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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
A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme
Mireille Dumoulin,Aline Desmyter,Klaas Decanniere,Denis Canet,Göran Larsson,Andrew Spencer,David B. Archer,Jurgen Sasse,Serge Muyldermans,Lode Wyns,Christina Redfield,André Matagne,Carol V. Robinson,Christopher M. Dobson +13 more
TL;DR: Reducing the ability of an amyloidogenic protein to form partly unfolded species can be an effective method of preventing its aggregation, suggesting approaches to the rational design of therapeutic agents directed against protein deposition diseases.
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ProteomeBinders: planning a European resource of affinity reagents for analysis of the human proteome
Michael J. Taussig,Oda Stoevesandt,Carl A.K. Borrebaeck,Andrew Bradbury,Dolores J. Cahill,Christian Cambillau,Antoine de Daruvar,Stefan Dübel,Jutta Eichler,Ronald Frank,Toby J. Gibson,David E. Gloriam,Larry Gold,Friedrich W. Herberg,Henning Hermjakob,Jörg D. Hoheisel,Thomas O. Joos,Olli Kallioniemi,Manfred Koegl,Zoltán Konthur,Bernhard Korn,Elisabeth Kremmer,Sylvia Krobitsch,Ulf Landegren,Silvère M. van der Maarel,John McCafferty,Serge Muyldermans,Per-Åke Nygren,Sandrine Palcy,Andreas Plückthun,Bojan Polić,Michael Przybylski,Petri Saviranta,Alan Sawyer,David James Sherman,Arne Skerra,Markus F. Templin,Marius Ueffing,Mathias Uhlén +38 more
TL;DR: ProteomeBinders is a new European consortium aiming to establish a comprehensive resource of well-characterized affinity reagents, including but not limited to antibodies, for analysis of the human proteome.
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Identification of a universal VHH framework to graft non-canonical antigen-binding loops of camel single-domain antibodies.
Dirk Saerens,Mireille Pellis,Remy Loris,Els Pardon,Mireille Dumoulin,Mireille Dumoulin,André Matagne,Lode Wyns,Serge Muyldermans,Katja Conrath +9 more
TL;DR: The cAbBCII10 framework was chosen essentially for its high level of stability, good expression level, and its ability to be functional in the absence of the conserved disulfide bond, and all five chimeras generated by grafting CDR-Hs, from donor VHHs belonging to subfamily 2 that encompass 75% of all antigen-specific V HHs, were functional and generally had an increased thermodynamic stability.
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Nanobodies as novel agents for cancer therapy
TL;DR: The favourable biophysical and pharmacological properties of nanobodies, together with the ease of formatting them into multifunctional protein therapeutics, leaves them ideally placed as a new generation of antibody-based therapeutics.
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Position and orientation of the globular domain of linker histone H5 on the nucleosome
TL;DR: It is shown, in contrast to an earlier model, that the globular domain forms a bridge between one terminus of chromatosomal DNA and the DNA in the vicinity of the dyad axis of symmetry of the core particle.