Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2010-11-24
pubmed:abstractText
The pathogenesis of Alzheimer's disease is attributed to misfolding of Amyloid-? (A?) peptides. A? is generated during amyloidogenic processing of A?-precursor protein (APP). Another characteristic of the AD brain is increased phosphorylation of APP amino acid Tyr(682). Tyr(682) is part of the Y(682)ENPTY(687) motif, a docking site for interaction with cytosolic proteins that regulate APP metabolism and signaling. For example, normal A? generation and secretion are dependent upon Tyr(682) in vitro. However, physiological functions of Tyr(682) are unknown.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1932-6203
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
e15503
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Tyr(682) in the intracellular domain of APP regulates amyloidogenic APP processing in vivo.
pubmed:affiliation
Department of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, New York, United States of America.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural