Stefan Jentsch has been elected a Fellow of AAAS by the Council of the American Association for the Advancement of Science. Each year the Council elects members whose efforts on behalf of the advancement of science or its applications are scientifically or socially distinguished. Stefan Jentsch is honored “for truly distinguished contributions to cell biology, by demonstrating the multiple roles of ubiquitin in protein degradation, protein sequestration, and DNA maintenance and repair”. more

F.-Ulrich Hartl received the Prize for “Biochemical Analytic” of the DGKL

This year, the German Society for Clinical Chemistry and Laboratory Medicine (Deutsche Vereinte Gesellschaft für Klinische Chemie und Laboratoriumsmedizin, DGKL) has awarded F.-Ulrich Hartl, Director at the Max Planck Institute of Biochemistry in Martinsried near Munich, with their “Prize of  Biochemical Analytic” which is endowed with the highest amount of prize money awarded by this society. The scientist´s research field, the folding of proteins, also plays an important role in Parkinson´s or Alzheimer´s disease. The award comes with a prize money of 50,000 Euros and was given to the laureate during the 10th annual meeting of the association in Dresden on October 23, 2013. more

MPIB Research Group Leader is Member of the New Training Network PloidyNet

The Research Group Leader Zuzana Storchova at the Max Planck Institute of Biochemistry in Martinsried near Munich is member of the new training network PloidyNet, which has been started on October 14, 2013. Nine academic and three industrial partners throughout Europe will train young scientists in the field of aneuploidy. Aneuploidy is known as the state of cells which have acquired an unbalanced chromosome content after cell division and play an important role in cancer. All members of the network are considered as key laboratories in Europe. more

In a cell, a protein can mediate different functions. To achieve this, proteins can be tailored for specific tasks by modifications. Stefan Jentsch and his team at the Max Planck Institute of Biochemistry in Martinsried near Munich, Germany, are studying how proteins are modified in cells to achieve these different tasks. For his project, Stefan Jentsch has now been awarded an Advanced Grant of the European Research Council (ERC). He will use the 2.48 Million Euros to investigate how the protein marker SUMO modifies entire groups of proteins. The ERC Advanced Grants allow exceptional established research leaders to pursue ground-breaking, high-risk projects that open new directions in their respective research fields. more

A molecular delivery service

Tiny hair-like structures (cilia) are found on the surface of most cells. Cilia are responsible for the locomotion of cells (e.g. sperm cells), they process external signals and coordinate the correct arrangement of the inner organs during the development of an organism. For proper assembly and function of cilia, they need to be supplied with the appropriate building blocks. Scientists at the Max Planck Institute of Biochemistry (MPIB) in Martinsried near Munich, Germany, now identified the mechanism of how Tubulin, the main building block of cilia, is transported within the cilium. The result have now been published in the journal Science. more

<p align="center"><strong>Feeding RNAs to a molecular shredder - <strong>Max Planck scientists unravel the structure of a regulatory protein complex in RNA disposal </strong><br /></strong></p>

Much in the same way as we use shredders to destroy documents that are no longer useful or that contain potentially damaging information, cells use molecular machines to degrade unwanted or defective macromolecules. Scientists of the Max Planck Institute  of Biochemistry in Martinsried near Munich have now decoded the structure of a protein complex (Ski complex) which plays an essential role in the process of degrading ribonucleic acids (RNAs). The study has now been published in the journal Cell. more

Blockade in Cellular Waste Disposal - Max Planck Scientists Show How Protein Aggregates Disrupt the Molecular Balance of the Cell

Proteins can only perform their complex functions in the cell when they assume a specific three-dimensional structure for each respective task. Because misfolded proteins are often toxic, they are immediately refolded or degraded. Scientists of the Max Planck Institute (MPI) of Biochemistry in Martinsried near Munich have now shown in the yeast model that specific protein aggregates block an important degradation pathway for defective proteins – and thus disrupt the fragile molecular balance of the cell. The results of the study have now been published in the journal Cell. more

Go to Editor View