| pubmed-article:9721914 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9721914 | lifeskim:mentions | umls-concept:C0033164 | lld:lifeskim |
| pubmed-article:9721914 | lifeskim:mentions | umls-concept:C1511997 | lld:lifeskim |
| pubmed-article:9721914 | lifeskim:mentions | umls-concept:C0439836 | lld:lifeskim |
| pubmed-article:9721914 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:9721914 | pubmed:dateCreated | 1998-11-18 | lld:pubmed |
| pubmed-article:9721914 | pubmed:abstractText | The conversion of normal, protease sensitive prion protein (PrP-sen) to the abnormal protease-resistant form (PrP-res) is of central importance in the pathogenesis of scrapie and other transmissible spongiform encephalopathies. In the present study, the effects of reduction of the disulfide bond on the PrP-sen to PrP-res conversion in a cell-free system were examined. The addition of the disulfide reducing agent dithiothreitol inhibited the cell-free conversion reaction with an IC50 of 2-2.5 mM. Separate pretreatment of either PrP-sen or PrP-res with dithiothreitol and an alkylating agent also inhibited the conversion reaction. Results of this study show that preservation of the disulfide bond is important in the conversion of PrP-sen to PrP-res. | lld:pubmed |
| pubmed-article:9721914 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9721914 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9721914 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9721914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9721914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9721914 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9721914 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9721914 | pubmed:issn | 0959-4965 | lld:pubmed |
| pubmed-article:9721914 | pubmed:author | pubmed-author:CaugheyBB | lld:pubmed |
| pubmed-article:9721914 | pubmed:author | pubmed-author:HerrmannL MLM | lld:pubmed |
| pubmed-article:9721914 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9721914 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:9721914 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:9721914 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9721914 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9721914 | pubmed:pagination | 2457-61 | lld:pubmed |
| pubmed-article:9721914 | pubmed:dateRevised | 2005-11-17 | lld:pubmed |
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| pubmed-article:9721914 | pubmed:meshHeading | pubmed-meshheading:9721914-... | lld:pubmed |
| pubmed-article:9721914 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9721914 | pubmed:articleTitle | The importance of the disulfide bond in prion protein conversion. | lld:pubmed |
| pubmed-article:9721914 | pubmed:affiliation | National Institute of Health, National Institute of Allergy and Infectious Disease, Rocky Mountain Laboratories, Laboratory of Persistent Viral Diseases, Hamilton, MT 59840, USA. | lld:pubmed |
| pubmed-article:9721914 | pubmed:publicationType | Journal Article | lld:pubmed |
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