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Incorporates a completely new architecture and programming language creating a robust high performance environment delivering rich visualization and analysis functionality.
TIMEPI takes advantage of a modern, portable, and platform agnostic approach, allowing it to run anywhere and on anything. By designing a C++ engine and optimizing it for low-level programming, it is able to provide millions of times the memory bandwidth over a simple assembly engine.
TIMEPI supports a set of I/O facilities allowing it to communicate with a wide range of complementary visualization software. Of particular importance is the integration of the OpenClonk project. This allows the visualization plugins, modelers, and analysis tools to communicate with TIMEPI using the same protocol, minimizing coding effort.
TIMEPI provides a powerful application framework for rapid application development, allowing users to create applications in a highly intuitive way.
Since it is written in C++, it is platform independent and can be run on any operating system, without requiring the use of emulation software.
Pricing and Availability
TIMEPI is now available in source code form and will be released as a free, open source project.
For more information on the TIMEPI application framework, including an overview of the architecture and source code, please refer to the available documentation.Importance of signalling from arginine:glycine amidinotransferase to NO production by nitric oxide synthase.
Biological synthesis of nitric oxide is critically dependent on the capacity of nitric oxide synthase (NOS) to use L-arginine as a substrate. L-Arginine:glycine amidinotransferase (AGT), a protein that catalyzes a rate-limiting step in L-arginine metabolism, transfers an amino group from L-arginine to glycine to form L-ornithine and L-glutamate. In the present study, we found that AGT is the most proximal enzyme in the L-arginine-to-NO metabolic pathway. The reaction with L-arginine by AGT does not require a cofactor or metal ion, but the product of the reaction, L-ornithine, is a substrate of NOS. In addition, we
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