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- W2159724596 abstract "Prion diseases are disorders of protein conformation and do not provoke an immune response. Raising antibodies to the prion protein (PrP) has been difficult due to conservation of the PrP sequence and to inhibitory activity of alpha-PrP antibodies toward lymphocytes. To circumvent these problems, we immunized mice in which the PrP gene was ablated (Prnp 0/0) and retrieved specific monoclonal antibodies (mAbs) through phage display libraries. This approach yielded alpha-PrP mAbs that recognize mouse PrP. Studies with these mAbs suggest that cellular PrP adopts an unusually open structure consistent with the conformational plasticity of this protein." @default.
- W2159724596 created "2016-06-24" @default.
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- W2159724596 date "1996-07-09" @default.
- W2159724596 modified "2023-09-23" @default.
- W2159724596 title "Circumventing tolerance to generate autologous monoclonal antibodies to the prion protein." @default.
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- W2159724596 doi "https://doi.org/10.1073/pnas.93.14.7279" @default.
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