Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-7-23
pubmed:abstractText
Spongiform transmissible encephalopathies are neurodegenerative diseases characterized by the accumulation, in infected brains, of a pathological form of a normal host-encoded protein called PrP. Previous data have shown that PrP could interact with cytosolic factors, including nuclear molecules, emphasizing the possible function of such interactions. Moreover, in infected cells, PrP is observed not only at the plasma membrane but also in the nuclear compartment. The N-terminal extremity of the mature PrP has been thought to harbor a nuclear localization signal reminiscent of the nuclear localization signal of the simian virus 40 large T antigen. By designing a fusion protein between the putative nuclear localization signal of PrP and the green fluorescent protein, we have shown that the N-terminal sequence of PrP is not efficient in targeting the protein in the nuclear compartment. This implies new insights regarding the way by which PrP could, however, reach the nuclear compartment.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1044-7431
pubmed:author
pubmed:copyrightInfo
Copyright 1998 Academic Press.
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
127-33
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Search for a nuclear localization signal in the prion protein.
pubmed:affiliation
Service de Neurovirologie, CEA, DSV/DRM/SSA, 60-68 avenue de la Division Leclerc, Fontenay-aux-Roses, 92265, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't