Reference : (1)H, (13)C and (15)N assignments of a camelid nanobody directed against human alpha-syn...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/75324
(1)H, (13)C and (15)N assignments of a camelid nanobody directed against human alpha-synuclein.
English
Vuchelen, Anneleen [> > > >]
O'Day, Elizabeth [> > > >]
De Genst, Erwin [> > > >]
Pardon, Els [> > > >]
Wyns, Lode [> > > >]
Dumoulin, Mireille mailto [Université de Liège - ULg > Département des sciences de la vie > Enzymologie et repliement des protéines >]
Dobson, Christopher M [> > > >]
Christodoulou, John [> > > >]
Hsu, Shang-Te Danny [> > > >]
2009
Biomolecular NMR Assignments
Springer
3
2
231-3
Yes (verified by ORBi)
International
1874-2718
1874-270X
Dordrecht
Netherlands
[en] Animals ; Camelids, New World ; Camels ; Humans ; Nuclear Magnetic Resonance, Biomolecular ; Single-Chain Antibodies/chemistry/immunology ; alpha-Synuclein/immunology
[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.
http://hdl.handle.net/2268/75324
10.1007/s12104-009-9182-4

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