3 research outputs found
Bacterial invasion of Caco-2 epithelial cells was determined by gentamicin protection assay at 0 (T0) and 3 (T3) h
Results are presented as the percentage of the inoculum intracellular (% Invasion). Data are means Ā± standard errors of two independent experiments performed in triplicate. K12 and . Enteritidis were used as negative and positive controls, respectively.<p><b>Copyright information:</b></p><p>Taken from "Virulence studies of isolates associated with a neonatal intensive care unit outbreak"</p><p>http://www.biomedcentral.com/1471-2180/8/64</p><p>BMC Microbiology 2008;8():64-64.</p><p>Published online 18 Apr 2008</p><p>PMCID:PMC2386127.</p><p></p
Identification of Novel Adenosine A<sub>2A</sub> Receptor Antagonists by Virtual Screening
Virtual screening was performed against experimentally
enabled
homology models of the adenosine A<sub>2A</sub> receptor, identifying
a diverse range of ligand efficient antagonists (hit rate 9%). By
use of ligand docking and Biophysical Mapping (BPM), hits <b>1</b> and <b>5</b> were optimized to potent and selective lead molecules
(<b>11</b>ā<b>13</b> from <b>5</b>, p<i>K</i><sub>I</sub> = 7.5ā8.5, 13- to >100-fold selective
versus adenosine A<sub>1</sub>; <b>14</b>ā<b>16</b> from <b>1</b>, p<i>K</i><sub>I</sub> = 7.9ā9.0,
19- to 59-fold selective)
Discovery of 1,2,4-Triazine Derivatives as Adenosine A<sub>2A</sub> Antagonists using Structure Based Drug Design
Potent, ligand efficient, selective, and orally efficacious
1,2,4-triazine
derivatives have been identified using structure based drug design
approaches as antagonists of the adenosine A<sub>2A</sub> receptor.
The X-ray crystal structures of compounds <b>4e</b> and <b>4g</b> bound to the GPCR illustrate that the molecules bind deeply
inside the orthosteric binding cavity. In vivo pharmacokinetic and
efficacy data for compound <b>4k</b> are presented, demonstrating
the potential of this series of compounds for the treatment of Parkinsonās
disease