Dimerization of the calcium-sensing receptor occurs within the extracellular domain and is eliminated by Cys --> Ser mutations at Cys101 and Cys236. (Q38325895)

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English	Dimerization of the calcium-sensing receptor occurs within the extracellular domain and is eliminated by Cys --> Ser mutations at Cys101 and Cys236.	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

2 September 2017

Dimerization of the calcium-sensing receptor occurs within the extracellular domain and is eliminated by Cys --> Ser mutations at Cys101 and Cys236. (English)

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Europe PubMed Central

PubMed publication ID

2 September 2017

author name string

Pace AJ

1

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2 September 2017

Gama L

2

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2 September 2017

Breitwieser GE

3

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2 September 2017

language of work or name

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publication date

1 April 1999

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2 September 2017

Journal of Biological Chemistry

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2 September 2017

274

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2 September 2017

17

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2 September 2017

11629-11634

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Europe PubMed Central

PubMed publication ID

2 September 2017

Molecular cloning and functional expression of human parathyroid calcium receptor cDNAs

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Cloned and expressed rat Ca2+-sensing receptor

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Amyloid-beta proteins activate Ca(2+)-permeable channels through calcium-sensing receptors

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The calcium-sensing receptor: insights into extracellular calcium homeostasis in health and disease

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The carboxyl terminus of the human calcium receptor. Requirements for cell-surface expression and signal transduction

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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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21 January 2018

Disulfide bonds in the extracellular calcium-polyvalent cation-sensing receptor correlate with dimer formation and its response to divalent cations in vitro

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Expression and characterization of inactivating and activating mutations in the human Ca2+o-sensing receptor

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

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Functional rescue of a constitutively desensitized beta2AR through receptor dimerization.

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Polar residues in the transmembrane domains of the type 1 angiotensin II receptor are required for binding and coupling. Reconstitution of the binding site by co-expression of two deficient mutants.

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A carboxyl-terminal domain controls the cooperativity for extracellular Ca2+ activation of the human calcium sensing receptor. A study with receptor-green fluorescent protein fusions

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Expression and purification of the extracellular ligand binding region of metabotropic glutamate receptor subtype 1.

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

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

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Mutational analysis of the cysteines in the extracellular domain of the human Ca2+ receptor: effects on cell surface expression, dimerization and signal transduction

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Identifiers

10.1074/JBC.274.17.11629

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

ResearchGate publication ID

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