Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

PCSK9 is required for the disposal of non-acetylated intermediates of the nascent membrane protein BACE1.

EMBO reports - 1 Sept 2008

Jonas Mary Cabell, Costantini Claudio, Puglielli Luigi

Abstract excerpt

We have recently identified a new form of post-translational regulation of BACE1 (beta-site amyloid precursor protein (APP)-cleaving enzyme 1), a membrane protein that acts as the rate-limiting enzyme in the generation of the Alzheimer disease amyloid beta-peptide (Abeta). Specifically, BACE1 is...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acetylation
Share to Amyloid Precursor Protein Secretases
Share to Aspartic Acid Endopeptidases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to CHO Cells

Share to Cricetulus

Share to Proprotein Convertase 9

Share to Proprotein Convertases

Share to Serine Endopeptidases

Source

Open in PubMed Open full text

Identifiers

PMID: 18660751
DOI: 10.1038/embor.2008.132
PMCID: PMC2529349

Genes

BACE1
PCSK9
APP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18660751-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

PCSK9 is required for the disposal of non-acetylated intermediates of the nascent membrane protein BACE1.PMID 18660751Read ↗

The role of amyloid precursor protein processing by BACE1, the beta-secretase, in Alzheimer disease pathophysiology.Semantic proximity Read ↗

BACE1 Structure and Function in Health and Alzheimers DiseaseSemantic proximity Read ↗

Seizure protein 6 and its homolog seizure 6-like protein are physiological substrates of BACE1 in neuronsSemantic proximity Read ↗

Physiological Functions of the β-Site Amyloid Precursor Protein Cleaving Enzyme 1 and 2Semantic proximity Read ↗

PS1 Affects the Pathology of Alzheimer's Disease by Regulating BACE1 Distribution in the ER and BACE1 Maturation in the Golgi Apparatus.Semantic proximity Read ↗

Cell surface presenilin-1 participates in the gamma-secretase-like proteolysis of Notch.Semantic proximity Read ↗

BIN1 regulates BACE1 intracellular trafficking and amyloid-β productionSemantic proximity Read ↗

Deficient ER Acetyl-CoA Import in Acinar Cells Leads to Chronic PancreatitisSemantic proximity Read ↗

Expression of the Alzheimer protease BACE1 is suppressed via its 5'-untranslated region.Semantic proximity Read ↗

The carboxyl-terminus of BACE contains a sorting signal that regulates BACE trafficking but not the formation of total A(beta).Semantic proximity Read ↗

Evidence for dimeric BACE-mediated APP processing.Semantic proximity Read ↗

Activation of protein kinase C modulates BACE1-mediated beta-secretase activity.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.