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The 1997 Nobel Prize in Physiology or Medicine is awarded to the American
Stanley Prusiner for his pioneering discovery of
Prions - a new biological principle of infection. Stanley
Prusiner has added prions to the list of well known infectious agents
including bacteria , viruses, fungi and parasites. Please find his recently
published paper concerning prion diseases and the BSE crisis. Please show
the abstract on your homepage and tell me what is
BSE.
BSE is bovine spongiform encephalopathy.
Abstract:
Bovine spongiform encephalopathy (BSE) and human
Creutzfeldt-Jakob disease (CJD) are among the most
notable central nervous system degenerative disorders caused by prions. CJD
may present as a sporadic,
genetic, or infectious illness. Prions are transmissible particles that are
devoid of nucleic acid and seem to be
composed exclusively of a modified protein (PrPSc). The normal, cellular
prion protein (PrPC) is converted
into PrPSc through a posttranslational process during which it acquires a
high beta-sheet content. It is thought
that BSE is a result of cannibalism in which faulty industrial practices
produced prion-contaminated feed for
cattle. There is now considerable concern that bovine prions may have been
passed to humans, resulting in a
new form of CJD.
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How many papers is referecned in MEDLINE, on line
biomedical abstract service, about prion? How many is
concerning its structure? Can you find the paper
describe the structure of mouse prion? Please show
its abstract on your homepage.
1306 papers about prion in Medline.
167 papers decribe prion structure.
28 papers decribe mouce prion structure.
NMR structure of the mouse prion protein domain PrP(121-231)
R Riek, S Hornemann, G Wider, M Billeter, R Glockshuber & K
Wuethrich
Proc Natl Acad Sci U S ANature 382, 180-182
(1996)
Abstract:
Spongiform encephalopathies such as scrapie, bovine spongiform
encephalopathy and Creutzfeldt-Jakob disease
are thought to be caused by a modified pathological form of a 'prion
protein' present in normal individuals. Point
mutations in certain parts of the prion protein may accelerate the
conversion process. Riek et al. have taken a
close look at the domain in question. Their study of the mouse prion
protein using nuclear magnetic resonance
(NMR) spectroscopy shows that this domain contains beta-sheet in
addition to the expected alpha-helix.
Disease-causing mutations lie within the regions of regular structure
or directly adjacent to them, suggesting how
the transition to the disease-causing form of the protein might occur.
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