(Q35579623)

English

GPCR dimerisation

scientific article published on December 5, 2003

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scholarly article

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Europe PubMed Central

PubMed publication ID

9 August 2017

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Europe PubMed Central

GPCR dimerisation (English)

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Europe PubMed Central

PubMed publication ID

9 August 2017

G protein-coupled receptor

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author name string

Graeme Milligan

1

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Europe PubMed Central

PubMed publication ID

9 August 2017

Douglas Ramsay

2

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Europe PubMed Central

PubMed publication ID

9 August 2017

Geraldine Pascal

3

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Europe PubMed Central

PubMed publication ID

9 August 2017

Juan J. Carrillo

4

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14607245

30 March 2024

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publication date

1 December 2003

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Europe PubMed Central

PubMed publication ID

9 August 2017

5 December 2003

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National Center for Biotechnology Information

PubMed publication ID

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=14607245

30 March 2024

number of pages

8

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https://api.elsevier.com/content/article/PII:S0024320503008233?httpAccept=text/xml

1 reference

10.1016/J.LFS.2003.09.005

https://api.crossref.org/works/10.1016/J.LFS.2003.09.005

30 March 2024

https://api.elsevier.com/content/article/PII:S0024320503008233?httpAccept=text/plain

1 reference

10.1016/J.LFS.2003.09.005

https://api.crossref.org/works/10.1016/J.LFS.2003.09.005

30 March 2024

1 reference

Europe PubMed Central

PubMed publication ID

9 August 2017

74

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Europe PubMed Central

PubMed publication ID

9 August 2017

2-3

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Europe PubMed Central

PubMed publication ID

9 August 2017

181-188

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Europe PubMed Central

PubMed publication ID

9 August 2017

AT1-receptor heterodimers show enhanced G-protein activation and altered receptor sequestration

1

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The angiotensin II AT2 receptor is an AT1 receptor antagonist.

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Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)

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Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer

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Ligand-independent dimerization of CXCR4, a principal HIV-1 coreceptor

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Agonist-dependent dissociation of oligomeric complexes of G protein-coupled cholecystokinin receptors demonstrated in living cells using bioluminescence resonance energy transfer

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Truncated isoforms inhibit [3H]prazosin binding and cellular trafficking of native human α1A-adrenoceptors

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Gonadotropin-releasing hormone receptor microaggregation. Rate monitored by fluorescence resonance energy transfer

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Dimerization of the delta opioid receptor: implication for a role in receptor internalization

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Homodimerization of neuropeptide y receptors investigated by fluorescence resonance energy transfer in living cells

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Heterodimerization of G-protein-coupled receptors: pharmacology, signaling and trafficking

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Applications of novel resonance energy transfer techniques to study dynamic hormone receptor interactions in living cells.

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Structural models for dimerization of G-protein coupled receptors: the opioid receptor homodimers.

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Prediction of heterodimerization interfaces of G-protein coupled receptors with a new subtractive correlated mutation method

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Heterodimerization of calcium sensing receptors with metabotropic glutamate receptors in neurons

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G-protein-coupled receptor oligomerization and its potential for drug discovery

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Dopamine D1 and adenosine A1 receptors form functionally interacting heteromeric complexes

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The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer.

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A peptide derived from a beta2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation.

19

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Coaggregation, cointernalization, and codesensitization of adenosine A2A receptors and dopamine D2 receptors

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Constitutive Agonist-independent CCR5 Oligomerization and Antibody-mediated Clustering Occurring at Physiological Levels of Receptors

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Probing intermolecular protein-protein interactions in the calcium-sensing receptor homodimer using bioluminescence resonance energy transfer (BRET).

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G-protein-coupled receptor heterodimerization modulates receptor function

23

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Opioids and their complicated receptor complexes

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Oligomerization of opioid receptors with beta 2-adrenergic receptors: a role in trafficking and mitogen-activated protein kinase activation

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Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer

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Oligomerization of the human thyrotropin receptor: fluorescent protein-tagged hTSHR reveals post-translational complexes

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Ligand-dependent inhibition of oligomerization at the human thyrotropin receptor

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Beta 1/beta 2-adrenergic receptor heterodimerization regulates beta 2-adrenergic receptor internalization and ERK signaling efficacy

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Inhibition of cell surface expression by mutant receptors demonstrates that D2 dopamine receptors exist as oligomers in the cell

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Oligomerization of opioid receptors: generation of novel signaling units

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Heterodimerization of G-protein-coupled receptors in the CNS.

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GABAB receptors - the first 7TM heterodimers.

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Receptor dimerization: a key step in chemokine signaling

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Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer

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GABAB receptors make it to the top--as dimers

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G-protein-coupled receptors function as oligomers in vivo

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The extracellular N-terminal domain and transmembrane domains 1 and 2 mediate oligomerization of a yeast G protein-coupled receptor

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Ligand binding to somatostatin receptors induces receptor-specific oligomer formation in live cells

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Photobleaching fluorescence resonance energy transfer reveals ligand-induced oligomer formation of human somatostatin receptor subtypes.

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Heterodimerization of somatostatin and opioid receptors cross-modulates phosphorylation, internalization, and desensitization

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Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers

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Functional significance of oligomerization of G-protein-coupled receptors.

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Heteromeric association creates a P2Y-like adenosine receptor

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Identifiers

10.1016/J.LFS.2003.09.005

1 reference

Europe PubMed Central

PubMed publication ID

9 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

9 August 2017

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