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S.g.d. (stefan) Rüdiger


Chemistry - Biomolecular Sciences - Cellular Protein Chemist
Utrecht University
Netherlands

Biography

A key challenge in molecular medicine is to develop cures for diseases for which no cure exists – such as Alzheimer, Parkinson or ALS, but also many other diseases with dramatic impact for the affected individual such as ataxias or cystic fibrosis. These diseases have in common that the molecular cause is related to uncontrolled consequences of protein damage and aggregation. Our body is not unprotected against protein damage. The fidelity of protein shape in the cell is maintained by a powerful proteostasis network, in which molecular chaperones and proteases play a key role. This networks supresses the appearance of most folding related diseases for the best part of our life. However, why does it suddently fail when we get older? Why do some individuals get a protein-aggregation related disease and others do not? What is the impact of the proteostasis network for the development of an entire organism? Can we boost the cellular defense system to prevent the origin of the disease, or at least prevent progress of the diseases for some cases? My group aims to understand protein folding processes in the cell and their consequence for the origin of fatal diseases.

Research Interest

protein folding

Publications

  • 44 Sinnige T, Karagöz GE, Rüdiger SGD#. Protein Folding and Chaperones. Encyclopedia of Life Sciences (ELS). John Wiley & Sons, Ltd: Chichester (2015). (# = corresponding author)

  • 45 Hagemans D, van Belzen IAEM, Morán Luengo T, Rüdiger SGD#. A script to highlight hydrophobicity and charge on protein surfaces. Frontiers Mol Biosci 2015;2:56. (# = corresponding author)

  • 46 Anvarian Z, Nojima H, van Kappel EC, Madl T, Spit M, Viertler M, Jordens I, Low TY, van Scherpenzeel R, Kuper I, Richter K, Heck AJR, Boelens R, Vincent JP, Rüdiger SGD#, Maurice MM#. Axin cancer mutants form nano-aggregates to rewire the Wnt signaling network. Nature Struct Mol Biol. 2016;23:324-32. (# = corresponding author)

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