Muyldermans Serge
Muyldermans Serge
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Naturally occurring antibodies devoid of light chains
C Hamers-Casterman, T Atarhouch, S Muyldermans, G Robinson, ...
Nature 363 (6428), 446-448, 1993
Nanobodies: natural single-domain antibodies
S Muyldermans
Annu Rev Biochem 82 (1), 775-797, 2013
Selection and identification of single domain antibody fragments from camel heavy‐chain antibodies
M Arbabi Ghahroudi, A Desmyter, L Wyns, R Hamers, S Muyldermans
FEBS letters 414 (3), 521-526, 1997
Single domain camel antibodies: current status
S Muyldermans
Reviews in molecular Biotechnology 74 (4), 277-302, 2001
A versatile nanotrap for biochemical and functional studies with fluorescent fusion proteins
U Rothbauer, K Zolghadr, S Muyldermans, A Schepers, MC Cardoso, ...
Molecular & Cellular Proteomics 7 (2), 282-289, 2008
Single‐domain antibody fragments with high conformational stability
M Dumoulin, K Conrath, A Van Meirhaeghe, F Meersman, K Heremans, ...
Protein Science 11 (3), 500-515, 2002
Targeting and tracing antigens in live cells with fluorescent nanobodies
U Rothbauer, K Zolghadr, S Tillib, D Nowak, L Schermelleh, A Gahl, ...
Nature methods 3 (11), 887-889, 2006
Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains
S Muyldermans, T Atarhouch, J Saldanha, J Barbosa, R Hamers
Protein Engineering, Design and Selection 7 (9), 1129-1135, 1994
Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies
E De Genst, K Silence, K Decanniere, K Conrath, R Loris, J Kinne, ...
Proceedings of the National Academy of Sciences 103 (12), 4586-4591, 2006
Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme
A Desmyter, TR Transue, MA Ghahroudi, MH Dao Thi, F Poortmans, ...
Nature structural biology 3 (9), 803-811, 1996
Potent enzyme inhibitors derived from dromedary heavy-chain antibodies
M Lauwereys, MA Ghahroudi, A Desmyter, J Kinne, W Hölzer, E De Genst, ...
The EMBO journal 17 (13), 3512-3520, 1998
A general protocol for the generation of Nanobodies for structural biology
E Pardon, T Laeremans, S Triest, SGF Rasmussen, A Wohlkönig, A Ruf, ...
Nature protocols 9 (3), 674-693, 2014
Camelid immunoglobulins and nanobody technology
S Muyldermans, TN Baral, VC Retamozzo, P De Baetselier, E De Genst, ...
Veterinary immunology and immunopathology 128 (1-3), 178-183, 2009
Modulation of protein properties in living cells using nanobodies
A Kirchhofer, J Helma, K Schmidthals, C Frauer, S Cui, A Karcher, ...
Nature structural & molecular biology 17 (1), 133-138, 2010
General strategy to humanize a camelid single-domain antibody and identification of a universal humanized nanobody scaffold
C Vincke, R Loris, D Saerens, S Martinez-Rodriguez, S Muyldermans, ...
Journal of Biological Chemistry 284 (5), 3273-3284, 2009
Efficient cancer therapy with a nanobody-based conjugate
V Cortez-Retamozo, N Backmann, PD Senter, U Wernery, P De Baetselier, ...
Cancer research 64 (8), 2853-2857, 2004
Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains
S Muyldermans, C Cambillau, L Wyns
Trends in biochemical sciences 26 (4), 230-235, 2001
Comparison of llama VH sequences from conventional and heavy chain antibodies
KB Vu, MA Ghahroudi, L Wyns, S Muyldermans
Molecular immunology 34 (16-17), 1121-1131, 1997
β-Lactamase Inhibitors Derived from Single-Domain Antibody Fragments Elicited in the Camelidae
KE Conrath, M Lauwereys, M Galleni, A Matagne, JM Frère, J Kinne, ...
Antimicrobial agents and chemotherapy 45 (10), 2807-2812, 2001
Camel single-domain antibodies as modular building units in bispecific and bivalent antibody constructs
KE Conrath, M Lauwereys, L Wyns, S Muyldermans
Journal of Biological Chemistry 276 (10), 7346-7350, 2001
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