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2 p, 1.3 MB Elongation of the C-terminal domain of an anti-amyloid β single-chain variable fragment increases its thermodynamic stability and decreases its aggregation tendency / Rivera Hernández, Geovanny (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Marin Argany, Marta (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Blasco Moreno, B. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Bonet, Jaume (Universitat Pompeu Fabra. Unitat de Recerca en Informàtica Biomèdica (GRIB)) ; Oliva Miguel, Baldomero (Universitat Pompeu Fabra. Unitat de Recerca en Informàtica Biomèdica (GRIB)) ; Villegas Hernández, Sandra (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Amyloid β (Aβ) immunotherapy is considered a promising approach to Alzheimer disease treatment. In contrast to the use of complete antibodies, administration of single-chain variable fragments (scFv) has not been associated with either eningoencephalitis or cerebral hemorrhage. [...]
2013 - 10.4161/mabs.25382
MAbs, Vol. 5 Issue 5 (Sep.-Oct. 2013) , p. 678-689  
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