75 research outputs found
Intra-articular supplementation with recombinant human GDF5 arrests disease progression and stimulates cartilage regeneration in the rat medial meniscus transection (MMT) model of osteoarthritis
Acute effects of resistance exercise and intermittent intense aerobic exercise on blood cell count and oxidative stress in trained middle-aged women
Common variations in the pretest environment influence genotypic comparisons in models of anxiety
Intra-articular supplementation with recombinant human GDF5 arrests disease progression and stimulates cartilage regeneration in the rat medial meniscus transection (MMT) model of osteoarthritis
On Some Two- and Three-dimensional D-minimax Designs for Estimating Slopes of a Third-order Response Surface
A potent new mode of β-lactamase inhibition revealed by the 1.7 Å X-ray crystallographic structure of the TEM-1–BLIP complex
International audienceThe structure of TEM-1 beta-lactamase complex with the inhibitor BLIP has been determined at 1.7 angstrom resolution. The two tandemly repeated domains of BLIP form a polar, concave surface that docks onto a predominantly polar, convex protrusion on the enzyme. The ability of BLIP to adapt to a variety of class A beta-lactamases is most likely due to an observed flexibility between the two domains of the inhibitor and to an extensive layer of water molecules entrapped between the enzyme and inhibitor. A beta-hairpin loop from domain 1 of BLIP is inserted into the active site of the beta-lactamase. The carboxylate of Asp 49 forms hydrogen bonds to four conserved, catalytic residues in the beta-lactamase, thereby mimicking the position of the penicillin G carboxylate observed in the acyl-enzyme complex of TEM-1 with substrate. This beta-hairpin may serve as a template with which to create a new family of peptide-analogue beta-lactamase inhibitors
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