Linked Life Data

8955115

Source:http://linkedlifedata.com/resource/pubmed/id/8955115

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
51
pubmed:dateCreated
1997-1-23
pubmed:abstractText
The epitope on tau protein recognized by the monoclonal antibody Alz50 was defined through internal deletion mutagenesis and quantified by affinity measurements. The epitope is discontinuous and requires both a previously identified N-terminal segment and the microtubule binding region for efficient binding of Alz50. The interaction between these regions is consistent with an intramolecular reaction mechanism, suggesting that Alz50 binding depends on the conformation of individual tau monomers. The results suggest that tau adopts a distinct conformation when polymerized into filaments and that this conformation is recognized selectively by Alz50.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
32789-95
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology.
pubmed:affiliation
Department of Cell and Molecular Biology, Northwestern University Medical School, and the Northwestern University Institute for Neuroscience, Chicago, Illinois 60611-3008, USA. JKuret@nwu.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.