Linked Life Data

12765773

Source:http://linkedlifedata.com/resource/pubmed/id/12765773

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2003-5-26
pubmed:abstractText
Prion diseases form a group of neurodegenerative disorders with the unique feature of being transmissible. These diseases involve a pathogenic protein, called PrP(Sc) for the scrapie isoform of the cellular prion protein (PrP(C)) which is an abnormally-folded counterpart of PrP(C). Many questions remain unresolved concerning the function of PrP(C) and the mechanisms underlying prion replication, transmission and neurodegeneration. PrP(C) is a glycosyl-phosphatidylinositol-anchored glycoprotein expressed at the cell surface of neurons and other cell types. PrP(C) may be present as distinct isoforms depending on proteolytic processing (full length and truncated), topology(GPI-anchored, transmembrane or soluble) and glycosylation (non- mono- and di-glycosylated). The present review focuses on the implications of PrP(C) glycosylation as to the function of the normal protein, the cellular pathways of conversion into PrP(Sc), the diversity of prion strains and the related selective neuronal targeting.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-9084
pubmed:author
pubmed:issnType
Print
pubmed:volume
85
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
33-45
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Evolving views in prion glycosylation: functional and pathological implications.
pubmed:affiliation
Laboratoire de Differenciation Cellulaire et Prions, UPR1983 CNRS, 7, rue Guy-Moquet, 94800 Villejuif, France. ermonval@vjf.cnrs.fr
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't