@article{RoeschKratzHeringetal.2016,
  author    = {R{\"o}sch, C. and Kratz, F. and Hering, T. and Trautmann, S. and Umanskaya, N. and Tippk{\"o}tter, Nils and M{\"u}ller-Renno, C.M. and Ulber, R. and Hannig, M. and Ziegler, C.},
  title     = {Albumin-lysozyme interactions: cooperative adsorption on titanium and enzymatic activity},
  series = {Colloids and Surfaces B: Biointerfaces},
  volume    = {149},
  journal   = {Colloids and Surfaces B: Biointerfaces},
  number    = {1},
  publisher = {Elsevier},
  address   = {Amsterdam},
  doi       = {10.1016/j.colsurfb.2016.09.048},
  pages     = {115 -- 121},
  year      = {2016},
  abstract  = {The interplay of albumin (BSA) and lysozyme (LYZ) adsorbed simultaneously on titanium was analyzed by gel electrophoresis and BCA assay. It was found that BSA and lysozyme adsorb cooperatively. Additionally, the isoelectric point of the respective protein influences the adsorption. Also, the enzymatic activity of lysozyme and amylase (AMY) in mixtures with BSA was considered with respect to a possible influence of protein-protein interaction on enzyme activity. Indeed, an increase of lysozyme activity in the presence of BSA could be observed. In contrast, BSA does not influence the activity of amylase.},
  language  = {en}
}
@article{SalpatiChuChenetal.2014,
  author    = {Salpati, Laurent and Chu, Xiaoyan and Chen, Liangfu and Prasad, Bhagwat and Dallas, Shannon and Evers, Raymond and Mamaril-Fishman, Donna and Geier, Ethan G. and Kehler, Jonathan and Kunta, Jeevan and Mezler, Mario and Laplanche, Loic and Pang, Jodie and Soars, Matthew G. and Unadkat, Jashvant D. and van Waterschoot, Robert A.B. and Yabut, Jocelyn and Schinkel, Alfred H. and Scheer, Nico and Rode, Anja},
  title     = {Evaluation of organic anion transporting polypeptide 1B1 and 1B3 humanized mice as a translational model to study the pharmacokinetics of statins},
  series = {Drug Metabolism and Disposition},
  volume    = {42},
  journal   = {Drug Metabolism and Disposition},
  number    = {8},
  publisher = {ASPET},
  address   = {Bethesda, Md.},
  issn      = {1521-009X},
  doi       = {10.1124/dmd.114.057976},
  pages     = {1301 -- 1313},
  year      = {2014},
  abstract  = {Organic anion transporting polypeptide (Oatp) 1a/1b knockout and OATP1B1 and -1B3 humanized mouse models are promising tools for studying the roles of these transporters in drug disposition. Detailed characterization of these models will help to better understand their utility for predicting clinical outcomes. To advance this approach, we carried out a comprehensive analysis of these mouse lines by evaluating the compensatory changes in mRNA expression, quantifying the amounts of OATP1B1 and -1B3 protein by liquid chromatography-tandem mass spectrometry, and studying the active uptake in isolated hepatocytes and the pharmacokinetics of some prototypical substrates including statins. Major outcomes from these studies were 1) mostly moderate compensatory changes in only a few genes involved in drug metabolism and disposition, 2) a robust hepatic expression of OATP1B1 and -1B3 proteins in the respective humanized mouse models, and 3) functional activities of the human transporters in hepatocytes isolated from the humanized models with several substrates tested in vitro and with pravastatin in vivo. However, the expression of OATP1B1 and -1B3 in the humanized models did not significantly alter liver or plasma concentrations of rosuvastatin and pitavastatin compared with Oatp1a/1b knockout controls under the conditions used in our studies. Hence, although the humanized OATP1B1 and -1B3 mice showed in vitro and/or in vivo functional activity with some statins, further characterization of these models is required to define their potential use and limitations in the prediction of drug disposition and drug-drug interactions in humans.},
  language  = {en}
}
@incollection{SamuelssonScheerWilsonetal.2017,
  author    = {Samuelsson, K. and Scheer, Nico and Wilson, I. and Wolf, C.R. and Henderson, C.J.},
  title     = {Genetically Humanized Animal Models},
  series = {Comprehensive Medicinal Chemistry III. 3rd Edition},
  booktitle = {Comprehensive Medicinal Chemistry III. 3rd Edition},
  editor    = {Chackalamannil, Samuel},
  publisher = {Elsevier},
  address   = {Saint Louis},
  isbn      = {978-0-12-803201-5},
  doi       = {10.1016/B978-0-12-409547-2.12376-5},
  pages     = {130 -- 149},
  year      = {2017},
  abstract  = {Genetically humanized mice for proteins involved in drug metabolism and toxicity and mice engrafted with human hepatocytes are emerging as promising in vivo models for improved prediction of the pharmacokinetic, drug-drug interaction, and safety characteristics of compounds in humans. This is an overview on the genetically humanized and chimeric liver-humanized mouse models, which are illustrated with examples of their utility in drug metabolism and toxicity studies. The models are compared to give guidance for selection of the most appropriate model by highlighting advantages and disadvantages to be carefully considered when used for studies in drug discovery and development.},
  language  = {en}
}
@article{ScheeleBongaertsMaureretal.2009,
