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Journal article

Electron microscopic structure of purified, active gamma-secretase reveals an aqueous intramembrane chamber and two pores.

Abstract:

Gamma-secretase is an intramembrane-cleaving aspartyl protease required for the normal development of metazoans because it processes Notch within cellular membranes to release its signaling domain. More than two dozen additional substrates of diverse functions have been reported, including the Notch ligands Delta and Jagged, N- and E-cadherins, and a sodium channel subunit. The protease is causally implicated in Alzheimer's disease because it releases the neurotoxic amyloid beta-peptide (Abet...

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Publication status:
Published

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Publisher copy:
10.1073/pnas.0602321103

Authors


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Institution:
University of Oxford
Division:
MPLS
Department:
Materials
Role:
Author
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Journal:
Proceedings of the National Academy of Sciences of the United States of America
Volume:
103
Issue:
18
Pages:
6889-6894
Publication date:
2006-05-01
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
Source identifiers:
22161
Language:
English
Keywords:
Pubs id:
pubs:22161
UUID:
uuid:9e904e58-b640-43b5-938c-857310a25b00
Local pid:
pubs:22161
Deposit date:
2012-12-19

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