个人简介
Rudolf Glockshuber has been Full Professor of Molecular Biology at the Institute of Molecular Biology and Biophysics at the ETH Zurich since January 2000. From April 1994 to March 1997 he was tenure track Assistant Professor and from April 1997 to December 1999 Associate Professor at the same institute.
Prof. Glockshuber was born on September 18, 1959 in Munich, Germany. He studied chemistry at the Ludwig-Maximilian University in Munich and received his doctorate in 1989 under Professor E.L. Winnacker and Dr. A. Plückthun at the Gene Center of the University of Munich with a dissertation on recombinant antibody fragments. From January 1990 to March 1994 he received a research grant from the German Research Society to work as a scientific assistant at the Institute for Biophysics and Physical Biochemistry at the University of Regensburg under Professor R. Jaenicke.
His work focused on the catalysis of protein folding, enzyme/inhibitor interactions, energy-dependent proteases and proteins from the eye lens.
His present research at the ETH Zurich concentrates on:
a) Structural and functional characterization of enzymes catalyzing disulfide bond formation during protein folding.
b) the assembly of macromolecular protein complexes, using bacterial type 1 pili as a model system. Type 1 pili are highly oligomeric protein complexes at the bacterial surface that enable pathogenic bacteria to bind to host cells.
c) the thermodynamics and kinetics of protein folding.
d) the mechanism of amyloid formation.
Prof. Glockshuber is adjunct professor at the A.N. Belozersky Institute of Moscow State University and member of EMBO and the German Academy of Natural Scientists Leopoldina.
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Helix swapping leads to dimerization of the N-terminal domain of the c-type cytochrome maturation protein CcmH from Escherichia coli
Ahuja, Umesh, Rozhkova, Anna, Glockshuber, Rudolf, Thoeny-Meyer, Linda and Einsle, Oliver (2008)
In the process of cytochrome c maturation, heme groups are covalently attached to reduced cysteines of specific heme-binding motifs (CXXCH) in an apocytochrome c sequence. In Escherichia coli, the CcmH protein maintains apo-protein cysteines in a reduced state prior to heme...
The Outer Membrane Usher Guarantees the Formation of Functional Pili by Selectively Catalyzing Donor-Strand Exchange between Subunits That Are Adjacent in the Mature Pilus
Nishiyama, Mireille and Glockshuber, Rudolf (2010)
Type 1 pili from uropathogenic Escherichia coli are a prototype of adhesive surface organelles assembled and secreted by the conserved chaperone/usher pathway. They are composed of four different homologous protein subunits that need to be assembled in a defined order. In the...
Direct Evidence for Self-Propagation Different Amyloid-β Fibril Conformations
Spirig, Thomas, Ovchinnikova, Oxana, Vagt, Toni and Glockshuber, Rudolf (2014)
Background: Amyloid fibrils formed by amyloid-β (Aβ) peptides are associated with Alzheimer's disease and can occur in a range of distinct morphologies that are not uniquely determined by the Aβ sequence. Whether distinct conformations of Aβ fibrils can be stably propagated...
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