S
Serge Muyldermans
Researcher at Vrije Universiteit Brussel
Publications - 323
Citations - 30516
Serge Muyldermans is an academic researcher from Vrije Universiteit Brussel. The author has contributed to research in topics: Single-domain antibody & Antibody. The author has an hindex of 80, co-authored 305 publications receiving 26561 citations. Previous affiliations of Serge Muyldermans include Dalian University of Technology & Université libre de Bruxelles.
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Journal ArticleDOI
Targeting and tracing antigens in live cells with fluorescent nanobodies
Ulrich Rothbauer,Kourosh Zolghadr,Sergey Tillib,Danny Nowak,Lothar Schermelleh,Anja Gahl,Natalija Backmann,Katja Conrath,Serge Muyldermans,M Christina Cardoso,Heinrich Leonhardt +10 more
TL;DR: It is demonstrated that chromobodies can recognize and trace antigens in different subcellular compartments throughout S phase and mitosis.
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Single-domain antibody fragments with high conformational stability
Mireille Dumoulin,Katja Conrath,Annemie Van Meirhaeghe,Filip Meersman,Karel Heremans,Leon Gerardus Joseph Frenken,Serge Muyldermans,Lode Wyns,André Matagne +8 more
TL;DR: All the fragments are rather resistant to heat‐induced denaturation, and display high conformational stabilities, which has never been reported for any functional conventional antibody fragment, even when engineered antigen binders are considered.
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Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies.
Erwin De Genst,Karen Silence,Klaas Decanniere,Katja Conrath,Remy Loris,Jörg Kinne,Serge Muyldermans,Lode Wyns +7 more
TL;DR: A single domain antigen-combining site has a clear structural advantage over a conventional dimeric format for targeting clefts on antigenic surfaces with a pronounced preference for heavy-chain antibodies of camelids.
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Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme
Aline Desmyter,Thomas R. Transue,Mehdi Arbabi Ghahroudi,Minh-Hoa Dao Thi,Freddy Poortmans,Raymond Hamers,Serge Muyldermans,Lode Wyns +7 more
TL;DR: The Camelidae is the only taxonomic family known to possess functional heavy-chain antibodies, lacking light chains, and the 2.5 Å resolution crystal structure of a camel VH in complex with its antigen, lysozyme is reported.
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A general protocol for the generation of Nanobodies for structural biology
Els Pardon,Toon Laeremans,Sarah Triest,Søren G. F. Rasmussen,Alexandre Wohlkonig,Armin Ruf,Serge Muyldermans,Wim G. J. Hol,Brian K. Kobilka,Jan Steyaert +9 more
TL;DR: A general protocol for the generation of Nanobodies to be used as crystallization chaperones for the structural investigation of diverse conformational states of flexible (membrane) proteins and complexes thereof.