✦ LIBER ✦

Structural Determination of Two Active Compounds That Bind to the Muscarinic M3 Receptor in Beer

✍ Scribed by Nahoko Yamaji; Yoshiaki Yokoo; Takashi Iwashita; Asuka Nemoto; Minako Koike; Yoshihide Suwa; Toshiyuki Wakimoto; Kuniro Tsuji; Haruo Nukaya

Book ID: 109123671
Publisher: John Wiley and Sons
Year: 2007
Tongue: English
Weight: 170 KB
Volume: 31
Category: Article
ISSN: 0145-6008
DOI: 10.1111/j.1530-0277.2006.00280.x

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Structural factors that determine the ab

Structural factors that determine the ability of adenosine and related compounds to activate the cardiac ryanodine receptor

✍ Wei Mun Chan; William Welch; Rebecca Sitsapesan 📂 Article 📅 2000 🏛 Nature Publishing Group 🌐 English ⚖ 284 KB

Contribution of Lateral Substituents in

Contribution of Lateral Substituents in Symmetrical and Non-symmetrical Heptane-bisammonio Compounds to the Allosteric Stabilization of N-methylscopolamine Binding to Muscarinic M2 Receptors

✍ Markus Staudt; Christian Tränkle; Klaus Mohr; Ulrike Holzgrabe 📂 Article 📅 2003 🏛 John Wiley and Sons 🌐 English ⚖ 133 KB

## Abstract Allosteric modulators are able to enhance or decrease the equilibrium binding of orthosteric agonists or antagonists. The treatment of Alzheimer's disease and the organophosphorus poisoning can take advantage of the enhancement of the ligand binding. Prerequisite is the formation of ter

The two neutrophil members of the formyl

The two neutrophil members of the formylpeptide receptor family activate the NADPH-oxidase through signals that differ in sensitivity to a gelsolin derived phosphoinositide-binding peptide

✍ Huamei Fu; Lena Björkman; Paul Janmey; Anna Karlsson; Jennie Karlsson; Charlotta 📂 Article 📅 2004 🏛 BioMed Central 🌐 English ⚖ 311 KB

## Background The formylpeptide receptor family members FPR and FPRL1, expressed in myeloid phagocytes, belong to the G-protein coupled seven transmembrane receptor family (GPCRs). They share a high degree of sequence similarity, particularly in the cytoplasmic domains involved in intracellular sig