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Biogenesis of mitochondrial porin

open access: yes, 1990
Pfaller, Rupert   +2 more
openaire   +1 more source
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Outer Membrane Porins

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
openaire   +2 more sources

Extramitochondrial Porin: Facts and Hypotheses

Journal of Bioenergetics and Biomembranes, 2000
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.
G. BATHORI   +8 more
openaire   +5 more sources

On the Structure of Mitochondrial Porins and Its Homologies with Bacterial Porins

Biochemical and Biophysical Research Communications, 1994
By 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
openaire   +3 more sources

New Findings Concerning Vertebrate Porin

Naturwissenschaften, 1997
Eukaryotic 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
openaire   +2 more sources

Porin and porin-associated protein (PAP) of Rhodospirillum rubrum FR1

Microbiology, 1995
The 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
openaire   +1 more source

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