Evidence map›Paper›PMID 9132410›Full record

ReviewJournal of bioenergetics and biomembranes1996

Anion channels of the inner membrane of mammalian and yeast mitochondria.

C Ballarin, M C Sorgato

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of bioenergetics and biomembranes, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

7 citing papers in PubMed, 20 citations in OpenAlex.

  1. Anion Channels of Mitochondria.Handbook of experimental pharmacology · 2017
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Mitochondrial channels revisited.Journal of bioenergetics and biomembranes · 1996
    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

2 authors at 1 institution in 1 country.

C BallarinDipartimento di Chimica Biologica, Universita di Padova, Italy.
M C Sorgato
University of Padua · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The inner membrane of yeast and mammalian mitochondria has been studied in situ with a patch clamp electrode. Anion channels were found in both cases, although their behavior and regulation are different. In mammalian mitochondria, the principal channel is of around 100 pS conductance and opens mainly under depolarized membrane potentials. As no physiological compound able to alter its peculiar voltage dependence has yet been found, it is proposed that this channel may serve as a safeguard mechanism for recharging the mitochondrial membrane potential. Two other anion channels, each with a distinct conductance (one of approx. 45 pS, the second of at least a tenfold higher value) and kinetics are harbored in the yeast inner membrane. Matrix ATP was found to interact with both, but with a different mechanism. It is proposed that the 45 pS channel may be involved in the homeostatic mechanism of mitochondrial volume.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateAnimalsCalciumElectrophysiologyHumansIntracellular MembranesIon ChannelsMitochondriaModels, BiologicalSaccharomyces cerevisiaeAdenosine DiphosphateAdenosine TriphosphateCalciumIon Channels

Identifiers

PMID9132410
OpenAlexW1995818230

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.