Evaluation of quinacrine treatment for prion diseases
A Barret, F Tagliavini, G Forloni, C Bate… - Journal of …, 2003 - Am Soc Microbiol
Based on in vitro observations in scrapie-infected neuroblastoma cells, quinacrine has
recently been proposed as a treatment for Creutzfeldt-Jakob disease (CJD), including a new
variant CJD which is linked to contamination of food by the bovine spongiform
encephalopathy (BSE) agent. The present study investigated possible mechanisms of action
of quinacrine on prions. The ability of quinacrine to interact with and to reduce the protease
resistance of PrP peptide aggregates and PrPres of human and animal origin were …
recently been proposed as a treatment for Creutzfeldt-Jakob disease (CJD), including a new
variant CJD which is linked to contamination of food by the bovine spongiform
encephalopathy (BSE) agent. The present study investigated possible mechanisms of action
of quinacrine on prions. The ability of quinacrine to interact with and to reduce the protease
resistance of PrP peptide aggregates and PrPres of human and animal origin were …
[PDF][PDF] Evaluation of Quinacrine Treatment for Prion
KT Adjou, N Salès, A Williams, C Lasmézas, JP Deslys… - Citeseer
Based on in vitro observations in scrapie-infected neuroblastoma cells, quinacrine has
recently been proposed as a treatment for Creutzfeldt-Jakob disease (CJD), including a new
variant CJD which is linked to contamination of food by the bovine spongiform
encephalopathy (BSE) agent. The present study investigated possible mechanisms of action
of quinacrine on prions. The ability of quinacrine to interact with and to reduce the protease
resistance of PrP peptide aggregates and PrPres of human and animal origin were …
recently been proposed as a treatment for Creutzfeldt-Jakob disease (CJD), including a new
variant CJD which is linked to contamination of food by the bovine spongiform
encephalopathy (BSE) agent. The present study investigated possible mechanisms of action
of quinacrine on prions. The ability of quinacrine to interact with and to reduce the protease
resistance of PrP peptide aggregates and PrPres of human and animal origin were …
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