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    Rudolf Virchow Center for Integrative and Translational Bioimaging

    RVZ News

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    Protein interactions can now be analysed more effectively: A phenomenon called Temperature Related Intensity Change (TRIC) makes it possible to achieve high binding signal intensity even with lowest amounts of sample. Our Maric research group established the method, which can be used to study protein complexes in highly regulated networks such as DNA transcription.

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    We are inviting applications for a Group Leader (f/m/d) in Chemical Biology. The RVZ appoints group leaders early in their career and provides them with a supportive, collaborative environment and generous work package for their independent position. Significant core funding and limited teaching responsibilities will allow you to embark on a visionary research program.

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    Artemisinins are pharmaceutical compounds used against the pathogen that causes malaria. However, these substances also have multiple targets in humans which may either be pharmacologically exploited or result in undesirable side effects. Recently, scientists from Würzburg have been able to elucidate one of the underlying molecular mechanisms by showing how these drugs inhibit the vitamin B6 generating enzyme in humans. The results were published in the scientific journal PNAS.

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    For the first time ever, expansion microscopy allows the imaging of even the finest details of cell membranes. This offers new insights into bacterial and viral infection processes.

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    The protein complex TFIIH is responsible for essential cellular functions such as transcription or DNA repair. These processes must be carried out with extreme precision in order to prevent serious diseases, such as cancer. The enzyme XPB is part of the TFIIH complex and is indispensable for both processes. How XPB is simultaneously activated and repressed by its interaction partners p8/p52 within the TFIIH complex has now been demonstrated by a Würzburg research group. The results improve the functional understanding of this intricate complex and were published in the journal Nucleic Acids Research.

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    New complex for damage detection in DNA identified.

     

    Our body can repair damage to our DNA that can lead to the development of cancer by means of repair complexes. But how does the repair machinery recognize the damage? Scientists from the University of Würzburg and the University of Kent have now identified a complex that plays an important role in damage recognition in nucleotide excision repair. Due to its key position, the complex represents a starting point for research on cancer drugs. The results were published in the renowned journal Nucleic Acids Research.

     

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    In stress situations, bacteria use special ion channels for defense. Understanding how they function provides the basis for combating harmful bacteria. A Würzburg research group in cooperation with ETH Zurich and the University of Oxford has now been able to decipher how two of these channels are structured and how they open up. The results were published in the renowned journal PNAS.

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    Collaborative work of research groups at the University of Würzburg and the TU Dresden has provided important new insights for cancer research. During cell division specific target proteins have to be turned over in a precisely regulated manner. To this end specialized enzymes label the target proteins with signaling molecules. However, the enzymes involved in this process can also label themselves, thus initiating their own degradation. In a multidisciplinary approach, the researchers identified a mechanism of how enzymes can protect themselves from such self-destruction and maintain sufficient concentrations in the cell. These results have been published in the latest issue of Science Signaling.

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    A research group from Würzburg has now been able to clarify the long-standing question of how the protein complex CDK-activating kinase (CAK), which controls the central processes of cell division and transcription, is activated. The group analyzed the active form of the protein/CAK complex and was able to decipher its function on a molecular level. These new findings provide the basis for further research on cancer drugs and were published in the renowned scientific journal PNAS.

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    Scientists from the University of Würzburg and the University of Strasbourg identified a new important molecular region in an essential human DNA repair complex, consisting of the proteins XPD and MAT1. This complex forms a central unit in the nucleotide excision DNA repair mechanism (NER) and thus protects our genetic information. The findings were published in the journal Nature Communications and could provide new starting points for cancer therapy.

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    On 23th March 2020, Professor Katrin Heinze officially started her new “Chair of Molecular Microscopy" at the Medical Faculty of the Julius Maximilians University (JMU) Würzburg, Germany. The physicist will boost the development of precise microscopy methods for biomedical imaging and spectroscopy.

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    Picture of the structure of the cytochrome bd oxidase.

    Scientists from the University of Würzburg and the University of Freiburg succeeded in determining the complex molecular structure of the bacterial enzyme cytochrome bd oxidase. Since humans do not have this type of oxidase, this enzyme could be an interesting target for novel antibiotics.

     

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    A team of researchers lead by Helmholtz Zentrum München and the University of Würzburg identified an enzyme as a novel and strong inhibitor of ferroptosis, the iron dependent form of cell death: ferroptosis suppressor protein-1, short FSP1. This protein is expressed in a variety of cancer cell lines and therefore represents an attractive drug target for cancer treatment. The results were published in the journal Nature.

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    [Translate to Englisch:] Bild von Dr. Grzegorz Sumara

    For the foundation of the first two Dioscuri centers our RVZ group leader Dr. Grzegorz Sumara will return to Poland. The Grzegorz Sumara centre will focus on elucidating signalling pathways involved in metabolic diseases.

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