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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Naturally occurring antibodies devoid of light chains
Cécile Hamers-Casterman,Touriya Atarhouch,Serge Muyldermans,Gene E. Robinson,Hamers C,Songa Eb,Bendahman N,Raymond Hamers +7 more
TL;DR: The presence of considerable amounts of IgG-like material of Mr 100K in the serum of the camel, which is composed of heavy-chain dimers and devoid of light chains, but nevertheless have an extensive antigen-binding repertoire, opens new perspectives in the engineering of antibodies.
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Nanobodies: Natural Single-Domain Antibodies
TL;DR: The facile identification of antigen-specific VHHs and their beneficial biochemical and economic properties have encouraged antibody engineering of these single-domain antibodies for use as a research tool and in biotechnology and medicine.
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Selection and identification of single domain antibody fragments from camel heavy-chain antibodies
TL;DR: The feasibility of immunising a dromedary, cloning the repertoire of the variable domains of its heavy‐chain antibodies and panning, leading to the successful identification of minimum sized antigen binders is shown.
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Single domain camel antibodies: current status.
TL;DR: Because of their smaller size and the above properties, the VHH clearly offer added-value over conventional antibody fragments, they are expected to open perspectives as enzyme inhibitors and intrabodies, as modular building units for multivalent or multifunctional constructs, or as immuno-adsorbents and detection units in biosensors.
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A Versatile Nanotrap for Biochemical and Functional Studies with Fluorescent Fusion Proteins
Ulrich Rothbauer,Kourosh Zolghadr,Serge Muyldermans,Aloys Schepers,M Christina Cardoso,Heinrich Leonhardt +5 more
TL;DR: This work engineered a specific binder for fluorescent proteins based on a 13-kDa GFP binding fragment derived from a llama single chain antibody that enables a unique combination of microscopic, biochemical, and functional analyses with one and the same protein.