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10.1021/acs.est.5b06294 http://scihub22266oqcxt.onion/10.1021/acs.est.5b06294 C5337124!5337124!27247993     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Environ+Sci+Technol 2016 ; 50 (13): 7095-105 Nephropedia Template TP {{tp|p=27247993|t=2016. Peroxymonosulfate Rapidly Inactivates the Disease-associated Prion Protein |pdf=|usr=}}{{27247993}} gab.com Text Peroxymonosulfate Rapidly Inactivates the Disease-associated Prion Protein JO: Environ Sci Technol http://www.kidney.de/pget.php?&tw=1&pmid=27247993 #FOAvip Prions, the etiological agents in transmissible spongiform encephalopathies, exhibit remarkable resistance to most methods of inactivation that are effective against conventional pathogens. Prions are composed of pathogenic conformers of the prion protein (PrPTSE). Some prion diseases are transmitted, in part, through environmental routes. The recalcitrance of prions to inactivation may lead to a persistent reservoir of infectivity that contributes to the environmental maintenance of epizootics. At present, few methods exist to remediate prion-contaminated lands. Here we examined the ability of peroxymonosulfate to degrade PrPTSE as an initial step toward developing an in situ chemical oxidation process to inactivate prions. We find that peroxymonosulfate rapidly degrades PrPTSE from two species. Transition metal-catalyzed decomposition of peroxymonosulfate to produce sulfate radicals appears to enhance degradation. We further demonstrate that exposure to peroxymonosulfate significantly reduced PrPC-to-PrPTSE converting ability as measured by protein misfolding cyclic amplification, used as a proxy for infectivity. Liquid chromatography-tandem mass spectrometry revealed that exposure to peroxymonosulfate results in oxidative modifications to methionine and tryptophan residues. This study indicates that peroxymonosulfate may hold promise for in situ remediation of prion-contaminated surfaces. Twit Text FOAVip Peroxymonosulfate Rapidly Inactivates the Disease-associated Prion Protein ????Environ Sci Technol http://www.kidney.de/pget.php?&tw=1&pmid=27247993 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27247993 #FOAvip English Wikipedia <ref>{{Cite pmid|27247993}}</ref> Peroxymonosulfate Rapidly Inactivates the Disease-associated Prion Protein #MMPMID27247993 Chesney AR; Booth CJ; Lietz CB; Li L; Pedersen JA Environ Sci Technol 2016[Jul]; 50 (13): 7095-105 PMID27247993show ga Prions, the etiological agents in transmissible spongiform encephalopathies, exhibit remarkable resistance to most methods of inactivation that are effective against conventional pathogens. Prions are composed of pathogenic conformers of the prion protein (PrPTSE). Some prion diseases are transmitted, in part, through environmental routes. The recalcitrance of prions to inactivation may lead to a persistent reservoir of infectivity that contributes to the environmental maintenance of epizootics. At present, few methods exist to remediate prion-contaminated lands. Here we examined the ability of peroxymonosulfate to degrade PrPTSE as an initial step toward developing an in situ chemical oxidation process to inactivate prions. We find that peroxymonosulfate rapidly degrades PrPTSE from two species. Transition metal-catalyzed decomposition of peroxymonosulfate to produce sulfate radicals appears to enhance degradation. We further demonstrate that exposure to peroxymonosulfate significantly reduced PrPC-to-PrPTSE converting ability as measured by protein misfolding cyclic amplification, used as a proxy for infectivity. Liquid chromatography-tandem mass spectrometry revealed that exposure to peroxymonosulfate results in oxidative modifications to methionine and tryptophan residues. This study indicates that peroxymonosulfate may hold promise for in situ remediation of prion-contaminated surfaces. äPeroxymonosulfate Rapidly Inactivates the Disease-associated Prion Pro(epmc).pdf DeepDyve Pubget Overpricing