Dimerization of ABCG2 Analysed by Bimolecular Fluorescence Complementation

@inproceedings{Haider2011DimerizationOA,
  title={Dimerization of ABCG2 Analysed by Bimolecular Fluorescence Complementation},
  author={Ameena J. Haider and Deborah Briggs and Tim J. Self and Hannah L. Chilvers and Nicholas D. Holliday and Ian D Kerr},
  booktitle={PloS one},
  year={2011}
}
ABCG2 is one of three human ATP binding cassette transporters that are functionally capable of exporting a diverse range of substrates from cells. The physiological consequence of ABCG2 multidrug transport activity in leukaemia, and some solid tumours is the acquisition of cancer multidrug resistance. ABCG2 has a primary structure that infers that a minimal functional transporting unit would be a homodimer. Here we investigated the ability of a bimolecular fluorescence complementation approach… CONTINUE READING

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