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Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin
Site-specific N-glycan profiles of α<sub>5</sub> β<sub>1</sub> integrin from rat liver.
Biology of the cell 2022
read onlineStructure of a Tc holotoxin pore provides insights into the translocation mechanism
Lethal injections with unique injection mechanism,Giftspritzen mit einzigartigem Injektionsmechanismus
BioSpektrum 2019
read onlineCommon architecture of Tc toxins from human and insect pathogenic bacteria
Science Advances 2019
read onlineTc toxin complexes: Assembly, membrane permeation, and protein translocation
Annual Review of Microbiology 2019
read onlineSPHIRE-crYOLO is a fast and accurate fully automated particle picker for cryo-EM
Communications Biology 2019
read onlineTowards the application of Tc toxins as a universal protein translocation system
Nature Communications 2019
read onlineMembrane insertion of a Tc toxin in near-atomic detail
Nature Structural and Molecular Biology 2016
read onlineSoluble oligomers of the pore-forming toxin cytolysin a from Escherichia coli are off-pathway products of pore assembly
Journal of Biological Chemistry 2016
read onlineAcceleration of the Rate-Limiting Step of Thioredoxin Folding by Replacement of its Conserved cis-Proline with (4S)-Fluoroproline
ChemBioChem 2015
read onlineThe assembly dynamics of the cytolytic pore toxin ClyA
Nature Communications 2015
read onlineAcceleration of protein folding by four orders of magnitude through a single amino acid substitution
Scientific Reports 2015
read onlineThe Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) is part of the Forschungsverbund Berlin e.V. (FVB), which legally represents seven non-university research institutes - members of the Leibniz Association - in Berlin.
Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP)
Campus Berlin-Buch
Robert-Roessle-Str. 10,
13125 Berlin, Germany