Evidence map›Paper›PMID 27708266›Full record

ArticleNature communications2016

Mechanism of pH-dependent activation of the sodium-proton antiporter NhaA.

Yandong Huang, Wei Chen, David L Dotson, Oliver Beckstein, Jana Shen

Abstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
–field-weighted citation impact
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

55 citing papers in PubMed.

  1. pH-dependent activation of the NaNature communications · 2026
    Article
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  7. Review
  8. Article
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  15. Review
  16. Crystal structure of the NaNature communications · 2022
    Article
  17. Prokaryotic NaInternational journal of molecular sciences · 2022
    Review
  18. The Remaining Conundrum of the Role of the NaReviews in cardiovascular medicine · 2022
    Review
  19. Article
  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

5 authors.

Yandong HuangDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, Maryland 21201, USA.
Wei ChenDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, Maryland 21201, USA.
David L DotsonDepartment of Physics, Arizona State University, Tempe, Arizona 85287, USA.ORCID 0000-0001-5879-2942
Oliver BecksteinDepartment of Physics, Arizona State University, Tempe, Arizona 85287, USA.ORCID 0000-0003-1340-0831
Jana ShenDepartment of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, Maryland 21201, USA.ORCID 0000-0002-3234-0769

Funding

Electrostatic modulation of protein stability and foldingR01GM098818 · NIGMS · UNIVERSITY OF OKLAHOMA · PI SHEN, JANA · 2011 to 2021
$2.9M
NIGMS NIH HHS R01 GM098818
6 · The paper itself

Abstract

Escherichia coli NhaA is a prototype sodium-proton antiporter, which has been extensively characterized by X-ray crystallography, biochemical and biophysical experiments. However, the identities of proton carriers and details of pH-regulated mechanism remain controversial. Here we report constant pH molecular dynamics data, which reveal that NhaA activation involves a net charge switch of a pH sensor at the entrance of the cytoplasmic funnel and opening of a hydrophobic gate at the end of the funnel. The latter is triggered by charging of Asp164, the first proton carrier. The second proton carrier Lys300 forms a salt bridge with Asp163 in the inactive state, and releases a proton when a sodium ion binds Asp163. These data reconcile current models and illustrate the power of state-of-the-art molecular dynamics simulations in providing atomic details of proton-coupled transport across membrane which is challenging to elucidate by experimental techniques.

Indexed as

Aspartic AcidCatalytic DomainComputer SimulationCrystallography, X-RayCytoplasmEscherichia coliEscherichia coli ProteinsHydrogen-Ion ConcentrationHydrophobic and Hydrophilic InteractionsIonsLysineMolecular Dynamics SimulationProtein ConformationProtein DomainsProtonsSodiumAspartic AcidEscherichia coli ProteinsIonsLysineNhaA protein, E coliProtonsSodiumSodium-Hydrogen Exchangers

Identifiers

PMID27708266
PMCPMC5059715

What OpenQuestion holds

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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.