ReviewJournal of bioenergetics and biomembranes2000
Extramitochondrial porin: facts and hypotheses.
Review in Journal of bioenergetics and biomembranes, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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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.
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.
Who cites it
19 citing papers in PubMed, 59 citations in OpenAlex.
- The compartment-specific interactome of VDAC1 reveals its emerging role beyond mitochondria in breast cancer.Scientific reports · 2026Article
- Is the Voltage-Dependent Anion Channel a Major Player in Neurodegenerative Diseases?International journal of molecular sciences · 2025Review
- VDAC1 at the Intersection of Cell Metabolism, Apoptosis, and Diseases.Biomolecules · 2020Review
- Mitochondrial CaFrontiers in cell and developmental biology · 2020Article
- Pharmacological modulation of mitochondrial ion channels.British journal of pharmacology · 2019Review
- Targeting Mitochondrial Ion Channels to Fight Cancer.International journal of molecular sciences · 2018Review
- VDAC1 at the crossroads of cell metabolism, apoptosis and cell stress.Cell stress · 2017Article
- Effects of Hypoxia on Erythrocyte Membrane Properties-Implications for Intravascular Hemolysis and Purinergic Control of Blood Flow.Frontiers in physiology · 2017Review
- Voltage-Dependent Anion Channel 1 As an Emerging Drug Target for Novel Anti-Cancer Therapeutics.Frontiers in oncology · 2017Review
- News about VDAC1 in Hypoxia.Frontiers in oncology · 2016Article
- Imaging exocytosis of ATP-containing vesicles with TIRF microscopy in lung epithelial A549 cells.Purinergic signalling · 2012Article
- VDAC1: from structure to cancer therapy.Frontiers in oncology · 2012Article
- The maxi-anion channel: a classical channel playing novel roles through an unidentified molecular entity.The journal of physiological sciences : JPS · 2009Review
- Porin isoform 2 has a different localization in Drosophila melanogaster ovaries than porin 1.Journal of bioenergetics and biomembranes · 2008Article
- High-level expression, refolding and probing the natural fold of the human voltage-dependent anion channel isoforms I and II.The Journal of membrane biology · 2007Article
- Biophysical properties of the apoptosis-inducing plasma membrane voltage-dependent anion channel.Biophysical journal · 2006Article
- ATP release via anion channels.Purinergic signalling · 2005Article
- Molecular and cell biology of a family of voltage-dependent anion channel porins in Lotus japonicus.Plant physiology · 2004Article
- The beta-barrel finder (BBF) program, allowing identification of outer membrane beta-barrel proteins encoded within prokaryotic genomes.Protein science : a publication of the Protein Society · 2002Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Mitochondrial porin, or VDAC, is a pore-forming protein abundant in the outer mitochondrial membrane. Several publications have reported extramitochondrial localizations as well, but the evidence was considered insufficient by many, and the presence of porin in nonmitochondrial cellular compartments has remained in doubt for a long time. We have now obtained new data indicating that the plasma membrane of hematopoietic cells contains porin, probably located mostly in caveolae or caveolae-like domains. Porin was purified from the plasma membrane of intact cells by a procedure utilizing the membrane-impermeable labeling reagent NH-SS-biotin and streptavidin affinity chromatography, and shown to have the same properties as mitochondrial porin. A channel with properties similar to that of isolated VDAC was observed by patch-clamping intact cells. This review discusses the evidence supporting extramitochondrial localization, the putative identification of the plasma membrane porin with the "maxi" chloride channel, the hypothetical mechanisms of sorting porin to various cellular membrane structures, and its possible functions.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.