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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Heavy-chain antibodies in Camelidae; a case of evolutionary innovation.
TL;DR: It appears that innovative evolutionary changes in Camelidae have led to a new level of antigen binding repertoire diversification and have allowed acquisition of novel antigen-receptor properties.
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The specific variable domain of camel heavy-chain antibodies is encoded in the germline
TL;DR: The analysis of an unrearranged dromedary DNA library revealed that the specific VHH gene with its characteristic amino acid substitutions is encoded in the germline, and it is concluded that the VHHs do not arise through an ontogenic process of somatic hypermutation.
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Nanobody-Based Delivery Systems for Diagnosis and Targeted Tumor Therapy
TL;DR: The state of the art of Nb-based targeted cancer therapy is reviewed and recent developments with Nbs as targeting moieties for drug delivery systems in cancer therapy and cancer imaging are focused on.
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Engineering Camel Single-Domain Antibodies and Immobilization Chemistry for Human Prostate-Specific Antigen Sensing
Dirk Saerens,Filip Frederix,Gunter Reekmans,Katja Conrath,Karolien Jans,Lea Brys,Lieven Huang,Eugene Bosmans,Guido Maes,Gustaaf Borghs,Serge Muyldermans +10 more
TL;DR: VHHs are presented as a novel class of biosensor probes rivaling conventional antibodies and their derived antibody fragments rivaled by SPR technology, and the intrinsic protein stability is presented as an important probe design factor.
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Disulfide bond introduction for general stabilization of immunoglobulin heavy-chain variable domains.
TL;DR: A strategy is proposed whereby consistent gain in stability is accomplished by introducing a specific disulfide bond between two opposite beta-strands in the hydrophobic core of the immunoglobulin heavy-chain variable domain of heavy- chain antibodies (Nanobody).