S Muyldermans

Summary

Affiliation: Vrije Universiteit Brussel
Country: Belgium

Publications

  1. pmc Nanobody(R)-based chromatin immunoprecipitation/micro-array analysis for genome-wide identification of transcription factor DNA binding sites
    Trong Nguyen-Duc
    Research group of Cellular and Molecular Immunology, Vrije Universiteit Brussel, Pleinlaan 2, B 1050 Brussel, Belgium
    Nucleic Acids Res 41:e59. 2013
  2. doi request reprint Camelid single-domain antibody-fragment engineering for (pre)clinical in vivo molecular imaging applications: adjusting the bullet to its target
    Jens De Vos
    Laboratory of Cellular and Molecular Immunology CMIM, Vrije Universiteit Brussel, Pleinlaan 2, Building E 8, 1050 Brussels, Belgium
    Expert Opin Biol Ther 13:1149-60. 2013
  3. doi request reprint Nanobodies: natural single-domain antibodies
    Serge Muyldermans
    Research group Cellular and Molecular Immunology, Vrije Universiteit Brussel, 1050 Brussels, Belgium
    Annu Rev Biochem 82:775-97. 2013
  4. pmc Heating as a rapid purification method for recovering correctly-folded thermotolerant VH and VHH domains
    Aurelien Olichon
    Cell Biology Unit, EMBL Meyerhofstr 1, D 69117, Heidelberg, Germany
    BMC Biotechnol 7:7. 2007
  5. ncbi request reprint Camelid immunoglobulins and nanobody technology
    S Muyldermans
    Laboratory of Cellular and Molecular Immunology, Department of Molecular and Cellular Interactions, VIB, Vrije Universiteit Brussel, Brussels, Belgium
    Vet Immunol Immunopathol 128:178-83. 2009
  6. ncbi request reprint Single domain camel antibodies: current status
    S Muyldermans
    Vrije Universiteit Brussel, Vlaams Interuniversitair Instituut voor Biotechnologie, Sint Genesius Rode, Belgium
    J Biotechnol 74:277-302. 2001
  7. ncbi request reprint Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains
    S Muyldermans
    Vrije Universiteit Brussel, Vlaams Interuniversitair Instituut Biotechnologie, 65, B 1640 Sint Genesius Rode, Paardenstraat, Belgium
    Trends Biochem Sci 26:230-5. 2001
  8. ncbi request reprint Unique single-domain antigen binding fragments derived from naturally occurring camel heavy-chain antibodies
    S Muyldermans
    Ultrastructure, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, B 1640 Sint Genesius Rode, Belgium
    J Mol Recognit 12:131-40. 1999
  9. ncbi request reprint A single-domain antibody fragment in complex with RNase A: non-canonical loop structures and nanomolar affinity using two CDR loops
    K Decanniere
    Laboratorium voor Ultrastructuur, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, B 1640 St Genesius Rode, Belgium
    Structure 7:361-70. 1999
  10. pmc Potent enzyme inhibitors derived from dromedary heavy-chain antibodies
    M Lauwereys
    Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, 1640 Sint Genesius Rode, Belgium
    EMBO J 17:3512-20. 1998

