@article{LampidisGrossSokolovicetal.1994, author = {Lampidis, Robert and Gross, Roy and Sokolovic, Zeljka and Goebel, Werner and Kreft, J{\"u}rgen}, title = {The virulence regulator protein of Listeria ivanovii is highly homologous to PrfA from Listeria monocytogenes and both belong to the Crp-Fnr family of transcription regulators}, url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60503}, year = {1994}, abstract = {No abstract available}, subject = {Biologie}, language = {en} } @article{GruendemannGorboulevGambaryanetal.1994, author = {Gr{\"u}ndemann, Dirk and Gorboulev, Valentin and Gambaryan, Stepan and Veyhl, Maike and Koepsell, Hermann}, title = {Drug excretion mediated by a new prototype of polyspecific transporter}, url = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-59327}, year = {1994}, abstract = {CATIO~IC drugs of different types and structures (antihistaminics, antiarrhythmics, sedatives, opiates, cytostatics and antibiotics, for example) are excreted in mammals by epithelial cells of the renal proximal tubules and by hepatocytes in the liver1-4. In the proximal tubules, two functionally disparate transport systems are involved which are localized in the basolateral and luminal plasma membrane and are different from the previously identified neuronal monoamine transporters and A TP-dependent multidrug exporting proteins1-3,5-12. Here we report the isolation of a complementary DNA from rat kidney that encodes a 556-amino-acid membrane protein, OCT1, which has the functional characteristics of organic cation uptake over the basolateral membrane of renal proximal tubules and of organic cation uptake into hepatocytes. OCTl is not homologous to any other known protein and is found in kidney, liver and intestine. As OCTl translocates hydrophobic and hydrophilic organic cations of different structures, it is considered to be a new prolotype of polyspecific transporters that are important for drug elimination.}, subject = {Biologie}, language = {en} }