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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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A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme

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

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.

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.