Linked Life Data

12935881

Source:http://linkedlifedata.com/resource/pubmed/id/12935881

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2003-8-25
pubmed:abstractText
To gain insight into presenilin-1 (PS1) structural aspects, we explored the structure-function relationship of its N- and C-terminal (NTF and CTF, respectively) complexes. We demonstrated that both NTF and CTF act as independent but inter-changing binding units capable of binding each other (NTF/CTF) or their homologues (NTF/NTF; CTF/CTF). The Alzheimer's disease-associated PS1 mutations Y115H and M146L do not affect their ability to hetero- and/or homodimerize, thus conserving their basic integrity and function(s). These results suggest that PS1 associates intra-molecularly to form higher order complexes, which may be needed for endoproteolytic cleavage and/or gamma-secretase-associated activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
550
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
30-4
pubmed:dateRevised
2010-5-27
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Oligomerization of human presenilin-1 fragments.
pubmed:affiliation
Molecular and Human Genetics Unit, CHUQ-Pavillon St-François d'Assise, 10 rue de l'Espinay, Quebec, QC, Canada G1L 3L5.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't