Evidence map›Paper›PMID 18986966›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2009

Review. Peering into an ATPase ion pump with single-channel recordings.

David C Gadsby, Ayako Takeuchi, Pablo Artigas, Nicolás Reyes

Open access · greenAbstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. The KdpFABC complex - KMolecular membrane biology · 2019
    Article
  6. Article
  7. A hyperpolarization-activated ion current of amphibian oocytes.Pflugers Archiv : European journal of physiology · 2013
    Article
  8. Article
  9. Article
  10. Mechanism of proton/substrate coupling in the heptahelical lysosomal transporter cystinosin.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  11. Article
  12. Article
  13. Structures of membrane proteins.Quarterly reviews of biophysics · 2010
    Review
  14. Review
  15. Review
  16. Introduction. The blurred boundary between channels and transporters.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2009
    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

4 authors at 2 institutions in 1 country.

David C GadsbyLaboratory of Cardiac/Membrane Physiology, The Rockefeller University, New York, NY 10065, USA. gadsby@rockefeller.edu
Ayako Takeuchi
Pablo Artigas
Nicolás Reyes
Google (United States) · USRockefeller University · US

Funding

MECHANISMS OF CURRENT MODULATION IN CARDIAC MYOCYTESR37HL049907 · NHLBI · ROCKEFELLER UNIVERSITY · PI GADSBY, DAVID C · 1998 to 2007
$2.2M
MECHANISMS OF CURRENT MODULATION IN CARDIAC MYOCYTESR01HL049907 · NHLBI · ROCKEFELLER UNIVERSITY · PI GADSBY, DAVID C · 1993 to 1997
–
UPPER AIRWAY STABILITY WITH LOADING IN THE HUMAN NEONATER23HL036873 · NHLBI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI DUARA, SHAHNAZ · 1986 to 1988
–
NHLBI NIH HHS HL36873NHLBI NIH HHS HL49907NHLBI NIH HHS R37 HL049907
6 · The paper itself

Abstract

In principle, an ion channel needs no more than a single gate, but a pump requires at least two gates that open and close alternately to allow ion access from only one side of the membrane at a time. In the Na+,K+-ATPase pump, this alternating gating effects outward transport of three Na+ ions and inward transport of two K+ ions, for each ATP hydrolysed, up to a hundred times per second, generating a measurable current if assayed in millions of pumps. Under these assay conditions, voltage jumps elicit brief charge movements, consistent with displacement of ions along the ion pathway while one gate is open but the other closed. Binding of the marine toxin, palytoxin, to the Na+,K+-ATPase uncouples the two gates, so that although each gate still responds to its physiological ligand they are no longer constrained to open and close alternately, and the Na+,K+-ATPase is transformed into a gated cation channel. Millions of Na+ or K+ ions per second flow through such an open pump-channel, permitting assay of single molecules and allowing unprecedented access to the ion transport pathway through the Na+,K+-ATPase. Use of variously charged small hydrophilic thiol-specific reagents to probe cysteine targets introduced throughout the pump's transmembrane segments allows mapping and characterization of the route traversed by transported ions.

Indexed as

Adenosine TriphosphatasesElectrochemistryIon Channel GatingIon PumpsModels, MolecularProtein ConformationAdenosine TriphosphatasesIon Pumps

Identifiers

PMID18986966
PMCPMC2674102
OpenAlexW2105600530

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.