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1.
Protein misfolding and disease: the case of prion disorders 总被引:2,自引:0,他引:2
Recent findings strongly support the hypothesis that diverse human disorders, including the most common neurodegenerative
diseases, arise from misfolding and aggregation of an underlying protein. Despite the good evidence for the involvement of
protein misfolding in disease pathogenesis, the mechanism by which protein conformational changes participate in the disease
is still unclear. Among the best-studied diseases of this group are the transmissible spongiform encephalopathies or prion-related
disorders, in which misfolding of the normal prion protein plays a key role in the disease. In this article we review recent
data on the link between prion protein misfolding and the pathogensis of spongiform encephalopathies.
Received 15 July 2002; received after revision 19 August 2002; accepted 23 August 2002
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2.
R. J. Capon K. Elsbury M. S. Butler C. C. Lu J. N. A. Hooper J. A. P. Rostas K. J. O'Brien L. -M. Mudge A. T. R. Sim 《Cellular and molecular life sciences : CMLS》1993,49(3):263-264
The Antarctic marine spongeTedania charcoti has been shown to contain extraordinarily high natural concentrations of cadmium and zinc, which have in turn been correlated to the ability of the crude ethanol extract to modulate protein phosphorylation in chicken forebrain and to inhibit the growth of several test bacteria. 相似文献