Results 171 to 180 of about 24,819 (205)
Characterization of Antibiotic Resistance in <i>Shewanella</i> Species: An Emerging Pathogen in Clinical and Environmental Settings. [PDF]
Sher S +3 more
europepmc +1 more source
Whole-genome analysis of NDM-producing <i>Providencia hangzhouensis</i> associated with recurrent bacteraemia with rapid development of aztreonam-avibactam resistance. [PDF]
Chew KL +6 more
europepmc +1 more source
Some of the next articles are maybe not open access.
Related searches:
Related searches:
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
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
openaire +5 more sources
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
openaire +3 more sources
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
openaire +2 more sources
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
openaire +1 more source

