Pharmacological characterization of H3 receptor antagonists with imidazole, thioimidazole and thioimidazoline polar groups in the side chain

2000 ◽  
Vol 49 (S1) ◽  
pp. 62-63 ◽  
Author(s):  
E. Barocelli ◽  
V. Ballabeni ◽  
M. Chiavarini ◽  
S. Bertoni ◽  
M. Mor ◽  
...  
Keyword(s):  
Side Chain ◽  
Receptor Antagonists ◽  
Pharmacological Characterization ◽  
Polar Groups ◽  
H3 Receptor

Detailed pharmacological characterization of GT-2331 for the rat histamine H3 receptor

2006 ◽  
Vol 529 (1-3) ◽  
pp. 40-46 ◽  
Author(s):  
Sayaka Ito ◽  
Ryo Yoshimoto ◽  
Yasuhisa Miyamoto ◽  
Yuko Mitobe ◽  
Takao Nakamura ◽  
...  
Keyword(s):  
Pharmacological Characterization ◽  
Histamine H3 Receptor ◽  
H3 Receptor ◽  
Histamine H3

Pharmacological characterization of human NPFF1 and NPFF2 receptors expressed in CHO cells by using NPY Y1 receptor antagonists

2002 ◽  
Vol 451 (3) ◽  
pp. 245-256 ◽  
Author(s):  
Catherine Mollereau ◽  
Honoré Mazarguil ◽  
Delphine Marcus ◽  
Isabelle Quelven ◽  
Masato Kotani ◽  
...  
Keyword(s):  
Cho Cells ◽  
Receptor Antagonists ◽  
Pharmacological Characterization ◽  
Y1 Receptor

A new convenient synthetic method and preliminary pharmacological characterization of triazinediones as prokineticin receptor antagonists

2014 ◽  
Vol 81 ◽  
pp. 334-340 ◽  
Author(s):  
Cenzo Congiu ◽  
Valentina Onnis ◽  
Alessandro Deplano ◽  
Severo Salvadori ◽  
Veronica Marconi ◽  
...  
Keyword(s):  
Synthetic Method ◽  
Receptor Antagonists ◽  
Pharmacological Characterization

scholarly journals Dynamic closed states of a ligand-gated ion channel captured by cryo-EM and simulations

2021 ◽  
Vol 4 (8) ◽  
pp. e202101011
Author(s):  
Urška Rovšnik ◽  
Yuxuan Zhuang ◽  
Björn O Forsberg ◽  
Marta Carroni ◽  
Linnea Yvonnesdotter ◽  
...  
Keyword(s):  
Ion Channel ◽  
Structural Data ◽  
Side Chain ◽  
Pharmacological Characterization ◽  
Receptor Proteins ◽  
Cryo Electron Microscopy ◽  
Electrochemical Signal ◽  
Ph Conditions ◽  
Dynamics Simulations

Ligand-gated ion channels are critical mediators of electrochemical signal transduction across evolution. Biophysical and pharmacological characterization of these receptor proteins relies on high-quality structures in multiple, subtly distinct functional states. However, structural data in this family remain limited, particularly for resting and intermediate states on the activation pathway. Here, we report cryo-electron microscopy (cryo-EM) structures of the proton-activated Gloeobacter violaceus ligand-gated ion channel (GLIC) under three pH conditions. Decreased pH was associated with improved resolution and side chain rearrangements at the subunit/domain interface, particularly involving functionally important residues in the β1–β2 and M2–M3 loops. Molecular dynamics simulations substantiated flexibility in the closed-channel extracellular domains relative to the transmembrane ones and supported electrostatic remodeling around E35 and E243 in proton-induced gating. Exploration of secondary cryo-EM classes further indicated a low-pH population with an expanded pore. These results allow us to define distinct protonation and activation steps in pH-stimulated conformational cycling in GLIC, including interfacial rearrangements largely conserved in the pentameric channel family.

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