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Structure and action of the binary C2 toxin from Clostridium botulinum.
C2 toxin from Clostridium botulinum is composed of the enzyme component C2-I, which ADP-ribosylates actin, and the binding and translocation component C2-II, responsible for the interaction withExpand
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High-resolution crystal structure of the snake venom metalloproteinase BaP1 complexed with a peptidomimetic: insight into inhibitor binding.
BaP1, a zinc-dependent endopeptidase belonging to the P-I class of snake venom metalloproteinases, exerts multiple tissue-damaging activities, leading to hemorrhage, myonecrosis, dermonecrosis,Expand
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Binding structure of elastase inhibitor scyptolin A.
Natural bioactive compounds are of general interest to pharmaceutical research because they may be used as leads in drug development campaigns. Among them, scyptolin A and B from Scytonema hofmanniExpand
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Engineering a function into a glycosyltransferase.
As glycosyltransferases found in nature often show distinct substrate specificity, glycosyltransferase engineering is an important research field. In this work, we were able to introduce an activityExpand
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Structure and Action of a CC Bond Cleaving α/β-Hydrolase Involved in Nicotine Degration
Abstract The enzyme 2,6-dihydroxy-pseudo-oxynicotine hydrolase from the nicotine-degradation pathway of Arthrobacter nicotinovorans was crystallized and the structure was determined by an X-rayExpand
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Binding structure of the leucine aminopeptidase inhibitor microginin FR1
Natural bioactive compounds are of general interest for pharmaceutical research because they may serve as leads in drug development campaigns. Among them, microginins are linear peptides known toExpand
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Structure and action of a C-C bond cleaving alpha/beta-hydrolase involved in nicotine degradation.
The enzyme 2,6-dihydroxy-pseudo-oxynicotine hydrolase from the nicotine-degradation pathway of Arthrobacter nicotinovorans was crystallized and the structure was determined by an X-ray diffractionExpand
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