ReviewFrontiers in physiology2021
Historical Perspective of Pore-Forming Activity Studies of Voltage-Dependent Anion Channel (Eukaryotic or Mitochondrial Porin) Since Its Discovery in the 70th of the Last Century.
Review in Frontiers in physiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- How to isolate channel-forming membrane proteins using the E. coli expression system.Nature protocols · 2025Review
- Congrong Shujing Granules ameliorates mitochondrial associated membranes to against MPPFrontiers in pharmacology · 2025Article
- Developing a Novel and Optimized Yeast Model for Human VDAC Research.International journal of molecular sciences · 2024Article
- Phospholipid Scramblase Activity of VDAC Dimers: New Implications for Cell Death, Autophagy and Ageing.Biomolecules · 2024Review
- Solute Transport through Mitochondrial Porins In Vitro and In Vivo.Biomolecules · 2024Review
- Tracking the Activity and Position of Mitochondrial β-Barrel Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Beta-Barrel Channel Response to High Electric Fields: Functional Gating or Reversible Denaturation?International journal of molecular sciences · 2023Article
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic porin, also known as Voltage-Dependent Anion Channel (VDAC), is the most frequent protein in the outer membrane of mitochondria that are responsible for cellular respiration. Mitochondria are most likely descendants of strictly aerobic Gram-negative bacteria from the α-proteobacterial lineage. In accordance with the presumed ancestor, mitochondria are surrounded by two membranes. The mitochondrial outer membrane contains besides the eukaryotic porins responsible for its major permeability properties a variety of other not fully identified channels. It encloses also the TOM apparatus together with the sorting mechanism SAM, responsible for the uptake and assembly of many mitochondrial proteins that are encoded in the nucleus and synthesized in the cytoplasm at free ribosomes. The recognition and the study of electrophysiological properties of eukaryotic porin or VDAC started in the late seventies of the last century by a study of Schein et al., who reconstituted the pore from crude extracts of
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