1999
DOI: 10.1006/mcne.1999.0811
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Identification of a Novel Aspartic Protease (Asp 2) as β-Secretase

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Cited by 1,027 publications
(654 citation statements)
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“…In 1999, BACE1 (also: b-secretase 1 or memapsin 2) was identified as a b-site APP-cleaving enzyme, [7][8][9][10][11] and, 2 years later, confirmed as the major b-secretase in vivo. 12 BACE1 initiates the amyloidogenic pathway of APP processing.…”
Section: Role Of Bace1 In Admentioning
confidence: 99%
“…In 1999, BACE1 (also: b-secretase 1 or memapsin 2) was identified as a b-site APP-cleaving enzyme, [7][8][9][10][11] and, 2 years later, confirmed as the major b-secretase in vivo. 12 BACE1 initiates the amyloidogenic pathway of APP processing.…”
Section: Role Of Bace1 In Admentioning
confidence: 99%
“…This enzymatic action leads to the release of a large soluble extracellular amino terminal fragment of APP (sAPP α ) and of a non-amyloidogenic 83-amino acid C-terminal fragment (C83). Conversely, in an amyloidogenic pathway, APP could be alternatively cleaved at a position located 99 amino acids from the C-terminus by a β -secretase, an aspartyl protease known as BACE1 ( β -site APP-cleaving enzyme) (Hussain et al , 1999 ). Cleavage by β -secretase releases a slightly shorter soluble APP peptide (sAPP β ) in the extracellular space and leaves a 99-amino acids C-terminal fragment (C99) within the membrane.…”
Section: App Metabolism and A β Formationmentioning
confidence: 99%
“…Nowadays, β-secretase is considered the initial and rate-limiting enzyme during this process. β-site APP cleavage enzyme (BACE), a type I integral membrane aspartic protease, was identified as the main β-secretase [3][4][5][6][7]. As formation of senile plaques could not be detected in BACE-deficient mice [8,9], BACE has attracted major attentions in AD research during recent years.…”
Section: Introductionmentioning
confidence: 99%