Basic Pharmacological and Structural Evidence for Class A G-Protein-Coupled Receptor Heteromerization

@article{Franco2016BasicPA,
  title={Basic Pharmacological and Structural Evidence for Class A G-Protein-Coupled Receptor Heteromerization},
  author={R. Franco and E. Mart{\'i}nez-Pinilla and J. Lanciego and Gemma Navarro},
  journal={Frontiers in Pharmacology},
  year={2016},
  volume={7}
}
  • R. Franco, E. Martínez-Pinilla, +1 author Gemma Navarro
  • Published 2016
  • Medicine, Biology
  • Frontiers in Pharmacology
  • Cell membrane receptors rarely work on isolation, often they form oligomeric complexes with other receptor molecules and they may directly interact with different proteins of the signal transduction machinery. For a variety of reasons, rhodopsin-like class A G-protein-coupled receptors (GPCRs) seem an exception to the general rule of receptor–receptor direct interaction. In fact, controversy surrounds their potential to form homo- hetero-dimers/oligomers with other class A GPCRs; in a sense… CONTINUE READING

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    References

    Publications referenced by this paper.
    SHOWING 1-10 OF 134 REFERENCES
    Heterodimerization of G Protein-Coupled Receptors: Specificity and Functional Significance
    353
    Class A G-protein-coupled receptor (GPCR) dimers and bivalent ligands.
    85
    Rescue of defective G protein–coupled receptor function in vivo by intermolecular cooperation
    162
    GPCR Dimers Fall Apart
    61
    Class A GPCR heterodimers: evidence from binding studies.
    69
    G protein-coupled receptor transactivation: from molecules to mice.
    11