A research group of the Tübingen University Hospital studied a small, body-derived molecule called di-methyl fumarate (DMF), hat is the first molecule improving both diseases psoriasis and multiple sclerosis. They found that this body-derived molecule strongly influences natures most potent ‘immune stimulators’, the dendritic cells that have recently been awarded by the Nobel Prize to Ralph Steinman.
Normally, dendritic cells should recognize danger caused by bacteria or viruses, alarm the immune system and raise protective responses. Unfortunately, when fooled, dendritic cells induce by error immunity against the body’s own cells and start to destroy them.The Tübingen team has now shown, that small molecules like DMF re-educate the dendritic cells and turn them into a cell that protects from tissue destruction, the so-called ‚type 2 dendritic cells’. Using complex series of experiments, they uncover the mechanisms underly-ing this ‘re-education of the dendritic cells’. This establishes general rules for the develop-ment of new, most likely safe drugs that will significantly improve the life of patients with se-vere autoimmune diseases, namely psoriasis or multiple sclerosis.
The University of Tübingen holds a patent on this principle.Published in the Journal of Experimental Medicine 2011, October online
Dr. Ellen Katz | idw
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Researchers from the Department of Atomically Resolved Dynamics of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg, the University of Hamburg and the European Molecular Biology Laboratory (EMBL) outstation in the city have developed a new method to watch biomolecules at work. This method dramatically simplifies starting enzymatic reactions by mixing a cocktail of small amounts of liquids with protein crystals. Determination of the protein structures at different times after mixing can be assembled into a time-lapse sequence that shows the molecular foundations of biology.
The functions of biomolecules are determined by their motions and structural changes. Yet it is a formidable challenge to understand these dynamic motions.
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Researchers from the Department of Atomically Resolved Dynamics of the Max Planck Institute for the Structure and Dynamics of Matter (MPSD) at the Center for Free-Electron Laser Science in Hamburg, the University of Potsdam (both in Germany) and the University of Toronto (Canada) have pieced together a detailed time-lapse movie revealing all the major steps during the catalytic cycle of an enzyme. Surprisingly, the communication between the protein units is accomplished via a water-network akin to a string telephone. This communication is aligned with a ‘breathing’ motion, that is the expansion and contraction of the protein.
This time-lapse sequence of structures reveals dynamic motions as a fundamental element in the molecular foundations of biology.
Two research teams have succeeded simultaneously in measuring the long-sought Thorium nuclear transition, which enables extremely precise nuclear clocks. TU Wien (Vienna) is part of both teams.
If you want to build the most accurate clock in the world, you need something that "ticks" very fast and extremely precise. In an atomic clock, electrons are...
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