  author    = {Scheele, S. and Bongaerts, Johannes and Maurer, K.-H. and Freudl, R.},
  title     = {Sekretion einer Kofaktor-haltigen Oxidase durch Corynebacterium glutamicum},
  series = {Chemie - Ingenieur - Technik (CIT)},
  volume    = {Vol. 81},
  journal   = {Chemie - Ingenieur - Technik (CIT)},
  number    = {Iss. 8},
  issn      = {1522-2640 (E-Journal); 0009-286X (Print)},
  pages     = {1309},
  year      = {2009},
  language  = {de}
}
@article{ScheeleOertelBongaertsetal.2013,
  author    = {Scheele, Sandra and Oertel, Dan and Bongaerts, Johannes and Evers, Stefan and Hellmuth, Hendrik and Maurer, Karl-Heinz and Bott, Michael and Freudl, Roland},
  title     = {Secretory production of an FAD cofactor-containing cytosolic enzyme (sorbitol-xylitol oxidase from Streptomyces coelicolor) using the twin-arginine translocation (Tat) pathway of Corynebacterium glutamicum},
  series = {Microbial biotechnology},
  journal   = {Microbial biotechnology},
  publisher = {Wiley-Blackwell},
  address   = {Oxford},
  issn      = {1751-7915},
  pages     = {202 -- 206},
  year      = {2013},
  language  = {en}
}
@article{ScheerBalimaneHaywardetal.2012,
  author    = {Scheer, Nico and Balimane, Praveen and Hayward, Michael D. and Buechel, Sandra and Kauselmann, Gunther and Wolf, C. Roland},
  title     = {Generation and Characterization of a Novel Multidrug Resistance Protein 2 Humanized Mouse Line},
  series = {Drug Metabolism and Disposition},
  volume    = {40},
  journal   = {Drug Metabolism and Disposition},
  number    = {11},
  publisher = {ASPET},
  address   = {Bethesda, Md.},
  issn      = {1521-0111},
  doi       = {10.1124/dmd.112.047605},
  pages     = {2212 -- 2218},
  year      = {2012},
  abstract  = {The multidrug resistance protein (MRP) 2 is predominantly expressed in liver, intestine, and kidney, where it plays an important role in the excretion of a range of drugs and their metabolites or endogenous compounds into bile, feces, and urine. Mrp knockout [Mrp2(-/-)] mice have been used recently to study the role of MRP2 in drug disposition. Here, we describe the first generation and initial characterization of a mouse line humanized for MRP2 (huMRP2), which is nulled for the mouse Mrp2 gene and expresses the human transporter in the organs and cell types where MRP2 is normally expressed. Analysis of the mRNA expression for selected cytochrome P450 and transporter genes revealed no major changes in huMRP2 mice compared with wild-type controls. We show that human MRP2 is able to compensate functionally for the loss of the mouse transporter as demonstrated by comparable bilirubin levels in the humanized mice and wild-type controls, in contrast to the hyperbilirubinemia phenotype that is observed in MRP2(-/-) mice. The huMRP2 mouse provides a model to study the role of the human transporter in drug disposition and in assessing the in vivo consequences of inhibiting this transporter by compounds interacting with human MRP2.},
  language  = {en}
}
@article{ScheerCamposOrtega1999,
  author    = {Scheer, Nico and Campos-Ortega, Jos{\´e} A.},
  title     = {Use of the Gal4-UAS technique for targeted gene expression in the zebrafish},
  series = {Mechanism of Development},
  volume    = {80},
  journal   = {Mechanism of Development},
  number    = {2},
  issn      = {0925-4773},
  doi       = {10.1016/S0925-4773(98)00209-3},
  pages     = {153 -- 158},
  year      = {1999},
  language  = {en}
}
@incollection{ScheerChuSalphatietal.2016,
  author    = {Scheer, Nico and Chu, Xiaoyan and Salphati, Laurent and Zamek-Gliszczynski, Maciej J.},
  title     = {Knockout and humanized animal models to study membrane transporters in drug development},
  series = {Drug Transporters: Volume 1: Role and Importance in ADME and Drug Development},
  booktitle = {Drug Transporters: Volume 1: Role and Importance in ADME and Drug Development},
  editor    = {Nicholls, Glynis},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  isbn      = {978-1-78262-379-3},
  doi       = {10.1039/9781782623793-00298},
  pages     = {298 -- 332},
  year      = {2016},
  language  = {en}
}
@article{ScheerGrothHansetal.2001,
  author    = {Scheer, Nico and Groth, Anne and Hans, Stefan and Campos-Ortega, Jos{\´e} A.},
  title     = {An instructive function for Notch in promoting gliogenesis in the zebrafish retina},
  series = {Development},
  volume    = {128},
  journal   = {Development},
  number    = {7},
  issn      = {0950-1991},
  pages     = {1099 -- 1107},
  year      = {2001},
  language  = {en}
}
@article{ScheerHendersonKapelyukhetal.2019,
  author    = {Scheer, Nico and Henderson, Colin James and Kapelyukh, Yury and Rode, Anja and Mclaren, Aileen W. and MacLeod, Alastair Kenneth and Lin, De and Wright, Jayne and Stanley, Lesley and Wolf, C. Roland},
  title     = {An extensively humanised mouse model to predict pathways of drug disposition, drug/drug interactions, and to facilitate the design of clinical trials},
  series = {Drug Metabolism and Disposition},
  journal   = {Drug Metabolism and Disposition},
  number    = {Early view},
  doi       = {10.1124/dmd.119.086397},
  pages     = {69 Seiten},
  year      = {2019},
  language  = {en}
}