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注意：仅列出部分参考文献，下载原文获取全部文献信息。A Naturally Occurring C-terminal Fragment of the Prion Protein (PrP) Delays Disease and Acts as a Dominant-negative Inhibitor of PrPSc Formation
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Cellular Prion Protein Promotes Regeneration of Adult Muscle Tissue
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The α-Secretase-derived N-terminal Product of Cellular Prion, N1, Displays Neuroprotective Function in Vitro and in Vivo
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Cellular prion protein coupling to TACE-dependent TNF-α shedding controls neurotransmitter catabolism in neuronal cells
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Activation of Prn-p gene and stable transfection of Prn-p cDNA in leukemia MEL and neuroblastorna N2a cells increased production of PrPC but not prevented DNA fragmentation initiated by serum deprivation
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Inducible overexpression of wild-type prion protein in the muscles leads to a primary myopathy in transgenic mice
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TACE release of TNF-α mediates mechanotransduction-induced activation of p38 MAPK and myogenesis
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Primary cultured neurons devoid of cellular prion display lower responsiveness to Staurosporine through the control of p53 at both transcriptional and post-transcriptional levels
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Overexpression of PrPc triggers caspase 3 activation:: potentiation by proteasome inhibitors and blockade by anti-PrP antibodies
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Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons
B Vincent et al.
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Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation
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