Collaborators

Detail Information

Publications24

  1. pmc Nanobody(R)-based chromatin immunoprecipitation/micro-array analysis for genome-wide identification of transcription factor DNA binding sites
    Trong Nguyen-Duc
    Research group of Cellular and Molecular Immunology, Vrije Universiteit Brussel, Pleinlaan 2, B 1050 Brussel, Belgium
    Nucleic Acids Res 41:e59. 2013
    ....
  2. doi request reprint Camelid single-domain antibody-fragment engineering for (pre)clinical in vivo molecular imaging applications: adjusting the bullet to its target
    Jens De Vos
    Laboratory of Cellular and Molecular Immunology CMIM, Vrije Universiteit Brussel, Pleinlaan 2, Building E 8, 1050 Brussels, Belgium
    Expert Opin Biol Ther 13:1149-60. 2013
    ..Molecular imaging is a fast developing field and there is a growing need for specific imaging tracers in the clinic. Camelid single-domain antibody-fragments (sdAbs) recently emerged as a new class of molecular imaging tracers...
  3. doi request reprint Nanobodies: natural single-domain antibodies
    Serge Muyldermans
    Research group Cellular and Molecular Immunology, Vrije Universiteit Brussel, 1050 Brussels, Belgium
    Annu Rev Biochem 82:775-97. 2013
    ....
  4. pmc Heating as a rapid purification method for recovering correctly-folded thermotolerant VH and VHH domains
    Aurelien Olichon
    Cell Biology Unit, EMBL Meyerhofstr 1, D 69117, Heidelberg, Germany
    BMC Biotechnol 7:7. 2007
    ..Their heat tolerance is a particularly interesting feature because it has been recently related to both high yields during recombinant expression and selective purification of folded protein...
  5. ncbi request reprint Camelid immunoglobulins and nanobody technology
    S Muyldermans
    Laboratory of Cellular and Molecular Immunology, Department of Molecular and Cellular Interactions, VIB, Vrije Universiteit Brussel, Brussels, Belgium
    Vet Immunol Immunopathol 128:178-83. 2009
    ..We have successfully developed recombinant Nbs for research purposes, as probe in biosensors, to diagnose infections, and to treat diseases like cancer or trypanosomosis...
  6. ncbi request reprint Single domain camel antibodies: current status
    S Muyldermans
    Vrije Universiteit Brussel, Vlaams Interuniversitair Instituut voor Biotechnologie, Sint Genesius Rode, Belgium
    J Biotechnol 74:277-302. 2001
    ..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...
  7. ncbi request reprint Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains
    S Muyldermans
    Vrije Universiteit Brussel, Vlaams Interuniversitair Instituut Biotechnologie, 65, B 1640 Sint Genesius Rode, Paardenstraat, Belgium
    Trends Biochem Sci 26:230-5. 2001
    ..The VHH has a potent antigen-binding capacity and provides the advantage of interacting with novel epitopes that are inaccessible to conventional VH-VL pairs...
  8. ncbi request reprint Unique single-domain antigen binding fragments derived from naturally occurring camel heavy-chain antibodies
    S Muyldermans
    Ultrastructure, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, B 1640 Sint Genesius Rode, Belgium
    J Mol Recognit 12:131-40. 1999
    ....
  9. ncbi request reprint A single-domain antibody fragment in complex with RNase A: non-canonical loop structures and nanomolar affinity using two CDR loops
    K Decanniere
    Laboratorium voor Ultrastructuur, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, B 1640 St Genesius Rode, Belgium
    Structure 7:361-70. 1999
    ..In the case of the VHH fragment cAb-Lys3, part of the 24 amino acid long CDR3 loop protrudes from the antigen-binding surface and inserts into the active-site cleft of its antigen, rendering cAb-Lys3 a competitive enzyme inhibitor...
  10. pmc Potent enzyme inhibitors derived from dromedary heavy-chain antibodies
    M Lauwereys
    Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, 1640 Sint Genesius Rode, Belgium
    EMBO J 17:3512-20. 1998
    ..The low complexity of the antigen-binding site of these single-domain antibodies composed of only three loops could be valuable for designing smaller synthetic inhibitors...
  11. ncbi request reprint Camel single-domain antibodies as modular building units in bispecific and bivalent antibody constructs
    K Els Conrath
    Department of Ultrastructure, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, B 1640 Sint Genesius Rode, Belgium
    J Biol Chem 276:7346-50. 2001
    ..The easy generation steps and the biophysical properties of these bispecific and bivalent constructs based on camel single-domain antibody fragments makes them particularly attractive for use in therapeutic or diagnostic programs...
  12. ncbi request reprint The regulated expression of an intrabody produces a mutant phenotype in Drosophila
