The 35,000 or so genes within a human cell are something like players on a sports team: If their activity isnt controlled and coordinated, the result can be disastrous.
So just as coaches tell individual players when to scramble onto the field and when to stay on the bench, molecules called transcription factors prompt particular genes to be active or stay quiet. Transcription factors occur naturally in cells, but researchers have been working to develop artificial transcription factors (ATFs) that can be tailored to regulate particular genes or sets of genes. These molecules can help scientists probe transcription, the first step in the process through which instructions coded in genes are used to produce proteins. And because errors in transcription are linked to diseases ranging from diabetes to cancer, ATFs eventually might also be used to correct those mistakes.
Using a new approach to developing ATFs, University of Michigan assistant professor of chemistry Anna Mapp and coworkers have gained important insights into the workings of gene-activating transcription factors. They recently discovered that the gene-activating power of a transcription factor likely depends on where the factor binds to the cells transcriptional machinery, as well as on how tightly it binds. Previously, researchers had thought that binding affinity (tightness) was the main determinant of a gene activators potency. Mapp presented the groups results at the annual meeting of the American Chemical Society in New York today (Sept. 8).
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Researchers from the University of Hamburg in Germany, in collaboration with colleagues from the University of Aarhus in Denmark, have synthesized a new superconducting material by growing a few layers of an antiferromagnetic transition-metal chalcogenide on a bismuth-based topological insulator, both being non-superconducting materials.
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At TU Wien, an alternative for resource intensive formwork for the construction of concrete domes was developed. It is now used in a test dome for the Austrian Federal Railways Infrastructure (ÖBB Infrastruktur).
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Many pathogens use certain sugar compounds from their host to help conceal themselves against the immune system. Scientists at the University of Bonn have now, in cooperation with researchers at the University of York in the United Kingdom, analyzed the dynamics of a bacterial molecule that is involved in this process. They demonstrate that the protein grabs onto the sugar molecule with a Pac Man-like chewing motion and holds it until it can be used. Their results could help design therapeutics that could make the protein poorer at grabbing and holding and hence compromise the pathogen in the host. The study has now been published in “Biophysical Journal”.
The cells of the mouth, nose and intestinal mucosa produce large quantities of a chemical called sialic acid. Many bacteria possess a special transport system...
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