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Skip to Search Results- 3Aguzzi, Adriano
- 3James, Michael N. G.
- 2Baral, Pravas K.
- 2Kav, Nat N. V.
- 2Polymenidou, Magdalini
- 2Swayampakula, Mridula
- 2Antibodies
- 1Cloning
- 1Enzyme-Linked Immunoassays
- 1Fab Fragments
- 1Flow Cytometry
- 1Immunohistochemistry Techniques
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Crystallization and preliminary X-ray diffraction analysis of prion protein bound to the Fab fragment of the POM1 antibody
Download2011
James, Michael N. G., Swayampakula, Mridula , Polymenidou, Magdalini , Kav, Nat N. V., Aguzzi, Adriano, Wieland, Barbara, Baral, Pravas K.
Prion diseases are neurodegenerative diseases that are characterized by the conversion of the cellular prion protein PrPc to the pathogenic isoform PrPsc. Several antibodies are known to interact with the cellular prion protein and to inhibit this transition. An antibody Fab fragment, Fab POM1,...
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Structural studies on the folded domain of the human prion protein bound to the Fab fragment of the antibody POM1
Download2012
Kav, Nat N. V., Polymenidou, Magdalini , Rahman, Muhammad H., Aguzzi, Adriano, Swayampakula, Mridula , James, Michael N. G., Baral, Pravas K., Wieland, Barbara
Prion diseases are neurodegenerative diseases characterized by the conversion of the cellular prion protein PrPc into a pathogenic isoform PrPsc. Passive immunization with antiprion monoclonal antibodies can arrest the progression of prion diseases. Here, the crystal structure of the Fab fragment...
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The POM monoclonals: A comprehensive set of antibodies to non-overlapping prion protein epitopes
Download2008
Hafner-Bratkovič, Iva, Aguzzi, Adriano, Vey, Martin, Polymenidou, Magdalini, Yajima, Bill , James, Michael N. G., Jerala, Roman, Moos, Rita, Scott, Mike, Shi, Yong-zhong, Wuthrich, Kurt, Garen, Graciela, Sigurdson, Christina, Hornemann, Simone, Bellon, Anne, Kav, Nat
PrPSc, a misfolded and aggregated form of the cellular prion protein PrPC, is the only defined constituent of the transmissible agent causing prion diseases. Expression of PrPC in the host organism is necessary for prion replication and for prion neurotoxicity. Understanding prion diseases...