    G Hassanzadeh GH
    Department of Ultrastructure, Immunology and Parasitology, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Sint Genesius Rode, Belgium
    FEBS Lett 437:81-6. 1998
    ..The antisense approach was used as control. Parameters that can affect the success of intrabody technology are described...
  13. pmc Beta-lactamase inhibitors derived from single-domain antibody fragments elicited in the camelidae
    K E Conrath
    Department of Ultrastructure, Vrije Universiteit Brussel, Pardenstraat 65, B 1640 St Genesius Rode, Belgium
    Antimicrob Agents Chemother 45:2807-12. 2001
    ..This innovative strategy could generate multiple potent inhibitors for all types of beta-lactamases...
  14. pmc Camel heavy-chain antibodies: diverse germline V(H)H and specific mechanisms enlarge the antigen-binding repertoire
    V K Nguyen
    Department Ultrastructure, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, B 1640 Sint Genesius Rode, Belgium
    EMBO J 19:921-30. 2000
    ..These diversification processes are driven by hypermutation and recombination hotspots embedded in the V(H)H germline genes at the regions affecting the structure of the antigen-binding loops...
  15. ncbi request reprint Canonical antigen-binding loop structures in immunoglobulins: more structures, more canonical classes?
    K Decanniere
    Department Ultrastructure Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, Brussel, B 1640, Belgium
    J Mol Biol 300:83-91. 2000
    ..Their discovery indicates that the currently used set of canonical structures is incomplete and that the prediction algorithms should be extended to include these new structures...
  16. ncbi request reprint Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibody
    A Desmyter
    Department Ultrastructure, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, B 1640 Sint Genesius Rode, Belgium
    J Biol Chem 276:26285-90. 2001
    ....
  17. ncbi request reprint The interaction of histone H5 and its globular domain with core particles, depleted chromatosomes, polynucleosomes, and a DNA decamer
    A Segers
    Instituut voor Molekulaire Biologie, Vrije Universiteit Brussel, Belgium
    J Biol Chem 266:1502-8. 1991
    ..A salt dependence analysis of GH5 binding to H5-depleted chromatosomes indicates that GH5 displaces a number of ions similar to the total H1 linker histone, suggesting a delocalized binding of the carboxyl- and amino-terminal tails...
  18. ncbi request reprint Emergence and evolution of functional heavy-chain antibodies in Camelidae
    K E Conrath
    Department of Immunology, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, B 1640, Sint Genesius Rode, Belgium
    Dev Comp Immunol 27:87-103. 2003
    ....
  19. ncbi request reprint Degenerate interfaces in antigen-antibody complexes
    K Decanniere
    Vrije Universiteit Brussel Dienst Ultrastructuur, Vlaams Instituut voor Biotechnologie, Paardenstraat 65, B 1640 St Genesius Rode, Belgium
    J Mol Biol 313:473-8. 2001
    ..Consideration should be given to this type of observation when trying to establish general protein-protein interface characteristics...
  20. ncbi request reprint Loss of splice consensus signal is responsible for the removal of the entire C(H)1 domain of the functional camel IGG2A heavy-chain antibodies
    V K Nguyen
    Department of Ultrastructure, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Belgium
    Mol Immunol 36:515-24. 1999
    ..Additionally, a closer analysis of the hinge exon suggests the possible involvement of transposons in the genetic variation of mammalian Cgamma hinges...
  21. ncbi request reprint Isolation and characterization of single-chain Fv genes encoding antibodies specific for Drosophila Poxn protein
    G Hassanzadeh GH
    Department of Ultrastructure, Immunology and Parasitology, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Sint Genesius Rode, Belgium
    FEBS Lett 437:75-80. 1998
    ..The alpha-Poxn5 scFv also recognizes denatured Poxn but either does not recognize native Poxn or its half maximal inhibition value for native Poxn is high...
  22. ncbi request reprint Camel single-domain antibody inhibits enzyme by mimicking carbohydrate substrate
    T R Transue
    Department of Ultrastructure, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Belgium
    Proteins 32:515-22. 1998
    ....
  23. ncbi request reprint DNA sequence organization in chromatosomes
    S Muyldermans
    Vrije Universiteit Brussel, Instituut voor Moleculaire Biologie, St Genesius Rode, Belgium
    J Mol Biol 235:855-70. 1994
    ..The implications for the positioning of GH5 relative to the path of the DNA superhelix are discussed...