Conformational dynamics as an intrinsic determinant of prion protein misfolding and neurotoxicity  

作　　者：Alessandro Cembran Pedro Fernandez-Funez 

机构地区：[1]Department of Chemistry and Biochemistry,University of Minnesota Duluth,Duluth,MN,USA [2]Department of Biomedical Sciences,University of Minnesota Medical School,Duluth Campus,Duluth,MN,USA

出　　处：《Neural Regeneration Research》2024年第10期2095-2096,共2页中国神经再生研究（英文版）

基　　金：supported by the NIH grant7R21 NS09662 7-02 to PFF;the Winston and Maxine Wallin Neuroscience Discovery Fund award CON000000083928 to PFF and AC。

摘　　要：The prion protein(PrP) is the key molecular and pathological mediator of prion diseases,a heterogeneous group of brain disorders with fatal outcomes.Prion diseases are rare but deserve special attention because of their unique familial,sporadic,and transmissible etiologies,all caused by a single agent:misfolded conformations of PrP.

关 键 词：FOLDING INTRINSIC DYNAMICS 

分 类 号：R741[医药卫生—神经病学与精神病学]