D. W. Wang

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The ability of PrP Sc to convert PrP C into protease-resistance isoforms has been exploited using a variety of techniques such as protein misfolding cyclic amplification (PMCA), quaking induced conversion (QuIC) and most recently, real-time quaking induced conversion (RT-QuIC). 1 These cell-free assays have enabled a better understanding of prion diseases(More)
Infectious prions contain a self-propagating, misfolded conformer of the prion protein termed PrPSc. A critical prediction of the protein-only hypothesis is that autocatalytic PrPSc molecules should be infectious. However, some autocatalytic recombinant PrPSc molecules have low or undetectable levels of specific infectivity in bioassays, and the essential(More)
The chaperonin protein GroEL, also known as heat shock protein 60 (Hsp60), is a prominent antigen in the human and mouse antibody response to the facultative intracellular bacterium Francisella tularensis (Ft), the causative agent of tularemia. In addition to its presumed cytoplasmic location, FtGroEL has been reported to be a potential component of the(More)
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