(Q40697123)

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

scientific article published on October 2002

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scholarly article

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Europe PubMed Central

PubMed publication ID

22 September 2017

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

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

bioluminescence

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protein-protein interaction

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based on heuristic

inferred from title

Anders A Jensen

1

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Hans Bräuner-Osborne

4

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Jakob Lerche Hansen

2

object named as

Jakob L Hansen

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author name string

Jakob L Hansen

2

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Søren P Sheikh

3

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Europe PubMed Central

PubMed publication ID

22 September 2017

language of work or name

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publication date

1 October 2002

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Europe PubMed Central

PubMed publication ID

22 September 2017

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

269

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Europe PubMed Central

PubMed publication ID

22 September 2017

20

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

5076-5087

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Ligands for glutamate receptors: design and therapeutic prospects

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The agonist-binding domain of the calcium-sensing receptor is located at the amino-terminal domain

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Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor

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GABA(B)-receptor subtypes assemble into functional heteromeric complexes.

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Heterodimerization is required for the formation of a functional GABA(B) receptor

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GABA(B) receptors function as a heteromeric assembly of the subunits GABA(B)R1 and GABA(B)R2.

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Dimerization of the extracellular calcium-sensing receptor (CaR) on the cell surface of CaR-transfected HEK293 cells

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Identification of the cysteine residues in the amino-terminal extracellular domain of the human Ca(2+) receptor critical for dimerization. Implications for function of monomeric Ca(2+) receptor

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The extracellular calcium-sensing receptor dimerizes through multiple types of intermolecular interactions

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Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins

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The two-state model of receptor activation

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Cell signaling by receptor tyrosine kinases

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

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A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins

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Homo- and hetero-oligomeric interactions between G-protein-coupled receptors in living cells monitored by two variants of bioluminescence resonance energy transfer (BRET): hetero-oligomers between receptor subtypes form more efficiently than between

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Sequence and expression of a metabotropic glutamate receptor

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Identifiers

10.1046/J.1432-1033.2002.03218.X

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

ResearchGate publication ID

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