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Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity.

The central event underlying prion diseases involves conformational change of the cellular form of the prion protein (PrP(C)) into the disease-associated, transmissible form (PrP(Sc)). Pr(PC) is a sialoglycoprotein that contains two conserved N-glycosylation sites. Among the key parameters that cont...

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書誌詳細
主要な著者: Elizaveta Katorcha, Natallia Makarava, Regina Savtchenko, Alessandra D'Azzo, Ilia V Baskakov
フォーマット: Artigo
言語:Inglês
出版事項: Public Library of Science (PLoS) 2014-09-01
シリーズ:PLoS Pathogens
オンライン・アクセス:http://europepmc.org/articles/PMC4161476?pdf=render
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