Evidence map›Paper›PMID 18026982›Full record

ReviewPflugers Archiv : European journal of physiology2009

V-ATPase functions in normal and disease processes.

Ayana Hinton, Sarah Bond, Michael Forgac

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 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

97 citing papers in PubMed, 204 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. ModelingJournal of cellular immunology · 2025
    Article
  9. Structure of yeast RAVE bound to a partial VProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Review
  12. Eukaryotic yeast VFrontiers in molecular biosciences · 2024
    Article
  13. Article
  14. Article
  15. Review
  16. Structural basis of V-ATPase VProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Review
  18. Article
  19. Review
  20. The transcriptomic response ofFrontiers in cellular and infection microbiology · 2023
    Article

37 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Ayana HintonDepartment of Physiology, Tufts University School of Medicine, 136 Harrison Ave, Boston, MA 02111, USA.
Sarah Bond
Michael Forgac
Tufts University · US

Funding

Training in Education and Critical Research SkillsK12GM074869 · NIGMS · TUFTS UNIVERSITY BOSTON · PI MOORE, CLAIRE L · 2006 to 2017
$8.5M
Structure, Mechanism and Regulation of the V-ATPasesR37GM034478 · NIGMS · TUFTS UNIVERSITY BOSTON · PI FORGAC, MICHAEL D · 2001 to 2010
$5.0M
PATHOBIOLOGY OF DIGESTIVE DISEASEST32DK007542 · NIDDK · TUFTS UNIVERSITY BOSTON · PI LISCUM, LAURA · 1986 to 2010
$3.5M
STRUCTURE, MECHANISM AND REGULATION OF THE V-ATPASESR01GM034478 · NIGMS · TUFTS UNIVERSITY BOSTON · PI FORGAC, MICHAEL D · 1985 to 2015
$1.9M
NIDDK NIH HHS DK 07542NIGMS NIH HHS GM34478NIGMS NIH HHS R37 GM034478
6 · The paper itself

Abstract

Eukaryotic cells have evolved a family of ATP-dependent proton pumps known as the vacuolar (H(+))-ATPases (or V-ATPases) to regulate the pH of intracellular compartments, the extracellular space, and the cytoplasm. V-ATPases present within intracellular compartments are important for such normal cellular processes as receptor-mediated endocytosis and intracellular membrane traffic, protein processing and degradation and coupled transport of small molecules and ions. They also facilitate the entry of a number of envelope viruses and bacterial toxins, including influenza virus and anthrax toxin. V-ATPases present in the plasma membranes of cells are also important in normal physiology. They facilitate bone resorption by osteoclasts, acid secretion by intercalated cells of the kidney, pH homeostasis in macrophages and neutrophils, angiogenesis by endothelial cells, and sperm maturation and storage in the male reproductive tract. In the insect midgut, they establish a membrane potential used to drive K(+) secretion. Plasma membrane V-ATPases are especially important in human disease, with genetic defects in V-ATPases expressed in osteoclasts and intercalated cells leading to the diseases osteopetrosis and renal tubule acidosis, respectively. Plasma membrane V-ATPases have also been implicated in tumor cell invasion. V-ATPases are thus emerging as potential targets in the treatment of diseases such as osteoporosis and cancer.

Indexed as

DiseaseAnimalsCell MembraneHumansHydrogen-Ion ConcentrationOrganellesProton PumpsProtonsVacuolar Proton-Translocating ATPasesProton PumpsProtonsVacuolar Proton-Translocating ATPases

Identifiers

PMID18026982
OpenAlexW1995943575

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.