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2019
The transport of small molecules across membranes is essential for the import of nutrients and other energy sources into the cell and, for the export of waste and other potentially harmful byproducts out of the cell. While hydrophobic molecules are permeable to membranes, ions and other small polar molecules require transport via specialized membrane ...
Masi, Muriel +2 more
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The transport of small molecules across membranes is essential for the import of nutrients and other energy sources into the cell and, for the export of waste and other potentially harmful byproducts out of the cell. While hydrophobic molecules are permeable to membranes, ions and other small polar molecules require transport via specialized membrane ...
Masi, Muriel +2 more
openaire +2 more sources
Extramitochondrial Porin: Facts and Hypotheses
Journal of Bioenergetics and Biomembranes, 2000Mitochondrial 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.
G. BATHORI +8 more
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On the Structure of Mitochondrial Porins and Its Homologies with Bacterial Porins
Biochemical and Biophysical Research Communications, 1994By use of computer modelling, we have predicted a model of 16 transmembrane beta-strands for mitochondrial porins structure from human, Saccharomyces cerevisiae, Neurospora crassa and Dictyostelium discoideum. The proposed model takes into account biochemical and immunological data reported in the literature, as well as electrophysiological results ...
G Rauch, O Moran
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New Findings Concerning Vertebrate Porin
Naturwissenschaften, 1997Eukaryotic porin can be considered to be a good candidate for forming the channel component of the protein complex which, depending on the approach used, may realize its expression either as the outwardly-rectifying depolarization-induced chloride channel or as the volume-sensitive organic osmolyte-anion channel.
F P, Thinnes, S, Reymann
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Porin and porin-associated protein (PAP) of Rhodospirillum rubrum FR1
Microbiology, 1995The porin of Rhodospirillum rubrum FR1 was found in the outer membrane as a complex with a relatively small (32 kDa) porin-associated protein (PAP). The porin moiety of the complex consisted of a trimer which revealed a mainly β-sheet structure, while the porin-PAP complex also contained a significant α-helical portion.
U. Neumann +4 more
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Purification of Mammalian Porins
1989The matrix space of mitochondria is surrounded by two unit membranes. Whereas the role of the inner membrane in oxidative phosphorylation was studied in full detail in recent years, the role of the mitochondrial outer membrane in the mitochondrial metabolism has been neglected because of its apparently high permeability for small hydrophilic solutes ...
DE PINTO, Vito Nicola +3 more
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A light-triggered transmembrane porin
Chemical Communications, 2018Porins are ideal model systems for channel engineering. Here, we present a photocaged diethylaminocoumarin (DEACM) hybrid of the transmembrane porin OmpG.
J. Kahlstatt +5 more
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1995
The mitochondrial outer membrane contains a permeability channel that is responsible for the passage of hydrophilic compounds across the membrane. The transmembrane protein, called mitochondrial porin is not particularly hydrophobic and its primary structure does not contain any indication for the existence of transmembrane hydrophobic α-helical ...
Roland Benz +3 more
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The mitochondrial outer membrane contains a permeability channel that is responsible for the passage of hydrophilic compounds across the membrane. The transmembrane protein, called mitochondrial porin is not particularly hydrophobic and its primary structure does not contain any indication for the existence of transmembrane hydrophobic α-helical ...
Roland Benz +3 more
openaire +1 more source