Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-12-30
pubmed:abstractText
By utilizing double-labeled fluorescent cellular prion protein (PrPC), we revealed that the NH2-terminal and COOH-terminal PrPC fragments exhibit distinct distribution patterns in mouse neuroblastoma neuro2a (N2a) cells and HpL3-4, a hippocampal cell line established from prnp gene-ablated mice [Nature 400 (1999) 225]. Of note, the NH2-terminal PrPC fragment, which predominantly localized in the intracellular compartments, congregated in the cytosol after the treatment with a microtubule depolymerizer (nocodazole). Truncated PrPC with the amino acid residues 1-121, 1-111, and 1-91 in mouse (Mo) PrP exhibited a proper distribution profile, whereas those with amino acid residues 1-52 and 1-33 did not. These data indicate the microtubules-associated intracellular localization of the NH2-terminal PrPC fragment containing at least the 1-91 amino acid residues.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
313
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
818-23
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Microtubules-associated intracellular localization of the NH2-terminal cellular prion protein fragment.
pubmed:affiliation
Department of Cortical Function Disorders, National Institute of Neuroscience, National Center of Neurology and Psychiatry, Tokyo 187-8502, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't