Evidence map›Paper›PMID 16691477›Full record

ReviewJournal of bioenergetics and biomembranes2005

Physiological and metabolic implications of V-ATPase isoforms in the kidney.

Fiona E Karet

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of bioenergetics and biomembranes, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

  1. Article
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  5. Review
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  8. Review
  9. Review
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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

1 author.

Fiona E KaretDivision of Renal Medicine and Department of Medical Genetics, Cambridge Institute for Medical Research, University of Cambridge, Box 139, Addenbrooke's Hospital, Hills Road, Cambridge, CB2 2XY, UK. fek1000@cam.ac.uk

Funding

Wellcome Trust
6 · The paper itself

Abstract

Not all vacuolar-type H(+)-ATPases (V-ATPases) are alike; those responsible for H(+) movement across plasma membranes contain some different, tissue-specific subunit isoforms. This brief review outlines those that have special relevance to the kidney, and illustrates their importance by describing various human diseases where loss of local proton pump function not only confers a severe phenotype, but has revealed related tissues where these same isoforms are expressed, signifying their physiological importance.

Indexed as

Acidosis, Renal TubularHumansKidneyProtein IsoformsProtein SubunitsTissue DistributionVacuolar Proton-Translocating ATPasesProtein IsoformsProtein SubunitsVacuolar Proton-Translocating ATPases

Identifiers

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.