Prof. Michael Sattler
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NMR and integrative structural biology and structure-based drug discovery
We study the structure, interactions and dynamics of biological macromolecules in solution using Nuclear Magnetic Resonance (NMR) spectroscopy and integrative structural biology.
Molecular mechanisms and regulation of proteins and RNAs in RNA-based gene regulation (alternative splicing and non-coding RNA pathways), and cellular signaling (molecular chaperones, peroxisome biogenesis), are unraveled by combining NMR with X-ray crystallography, small angle scattering (SAXS/SANS), cryo-EM and biophysical techniques.
Structure based drug discovery is used for the development of small molecule-based therapeutics.
Links:
Bayerisches NMR Zentrum (BNMRZ)
Homepage Prof. Sattler
Publikationen werden geladen...
Proceedings of the National Academy of Sciences of the United States of America
Abstract: PEX19 is a cytosolic receptor that directs membrane proteins posttranslationally to peroxisomes, as well as to mitochondria, lipid droplets, and the endoplasmic reticulum. A comprehensive Trypanosoma…
Cell
Abstract: Ferroptosis, driven by uncontrolled peroxidation of membrane phospholipids, is distinct from other cell death modalities because it lacks an initiating signal and is surveilled by endogenous…
International Journal of Molecular Sciences
Abstract: Modulation of protein–protein interactions (PPIs) by small molecules is a vital strategy in drug discovery. Nevertheless, due to the inherent nature of PPI interfaces, practical implementation of this…
Molecular Cell
Abstract: The Hsp90 molecular chaperone system is regulated by numerous co-chaperones that modulate its function. In Saccharomyces cerevisiae , most of these cofactors can be deleted without affecting…
Structure
Abstract: Incorporating metal cofactors into computationally designed protein scaffolds provides a versatile route to novel protein functions, including the potential for new-to-nature enzyme catalysis.…
Journal of the American Chemical Society
Abstract: Phosphorylation is among the most ubiquitous and essential posttranslational modifications in biological systems. It is regulated by highly complex enzymatic networks. Here, we explore enzyme-free…
Journal of the American Chemical Society
Abstract: The molecular chaperone Hsp90 is an abundant and essential homodimer that supports the stability and folding of hundreds of client proteins in cells. Its C-terminal domain (CTD) mediates dimerization…
Nucleic Acids Research
Abstract: Adenosine-to-inosine (A-to-I) editing is a highly abundant modification of double-stranded RNA (dsRNA) and plays an important role in posttranscriptional gene regulation. Editing of multiple inosines…
Cell
Abstract: Recognition of exogenous RNA by Toll-like receptors (TLRs) is central to pathogen defense. Using two distinct binding pockets, TLR7 and TLR8 recognize RNA degradation products generated by…
European Journal of Medicinal Chemistry
Abstract: Targeting protein-protein interactions (PPIs) is a promising strategy in drug development. However, despite the considerable progress in the field, targeting PPIs with small molecules remains…