Evidence map›Paper›PMID 16524922›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2006

The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase.

Patricia M Kane

Open access · greenAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 230 papers.

0numbers the graph read from it
0cells of the map it votes in
230citing papers in PubMed
11.9field-weighted citation impact, top 1% 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

230 citing papers in PubMed, 389 citations in OpenAlex.

  1. Article
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  5. Quantifying the fitness contribution of phagocytosis.bioRxiv : the preprint server for biology · 2025
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  6. Mangiferin Exerts Antifungal Activity againstJournal of microbiology and biotechnology · 2025
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  7. Cell membrane asymmetries and cellular aging.The Biochemical journal · 2025
    Review
  8. Article
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  11. Article
  12. Article
  13. Article
  14. Eukaryotic yeast VFrontiers in molecular biosciences · 2024
    Article
  15. Review
  16. Differences of protein expression in enterococcus faecalis biofilm during resistance to environmental pressures.Technology and health care : official journal of the European Society for Engineering and Medicine · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Article

170 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

1 author at 1 institution in 1 country.

Patricia M KaneDepartment of Biochemistry and Molecular Biology, SUNY Upstate Medical University, 750 East Adams St., Syracuse, NY 13210, USA. kanepm@upstate.edu
SUNY Upstate Medical University · US

Funding

SUBUNIT STRUCTURE/FUNCTION IN VACUOLAR H+ ATPASESR01GM050322 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI KANE, PATRICIA M · 1994 to 2015
$4.1M
A Skpl-containing Complex Regulating V-ATPase ActivityR01GM063742 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI KANE, PATRICIA M · 2002 to 2005
$851k
NIGMS NIH HHS R01 GM050322NIGMS NIH HHS R01 GM063742NIGMS NIH HHS R01 GM50322NIGMS NIH HHS R01 GM63742
6 · The paper itself

Abstract

All eukaryotic cells contain multiple acidic organelles, and V-ATPases are central players in organelle acidification. Not only is the structure of V-ATPases highly conserved among eukaryotes, but there are also many regulatory mechanisms that are similar between fungi and higher eukaryotes. These mechanisms allow cells both to regulate the pHs of different compartments and to respond to changing extracellular conditions. The Saccharomyces cerevisiae V-ATPase has emerged as an important model for V-ATPase structure and function in all eukaryotic cells. This review discusses current knowledge of the structure, function, and regulation of the V-ATPase in S. cerevisiae and also examines the relationship between biosynthesis and transport of V-ATPase and compartment-specific regulation of acidification.

Indexed as

AcidsOrganellesProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolar Proton-Translocating ATPasesVacuolesAcidsSaccharomyces cerevisiae ProteinsVacuolar Proton-Translocating ATPases

Identifiers

PMID16524922
PMCPMC1393255
OpenAlexW2132694729

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.