Stephan A. Sieber

Natural product-derived azaphilones are selective scaffolds for covalent lysine liganding in live cells

This study identifies natural product-derived azaphilones as selective scaffolds for covalent lysine liganding in live cells, revealing bacterial chemotaxis as a major target pathway.

Mitochondrial protein import couples proteostasis failure to mitochondrial permeabilization

This study identifies mitochondrial protein import as a pathway linking proteostasis failure to mitochondrial permeabilization, showing that Raptinal impairs protein folding and VBIT4 inhibits this process.

The glucocorticoid dexamethasone influences motility of the sulfate-reducing bacterium Desulfovibrio desulfuricans by targeting the filament cap protein FliD

This paper shows dexamethasone affects Desulfovibrio desulfuricans motility by binding to FliD, a flagellar cap protein, without relying on metabolism.

Decoding antibiotic modes of action from multimodal cellular responses

This study develops MAPPER, a framework for predicting antibiotic modes of action using proteomics and chemical data, showing it can classify mechanisms and detect novel compounds.

Active Site-Directed Probes for targeting Bacterial Phosphoarginine Phosphatases

This paper introduces covalent activity-based probes to study phosphoarginine phosphatases, identifying new enzymes and expanding understanding of bacterial signal transduction.

Cystobactamid off-target profiling reveals favorable safety, superoxide reduction, and SCARB1 inhibition in eukaryotes

This study profiles cystobactamids' off-target effects in eukaryotes, showing safety, superoxide reduction, and SCARB1 inhibition with therapeutic potential.

Helicobacter pylori gamma-glutamyltransferase relates to proteomic adaptions important for gastric colonization

This study investigates the role of Helicobacter pylori gamma-glutamyltransferase (gGT) in gastric colonization and identifies compensatory mechanisms when gGT is absent.

Cryo-EM structure of the ClpXP protein degradation machinery

This paper presents the first high-resolution cryo-EM structure of ClpXP from Listeria monocytogenes, revealing the binding interface and activation mechanism of the complex.