21 research outputs found
Prise en charge des voies aériennes – 1re partie – Recommandations lorsque des difficultés sont constatées chez le patient inconscient/anesthésié
Get PDFComparison of low‐fresh gas flow technique to standard technique of sevoflurane induction in children—A randomized controlled trial
No full textThe addition of tramadol to morphine via patient‐controlled analgesia does not lead to better post‐operative pain relief after total knee arthroplasty
No full textStatistic analysis of 6891 cancer-paining patients’ information from Gansu Province Tumour Hospital, China
No full textCorrection: Small Molecule Inhibitors of the LEDGF Site of Human Immunodeficiency Virus Integrase Identified by Fragment Screening and Structure Based Design.
No full textCorrection: Small Molecule Inhibitors of the LEDGF Site of Human Immunodeficiency Virus Integrase Identified by Fragment Screening and Structure Based Design
No full textCorrection: Small Molecule Inhibitors of the LEDGF Site of Human Immunodeficiency Virus Integrase Identified by Fragment Screening and Structure Based Design
No full textSmall Molecule Inhibitors of the LEDGF Site of Human Immunodeficiency Virus Integrase Identified by Fragment Screening and Structure Based Design
Get PDF<div><p>A fragment-based screen against human immunodeficiency virus type 1 (HIV) integrase led to a number of compounds that bound to the lens epithelium derived growth factor (LEDGF) binding site of the integrase catalytic core domain. We determined the crystallographic structures of complexes of the HIV integrase catalytic core domain for 10 of these compounds and quantitated the binding by surface plasmon resonance. We demonstrate that the compounds inhibit the interaction of LEDGF with HIV integrase in a proximity AlphaScreen assay, an assay for the LEDGF enhancement of HIV integrase strand transfer and in a cell based assay. The compounds identified represent a potential framework for the development of a new series of HIV integrase inhibitors that do not bind to the catalytic site of the enzyme.</p> </div
Chemical compounds explored to determine structure activity relationship with IN.
No full text<p>Chemical compounds explored to determine structure activity relationship with IN.</p
SPR sensorgrams showing three compounds binding to immobilized HIV integrase core3H (left panels) and core4H (right panels).
No full text<p>(A) Compounds <b>11</b> and (B) <b>10</b> were injected as a ten-cycle, two-fold dilution series with a top concentration of 256 µM; compound <b>2</b> (C) was injected as a six-cycle, two-fold dilution series with a top concentration of 512 µM. Duplicate overlaid binding data are shown. Inset diagrams (top right in each panel) show the fit of the binding responses at equilibrium (t = 25–28, plotted against compound concentration) to a simple binding isotherm. Affinity estimates (K<sub>D</sub> values) for these binding interactions are listed in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0040147#pone-0040147-t001" target="_blank">Table 1</a>. For compounds that failed to reach maximal binding response (R<sub>max</sub>) for top injected concentration (256 or 512 µM), K<sub>D</sub> values were estimated using R<sub>max</sub> values determined from binding fits obtained for <b>10</b>.</p
