1.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. 
Answer:
Here is the paper and the abstract.
SO:	Science 1997 Oct 10;278(5336):245-251 
TI:	Prion diseases and the BSE crisis.
AU:	Prusiner SB
	Department of Neurology (address for correspondence) and Department 
	of Biochemistry andBiophysics, University of California, 
	San Francisco, CA 94143, USA. 
AB:	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.
PMID: 9323196, MUID: 97465970 

And BSE is bovine spongiform encephalopathy.


2.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. 
Answer:
There are 1306 papers described about prion, 167papers about prion structure, and 28 papers about the structure of mouse prion.
Here is the paper and the abstract.
SO:	FEBS Lett 1997 Aug 18;413(2):277-281 
TI:	Recombinant full-length murine prion protein, mPrP(23-231): purification and spectroscopic characterization.
AU:	Hornemann S, Korth C, Oesch B, Riek R, Wider G, Wuthrich K, Glockshuber R
	Institut fur Molekularbiologie und Biophysik, Eidgenossische 
	Technische Hochschule Honggerberg, Zurich, Switzerland. 
AB:	The cellular prion protein of the mouse, mPrP(C), consists of 208 
	amino acids (residues 23-231). It contains a carboxy-terminal domain, 
	mPrP(121-231), which represents an autonomous folding unit with three 
	alpha-helices and a two-stranded antiparallel beta-sheet. We expressed 
	the complete amino acid sequence of the prion protein, mPrP(23-231), in 
	the cytoplasm of Escherichia coli. mPrP(23-231) was solubilized from 
	inclusion bodies by 8 M urea, oxidatively refolded and purified to 
	homogeneity by conventional chromatographic techniques. Comparison of 
	near-UV circular dichroism, fluorescence and one-dimensional 1H-NMR 
	spectra of mPrP(23-231) and mPrP(121-231) shows that the amino-terminal 
	segment 23-120, which includes the five characteristic octapeptide 
	repeats, does not contribute measurably to the manifestation of three-
	dimensional structure as detected by these techniques, indicating that 
	the residues 121-231 might be the only polypeptide segment of PrP(C) 
	with a defined three-dimensional structure. 
PMID: 9280297, MUID: 97424375