ArticlePrion2012
Regulation of amyloid-β production by the prion protein.
Article in Prion, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 20 citations in OpenAlex.
- CHRNA5 links chandelier cells to severity of amyloid pathology in aging and Alzheimer's disease.Translational psychiatry · 2024Article
- Review
- Harnessing the Physiological Functions of Cellular Prion Protein in the Kidneys: Applications for Treating Renal Diseases.Biomolecules · 2021Review
- Cellular Prion Protein (PrPc): Putative Interacting Partners and Consequences of the Interaction.International journal of molecular sciences · 2020Review
- Early-onset Alzheimer's disease patient with prionNeuropsychiatric disease and treatment · 2019Article
- Article
- Role of PrP(C) Expression in Tau Protein Levels and Phosphorylation in Alzheimer's Disease Evolution.Molecular neurobiology · 2015Article
- Alzheimer's disease and prion protein.Intractable & rare diseases research · 2013Review
- Article
- Amyloid beta precursor protein and prion protein have a conserved interaction affecting cell adhesion and CNS development.PloS one · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Alzheimer disease (AD) is characterized by the amyloidogenic processing of the amyloid precursor protein (APP), culminating in the accumulation of amyloid-β peptides in the brain. The enzymatic action of the β-secretase, BACE1 is the rate-limiting step in this amyloidogenic processing of APP. BACE1 cleavage of wild-type APP (APPWT) is inhibited by the cellular prion protein (PrP (C) ). Our recent study has revealed the molecular and cellular mechanisms behind this observation by showing that PrP (C) directly interacts with the pro-domain of BACE1 in the trans-Golgi network (TGN), decreasing the amount of BACE1 at the cell surface and in endosomes where it cleaves APPWT, while increasing BACE1 in the TGN where it preferentially cleaves APP with the Swedish mutation (APPSwe). PrP (C) deletion in transgenic mice expressing the Swedish and Indiana familial mutations (APPSwe,Ind) failed to affect amyloid-β accumulation, which is explained by the differential subcellular sites of action of BACE1 toward APPWT and APPSwe. This, together with our observation that PrP (C) is reduced in sporadic but not familial AD brain, suggests that PrP (C) plays a key protective role against sporadic AD. It also highlights the need for an APPWT transgenic mouse model to understand the molecular and cellular mechanisms underlying sporadic AD.
Indexed as
Identifiers
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.