Evidence map›Paper›PMID 27013734›Full record

ArticleScience (New York, N.Y.)2016

Direct observation of proton pumping by a eukaryotic P-type ATPase.

Salome Veshaguri, Sune M Christensen, Gerdi C Kemmer, Garima Ghale, Mads P Møller, Christina Lohr, Andreas L Christensen, Bo H Justesen, Ida L Jørgensen, Jürgen Schiller and 4 more

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

46 citing papers in PubMed, 97 citations in OpenAlex.

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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

14 authors at 3 institutions in 2 countries.

Salome VeshaguriBionanotecnology and Nanomedicine Laboratory, University of Copenhagen, Copenhagen, Denmark. Department of Chemistry, University of Copenhagen, Copenhagen, Denmark. Nano-Science Center, University of Copenhagen, Copenhagen, Denmark. Lundbeck Foundation Center Biomembranes in Nanomedicine, University of Copenhagen, Copenhagen, Denmark.
Sune M ChristensenBionanotecnology and Nanomedicine Laboratory, University of Copenhagen, Copenhagen, Denmark. Department of Chemistry, University of Copenhagen, Copenhagen, Denmark. Nano-Science Center, University of Copenhagen, Copenhagen, Denmark. Lundbeck Foundation Center Biomembranes in Nanomedicine, University of Copenhagen, Copenhagen, Denmark.
Gerdi C KemmerCentre for Membrane Pumps in Cells and Disease - PUMPKIN, Department of Plant and Environmental Sciences, University of Copenhagen, Frederiksberg Denmark.
Garima GhaleBionanotecnology and Nanomedicine Laboratory, University of Copenhagen, Copenhagen, Denmark. Department of Chemistry, University of Copenhagen, Copenhagen, Denmark. Nano-Science Center, University of Copenhagen, Copenhagen, Denmark. Lundbeck Foundation Center Biomembranes in Nanomedicine, University of Copenhagen, Copenhagen, Denmark.
Mads P MøllerBionanotecnology and Nanomedicine Laboratory, University of Copenhagen, Copenhagen, Denmark. Department of Chemistry, University of Copenhagen, Copenhagen, Denmark. Nano-Science Center, University of Copenhagen, Copenhagen, Denmark. Lundbeck Foundation Center Biomembranes in Nanomedicine, University of Copenhagen, Copenhagen, Denmark.
Christina LohrBionanotecnology and Nanomedicine Laboratory, University of Copenhagen, Copenhagen, Denmark. Department of Chemistry, University of Copenhagen, Copenhagen, Denmark. Nano-Science Center, University of Copenhagen, Copenhagen, Denmark. Lundbeck Foundation Center Biomembranes in Nanomedicine, University of Copenhagen, Copenhagen, Denmark.
Andreas L ChristensenBionanotecnology and Nanomedicine Laboratory, University of Copenhagen, Copenhagen, Denmark. Department of Chemistry, University of Copenhagen, Copenhagen, Denmark. Nano-Science Center, University of Copenhagen, Copenhagen, Denmark. Lundbeck Foundation Center Biomembranes in Nanomedicine, University of Copenhagen, Copenhagen, Denmark.
Bo H JustesenCentre for Membrane Pumps in Cells and Disease - PUMPKIN, Department of Plant and Environmental Sciences, University of Copenhagen, Frederiksberg Denmark.
Ida L JørgensenCentre for Membrane Pumps in Cells and Disease - PUMPKIN, Department of Plant and Environmental Sciences, University of Copenhagen, Frederiksberg Denmark.
Jürgen SchillerInstitute of Medical Physics and Biophysics, Faculty of Medicine, University of Leipzig, Leipzig, Germany.
Nikos S HatzakisBionanotecnology and Nanomedicine Laboratory, University of Copenhagen, Copenhagen, Denmark. Department of Chemistry, University of Copenhagen, Copenhagen, Denmark. Nano-Science Center, University of Copenhagen, Copenhagen, Denmark. Lundbeck Foundation Center Biomembranes in Nanomedicine, University of Copenhagen, Copenhagen, Denmark.
Michael GrabeCardiovascular Research Institute, Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143, USA.
Thomas Günther PomorskiCentre for Membrane Pumps in Cells and Disease - PUMPKIN, Department of Plant and Environmental Sciences, University of Copenhagen, Frederiksberg Denmark.
Dimitrios StamouBionanotecnology and Nanomedicine Laboratory, University of Copenhagen, Copenhagen, Denmark. Department of Chemistry, University of Copenhagen, Copenhagen, Denmark. Nano-Science Center, University of Copenhagen, Copenhagen, Denmark. Lundbeck Foundation Center Biomembranes in Nanomedicine, University of Copenhagen, Copenhagen, Denmark.
University of Copenhagen · DKLundbeck Foundation · DKLeipzig University · DE

Funding

Computer simulations of lysosomal and osteoclast microphysiologyR21GM100224 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GRABE, MICHAEL · 2012 to 2013
$403k
NIGMS NIH HHS R21 GM100224NIGMS NIH HHS R21-GM100224
6 · The paper itself

Abstract

In eukaryotes, P-type adenosine triphosphatases (ATPases) generate the plasma membrane potential and drive secondary transport systems; however, despite their importance, their regulation remains poorly understood. We monitored at the single-molecule level the activity of the prototypic proton-pumping P-type ATPase Arabidopsis thaliana isoform 2 (AHA2). Our measurements, combined with a physical nonequilibrium model of vesicle acidification, revealed that pumping is stochastically interrupted by long-lived (~100 seconds) inactive or leaky states. Allosteric regulation by pH gradients modulated the switch between these states but not the pumping or leakage rates. The autoinhibitory regulatory domain of AHA2 reduced the intrinsic pumping rates but increased the dwell time in the active pumping state. We anticipate that similar functional dynamics underlie the operation and regulation of many other active transporters.

Indexed as

ProtonsAllosteric RegulationArabidopsis ProteinsHydrogen-Ion ConcentrationIon TransportMembrane PotentialsMolecular ImagingProtein Structure, TertiaryProton-Translocating ATPasesValinomycinAHA2 protein, ArabidopsisArabidopsis ProteinsProtonsProton-Translocating ATPasesValinomycin

Identifiers

PMID27013734
PMCPMC5023152
OpenAlexW2305806492

What OpenQuestion holds

Textmetadata
LicenceTDM
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.