Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-9-16
pubmed:abstractText
The conversion of the host-encoded prion protein (PrPc) into the insoluble, protease-resistant isoform (PrPsc) is the main pathogenic mechanism of transmissible spongiform encephalopathies. They are fatal neurodegenerative disorders, which in human occur as sporadic, inherited or familial forms. These last forms are linked to insert or point mutations of PrPc which may facilitate the spontaneous conversion into PrPsc. We have established stably transfected human neuroblastoma cells (SH-SY5Y) expressing mutant V210I, or wild-type PrPc. Both proteins were expressed and attached to the cell surface. The mutation in position 210 did not alter the biochemical properties of the protein in comparison with the wild-type protein nor induced any conformational changes similar to those observed in PrPsc.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0304-3940
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
41-4
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Expression of wild-type and V210I mutant prion protein in human neuroblastoma cells.
pubmed:affiliation
Laboratory of Virology, Istituto Superiore di Sanità, Rome, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't