Intermolecular interactions between dimeric calcium-sensing receptor monomers are important for its normal function (Q35061467)

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Language	Label	Description	Also known as
English	Intermolecular interactions between dimeric calcium-sensing receptor monomers are important for its normal function	scientific article

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Intermolecular interactions between dimeric calcium-sensing receptor monomers are important for its normal function (English)

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

author name string

M Bai

1

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

S Trivedi

2

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

O Kifor

3

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

S J Quinn

4

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

E M Brown

5

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

publication date

1 March 1999

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Proceedings of the National Academy of Sciences of the United States of America

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Europe PubMed Central

PubMed publication ID

6 August 2017

96

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

6

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

2834-2839

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

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

1 reference

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

1 reference

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

1 reference

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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

1 reference

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Familial hypoparathyroidism: identification of a novel gain of function mutation in transmembrane domain 5 of the calcium-sensing receptor

1 reference

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Modes of peptide binding in G protein-coupled receptors

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1 reference

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In vivo and in vitro characterization of neonatal hyperparathyroidism resulting from a de novo, heterozygous mutation in the Ca2+-sensing receptor gene: normal maternal calcium homeostasis as a cause of secondary hyperparathyroidism in familial [...]

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Functional characterization of calcium-sensing receptor mutations expressed in human embryonic kidney cells

1 reference

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A familial syndrome of hypocalcemia with hypercalciuria due to mutations in the calcium-sensing receptor

1 reference

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

1 reference

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

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Coexpression studies with mutant muscarinic/adrenergic receptors provide evidence for intermolecular "cross-talk" between G-protein-linked receptors

1 reference

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Cloning and characterization of an extracellular Ca(2+)-sensing receptor from bovine parathyroid

1 reference

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Mutations in the human Ca(2+)-sensing receptor gene cause familial hypocalciuric hypercalcemia and neonatal severe hyperparathyroidism

1 reference

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Autosomal dominant hypocalcaemia caused by a Ca(2+)-sensing receptor gene mutation

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Plasma Membrane Localization and Functional Rescue of Truncated Forms of a G Protein-coupled Receptor

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Oligomeric structure of muscarinic receptors is shown by photoaffinity labeling: subunit assembly may explain high- and low-affinity agonist states

1 reference

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Chimeric alpha 2-,beta 2-adrenergic receptors: delineation of domains involved in effector coupling and ligand binding specificity

1 reference

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8 July 2018

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

1 reference

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27 September 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=15855

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

1 reference

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1 reference

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27 September 2018

Identifiers

10.1073/PNAS.96.6.2834

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

ResearchGate publication ID

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