ParamMacros demo video

http://deepblue.lib.umich.edu/bitstream/2027.42/191952/1/ParamMacros Creating UI Automation Leveraging End-User Natural Language Parameterization.mp4Description of ParamMacros Creating UI Automation Leveraging End-User Natural Language Parameterization.mp4 : demo videoSEL

Web automation IDE demo video

http://deepblue.lib.umich.edu/bitstream/2027.42/191953/1/Providing Feedback and UI Context to Programmers Writing Web Automation Scripts.mp4Description of Providing Feedback and UI Context to Programmers Writing Web Automation Scripts.mp4 : demo videoSEL

ScrapeViz demo video

http://deepblue.lib.umich.edu/bitstream/2027.42/191951/1/scrapeviz_video1299287933.mp4Description of scrapeviz_video1299287933.mp4 : demo videoSEL

Synergistic effect of aptamers that inhibit exosites 1 and 2 on thrombin

Thrombin is a multifunctional protease that plays a key role in hemostasis, thrombosis, and inflammation. Most thrombin inhibitors currently used as antithrombotic agents target thrombin's active site and inhibit all of its myriad of activities. Exosites 1 and 2 are distinct regions on the surface of thrombin that provide specificity to its proteolytic activity by mediating binding to substrates, receptors, and cofactors. Exosite 1 mediates binding and cleavage of fibrinogen, proteolytically activated receptors, and some coagulation factors, while exosite 2 mediates binding to heparin and to platelet receptor GPIb-IX-V. The crystal structures of two nucleic acid ligands bound to thrombin have been solved. Previously Padmanabhan and colleagues solved the structure of a DNA aptamer bound to exosite 1 and we reported the structure of an RNA aptamer bound to exosite 2 on thrombin. Based upon these structural studies we speculated that the two aptamers would not compete for binding to thrombin. We observe that simultaneously blocking both exosites with the aptamers leads to synergistic inhibition of thrombin-dependent platelet activation and procoagulant activity. This combination of exosite 1 and exosite 2 inhibitors may provide a particularly effective antithrombotic approach