Tijn T. van der Velden

This paper identifies a novel compound targeting Mycobacterium tuberculosis cytochrome bd through in vitro screening and structural analysis, showing growth inhibition and competitive inhibition at the quinol-binding site.

The paper presents cryo-EM structures of Escherichia coli cytochrome bd-I to elucidate its mechanism of quinol oxidation and inhibition, identifying key residues and structural changes involved in catalysis and drug binding.

This paper describes a method using a Vesicle Nucleating Peptide (VNp) to produce recombinant extracellular vesicles in E. coli that are distinct from natural OMVs, enabling efficient protein production and purification.

This study investigates the redox regulation of Mycobacterium tuberculosis cytochrome bd by its disulfide bond and quinone specificity, showing reduced activity upon disulfide reduction and substrate inhibition with menaquinol.

This paper presents a cryo-ET structure of CRP bound to C1 complex and PC ligands, revealing how CRP activates complement and identifies residues for therapeutic targeting.