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The first three-dimensional structures of the IgE antibody triggering allergic reactions. To the left is shown the experimental data obtained with electron microscopy that were combined to yield the three dimensional structure of IgE itself. To the right is depicted the experimental data and the resulting three dimensional structure for IgE bound to a fragment of the drug candidate Ligelizumab. Figure: Rasmus Kjeldsen Jensen, AU

2020.02.24 | Research

Electron microscopy allows scientists to understand the molecular trigger of allergic reactions

An international research team has been able to describe the overall structure of the antibody type IgE, which is the key molecule in allergic diseases. This is a scientific breakthrough which provides important insights into basic mechanisms of allergic reactions and may pave the way for more effective allergy medicine. The new research results…

Nuclear transcripts without poly(A)-tagged 3’ends (‘pA-‘) are normally targeted to the RNA exosome via the cofactor NEXT (left), whereas transcripts with a poly(A) tail (‘pA+’) are targeted via PAXT (right). If NEXT-dependent decay fails, target RNAs acquire a poly(A)-tail and are handed to the exosome by PAXT. Such two-layered targeting ensures the robust decay of potentially hazardous RNAs. Figure: Guifen Wu and Manfred Schmid.

2020.02.19 | Research

How to keep the nucleus clean

RNA turnover in the nuclei of eukaryotic cells is controlled by the RNA exosome aided by numerous cofactors. Researchers at Aarhus University and Copenhagen University now show how two major nuclear exosome cofactors recognize their RNA targets to keep a clean nuclear environment. This is important for the health of our cells – and thus humans.

Results published by AU researchers reveal that surfactant-mediated unfolding and refolding of proteins are complex processes with several structures present, and rearrangements occur on time scales from sub-milliseconds to minutes. (Image: Reproduced with permission from the Royal Society of Chemistry).

2020.02.17 | Research

Caught soap-handed: Understanding how soap molecules help proteins get in and out of shape

Controlling protein structure is crucial in the production of detergents and cosmetics. Up to now we have not had a clear understanding of how soap molecules and proteins work together to change protein structure. Now AU researchers have succeeded in creating a detailed picture of both unfolding and refolding of a protein by soap molecules on the…