scispace - formally typeset
Journal ArticleDOI

A biologically active analogue of oxytocin not containing a disulfide group.

TLDR
Die Synthese eines Analogen des Deamino-oxytocins, in dem ein Schwefelatom der Disulfidbrücke durch eine Methylengruppe ersetzt ist (I,X = CH2,R=H), wird beschrieben.
Abstract
Die Synthese eines Analogen des Deamino-oxytocins, in dem ein Schwefelatom der Disulfidbrucke durch eine Methylengruppe ersetzt ist (I,X = CH2,R=H), wird beschrieben. Die Verbindung hat oxytocinahnliche biologische Wirkungen.

read more

Citations
More filters
Journal ArticleDOI

Highly active cyclic and bicyclic somatostatin analogues of reduced ring size

TL;DR: The preparation of conformationally constrained analogues of somatostatin which are highly active inhibitors of the release of insulin, glucagon and growth hormone in vivo are reported.
Journal ArticleDOI

Vinyl sulfide cyclized analogues of angiotensin II with high affinity and full agonist activity at the AT(1) receptor.

TL;DR: The cyclic vinyl sulfides that have agonist activity were both shown to possess low-energy conformers compatible with the previously proposed 3D model for the bioactive conformation of Ang II.
Journal ArticleDOI

Diaminodiacid-based solid-phase synthesis of peptide disulfide bond mimics.

TL;DR: These disulfide surrogates wereusually synthesized through thiol alkylation, azide–alkynecycloaddition, or olefin metathesis reactions occurring at thepeptide side chains after the peptide skeletons are fullyassembled.
Book ChapterDOI

Basic Pharmacological Properties of Synthetic Analogues and Homologues of the Neurohypophysial Hormones

B. Berde, +1 more
TL;DR: The principal aim of all this work was to try to establish relationships between the chemical structure and the biological activities of these hormones.
References
More filters
Journal ArticleDOI

A highly potent analogue of oxytocin, desamino-oxytocin.

TL;DR: The synthesis and biological activities of desamino-oxytocin, an analogue lacking the free amino group present in oxytocin, are described and the presence of an amino group is vital to the possession of pharmacological activity is determined.
Journal Article

The isolation of a protein from the pars neuralis of the ox pituitary with constant oxytocic, pressor and diuresis-inhibiting activities

TL;DR: Experiments designed to demonstrate that the oxytocic and vasopressor activities are moieties chemically united with the protein are described, and reduction of the cystine in the protein by thioglycollic acid nearly abolishes the activity.
Related Papers (5)