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.
Papers
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Journal ArticleDOI
Fast One-Step Ultrasensitive Detection of Toxocara canis Antigens by a Nanobody-Based Electrochemical Magnetosensor
Francisco Morales-Yánez,Francisco Morales-Yánez,Stanislav Trashin,Marie Hermy,Idalia Sariego,Katja Polman,Serge Muyldermans,Karolien De Wael +7 more
TL;DR: To the authors' knowledge, this is the most sensitive method to quantify TES antigen so far and has great potential to develop point of care diagnostic systems in other conditions where high sensitivity and specificity are required.
Journal ArticleDOI
Llama peripheral B-cell populations producing conventional and heavy chain-only IgG subtypes are phenotypically indistinguishable but immunogenetically distinct
Kevin A. Henry,Henk van Faassen,Doreen Harcus,Anne Marcil,Jennifer J. Hill,Serge Muyldermans,C. Roger MacKenzie,C. Roger MacKenzie +7 more
TL;DR: The distinct molecular features of llama IgG1, IgG2b and IgC2c antibodies imply that these subclasses may have divergent immunological functions and suggest that specific mechanisms operate to diversify HCAb repertoires in the absence of a light chain.
Journal ArticleDOI
Expression, purification and X-ray crystallographic analysis of the Helicobacter pylori blood group antigen-binding adhesin BabA
Suresh Subedi,Kristof Moonens,Ema Romão,Alvin W. Lo,Guy Vandenbussche,Jeanna Bugaytsova,Serge Muyldermans,Serge Muyldermans,Thomas Borén,Han Remaut +9 more
TL;DR: The recombinant expression and crystallization of a soluble BabA truncation (BabA(25-460)) corresponding to the predicted extracellular adhesin domain of the protein are reported.
Journal ArticleDOI
Structural basis for the high specificity of a Trypanosoma congolense immunoassay targeting glycosomal aldolase.
Joar Pinto,Steven Odongo,Felicity Lee,Vaiva Gaspariunaite,Serge Muyldermans,Stefan Magez,Stefan Magez,Yann G.-J. Sterckx +7 more
TL;DR: The results show that the high specificity of the N b474-based immunoassay is not determined by the initial recognition event between Nb474 and TcoALD, but rather by its homologous sandwich design, providing insights into the optimal set-up of the assay.
Book ChapterDOI
Nanobodies, Single-Domain Antigen-Binding Fragments of Camelid Heavy-Chain Antibodies
TL;DR: Antibodies or immunoglobulins are glycoproteins produced by B-cells and play a central role in host immune defense and placed themselves among the most attractive reagents for both fundamental and applied sciences.