Substitution of the Side-Chain-Constrained Amino Acids β-Methyl-2‘,6‘-Dimethyl-4‘-Methoxytyrosine in Position 2 of a Bicyclic Oxytocin Analogue Provides Unique Insights into the Bioactive Topography of Oxytocin Antagonists
- 1 July 1998
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 120 (29) , 7393-7394
- https://doi.org/10.1021/ja980848b
Abstract
No abstract availableThis publication has 19 references indexed in Scilit:
- Solution Conformations of Potent Bicyclic Antagonists of Oxytocin by Nuclear Magnetic Resonance Spectroscopy and Molecular Dynamics SimulationsJournal of the American Chemical Society, 1997
- Probing the Stereochemical Requirements for Receptor Recognition of δ Opioid Agonists through Topographic Modifications in Position 1Journal of the American Chemical Society, 1996
- Newly discovered stereochemical requirements in the side-chain conformation of .delta. opioid agonists for recognizing opioid .delta. receptorsJournal of Medicinal Chemistry, 1994
- Conformational and topographical considerations in the design of biologically active peptidesBiopolymers, 1993
- Structure-activity studies of a novel bicyclic oxytocin antagonistJournal of Medicinal Chemistry, 1992
- Macromodel—an integrated software system for modeling organic and bioorganic molecules using molecular mechanicsJournal of Computational Chemistry, 1990
- Conformationally restricted peptides through short‐range cyclizationsInternational Journal of Peptide and Protein Research, 1990
- Conformational restrictions of biologically active peptides via amino acid side chain groupsLife Sciences, 1982
- CARBON ISOTOPE CONSTITUTION OF SOME ACETIC ACIDSJournal of the American Chemical Society, 1953
- ENZYMATIC CLEAVAGE OF GLYCINAMIDE FROM VASOPRESSIN AND A PROPOSED STRUCTURE FOR THIS PRESSOR-ANTIDIURETIC HORMONE OF THE POSTERIOR PITUITARYJournal of the American Chemical Society, 1953