Extracellular release of BACE1 holoproteins from human neuronal cells.
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Summary
During the characterization of BACE1 shedding from human neuroblastoma SH-SY5Y cells stably expressing BACE 1, it was unexpectedly found that detectable amounts of Bace1 holoproteins were released extracellularly along with soluble BACE2, suggesting that the release of B ACE1 holiproteins may be a physiologically relevant cellular process.
- Type
- dissertation
- Published
- 2005-12-16
- Cited by
- 28
- References
- 41
- OpenAlex
- https://openalex.org/W16243299
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:28982047
Keywords
Humanities, Physics, Political science, Art
References
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Cited by
- Transmembrane Amyloid-Related Proteins in CSF as Potential Biomarkers for Alzheimer’s Disease
- Neuronal β-amyloid generation is independent of lipid raft association of β-secretase BACE1: analysis with a palmitoylation-deficient mutant
- BACE1 as a potential biomarker for Alzheimer’s disease
- β- and γ-Secretases and Lipid Rafts
- Statins Reduce Amyloid β-Peptide Production by Modulating Amyloid Precursor Protein Maturation and Phosphorylation Through a Cholesterol-Independent Mechanism in Cultured Neurons
- BACE1 structure and function in health and Alzheimer's disease.
- Study on Aβ34 biology and detection in transgenic mice brains.
- Development of a specific ELISA to measure BACE1 levels in human tissues
- Reticulons RTN3 and RTN4‐B/C interact with BACE1 and inhibit its ability to produce amyloid β‐protein
- The Basic Biology of BACE1: A Key Therapeutic Target for Alzheimer’s Disease
- The two‐hydrophobic domain tertiary structure of reticulon proteins is critical for modulation of β‐secretase BACE1
- A Cellular Model of Amyloid Precursor Protein Processing and Amyloid-β Peptide Production
- Expression of reticulon 3 in Alzheimer’s disease brain
- The Alzheimer's disease β-secretase enzyme, BACE1
- BACE1 Levels by APOE Genotype in Non-Demented and Alzheimer’s Post-Mortem Brains
- Cell biology, regulation and inhibition of β‐secretase (BACE‐1)
- Amyloid β-protein oligomers upregulate the β-secretase, BACE1, through a post-translational mechanism involving its altered subcellular distribution in neurons
- LRP1 Downregulates the Alzheimer’s β-Secretase BACE1 by Modulating Its Intraneuronal Trafficking,,
- LRP1 Downregulates the Alzheimer's -Secretase BACE1 by Modulating Its Intraneuronal
- BACE1 levels are increased in plasma of Alzheimer's disease patients compared with matched cognitively healthy controls.
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