Koehnke, Jesko
Jesko Koehnke researcher
VIAF ID: 34154257807524150886 (Personal)
Permalink: http://viaf.org/viaf/34154257807524150886
Preferred Forms
- 100 0 _ ‡a Jesko Koehnke ‡c researcher
- 100 1 _ ‡a Koehnke, Jesko
- 100 1 _ ‡a Koehnke, Jesko
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- 100 1 _ ‡a Koehnke, Jesko
4xx's: Alternate Name Forms (3)
Works
Title | Sources |
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Adaptation of a Bacterial Multidrug Resistance System Revealed by the Structure and Function of AlbA | |
Binding Mode Characterization and Early in Vivo Evaluation of Fragment-Like Thiols as Inhibitors of the Virulence Factor LasB from Pseudomonas aeruginosa. | |
The bottromycin epimerase BotH defines a group of atypical α/β-hydrolase-fold enzymes | |
Characterization of the Stereoselective P450 Enzyme BotCYP Enables the In Vitro Biosynthesis of the Bottromycin Core Scaffold | |
Cyclic peptides : from bioorganic synthesis to applications | |
Macroamidine Formation in Bottromycins Is Catalyzed by a Divergent YcaO Enzyme. | |
The natural product carolacton inhibits folate-dependent C1 metabolism by targeting FolD/MTHFD. | |
New developments in RiPP discovery, enzymology and engineering | |
Photorhabdus luminescens lectin A (PllA): A new probe for detecting α-galactoside-terminating glycoconjugates | |
The role of protein-protein interactions in the biosynthesis of ribosomally synthesized and post-translationally modified peptides | |
Structure-Activity Relationship and Mode-Of-Action Studies Highlight 1-(4-Biphenylylmethyl)-1H-imidazole-Derived Small Molecules as Potent CYP121 Inhibitors | |
Structure and Substrate Recognition of the Bottromycin Maturation Enzyme BotP | |
The structure of CgnJ, a domain of unknown function protein from the crocagin gene cluster | |
Tackling Pseudomonas aeruginosa Virulence by a Hydroxamic Acid-Based LasB Inhibitor | |
Thiazoline-Specific Amidohydrolase PurAH Is the Gatekeeper of Bottromycin Biosynthesis | |
Thioholgamides: Thioamide-Containing Cytotoxic RiPP Natural Products | |
Tutuilamides A-C: Vinyl-Chloride-Containing Cyclodepsipeptides from Marine Cyanobacteria with Potent Elastase Inhibitory Properties |