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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Journal ArticleDOI
Nanobodies as Tools for In Vivo Imaging of Specific Immune Cell Types
Kurt De Groeve,Nick Deschacht,Celine De Koninck,Vicky Caveliers,Tony Lahoutte,Nick Devoogdt,Serge Muyldermans,Patrick De Baetselier,Geert Raes +8 more
TL;DR: Nanobodies represent elegant targeting probes for imaging the in vivo biodistribution of specific immune cell types and reflects the main in vivo locations of the cells recognized by the Nanobodies and is determined by the antigen-binding loops of the nanobodies.
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Camelid single-domain antibody-fragment engineering for (pre)clinical in vivo molecular imaging applications: adjusting the bullet to its target
TL;DR: This work reviews the importance of molecular imaging in the clinic and the use of camelid single-domain antibody-fragments (sdAbs) as in vivo molecular imaging tracers and expects that the development and use of sdAbs as tracers for both preclinical and clinical molecular imaging applications will become widespread.
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An S-layer heavy chain camel antibody fusion protein for generation of a nanopatterned sensing layer to detect the prostate-specific antigen by surface plasmon resonance technology.
Magdalena Pleschberger,Dirk Saerens,Stefan Weigert,Uwe B. Sleytr,Serge Muyldermans,Margit Sara,Eva M. Egelseer +6 more
TL;DR: The bacterial cell surface layer (S-layer) protein of Bacillus sphaericus CCM 2177 assembles into a square lattice structure and recognizes a distinct type of secondary cell wall polymer (SCWP) as the proper anchoring structure in the rigid cell wall layer.
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Homo- and Heteronuclear Two-Dimensional NMR Studies of the Globular Domain of Histone H1: Full Assignment, Tertiary Structure, and Comparison with the Globular Domain of Histone H5
Corinne Cerf,Guy Lippens,Venki Ramakrishnan,Serge Muyldermans,Alain Segers,Lode Wyns,Shoshana J. Wodak,Klaas Hallenga +7 more
TL;DR: The globular domain of chicken histone H1 (GH1) has been studied by 1H homonuclear and 1H-15N heteronuclear 2D NMR spectroscopy and the location of the most positively charged regions seems to agree with the model where nucleosome binding takes place through contact points located at one DNA terminus and close to the dyad axis of the nucleosomes.
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Applications of Nanobodies
TL;DR: Unique, functional, homodimeric heavy chain-only antibodies, devoid of light chains, are circulating in the blood of Camelidae, and several Nanobody-based constructs have been designed to develop new therapeutic products.