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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2009-11-20
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pubmed:abstractText |
Presenilin 1(PS1) is the catalytic subunit of gamma-secretase, the enzyme responsible for the Abeta C-terminal cleavage site, which results in the production of Abeta peptides of various lengths. Production of longer forms of the Abeta peptide occur in patients with autosomal dominant Alzheimer disease (AD) due to mutations in presenilin. Many modulators of gamma-secretase function have been described. We hypothesize that these modulators act by a common mechanism by allosterically modifying the structure of presenilin.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19924286-10206644,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19924286-10878813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19924286-10882062,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19924286-10993067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19924286-11557046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19924286-11700559,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19924286-11792846,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19924286-12110170,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19924286-12660785,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19924286-12805356,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19924286-14566063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19924286-15304503,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19924286-15448688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19924286-15772361,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19924286-9450754
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1932-6203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
e7893
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:19924286-Allosteric Site,
pubmed-meshheading:19924286-Amyloid Precursor Protein Secretases,
pubmed-meshheading:19924286-Amyloid beta-Peptides,
pubmed-meshheading:19924286-Animals,
pubmed-meshheading:19924286-Binding Sites,
pubmed-meshheading:19924286-CHO Cells,
pubmed-meshheading:19924286-Cell Line,
pubmed-meshheading:19924286-Cricetinae,
pubmed-meshheading:19924286-Cricetulus,
pubmed-meshheading:19924286-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:19924286-Green Fluorescent Proteins,
pubmed-meshheading:19924286-Humans,
pubmed-meshheading:19924286-Mice,
pubmed-meshheading:19924286-Mutation,
pubmed-meshheading:19924286-Presenilin-1,
pubmed-meshheading:19924286-Presenilins,
pubmed-meshheading:19924286-Protein Conformation
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pubmed:year |
2009
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pubmed:articleTitle |
Allosteric modulation of PS1/gamma-secretase conformation correlates with amyloid beta(42/40) ratio.
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pubmed:affiliation |
Alzheimer Research Unit, MassGeneral Institute for Neurodegenerative Diseases, Massachusetts General Hospital, Charlestown, Massachusetts, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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