Source:http://linkedlifedata.com/resource/pubmed/id/10965118
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3-4
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| pubmed:dateCreated |
2000-9-21
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| pubmed:databankReference | |
| pubmed:abstractText |
Down syndrome individuals develop abnormalities of most organs, including all the pathological and neurochemical features of Alzheimer's disease, by the early age of 30 yr. Here, we report the isolation and characterization of BACE2, a gene mapping on human chromosome 21q22.3, which is highly similar to a transmembrane aspartyl protease, BACE (for beta-site APP-cleaving enzyme), which is able to catalyze the beta-secretase cleavage of Alzheimer's amyloid precursor protein (APP). BACE2 is expressed in a wide variety of organs and tissues, with several transcripts due to alternative splicing and the use of two polyadenylation signals. The BACE2 gene product is a 518 amino acid protein with the signature of an aspartic protease, a 20-residue signal peptide, and two putative N-glycosylation sites. In addition, and similarly to BACE, BACE2 differs from the other members of the human aspartic protease family in the number and distribution of putative disulfide bonds and in the presence of an extended C-terminal region which contains a predicted transmembrane segment. BACE2 could be involved in the Alzheimer-like neuropathology of Down syndrome, as well as in Alzheimer's disease linked to chromosome 21 but not showing mutations in APP.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Protein Precursor,
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
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| pubmed:status |
MEDLINE
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| pubmed:issn |
0301-0171
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 2000 S. Karger AG, Basel.
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| pubmed:issnType |
Print
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| pubmed:volume |
89
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
177-84
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:10965118-Alternative Splicing,
pubmed-meshheading:10965118-Alzheimer Disease,
pubmed-meshheading:10965118-Amino Acid Sequence,
pubmed-meshheading:10965118-Amyloid beta-Protein Precursor,
pubmed-meshheading:10965118-Aspartic Acid Endopeptidases,
pubmed-meshheading:10965118-Base Sequence,
pubmed-meshheading:10965118-Blotting, Northern,
pubmed-meshheading:10965118-Chromosome Mapping,
pubmed-meshheading:10965118-Chromosomes, Human, Pair 21,
pubmed-meshheading:10965118-DNA,
pubmed-meshheading:10965118-DNA, Complementary,
pubmed-meshheading:10965118-Exons,
pubmed-meshheading:10965118-Female,
pubmed-meshheading:10965118-Genes,
pubmed-meshheading:10965118-Humans,
pubmed-meshheading:10965118-Introns,
pubmed-meshheading:10965118-Molecular Sequence Data,
pubmed-meshheading:10965118-RNA, Messenger,
pubmed-meshheading:10965118-Sequence Alignment,
pubmed-meshheading:10965118-Sequence Analysis, DNA,
pubmed-meshheading:10965118-Sequence Homology, Amino Acid,
pubmed-meshheading:10965118-Tissue Distribution
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| pubmed:year |
2000
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| pubmed:articleTitle |
A new aspartyl protease on 21q22.3, BACE2, is highly similar to Alzheimer's amyloid precursor protein beta-secretase.
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| pubmed:affiliation |
Down Syndrome Research Group, Medical and Molecular Genetics Center, IRO, Hospital Duran i Reynals, Barcelona, Spain.
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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