(Q24291471)

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The transmembrane domain of the Alzheimer's beta-secretase (BACE1) determines its late Golgi localization and access to beta -amyloid precursor protein (APP) substrate

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The transmembrane domain of the Alzheimer's beta-secretase (BACE1) determines its late Golgi localization and access to beta -amyloid precursor protein (APP) substrate (English)

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Alzheimer's disease

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based on heuristic

inferred from title

transmembrane protein

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Beta-secretase 1

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GOA release 2020-03-11

4

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author name string

R Yan

1

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P Han

2

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H Miao

3

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H Xu

5

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language of work or name

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publication date

28 September 2001

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Journal of Biological Chemistry

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276

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36788-96

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39

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Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein.

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Targeting and retention of Golgi membrane proteins

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Amyloid, the presenilins and Alzheimer's disease

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Identification of beta-secretase-like activity using a mass spectrometry-based assay system

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Mice deficient in BACE1, the Alzheimer's beta-secretase, have normal phenotype and abolished beta-amyloid generation

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BACE1 is the major beta-secretase for generation of Abeta peptides by neurons

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

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

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Alzheimer's A beta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells

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Processing of Alzheimer beta/A4 amyloid precursor protein: modulation by agents that regulate protein phosphorylation

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Generation of Alzheimer beta-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation

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Endoplasmic reticulum and trans-Golgi network generate distinct populations of Alzheimer beta-amyloid peptides

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Recycling of furin from the plasma membrane. Functional importance of the cytoplasmic tail sorting signals and interaction with the AP-2 adaptor medium chain subunit

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Functional cooperation of two independent targeting domains in syntaxin 6 is required for its efficient localization in the trans-golgi network of 3T3L1 adipocytes

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Maturation and pro-peptide cleavage of beta-secretase

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Maturation and endosomal targeting of beta-site amyloid precursor protein-cleaving enzyme. The Alzheimer's disease beta-secretase

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A furin-like convertase mediates propeptide cleavage of BACE, the Alzheimer's beta -secretase

1 reference

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Processing of beta-secretase by furin and other members of the proprotein convertase family

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The pro domain of beta-secretase does not confer strict zymogen-like properties but does assist proper folding of the protease domain

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Post-translational processing of beta-secretase (beta-amyloid-converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activity and amyloid-beta production

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Phosphorylation regulates intracellular trafficking of beta-secretase

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BACE2 functions as an alternative alpha-secretase in cells

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Cholesterol and the Golgi apparatus

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Identifiers

10.1074/JBC.M104350200

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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