Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Falcon deep research report for BACE1
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The grounded Falcon (Edison) report corroborates the review's core picture of BACE1 as the rate-limiting beta-secretase that initiates amyloidogenic APP processing, and refines it by surfacing BACE1's complementary amyloidolytic cleavage of longer amyloid-beta species at the beta34 site.
"BACE1 serves as the initiating and rate-limiting enzyme in the amyloidogenic processing pathway of amyloid precursor protein"
Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE.
Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein.
Characterization of Alzheimer's beta -secretase protein BACE. A pepsin family member with unusual properties.
The transmembrane domain of the Alzheimer's beta-secretase (BACE1) determines its late Golgi localization and access to beta -amyloid precursor protein (APP) substrate.
The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblasts.
Identification of phospholipid scramblase 1 as a novel interacting molecule with beta -secretase (beta -site amyloid precursor protein (APP) cleaving enzyme (BACE)).
Presenilin-1 interacts directly with the beta-site amyloid protein precursor cleaving enzyme (BACE1).
BACE (beta-secretase) modulates the processing of APLP2 in vivo.
Reticulon family members modulate BACE1 activity and amyloid-beta peptide generation.
Demonstration of BACE (beta-secretase) phosphorylation and its interaction with GGA1 in cells by fluorescence-lifetime imaging microscopy.
GGA proteins mediate the recycling pathway of memapsin 2 (BACE).
GGA proteins regulate retrograde transport of BACE1 from endosomes to the trans-Golgi network.
BACE is degraded via the lysosomal pathway.
Interaction of the cytosolic domains of sorLA/LR11 with the amyloid precursor protein (APP) and beta-secretase beta-site APP-cleaving enzyme.
A reversible form of lysine acetylation in the ER and Golgi lumen controls the molecular stabilization of BACE1.
Cellular prion protein regulates beta-secretase cleavage of the Alzheimer's amyloid precursor protein.
A novel sorting nexin modulates endocytic trafficking and alpha-secretase cleavage of the amyloid precursor protein.
Two endoplasmic reticulum (ER)/ER Golgi intermediate compartment-based lysine acetyltransferases post-translationally regulate BACE1 levels.
Proteomic identification of sorting nexin 6 as a negative regulator of BACE1-mediated APP processing.
The ATP-binding cassette transporter-2 (ABCA2) increases endogenous amyloid precursor protein expression and Aβ fragment generation.
Sorting nexin 12 interacts with BACE1 and regulates BACE1-mediated APP processing.
A mutation in APP protects against Alzheimer's disease and age-related cognitive decline.
BACE1 protein endocytosis and trafficking are differentially regulated by ubiquitination at lysine 501 and the Di-leucine motif in the carboxyl terminus.
BRI2 interacts with BACE1 and regulates its cellular levels by promoting its degradation and reducing its mRNA levels.
Pharmacologic inhibition of ROCK2 suppresses amyloid-β production in an Alzheimer's disease mouse model.
MicroRNA-339-5p down-regulates protein expression of β-site amyloid precursor protein-cleaving enzyme 1 (BACE1) in human primary brain cultures and is reduced in brain tissue specimens of Alzheimer disease subjects.
Flotillins bind to the dileucine sorting motif of β-site amyloid precursor protein-cleaving enzyme 1 and influence its endosomal sorting.
Clec4g (LSECtin) interacts with BACE1 and suppresses Aβ generation.
The Golgi-Localized γ-Ear-Containing ARF-Binding (GGA) Proteins Alter Amyloid-β Precursor Protein (APP) Processing through Interaction of Their GAE Domain with the Beta-Site APP Cleaving Enzyme 1 (BACE1).
Identification of Human Islet Amyloid Polypeptide as a BACE2 Substrate.
SEPT8 modulates β-amyloidogenic processing of APP by affecting the sorting and accumulation of BACE1.
BIN1 regulates BACE1 intracellular trafficking and amyloid-β production.
The Endosome-associated Deubiquitinating Enzyme USP8 Regulates BACE1 Enzyme Ubiquitination and Degradation.
MiR-124 acts as a target for Alzheimer's disease by regulating BACE1.
β-Secretase BACE1 Promotes Surface Expression and Function of Kv3.4 at Hippocampal Mossy Fiber Synapses.
Visualization of Alzheimer's Disease Related α-/β-/γ-Secretase Ternary Complex by Bimolecular Fluorescence Complementation Based Fluorescence Resonance Energy Transfer.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Inhibition of beta A4 production by specific modulation of beta-secretase activity.
BACE1 cleaves APP(18-770) to APP(18-671) and APP(672-770)
BACE1:GGA1,2,3 translocates from plasma membrane to endosome
BACE1 translocates from ER lumen to Golgi apparatus
FURIN cleaves 7K-BACE1 to 7K-BACE1(46-501)
BACE1(46-501) translocates from Golgi lumen to plasma membrane
Unknown deacetylase deacetylates 7K-BACE1(46-501)