural and Functional Studies of Potassium Channels by Solid State NMRR01GM088724 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI ANN E MCDERMOTT · 2009 to 2026
$5.6M
NIGMS NIH HHS R01 GM088724
6 · The paper itself

Abstract

The slow spontaneous inactivation of potassium channels exhibits classic signatures of transmembrane allostery. A variety of data support a model in which the loss of K

Indexed as

Ion Channel GatingProtonsAllosteric RegulationCations, MonovalentEscherichia coliEscherichia coli ProteinsLipid BilayersPotassiumPotassium ChannelsCations, MonovalentEscherichia coli ProteinsLipid BilayersPotassiumPotassium ChannelsProtonsallosteryinactivationmembrane proteinpotassium channelsolid-state NMR

Identifiers

PMID28768808
PMCPMC5565416
OpenAlexW2739617028

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.