Regulation of highly homologous major urinary proteins in house mice quantified with label-free proteomic methods† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c6mb00278a Click here for additional data file.

@inproceedings{Enk2016RegulationOH,
  title={Regulation of highly homologous major urinary proteins in house mice quantified with label-free proteomic methods†
†Electronic supplementary information (ESI) available. See DOI: 10.1039/c6mb00278a
Click here for additional data file.

},
  author={Viktoria M. Enk and Christian Baumann and Michaela Thoss and Kenneth C. Luzynski and Ebrahim Razzazi-Fazeli and Dustin J. Penn},
  booktitle={Molecular bioSystems},
  year={2016}
}
Major urinary proteins (MUPs) are highly homologous proteoforms that function in binding, transporting and releasing pheromones in house mice. The main analytical challenge for studying variation in MUPs, even for state-of-the-art proteomics techniques, is their high degree of amino acid sequence homology. In this study we used unique peptides for proteoform-specific identification. We applied different search engines (ProteinPilot™vs. PEAKS®) and protein databases (MUP database vs. SwissProt… CONTINUE READING
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