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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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Journal ArticleDOI
Assembly of oligonucleosomes into a limit series of multimeric higher-order chromatin structures.
TL;DR: It is shown that the same distribution of supranucleosomal structures (even those containing internal DNA scissions) can be reconstituted from unfolded nuclear chromatin extracts as present in 10 mM or 600 mM NaCl.
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NIRF-Molecular Imaging with Synovial Macrophages-Targeting Vsig4 Nanobody for Disease Monitoring in a Mouse Model of Arthritis.
Fang Zheng,Siyu Luo,Zhenlin Ouyang,Jinhong Zhou,Huanye Mo,Steve Schoonooghe,Serge Muyldermans,Patrick De Baetselier,Geert Raes,Yurong Wen +9 more
TL;DR: NIRF imaging with Cy7-Nb119 allows specific assessment of inflammation in experimental arthritis and provides complementary information to clinical scoring for quantitative, non-invasive and economical monitoring of the pathological process.
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The crystal structure of recombinant rat pancreatic RNase A
TL;DR: The three‐dimensional structure of rat pancreatic RNase A expressed in Escherichia coli was determined and it was inferred that the local conformation of the substrate governs the specificity of subtilisin.
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CS1-specific single-domain antibodies labeled with Actinium-225 prolong survival and increase CD8+ T cells and PD-L1 expression in Multiple Myeloma.
Kim De Veirman,Janik Puttemans,Ahmet Krasniqi,Thomas Ertveldt,Heleen Hanssens,Ema Romão,Dirk Hose,Cleo Goyvaert,Philip Vlummens,Philip Vlummens,Serge Muyldermans,Karine Breckpot,Frank Bruchertseifer,Alfred Morgenstern,Matthias D'Huyvetter,Nick Devoogdt +15 more
TL;DR: In this article, the authors developed and characterized single-domain antibodies (sdAbs) against the MM-antigen CS1 and evaluated its therapeutic potential in MM using TRNT.
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Structural basis of nanobody recognition of grapevine fanleaf virus and of virus resistance loss.
Igor Orlov,Caroline Hemmer,Léa Ackerer,Léa Ackerer,Bernard Lorber,Ahmed Ghannam,Vianney Poignavent,Kamal Hleibieh,Claude Sauter,Corinne Schmitt-Keichinger,Lorène Belval,Jean-Michel Hily,Aurélie Marmonier,Véronique Komar,Sophie Gersch,Pascale Schellenberger,Patrick Bron,Emmanuelle Vigne,Serge Muyldermans,Olivier Lemaire,Gérard Demangeat,Christophe Ritzenthaler,Bruno P. Klaholz +22 more
TL;DR: The high-resolution cryo electron microscopy structure of the GFLV–Nb23 complex provides the basis for molecular recognition by the Nb, and uncovers the epitope on the capsid surface, which is a composite binding site into which the antigen loop is accommodated through an induced fit mechanism.