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Molecular Microbiology|August 1, 1993
Role of the lipB gene product in the folding of the secreted lipase of Pseudomonas glumaeL G Frenken, A de Groot, J Tommassen, et al.
Protein Engineering|August 1, 1993
Pseudomonas glumae lipase: increased proteolytic stability by protein engineeringL G Frenken, M R Egmond, A M Batenburg, et al.
Protein Engineering|April 1, 1994
Analysis of the structure of Pseudomonas glumae lipaseM E Noble, A Cleasby, L N Johnson, et al.
FEBS Letters|September 27, 1993
The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartateM E Noble, A Cleasby, L N Johnson, et al.
Biochemistry|February 24, 2000
Camelid heavy-chain variable domains provide efficient combining sites to haptensS Spinelli, L G Frenken, P Hermans, et al.
Molecular Microbiology|August 1, 1993
An accessory gene, lipB, required for the production of active Pseudomonas glumae lipaseL G Frenken, J W Bos, C Visser, et al.
Antimicrobial Agents and Chemotherapy|August 26, 2004
Bactericidal effects of a fusion protein of llama heavy-chain antibodies coupled to glucose oxidase on oral bacteriaA Szynol, J J de Soet, E Sieben-van Tuyl, et al.
Applied and Environmental Microbiology|December 1, 1992
Cloning of the Pseudomonas glumae lipase gene and determination of the active site residuesL G Frenken, M R Egmond, A M Batenburg, et al.
Molecular Immunology|February 13, 2001
Llama heavy-chain V regions consist of at least four distinct subfamilies revealing novel sequence featuresM M Harmsen, R C Ruuls, I J Nijman, et al.
Biochemistry|January 5, 2001
Thermal unfolding of a llama antibody fragment: a two-state reversible processJ M Pérez, J G Renisio, J J Prompers, et al.
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