PARATHYROID-HORMONE RECEPTOR INTERACTIONS

被引：9

作者：

CAULFIELD, MP

ROSENBLATT, M

机构：

[1] Department of Biological Research and Molecular Biology, Merck Sharp and Dohme Research Laboratories, West Point, 19486

来源：

TRENDS IN ENDOCRINOLOGY AND METABOLISM | 1990年 / 1卷 / 03期

关键词：

D O I：

10.1016/1043-2760(90)90030-7

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

Identification of sites within the antagonist peptide of parathyroid hormone (PTH) that are "tolerant" of a wide range of amino acid substitutions has led to the design of new PTH antagonists. These antagonists have increased potency because of substitution, at appropriate sites, of amino acids that increase the interaction of the ligand with its receptor but do not cause signal transduction. Similar modifications in the parathyroid hormone-related protein (PTHrP) antagonist led to antagonists with increased potency. Further, the partial agonism of this analog could be removed by exchange of residues between PTH and PTHrP. © 1990.

引用

页码：164 / 168

页数：5

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