Linked Life Data

15036595

Source:http://linkedlifedata.com/resource/pubmed/id/15036595

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-3-23
pubmed:abstractText
Tau protein can aggregate, in an aberrant way, in Alzheimer's disease and other tauopathies. The formation of those aggregates could take place in vitro by the addition of different compounds like polyanions or fatty acids and their derivates. Now, we found that a protein, zeta 14-3-3, facilitates the assembly of tau as well as a tau peptide containing the self-assembly region of tau molecule and a site for PKA phosphorylation. Also, we have found that tau and tau peptide polymerization are reduced, but not abolished upon PKA phosphorylation. The involvement of a scaffolding protein like 14-3-3 in the generation of tau filaments in tauopathies, like AD, is suggested.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0304-3940
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
357
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
143-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Zeta 14-3-3 protein favours the formation of human tau fibrillar polymers.
pubmed:affiliation
Centro de Biología Molecular 'Severo Ochoa' (CSIC-UAM), Facultad de Ciencias, Campus de Cantoblanco, Universidad Autónoma de Madrid, 28049 Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't