Marc De Maeyer
Katholieke Universiteit Leuven
116 Papers
1.6K Citations
Marc De Maeyer is an academic researcher from Katholieke Universiteit Leuven. The author has contributed to research in topics: Integrase & Docking (molecular). The author has an hindex of 34, co-authored 116 publications. Previous affiliations of Marc De Maeyer include Catholic University of Leuven.
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Papers
Rational design of small-molecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication
Frauke Christ,Arnout Voet,Arnaud Marchand,Stefan Nicolet,Stefan Nicolet,Belete Ayele Desimmie,Damien Marchand,Dorothée Bardiot,Nam Joo Van der Veken,Barbara Van Remoortel,Sergei V. Strelkov,Marc De Maeyer,Patrick Chaltin,Zeger Debyser +13 more
TL;DR: This work demonstrates the feasibility of rational design of small molecules inhibiting the protein-protein interaction between a viral protein and a cellular host factor and defines the 2-(quinolin-3-yl)acetic acid derivatives as the first genuine allosteric HIV-1 integrase inhibitors.
All in one: a highly detailed rotamer library improves both accuracy and speed in the modelling of sidechains by dead-end elimination
TL;DR: It is shown that a very detailed rotamer library allows the introduction of a safe energy threshold rejection criterion, thereby increasing both the execution speed and the accuracy of the modelling program.
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A structural basis for the unique binding features of the human vitamin D-binding protein.
Christel Verboven,Anja Rabijns,Marc De Maeyer,Hugo Van Baelen,Roger Bouillon,Camiel J. De Ranter +5 more
TL;DR: The 2.3 Å crystal structure of DBP in complex with 25-hydroxyvitamin D3, a vitamin D3 metabolite, is reported, which reveals the vitamin D-binding site in the N-terminal part of domain I, explaining the unique vitamin D D3-binding property ofDBP.
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Tuning the size and properties of ClyA nanopores assisted by directed evolution
TL;DR: This work evolved Cytolysin A from Salmonella typhi (ClyA) to a high level of soluble expression and desired electrical properties in lipid bilayers and found that ClyA forms several nanopore species; among which three nanopore types most likely corresponding to the 12mer, 13mer, and 14mer oligomeric forms of ClyA are identified.
Identification of the LEDGF/p75 Binding Site in HIV-1 Integrase
Katrien Busschots,Arnout Voet,Marc De Maeyer,Jean-Christophe Rain,Stéphane Emiliani,Richard Benarous,Linda Desender,Zeger Debyser,Frauke Christ +8 more
TL;DR: Two regions within the enzyme involved in the interaction with LEDGF/p75 are identified and characterized, and an HIV-1 strain containing the W131A mutation in IN displays reduced replication capacity, whereas virus carrying IN(Q168A) is replication defective.
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