Identification of an Interaction between Residue 6 of the Natural Peptide Ligand and a Distinct Residue within the Amino-terminal Tail of the Secretin Receptor-Reference-Cited by-同舟云学术

Identification of an Interaction between Residue 6 of the Natural Peptide Ligand and a Distinct Residue within the Amino-terminal Tail of the Secretin Receptor

Published:1999-07 Issue:27 Volume:274 Page:19161-19167
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Dong Maoqing,Wang Yan,Hadac Elizabeth M.,Pinon Delia I.,Holicky Eileen,Miller Laurence J.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference38 articles.

1. Demonstration of a Direct Interaction between Residue 22 in the Carboxyl-terminal Half of Secretin and the Amino-terminal Tail of the Secretin Receptor Using Photoaffinity Labeling

2. Molecular cloning and expression of a cDNA encoding the secretin receptor.

3. Receptors for secretin, calcitonin, parathyroid hormone (PTH)/PTH-related peptide, vasoactive intestinal peptide, glucagonlike peptide 1, growth hormone-releasing hormone, and glucagon belong to a newly discovered G-protein-linked receptor family

4. Secretin and vasoactive intestinal peptide receptors: Members of a unique family of G protein–coupled receptors

5. Human Intestinal VIP Receptor: Cloning and Functional Expression of Two cDNA Encoding Proteins with Different N-Terminal Domains

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