The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Monitoring Receptor Oligomerization Using Time-resolved Fluorescence Resonance Energy Transfer and Bioluminescence Resonance Energy Transfer
Open accessAbstract
Oligomerization of the human delta-opioid receptor and its regulation by ligand occupancy were explored following expression in HEK293 cells using each of co-immunoprecipitation of differentially epitope-tagged forms of the receptor, bioluminescence resonance energy transfer and time-resolved fluorescence resonance energy transfer. All of the approaches identified constitutively formed receptor oligomers, and the time-resolved fluorescence studies confirmed the presence of such homo-oligomers at the cell surface. Neither the agonist ligand [d-Ala(2),d-Leu(5)]enkephalin nor the inverse agonist ligand ICI174864 were able to modulate the oligomerization status of this receptor. Interactions between co-expressed delta-opioid receptors and beta(2)-adrenoreceptors were observed in co-immunoprecipitation studies. Such hetero-oligomers could also be detected using bioluminescence resonance energy transfer although the signal obtained was substantially smaller than for homo-oligomers of either receptor type. Signal corresponding to the delta-opioid receptor-beta(2)-adrenoreceptor hetero-oligomer was increased in the presence of agonist for either receptor. However, substantial levels of this hetero-oligomer were not detected at the cell surface using time-resolved fluorescence resonance energy transfer. These studies demonstrate that, following transient transfection of HEK293 cells, constitutively formed oligomers of the human delta-opioid receptor can be detected by a variety of approaches. However, these are not regulated by ligand occupancy. They also indicate that time-resolved fluorescence resonance energy transfer represents a means to detect such oligomers at the cell surface in populations of intact cells.
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Cites
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Cited by
Waldhoer, M., Bartlett, S. E., & Whistler, J. L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073940 · Cited by 740
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Labeling and Single-Molecule Methods To Monitor G Protein-Coupled Receptor Dynamics
Tian, H., Fürstenberg, A., & Huber, T. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00084 · Cited by 114
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Metadata
- Authors
- McVey, M., Ramsay, D., Kellett, E., Rees, S., Wilson, S., Pope, A. J., & Milligan, G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-04
- Volume
- 276
- Issue
- 17
- Pages
- 14092-14099
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2130283831
- Cited by
- 257
- References
- 28
- FWCI
- 10.21
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- McVey, M., Ramsay, D., Kellett, E., Rees, S., Wilson, S., Pope, A. J., & Milligan, G. (2001). Monitoring Receptor Oligomerization Using Time-resolved Fluorescence Resonance Energy Transfer and Bioluminescence Resonance Energy Transfer. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m008902200
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