Linked Life Data

16542151

Source:http://linkedlifedata.com/resource/pubmed/id/16542151

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2006-3-17
pubmed:abstractText
A key molecular event in prion diseases is the conversion of cellular prion protein (PrP(c)) into an abnormal misfolded conformer (PrP(sc)). The PrP(c) N-terminal domain plays a central role in PrP(c) functions and in prion propagation. Because mammalian PrP(c) is found as a full-length and N-terminally truncated form, we examined the presence and amount of PrP(c) C-terminal fragment in the brain of different species. We found important variations between primates and rodents. In addition, our data show that the PrP(c) fragment is present in detergent-resistant raft domains, a membrane domain of critical importance for PrP(c) functions and its conversion into PrP(sc).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1431-6730
pubmed:author
pubmed:issnType
Print
pubmed:volume
387
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
297-300
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Truncated PrP(c) in mammalian brain: interspecies variation and location in membrane rafts.
pubmed:affiliation
INSERM Avenir Team-Human prion diseases, IFR70, Neuropathology, Salpêtrière Hospital, F-75013 Paris, France.
pubmed:publicationType
Journal Article