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Prolyl Oligopeptidase An Unusual β-Propeller Domain Regulates Proteolysis
TLDR
A resolution crystal structure of prolyl oligopeptidase, a large cytosolic enzyme that belongs to a new class of serine peptidases, is presented, which may facilitate drug design to treat memory disorders. Expand
Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis.
TLDR
The structure of prolyl oligopeptidase is obtained with a transition state inhibitor, which may facilitate drug design to treat memory disorders and protect larger peptides and proteins from proteolysis in the cytosol. Expand
Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes
PENICILLIN antibiotics are all produced from fermentation-derived penicillins because their chemical synthesis is not commercially viable. The key step in penicillin biosynthesis, in which both theExpand
Density of small diameter sensory nerve fibres in endometrium: a semi-invasive diagnostic test for minimal to mild endometriosis.
TLDR
The combined analysis of neural markers PGP9.5, VIP and SP could predict the presence of minimal-mild endometriosis with 95% sensitivity, 100% specificity and 97.5% accuracy. Expand
β Propellers: structural rigidity and functional diversity
Recently solved structures and proposed models have helped to reveal the structural characteristics of the beta-propeller fold, as well as the features that contribute to its high rigidity andExpand
Substrate Recognition Properties of Oligopeptidase B from Salmonella enterica Serovar Typhimurium
TLDR
The cloning and expression of the opdB homologue from Salmonella enterica serovar Typhimurium is reported and it is demonstrated that it exhibits amidolytic activity exclusively against substrates with basic residues in P(1), which supports the idea that the catalytic site of OpdB may be accessible only to unstructured oligopeptides, similar to the closely related prolyl oligopePTidase (POP). Expand
Structure-function properties of prolyl oligopeptidase family enzymes
TLDR
Crystal structures have been determined for representative members of three of the four subfamilies of Prolyl oligopeptidase and are facilitating a better understanding of the structure-function properties of these physiologically and pharmaceutically important enzymes. Expand
Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa.
TLDR
The structure suggests that, in the half-reduced functional form of the enzyme, the low-potential haem has to shed His71 in order to make the enzyme catalytically competent, and may introduce a new residues into the haem pocket. Expand
Desulfoferrodoxin structure determined by MAD phasing and refinement to 1.9-Å resolution reveals a unique combination of a tetrahedral FeS4 centre with a square pyramidal FeSN4 centre
Abstract The structure of desulfoferrodoxin (DFX), a protein containing two mononuclear non-heme iron centres, has been solved by the MAD method using phases determined at 2.8 Å resolution. The ironExpand
Beta propellers: structural rigidity and functional diversity.
Recently solved structures and proposed models have helped to reveal the structural characteristics of the beta-propeller fold, as well as the features that contribute to its high rigidity andExpand
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