Article (Scientific journals)
(1)H, (13)C and (15)N assignments of a camelid nanobody directed against human alpha-synuclein.
Vuchelen, Anneleen; O'Day, Elizabeth; De Genst, Erwin et al.
2009In Biomolecular NMR Assignments, 3 (2), p. 231-3
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Keywords :
Animals; Camelids, New World; Camels; Humans; Nuclear Magnetic Resonance, Biomolecular; Single-Chain Antibodies/chemistry/immunology; alpha-Synuclein/immunology
Abstract :
[en] Nanobodies are single chain antibodies that are uniquely produced in Camelidae, e.g. camels and llamas. They have the desirable features of small sizes (Mw < 14 kDa) and high affinities against antigens (Kd approximately nM), making them ideal as structural probes for biomedically relevant motifs both in vitro and in vivo. We have previously shown that nanobody binding to amyloidogenic human lysozyme variants can effectively inhibit their aggregation, the process that is at the origin of systemic amyloid disease. Here we report the NMR assignments of a new nanobody, termed NbSyn2, which recognises the C-terminus of the intrinsically disordered protein, human alpha-synuclein (aS), whose aberrant self-association is implicated in Parkinson's disease.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Vuchelen, Anneleen
O'Day, Elizabeth
De Genst, Erwin
Pardon, Els
Wyns, Lode
Dumoulin, Mireille  ;  Université de Liège - ULiège > Département des sciences de la vie > Enzymologie et repliement des protéines
Dobson, Christopher M
Christodoulou, John
Hsu, Shang-Te Danny
Language :
English
Title :
(1)H, (13)C and (15)N assignments of a camelid nanobody directed against human alpha-synuclein.
Publication date :
2009
Journal title :
Biomolecular NMR Assignments
ISSN :
1874-2718
eISSN :
1874-270X
Publisher :
Springer, Dordrecht, Netherlands
Volume :
3
Issue :
2
Pages :
231-3
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 09 November 2010

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