ReviewThe Journal of cell biology2004
A lipid boundary separates APP and secretases and limits amyloid beta-peptide generation.
Review in The Journal of cell biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
28 citing papers in PubMed, 75 citations in OpenAlex.
- Cholesterol-dependent amyloid β production: space for multifarious interactions between amyloid precursor protein, secretases, and cholesterol.Cell & bioscience · 2023Review
- Involvement of Lipids in Alzheimer's Disease Pathology and Potential Therapies.Frontiers in physiology · 2020Review
- The Bewildering Effect of AMPK Activators in Alzheimer's Disease: Review of the Current Evidence.BioMed research international · 2020Review
- A Novel Contrast Agent Based on Magnetic Nanoparticles for Cholesterol Detection as Alzheimer's Disease Biomarker.Nanoscale research letters · 2019Article
- Neurometabolic roles of ApoE and Ldl-R in mouse brain.Journal of bioenergetics and biomembranes · 2016Article
- Neuroprotective effects of estrogens: the role of cholesterol.Journal of endocrinological investigation · 2016Review
- Cellular membrane fluidity in amyloid precursor protein processing.Molecular neurobiology · 2014Review
- The intracellular domain of sortilin interacts with amyloid precursor protein and regulates its lysosomal and lipid raft trafficking.PloS one · 2013Article
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- The Membrane-Bound Aspartyl Protease BACE1: Molecular and Functional Properties in Alzheimer's Disease and Beyond.Frontiers in physiology · 2012Article
- Impacts of membrane biophysics in Alzheimer's disease: from amyloid precursor protein processing to aβ Peptide-induced membrane changes.International journal of Alzheimer's disease · 2011Article
- Effects of fatty acid unsaturation numbers on membrane fluidity and α-secretase-dependent amyloid precursor protein processing.Neurochemistry international · 2011Article
- Involvement of AMP-activated-protein-kinase (AMPK) in neuronal amyloidogenesis.Biochemical and biophysical research communications · 2010Article
- Membrane biophysics and mechanics in Alzheimer's disease.Molecular neurobiology · 2010Review
- Secretory phospholipase A2 type III enhances alpha-secretase-dependent amyloid precursor protein processing through alterations in membrane fluidity.Journal of lipid research · 2010Article
- Age-dependent increase in desmosterol restores DRM formation and membrane-related functions in cholesterol-free DHCR24-/- mice.Neurochemical research · 2009Article
- Apolipoprotein E and its receptors in Alzheimer's disease: pathways, pathogenesis and therapy.Nature reviews. Neuroscience · 2009Review
- Membrane microdomain switching: a regulatory mechanism of amyloid precursor protein processing.The Journal of cell biology · 2008Article
- Amyloid precursor protein and amyloid beta-peptide bind to ATP synthase and regulate its activity at the surface of neural cells.Molecular psychiatry · 2008Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Millions of patients suffer from Alzheimer's disease, and intensive efforts to find a cure for this devastating disorder center on the proteases, which release the deadly amyloid beta-peptide from its precursor. The cutting procedure is thought to be cholesterol dependent and strategies to lower cholesterol as therapeutic treatment are under intensive investigation. Recent findings suggest that the complete proteolytic machinery required for amyloid beta-peptide generation is located within lipid rafts. Data by Dotti and colleagues (Abad-Rodriguez et al., 2004), in this issue, suggest that rafts isolate the cutting machinery away from its deadly substrate. These findings describe a novel mechanism for controlling proteolytic activity by building a lipid boundary between proteases and their substrates.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.