Linked Life Data

11147714

Source:http://linkedlifedata.com/resource/pubmed/id/11147714

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2001-1-5
pubmed:abstractText
Pathological changes in the microtubule associated protein tau, leading to tau-containing filamentous lesions, are a major hallmark common to many types of human neurodegenerative diseases, including Alzheimer's disease (AD). No structural data are available which could rationalize the extensive conformational changes that occur when tau protein is converted to Alzheimer's paired helical filaments (PHF). The C-terminal portion of tau plays a crucial role in the aggregation of tau into PHF and in the truncation process that generates cytotoxic segments of tau. Therefore, we investigated the solution structure of the hydrophobic C-terminal segment 423-441 of tau protein (PQLATLADEVSASLAKQGL) by 1H 2D NMR spectroscopy. The peptide displays the typical NMR evidence consistent with a alpha-helix geometry with a stabilizing C-capping motif. The reported data represent the first piece of structural information on an important portion of the molecule and can have implications towards the understanding of its pathophysiology.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1075-2617
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
550-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
The solution structure of the C-terminal segment of tau protein.
pubmed:affiliation
Dipartimento di Scienze e Tecnologie Biomediche, Università di Udine, Italy. gesposito@makek.dstb.uniud.it
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't