Evidence map›Paper›PMID 30996281›Full record

ArticleScientific reports2019

Conformational plasticity in the KcsA potassium channel pore helix revealed by homo-FRET studies.

M Lourdes Renart, A Marcela Giudici, José A Poveda, Aleksander Fedorov, Mário N Berberan-Santos, Manuel Prieto, Clara Díaz-García, José M González-Ros, Ana Coutinho

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

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  12. Modulation of Function, Structure and Clustering of KInternational journal of molecular sciences · 2020
    Review
  13. 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
  14. 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

9 authors at 2 institutions in 2 countries.

M Lourdes RenartCQFM-IN and iBB-Institute for Bioengineering and Bioscience, Instituto Superior Técnico, Universidade de Lisboa, 1049-001, Lisboa, Portugal. lrenart@umh.es.ORCID http://orcid.org/0000-0002-6717-4756
A Marcela GiudiciIBMC and IDiBE-Instituto de Investigación, Desarrollo e Innovación en Biotecnología Sanitaria de Elche, Universidad Miguel Hernández, Elche, 03202, Alicante, Spain.
José A PovedaIBMC and IDiBE-Instituto de Investigación, Desarrollo e Innovación en Biotecnología Sanitaria de Elche, Universidad Miguel Hernández, Elche, 03202, Alicante, Spain.
Aleksander FedorovCQFM-IN and iBB-Institute for Bioengineering and Bioscience, Instituto Superior Técnico, Universidade de Lisboa, 1049-001, Lisboa, Portugal.
Mário N Berberan-SantosCQFM-IN and iBB-Institute for Bioengineering and Bioscience, Instituto Superior Técnico, Universidade de Lisboa, 1049-001, Lisboa, Portugal.
Manuel PrietoCQFM-IN and iBB-Institute for Bioengineering and Bioscience, Instituto Superior Técnico, Universidade de Lisboa, 1049-001, Lisboa, Portugal.
Clara Díaz-GarcíaCQFM-IN and iBB-Institute for Bioengineering and Bioscience, Instituto Superior Técnico, Universidade de Lisboa, 1049-001, Lisboa, Portugal.
José M González-RosIBMC and IDiBE-Instituto de Investigación, Desarrollo e Innovación en Biotecnología Sanitaria de Elche, Universidad Miguel Hernández, Elche, 03202, Alicante, Spain.
Ana CoutinhoCQFM-IN and iBB-Institute for Bioengineering and Bioscience, Instituto Superior Técnico, Universidade de Lisboa, 1049-001, Lisboa, Portugal. ana.coutinho@tecnico.ulisboa.pt.
University of Lisbon · PTUniversitat de Miguel Hernández d'Elx · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Potassium channels selectivity filter (SF) conformation is modulated by several factors, including ion-protein and protein-protein interactions. Here, we investigate the SF dynamics of a single Trp mutant of the potassium channel KcsA (W67) using polarized time-resolved fluorescence measurements. For the first time, an analytical framework is reported to analyze the homo-Förster resonance energy transfer (homo-FRET) within a symmetric tetrameric protein with a square geometry. We found that in the closed state (pH 7), the W67-W67 intersubunit distances become shorter as the average ion occupancy of the SF increases according to cation type and concentration. The hypothesis that the inactivated SF at pH 4 is structurally similar to its collapsed state, detected at low K

Indexed as

Protein ConformationAnisotropyBinding SitesCrystallography, X-RayEscherichia coliEscherichia coli ProteinsFluorescence PolarizationFluorescence Resonance Energy TransferHydrogen-Ion ConcentrationIon Channel GatingPotassiumPotassium ChannelsSodiumEscherichia coli ProteinsPotassiumPotassium ChannelsSodium

Identifiers

PMID30996281
PMCPMC6470172
OpenAlexW2939792638

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.