ReviewMolecular neurodegeneration2013
Overcoming barriers and thresholds - signaling of oligomeric Aβ through the prion protein to Fyn.
Review in Molecular neurodegeneration, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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
12 citing papers in PubMed, 18 citations in OpenAlex.
- Amyloid precursor protein (APP) and amyloid β (Aβ) interact with cell adhesion molecules: Implications in Alzheimer's disease and normal physiology.Frontiers in cell and developmental biology · 2022Review
- Isoform-specific upregulation of FynT kinase expression is associated with tauopathy and glial activation in Alzheimer's disease and Lewy body dementias.Brain pathology (Zurich, Switzerland) · 2021Article
- Alzheimer's Disease: An Overview of Major Hypotheses and Therapeutic Options in Nanotechnology.Nanomaterials (Basel, Switzerland) · 2020Review
- The Link of the Prion Protein with CaInternational journal of molecular sciences · 2019Review
- Analytical Strategy to Prioritize Alzheimer's Disease Candidate Genes in Gene Regulatory Networks Using Public Expression Data.Journal of Alzheimer's disease : JAD · 2017Article
- Neurological dysfunctions associated with altered BACE1-dependent Neuregulin-1 signaling.Journal of neurochemistry · 2016Review
- Glutamate receptors function as scaffolds for the regulation of β-amyloid and cellular prion protein signaling complexes.Molecular brain · 2015Review
- The prion protein constitutively controls neuronal store-operated Ca(2+) entry through Fyn kinase.Frontiers in cellular neuroscience · 2015Article
- Fragile X mental retardation protein: from autism to neurodegenerative disease.Frontiers in cellular neuroscience · 2015Article
- Review
- The low-density lipoprotein receptor-related protein 1 and amyloid-β clearance in Alzheimer's disease.Frontiers in aging neuroscience · 2014Review
- Premature lethality, hyperactivity, and aberrant phosphorylation in transgenic mice expressing a constitutively active form of Fyn.Frontiers in molecular neuroscience · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Evidence has been mounting for an involvement of the prion protein (PrP) in a molecular pathway assumed to play a critical role in the etiology of Alzheimer disease. A currently popular model sees oligomeric amyloid β (oAβ) peptides bind directly to PrP to emanate a signal that causes activation of the cytoplasmic tyrosine kinase Fyn, an essential player in a cascade of events that ultimately leads to NMDA receptor-mediated excitotoxicity and hyper-phosphorylation of tau. The model does not reveal, however, how extracellular binding of oAβ to PrP is communicated across the plasma membrane barrier to affect activation of Fyn. A scenario whereby PrP may adapt a transmembrane topology to affect Fyn activation in the absence of additional partners is currently not supported by evidence. A survey of known candidate PrP interactors leads to a small number of molecules that are known to acquire a transmembrane topology and understood to contribute to Fyn activation. Because multiple signaling pathways converge onto Fyn, a realistic model needs to take into account a reality of Fyn acting as a hub that integrates signals from multiple inhibitory and activating effectors. To clarify the role of PrP in oAβ-dependent excitotoxicity, future studies may need to incorporate experimental designs that can probe the contributions of Fyn modulator pathways and rely on analogous readouts, rather than threshold effects, known to underlie excitotoxic signaling.
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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.