Department News

Prions induce toxic Huntingtin oligomers

A research team at the MPIB was able to identify the toxic form of the Huntingtin protein, which plays a crucial role in Huntington's disease, in a yeast model system. more

Elena Conti and F. Ulrich Hartl

Elena Conti and F. Ulrich Hartl, directors at the Max Planck Institute of Biochemistry in Martinsried each receive an ERC grant worth 2.1 million euros.
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F. Ulrich Hartl is honored with HFSP Nakasone Award

F. Ulrich Hartl, Director at the Max Planck Institute of Biochemistry, together with his colleague Arthur L. Horwich, receives the HFSP Nakasone Prize 2022.
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Max Planck scientist receives Bavarian Maximilian Order

F. Ulrich Hartl, Director at the Max Planck Institute of Biochemistry in Martinsried was awarded the Bavarian Maximilian Order for Science and Art.
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<p style="text-align: left;" align="center">Novel mechanism for maintenance of bacterial proteostasis identified</p>

Researchers at the Max Planck Institute of Biochemistry (MPIB) have identified a novel mechanism that ensures proteostasis maintenance in E. coli when chaperone availability is limited. more

Repairing the photosynthetic enzyme Rubisco

Researchers at the Max Planck Institute of Biochemistry decipher the molecular mechanism of Rubisco activase in a recent study more

ASAP Grant for 3 MPIB Directors

Brenda Schulman, Ulrich Hartl and Wolfgang Baumeister receive a research grant to study Mechanisms of Parkinsons’s disease more

The special chaperonin of the bacteriophage EL

Researchers for protein folding helpers at the Max Planck Institute of Biochemistry have now deciphered the molecular structure of the EL phage chaperonin and discovered special features. more

F.-Ulrich Hartl receives Breakthrough Prize 2020

The biochemist Hartl and the geneticist Horwich are honored with the world’s highest science prize for their groundbreaking discovery of the protein folding, assistans, chaperones. more

The nucleolus – a known organelle with new tasks

The nucleolus is a well-known cellular structure that is easily visible under a light microscope. This nuclear structure is known as the site of ribosome production. In a recent study, researchers at the Max Planck Institute of Biochemistry in Martinsried, Germany, have shown that the nucleolus is also a site of quality control for proteins. When cells are stressed, proteins tend to misfold and to aggregate. To prevent proteins from clumping, some are temporarily stored in the nucleolus. The special biophysical conditions found in this organelle prevent harmful protein aggregation. The results of this study have now been published in the journal Science. more

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