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http://purl.uniprot.org/citations/3257719http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3257719http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3257719http://www.w3.org/2000/01/rdf-schema#comment"Two approaches--molecular cloning and immunochemical analysis--have identified one of the components of Alzheimer's disease amyloid deposits as the serine protease inhibitor alpha 1-antichymotrypsin. An antiserum against isolated Alzheimer amyloid deposits detected immunoreactivity in normal liver. The antiserum was then used to screen a liver cDNA expression library, yielding three related clones. DNA sequence analysis showed that these clones code for alpha 1-antichymotrypsin. Antisera against purified alpha 1-antichymotrypsin stained Alzheimer amyloid deposits, both in situ and after detergent extraction from brain. The anti-amyloid antiserum recognizes at least two distinct epitopes in alpha 1-antichymotrypsin, further supporting the presence of this protein in Alzheimer amyloid deposits. In addition to being produced in the liver and released into the serum, alpha 1-antichymotrypsin is expressed in Alzheimer brain, particularly in areas that develop amyloid lesions. Models by which alpha 1-antichymotrypsin could contribute to the development of Alzheimer amyloid deposits are discussed."xsd:string
http://purl.uniprot.org/citations/3257719http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(88)90462-x"xsd:string
http://purl.uniprot.org/citations/3257719http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(88)90462-x"xsd:string
http://purl.uniprot.org/citations/3257719http://purl.uniprot.org/core/author"Abraham C.R."xsd:string
http://purl.uniprot.org/citations/3257719http://purl.uniprot.org/core/author"Abraham C.R."xsd:string
http://purl.uniprot.org/citations/3257719http://purl.uniprot.org/core/author"Potter H."xsd:string
http://purl.uniprot.org/citations/3257719http://purl.uniprot.org/core/author"Potter H."xsd:string
http://purl.uniprot.org/citations/3257719http://purl.uniprot.org/core/author"Selkoe D.J."xsd:string
http://purl.uniprot.org/citations/3257719http://purl.uniprot.org/core/author"Selkoe D.J."xsd:string
http://purl.uniprot.org/citations/3257719http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/3257719http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/3257719http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/3257719http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/3257719http://purl.uniprot.org/core/pages"487-501"xsd:string
http://purl.uniprot.org/citations/3257719http://purl.uniprot.org/core/pages"487-501"xsd:string
http://purl.uniprot.org/citations/3257719http://purl.uniprot.org/core/title"Immunochemical identification of the serine protease inhibitor alpha 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease."xsd:string
http://purl.uniprot.org/citations/3257719http://purl.uniprot.org/core/title"Immunochemical identification of the serine protease inhibitor alpha 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease."xsd:string
http://purl.uniprot.org/citations/3257719http://purl.uniprot.org/core/volume"52"xsd:string
http://purl.uniprot.org/citations/3257719http://purl.uniprot.org/core/volume"52"xsd:string
http://purl.uniprot.org/citations/3257719http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3257719
http://purl.uniprot.org/citations/3257719http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3257719
http://purl.uniprot.org/citations/3257719http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/3257719
http://purl.uniprot.org/citations/3257719http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/3257719