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Anne-Marie Lambeir
Researcher at University of Antwerp
Publications - 182
Citations - 8588
Anne-Marie Lambeir is an academic researcher from University of Antwerp. The author has contributed to research in topics: Dipeptidyl peptidase & Oligopeptidase. The author has an hindex of 48, co-authored 181 publications receiving 7802 citations. Previous affiliations of Anne-Marie Lambeir include Université catholique de Louvain & International Institute of Minnesota.
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A kinetic study of glucagon-like peptide-1 and glucagon-like peptide-2 truncation by dipeptidyl peptidase IV, in vitro
TL;DR: The slower conversion rate observed for GLP-2 compared toGLP-1 was due to an approximately 10-fold reduction in catalytic rate constant, and the selectivity of DPP IV for the glucagon-like peptides was compared with data obtained for other natural substrates using the same enzyme source in identical conditions.
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In vivo inhibition of dipeptidyl peptidase IV activity by pro-pro-diphenyl-phosphonate (prodipine)
I. De Meester,A. Belyaev,Anne-Marie Lambeir,G.R.Y. De Meyer,N. Van Osselaer,A. Haemers,S. Scharpe +6 more
TL;DR: The in vivo applicability of this chemically stable, irreversible inhibitor of DPP IV opens new possibilities, not only to further unravel the biological functions of this intriguing ectopeptidase, but also to explore this enzyme as a new target in various fields of pharmacological research.
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The importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis
TL;DR: Four salt bridge mutants of Trypanosoma Brucei brucei TIM were characterized and the folding and stability of the mutants are impaired compared to the wild‐type enzyme.
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Characterisation of a novel series of aprotinin-derived anticoagulants. I. In vitro and pharmacological properties.
Jean Marie Stassen,Anne-Marie Lambeir,G Matthyssens,William C Ripka,Åke Nyström,Jan J. Sixma,Jos Vermylen +6 more
TL;DR: The aprotinin-derived analogues showed significantly increased inhibitory activity towards factor Xa, factor VIIa-tissue factor (TF) complex, factor XIa and plasma kallikrein or a combination of them, and a significantly decreased plasmin inhibition as compared to aProtinin, while the pharmacological profiles in hamsters were not significantly different.
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Search for substrates for prolyl oligopeptidase in porcine brain.
Inger Brandt,Kris De Vriendt,Bart Devreese,Jozef Van Beeumen,Walter Van Dongen,Koen Augustyns,Ingrid De Meester,Simon Scharpé,Anne-Marie Lambeir +8 more
TL;DR: Using MSMS peptide sequencing techniques, several fragments of intracellular proteins are identified as potential substrates for recombinant porcine PO in Porcine brain, which opens new perspectives for finding the function of PO in the intrACEllular space.