Corpus ID: 5929471

High-affinity interactions between human alpha1A-adrenoceptor C-terminal splice variants produce homo- and heterodimers but do not generate the alpha1L-adrenoceptor.

@article{Ramsay2004HighaffinityIB,
  title={High-affinity interactions between human alpha1A-adrenoceptor C-terminal splice variants produce homo- and heterodimers but do not generate the alpha1L-adrenoceptor.},
  author={Douglas A. Ramsay and I. Craig Carr and John D. Pediani and Juan F. L{\'o}pez-Gim{\'e}nez and Richard J Thurlow and Mark D Fidock and Graeme Milligan},
  journal={Molecular pharmacology},
  year={2004},
  volume={66 2},
  pages={
          228-39
        }
}
  • Douglas A. Ramsay, I. Craig Carr, +4 authors Graeme Milligan
  • Published 2004
  • Medicine
  • Molecular pharmacology
  • Using combinations of bioluminescence resonance energy transfer, time-resolved fluorescence resonance energy transfer and the functional complementation of pairs of inactive receptor-G protein fusion proteins, the human alpha(1A-1)-adrenoceptor was shown to form homodimeric/oligomeric complexes when expressed in human embryonic kidney (HEK) 293 cells. Saturation bioluminescence resonance energy transfer studies indicated the alpha(1A-1)-adrenoceptor homodimer interactions to be high affinity… CONTINUE READING

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