The high affinity state of the beta 2-adrenergic receptor requires unique interaction between conserved and non-conserved extracellular loop cysteines.-Reference-Cited by-同舟云学术

The high affinity state of the beta 2-adrenergic receptor requires unique interaction between conserved and non-conserved extracellular loop cysteines.

Published:1994-03 Issue:9 Volume:269 Page:6743-6752
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Noda K.,Saad Y.,Graham R.M.,Karnik S.S.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference43 articles.

1. Adenylyl cyclases

2. Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin

3. Palmitoylation of the human β2-adrenergic receptor

4. Role of extracellular disulfide-bonded cysteines in the ligand binding function of the .beta.2-adrenergic receptor

5. Evidence for essential disulfide bonds in beta1-adrenergic receptors of turkey erythrocyte membranes. Inactivation by dithiothreitol.

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