@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}
}
@article{HalbachScheer2000,
  author    = {Halbach, Thorsten and Scheer, Nico},
  title     = {Transcriptional activation by the PHD finger is inhibited through an adjacent leucine zipper that binds 14-3-3 proteins},
  series = {Nucleic Acids Research},
  volume    = {28},
  journal   = {Nucleic Acids Research},
  number    = {18},
  issn      = {1362-4962},
  doi       = {10.1093/nar/28.18.3542},
  pages     = {3542 -- 3550},
  year      = {2000},
  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{LawsonScheerPhametal.2001,
  author    = {Lawson, Nathan D. and Scheer, Nico and Pham, Van N. and Kim, Ceol-Hee and Chitnis, Ajay B. and Campos-Ortega, Jos{\´e} A. and Weinstein, Brant M.},
  title     = {Notch signaling is required for arterial-venous differentiation during embryonic vascular development},
  series = {Development},
  volume    = {128},
  journal   = {Development},
  number    = {19},
  issn      = {1477-9129},
  pages     = {3675 -- 3683},
  year      = {2001},
  language  = {en}
}
@article{ScheerRiedlWarrenetal.2002,
  author    = {Scheer, Nico and Riedl, Iris and Warren, J.T. and Kuwada, John Y. and Campos-Ortega, Jos{\´e} A.},
  title     = {A quantitative analysis of the kinetics of Gal4 activator and effector gene expression in the zebrafish},
  series = {Mechanism of Development},
  volume    = {112},
  journal   = {Mechanism of Development},
  number    = {1-2},
  issn      = {0925-4773},
  doi       = {10.1016/S0925-4773(01)00621-9},
  pages     = {9 -- 14},
  year      = {2002},
  language  = {en}
}
@article{HansScheerRiedletal.2004,
  author    = {Hans, Stefan and Scheer, Nico and Riedl, Iris and Weiz{\"a}cker, Elisabeth von and Blader, Patrick and Campos-Ortega, Jos{\´e} A.},
  title     = {her3, a zebrafish member of the hairy-E(spl) family, is repressed by Notch signalling},
  series = {Development},
  volume    = {131},
  journal   = {Development},
  number    = {12},
  issn      = {1477-9129},
  doi       = {10.1242/dev.01167},
  pages     = {2957 -- 2969},
  year      = {2004},
  language  = {en}
}
@article{ReugelsBoggettiScheeretal.2006,
  author    = {Reugels, Alexander M. and Boggetti, Barbara and Scheer, Nico and Campos-Ortega, Jos{\´e} A.},
  title     = {Asymmetric localization of Numb:EGFP in dividing neuroepithelial cells during neurulation in Danio rerio},
  series = {Developmental Dynamics},
  volume    = {235},
  journal   = {Developmental Dynamics},
  number    = {4},
  issn      = {1097-0177},
  doi       = {10.1002/dvdy.20699},
  pages     = {934 -- 948},
  year      = {2006},
  language  = {en}
}
@article{ScheerKapelyukhMcEwanetal.2012,
  author    = {Scheer, Nico and Kapelyukh, Yury and McEwan, Jillian and Beuger, Vincent and Stanley, Lesley A. and Rode, Anja and Wolf, C. Roland},
  title     = {Modeling Human Cytochrome P450 2D6 Metabolism and Drug-drug Interaction by a Novel Panel of Knockout and Humanized Mouse Lines},
  series = {Molecular Pharmacology},
  volume    = {81},
  journal   = {Molecular Pharmacology},
  number    = {1},
  publisher = {ASPET},
  address   = {Bethesda, Md.},
  issn      = {1521-0111},
  doi       = {10.1124/mol.111.075192},
  pages     = {63 -- 72},
  year      = {2012},
  abstract  = {The highly polymorphic human cytochrome P450 2D6 enzyme is involved in the metabolism of up to 25\% of all marketed drugs and accounts for significant individual differences in response to CYP2D6 substrates. Because of the differences in the multiplicity and substrate specificity of CYP2D family members among species, it is difficult to predict pathways of human CYP2D6-dependent drug metabolism on the basis of animal studies. To create animal models that reflect the human situation more closely and that allow an in vivo assessment of the consequences of differential CYP2D6 drug metabolism, we have developed a novel straightforward approach to delete the entire murine Cyp2d gene cluster and replace it with allelic variants of human CYP2D6. By using this approach, we have generated mouse lines expressing the two frequent human protein isoforms CYP2D6.1 and CYP2D6.2 and an as yet undescribed variant of this enzyme, as well as a Cyp2d cluster knockout mouse. We demonstrate that the various transgenic mouse lines cover a wide spectrum of different human CYP2D6 metabolizer phenotypes. The novel humanization strategy described here provides a robust approach for the expression of different CYP2D6 allelic variants in transgenic mice and thus can help to evaluate potential CYP2D6-dependent interindividual differences in drug response in the context of personalized medicine.},
  language  = {en}
}
@article{ScheerRossRodeetal.2008,
  author    = {Scheer, Nico and Ross, Jillian and Rode, Anja and Zevnik, Branko and Niehaves, Sandra and Faust, Nicole and Wolf, C. Roland},
  title     = {A novel panel of mouse models to evaluate the role of human pregnane X receptor and constitutive androstane receptor in drug response},
  series = {Journal of Clinical Investigation},
  volume    = {118},
  journal   = {Journal of Clinical Investigation},
  number    = {9},
  issn      = {1558-8238},
  doi       = {https://doi.org/10.1172/JCI35483},
  pages     = {3228 -- 3239},
  year      = {2008},
  language  = {en}
}
@article{ScheerRossKapelyukhetal.2010,
  author    = {Scheer, Nico and Ross, Jillian and Kapelyukh, Yury and Rode, Anja and Wolf, C. Roland},
  title     = {In vivo responses of the human and murine pregnane X receptor to dexamethasone in mice},
  series = {Drug Metabolism and Disposition},
  volume    = {38},
  journal   = {Drug Metabolism and Disposition},
  number    = {7},
  publisher = {ASPET},
  address   = {Bethesda},
  issn      = {1521-009X},
  doi       = {10.1124/dmd.109.031872},
  pages     = {1046 -- 1053},
  year      = {2010},
  abstract  = {Dexamethasone (DEX) is a potent and widely used anti-inflammatory and immunosuppressant glucocorticoid. It can bind and activate the pregnane X receptor (PXR), which plays a critical role as xenobiotic sensor in mammals to induce the expression of many enzymes, including cytochromes P450 in the CYP3A family. This induction results in its own metabolism. We have used a series of transgenic mouse lines, including a novel, improved humanized PXR line, to compare the induction profile of PXR-regulated drug-metabolizing enzymes after DEX administration, as well as looking at hepatic responses to rifampicin (RIF). The new humanized PXR model has uncovered further intriguing differences between the human and mouse receptors in that RIF only induced Cyp2b10 in the new humanized model. DEX was found to be a much more potent inducer of Cyp3a proteins in wild-type mice than in mice humanized for PXR. To assess whether PXR is involved in the detoxification of DEX in the liver, we analyzed the consequences of high doses of the glucocorticoid on hepatotoxicity on different PXR genetic backgrounds. We also studied these effects in an additional mouse model in which functional mouse Cyp3a genes have been deleted. These strains exhibited different sensitivities to DEX, indicating a protective role of the PXR and CYP3A proteins against the hepatotoxicity of this compound.},
  language  = {en}
}