The restoration and erection of the world's first elevated obelisk.

Obelisks presented an important element in the architecture of ancient Egypt. This research is concerned with the re-erection of an obelisk that belongs to the famous Pharoah Ramses II. It was found broken and was transported to the Grand Egyptian Museum for restoration and display. An observation of Ramses II Cartouche at the bottom side of the obelisk base inspired the authorities to provide an innovative architectural design to display the obelisk elevated. The supporting structure was designed to allow the visitors to walk underneath the obelisk and observe Ramses II's signature. The idea of elevating the obelisk presented several challenges including evaluating the obelisk's current condition, restoration and fixation methodology, structural stability, and uncertainties of material characteristics, amongst others. To control the obelisk deformations under lateral loading, state-of-the-art base isolators were introduced. For the task to be achieved, a multidisciplinary team including historians, conservators, archaeologists, architects, and engineers with different specialties was appointed. The team performed the task successfully and currently, the obelisk stands at the entrance piazza of the Grand Egyptian Museum representing the world's first elevated obelisk.

Close approximation of two platelet factor 4 tetramers by charge neutralization forms the antigens recognized by HIT antibodies.

OBJECTIVE: Heparin-induced thrombocytopenia (HIT) is a prothrombotic drug reaction caused by antibodies that recognize positively charged platelet factor 4 (PF4), bound to the polyanion, heparin. The resulting immune complexes activate platelets. Unfractionated heparin (UFH) causes HIT more frequently than low-molecular-weight heparin (LMWH), whereas the smallest heparin-like molecule (the pentasaccharide, fondaparinux), induces anti-PF4/heparin antibodies as frequently as LMWH, but without exhibiting cross-reactivity with these antibodies. To better understand these findings, we analyzed the molecular structure of the complexes formed between PF4 and UFH, LMWH, or fondaparinux. METHODS AND RESULTS: By atomic force microscopy and photon correlation spectroscopy, we show that with any of the 3 polyanions, but in the order, UFH>LMWH>>fondaparinux--PF4 forms clusters in which PF4 tetramers become closely apposed, and to which anti-PF4/heparin antibodies bind. By immunoassay, HIT antibodies bind strongly to PF4/H/PF4 complexes, but only weakly to single PF4/heparin molecules. CONCLUSIONS: HIT antigens are formed when charge neutralization by polyanion allows positively charged PF4 tetramers to undergo close approximation. Whereas such a model could explain why all 3 polyanions form antibodies with similar specificities, the striking differences in the relative size and amount of complexes formed likely correspond to the observed differences in immunogenicity (UFH>LMWH approximately fondaparinux) and clinically relevant cross-reactivity (UFH>LMWH>>fondaparinux).