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Cited by 290

The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.

β Subunits of Voltage-gated Sodium Channels Are Novel Substrates of β-Site Amyloid Precursor Protein-cleaving Enzyme (BACE1) and γ-Secretase

Open access
Wong, Hon-Kit, Sakurai, Takashi, Oyama, Fumitaka, Kaneko, Kumi, Wada, Koji, Miyazaki, Haruko, Kurosawa, Masaru, De Strooper, Bart, Saftig, Paul, Nukina, Nobuyuki·2005·Journal of Biological Chemistry

Abstract

Sequential processing of amyloid precursor protein (APP) by membrane-bound proteases, BACE1 and gamma-secretase, plays a crucial role in the pathogenesis of Alzheimer disease. Much has been discovered on the properties of these proteases; however, regulatory mechanisms of enzyme-substrate interaction in neurons and their involvement in pathological changes are still not fully understood. It is mainly because of the membrane-associated cleavage of these proteases and the lack of information on new substrates processed in a similar way to APP. Here, using RNA interference-mediated BACE1 knockdown, mouse embryonic fibroblasts that are deficient in either BACE1 or presenilins, and BACE1-deficient mouse brain, we show clear evidence that beta subunits of voltage-gated sodium channels are sequentially processed by BACE1 and gamma-secretase. These results may provide new insights into the underlying pathology of Alzheimer disease.

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Crossref · 10.1074/jbc.m414648200

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Metadata

Authors
Wong, H.-K., Sakurai, T., Oyama, F., Kaneko, K., Wada, K., Miyazaki, H., Kurosawa, M., De Strooper, B., Saftig, P., & Nukina, N.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2005-06
Volume
280
Issue
24
Pages
23009-23017
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2003659505
Cited by
290
References
6
FWCI
11.86
Type
journal article
Language
en
Open access
hybrid

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