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Humic substances in natural waters and their complexation with trace metals and radionuclides: a review. [129 references]
Section I introduces the material contained in the rest of the report. Section II presents the origin and characteristics of humic materials as we understand them today and outlines the methods that…
Discovery and structure-activity relationships of a series of pyroglutamic acid amide antagonists of the P2X7 receptor.
2,5-Diketopiperazines as potent and selective oxytocin antagonists 1: Identification, stereochemistry and initial SAR.
Identification and optimization of novel 1,3,4-oxadiazole EP1 receptor antagonists.
2,5-diketopiperazines as potent, selective, and orally bioavailable oxytocin antagonists. 3. Synthesis, pharmacokinetics, and in vivo potency.
A short, efficient, and highly stereoselective synthesis of a series of (3R,6R,7R)-2,5-diketopiperazine oxytocin antagonists and their pharmacokinetics in rat and dog is described. Prediction of the…
Synthesis and anti-HIV-1 activity of a series of imidazo[1,5-b]pyridazines.
It is proposed that key features of the interaction with RT include hydrogen-bond acceptor and aromatic pi-orbital bonding with the imidazopyridazine nucleus and a benzoyl function separated from the heterocycle by a suitable spacer group.
2,5-diketopiperazines as potent, selective, and orally bioavailable oxytocin antagonists. 2. Synthesis, chirality, and pharmacokinetics.
- A. D. Borthwick, D. E. Davies, P. Wyatt
- Biology, ChemistryJournal of medicinal chemistry
- 8 October 2005
The 2',4'-difluorophenyldiketopiperazine derivative 37 is a highly potent oxytocin antagonist against the human oxytocIn receptor that has >1000-fold selectivity over all three vasopressin receptors V1a, V2, and V1b.
Synthesis and structure-activity relationships of a series of (1H-pyrazol-4-yl)acetamide antagonists of the P2X7 receptor.
Identification of potent and selective oxytocin antagonists. Part 1: indole and benzofuran derivatives.
1,2,4-Triazolo-[1,5-a]pyridine HIF Prolylhydroxylase Domain-1 (PHD-1) Inhibitors With a Novel Monodentate Binding Interaction.
- Saleh A. Ahmed, A. Ayscough, A. Hendrick
- Chemistry, BiologyJournal of medicinal chemistry
- 24 June 2017
These inhibitors were shown to possess a novel binding mode by X-ray crystallography, in which the triazolo N1 atom coordinates in a hitherto unreported monodentate interaction with the active site Fe2+ ion, while the benzonitrile group accepts a hydrogen-bonding interaction from the side chain residue of Asn315.