Evidence map›Paper›PMID 18458946›Full record

ReviewPflugers Archiv : European journal of physiology2009

Protons and how they are transported by proton pumps.

M J Buch-Pedersen, B P Pedersen, B Veierskov, P Nissen, M G Palmgren

Abstract readReview
PubMed Publisher
In one paragraph

Review in Pflugers Archiv : European journal of physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

49 citing papers in PubMed, 115 citations in OpenAlex.

  1. Article
  2. Comparative analysis of STP6 and STP10 unravels molecular selectivity in sugar transport proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps.International journal of molecular sciences · 2023
    Review
  9. Article
  10. Article
  11. Review
  12. Regulation of Cytosolic pH: The Contributions of Plant Plasma Membrane HInternational journal of molecular sciences · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Plant glucose transporter structure and function.Pflugers Archiv : European journal of physiology · 2020
    Review
  18. Article
  19. Article
  20. The plasma membrane HYeast (Chichester, England) · 2019
    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 at 3 institutions in 1 country.

M J Buch-PedersenCentre for Membrane Pumps in Cells and Disease-PUMPKIN, Danish National Research Foundation, Arhus and Copenhagen, Denmark.
B P Pedersen
B Veierskov
P Nissen
M G Palmgren
Danish National Research Foundation · DKAarhus University · DKUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The very high mobility of protons in aqueous solutions demands special features of membrane proton transporters to sustain efficient yet regulated proton transport across biological membranes. By the use of the chemical energy of ATP, plasma-membrane-embedded ATPases extrude protons from cells of plants and fungi to generate electrochemical proton gradients. The recently published crystal structure of a plasma membrane H(+)-ATPase contributes to our knowledge about the mechanism of these essential enzymes. Taking the biochemical and structural data together, we are now able to describe the basic molecular components that allow the plasma membrane proton H(+)-ATPase to carry out proton transport against large membrane potentials. When divergent proton pumps such as the plasma membrane H(+)-ATPase, bacteriorhodopsin, and F(O)F(1) ATP synthase are compared, unifying mechanistic premises for biological proton pumps emerge. Most notably, the minimal pumping apparatus of all pumps consists of a central proton acceptor/donor, a positively charged residue to control pK(a) changes of the proton acceptor/donor, and bound water molecules to facilitate rapid proton transport along proton wires.

Indexed as

ProtonsAdenosine TriphosphatasesCell MembraneModels, MolecularProtein ConformationProton PumpsWaterAdenosine TriphosphatasesProton PumpsProtonsWater

Identifiers

PMID18458946
OpenAlexW1999306351

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.