- Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases
- Ornithine carbamoyltransferase from Pyrococcus furiosus.
- Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the 'penicillin-recognizing enzyme' family.
- A new variant of the Ntn hydrolase fold revealed by the crystal structure of L-aminopeptidase D-Ala-esterase/amidase from Ochrobactrum anthropi.
- Serine 948 and threonine 1042 are crucial residues for allosteric regulation of Escherichia coli carbamoylphosphate synthetase and illustrate coupling effects of activation and inhibition pathways.
- Crystallization and preliminary X-ray analysis of a new L-aminopeptidase-D-amidase/D-esterase activated by a Gly-Ser peptide bond hydrolysis.
The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures.
1998) PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 95(6). p.2801-2806 Mark(
- Structural and phylogenetic relationships among plant and animal cystatins.
- Aspartate carbamoyltransferase from two psychrophilic Vibrio strains: genetic organization and structural modelization.
- Preliminary crystal structure determination of the alkaline protease from the Antarctic psychrophile Pseudomonas aeruginosa.