Recent publishment of Dr.Prusiner
Science 1997 Oct 10;278(5336):245-251
Prion diseases and the BSE crisis
Prusiner SB
Department of Neurology (address for correspondence) and
Department of Biochemistry and Biophysics, University of California,
San Francisco, CA 94143, USA.
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.
On medline, I found 1306 papers about prion, 167 ones about the structure of prion, and 28 ones about prion structure in mouse. I show
the abstract of one of the 28 papers about mouse.
Science 1996 Dec 20;274(5295):2079-2082 Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity
Telling GC, Parchi P, DeArmond SJ, Cortelli P, Montagna P, Gabizon R, Mastrianni J, Lugaresi E, Gambetti P, Prusiner SB Department of Neurology, University of California, San Francisco, CA 94143, USA. The fundamental event in prion diseases seems to be a conformational change in cellular prion protein (PrPC) whereby it is converted into the pathologic isoform PrPSc. In fatal familial insomnia (FFI), the protease-resistant fragment of PrPSc after deglycosylation has a size of 19 kilodaltons, whereas that from other inherited and sporadic prion diseases is 21 kilodaltons. Extracts from the brains of FFI patients transmitted disease to transgenic mice expressing a chimeric human-mouse PrP gene about 200 days after inoculation and induced formation of the 19-kilodalton PrPSc fragment, whereas extracts from the brains of familial and sporadic Creutzfeldt-Jakob disease patients produced the 21-kilodalton PrPSc fragment in these mice. The results presented indicate that the conformation of PrPSc functions as a template in directing the formation of nascent PrPSc and suggest a mechanism to explain strains of prions where diversity is encrypted in the conformation of PrPSc. There are out of 1306 papers found on Medline. There are out of 167 papers found on Medline.