BACE2, a beta -secretase homolog, cleaves at the beta site and within the amyloid-beta region of the amyloid-beta precursor protein - Wikidata - wikimedia - TriplyDB

BACE2, a beta -secretase homolog, cleaves at the beta site and within the amyloid-beta region of the amyloid-beta precursor protein

BACE2, a beta -secretase homolog, cleaves at the beta site and within the amyloid-beta region of the amyloid-beta precursor protein

http://www.wikidata.org/entity/Q24675964

about

Pro-domain removal in ASP-2 and the cleavage of the amyloid precursor are influenced by pH Stepping closer to treating Alzheimer's disease patients with BACE1 inhibitor drugs Dense-core senile plaques in the Flemish variant of Alzheimer's disease are vasocentric Compounds that bind APP and inhibit Abeta processing in vitro suggest a novel approach to Alzheimer disease therapeutics Proteolytic processing of Alzheimer's β-amyloid precursor protein BACE1 and presenilin: two unusual aspartyl proteases involved in Alzheimer's disease Trafficking and proteolytic processing of APP Reticulon family members modulate BACE1 activity and amyloid-beta peptide generation BACE1 expression and activity: relevance in Alzheimer's disease beta-site APP cleaving enzyme mRNA expression in APP transgenic mice: anatomical overlap with transgene expression and static levels with aging The normal and pathologic roles of the Alzheimer's β-secretase, BACE1 A tale of two drug targets: the evolutionary history of BACE1 and BACE2 Take five--BACE and the gamma-secretase quartet conduct Alzheimer's amyloid beta-peptide generation.BACE1, a major determinant of selective vulnerability of the brain to amyloid-beta amyloidogenesis, is essential for cognitive, emotional, and synaptic functions.Reduced IGF-1 signaling delays age-associated proteotoxicity in mice Substrate and inhibitor profile of BACE (beta-secretase) and comparison with other mammalian aspartic proteases.Generation of C-terminally truncated amyloid-beta peptides is dependent on gamma-secretase activity.Identification of inhibitors using a cell-based assay for monitoring Golgi-resident protease activity.Observation of amyloid precursor protein cleavage and A beta generation in living cells by using multiphoton laser scanning microscopy.Physiological Functions of the β-Site Amyloid Precursor Protein Cleaving Enzyme 1 and 2 BACE1 and BACE2 enzymatic activities in Alzheimer's disease.Analysis of Alzheimer's disease severity across brain regions by topological analysis of gene co-expression networks.Central angiotensin II stimulation promotes β amyloid production in Sprague Dawley rats.Function, therapeutic potential and cell biology of BACE proteases: current status and future prospects.The secretases: enzymes with therapeutic potential in Alzheimer disease.An overview of APP processing enzymes and products.Prodomain processing of Asp1 (BACE2) is autocatalytic.β-site amyloid precursor protein cleaving enzyme 1(BACE1) regulates Notch signaling by controlling the cleavage of Jagged 1 (Jag1) and Jagged 2 (Jag2) proteins.Inhibition of BACE1 for therapeutic use in Alzheimer's disease.Regulation of APP cleavage by alpha-, beta- and gamma-secretases.Beta-secretase: structure, function, and evolution.Proteases and proteolysis in Alzheimer disease: a multifactorial view on the disease process.BACE1 (β-secretase) inhibitors for the treatment of Alzheimer's disease Enzymic properties of recombinant BACE2.Beta-amyloid therapies in Alzheimer's disease.Β-site APP-cleaving enzyme 1 trafficking and Alzheimer's disease pathogenesis.Secretases as therapeutic targets for the treatment of Alzheimer's disease.Identification of HKDC1 and BACE2 as genes influencing glycemic traits during pregnancy through genome-wide association studies.Association study of candidate gene polymorphisms with amnestic mild cognitive impairment in a Chinese population Targeting the β secretase BACE1 for Alzheimer's disease therapy.

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BACE2, a beta -secretase homolog, cleaves at the beta site and within the amyloid-beta region of the amyloid-beta precursor protein

http://www.wikidata.org/entity/Q24675964

description

2000 nî lūn-bûn

@nan

2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2000年の論文

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2000年論文

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2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

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2000年论文

@wuu

name

BACE2, a beta -secretase homol ...... amyloid-beta precursor protein

@ast

BACE2, a beta -secretase homol ...... amyloid-beta precursor protein

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BACE2, a beta -secretase homol ...... amyloid-beta precursor protein

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type

label

BACE2, a beta -secretase homol ...... amyloid-beta precursor protein

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BACE2, a beta -secretase homol ...... amyloid-beta precursor protein

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BACE2, a beta -secretase homol ...... amyloid-beta precursor protein

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prefLabel

BACE2, a beta -secretase homol ...... amyloid-beta precursor protein

@ast

BACE2, a beta -secretase homol ...... amyloid-beta precursor protein

@en

BACE2, a beta -secretase homol ...... amyloid-beta precursor protein

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P1433

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Proceedings of the National Academy of Sciences of the United States of America

P1476

BACE2, a beta -secretase homol ...... amyloid-beta precursor protein

@en

P2093

Choe H

http://www.w3.org/2001/XMLSchema#string

Farzan M

http://www.w3.org/2001/XMLSchema#string

Leung D

http://www.w3.org/2001/XMLSchema#string

Vasilieva N

http://www.w3.org/2001/XMLSchema#string

P2860

Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE

Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity

Purification and cloning of amyloid precursor protein beta-secretase from human brain

Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design

Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease

Early-onset Alzheimer's disease caused by mutations at codon 717 of the beta-amyloid precursor protein gene

Identification of a Novel Aspartic Protease (Asp 2) as β-Secretase

Translating cell biology into therapeutic advances in Alzheimer's disease.

Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids.

P304

9712-9717

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P31

scholarly article

P3181

88861

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10.1073/PNAS.160115697

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P433

17

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P478

97

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P50

Christine Schnitzler

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2000-08-01T00:00:00Z

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12388580

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P698

10931940

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P932

16930

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