ReviewCellular and molecular life sciences : CMLS2012
Allosteric function and dysfunction of the prion protein.
Review in Cellular and molecular life sciences : CMLS, 2012. 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
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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
28 citing papers in PubMed, 49 citations in OpenAlex.
- Article
- Review
- Cleavage site-directed antibodies reveal the prion protein in humans is shed by ADAM10 at Y226 and associates with misfolded protein deposits in neurodegenerative diseases.Acta neuropathologica · 2024Article
- The multiple functions of PrPJournal of molecular medicine (Berlin, Germany) · 2022Review
- Cellular prion protein activates Caspase 3 for apoptotic defense mechanism in astrocytes.Molecular and cellular biochemistry · 2021Article
- The Role of Cellular Prion Protein in Promoting Stemness and Differentiation in Cancer.Cancers · 2021Review
- The Role of Cellular Prion Protein in Cancer Biology: A Potential Therapeutic Target.Frontiers in oncology · 2021Review
- Emerging Role of Cellular Prion Protein in the Maintenance and Expansion of Glioma Stem Cells.Cells · 2019Review
- A Sequence-Dependent DNA Condensation Induced by Prion Protein.Journal of nucleic acids · 2018Article
- Membrane-enriched proteome changes and prion protein expression during neural differentiation and in neuroblastoma cells.BMC genomics · 2017Article
- The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling Modules.Frontiers in molecular neuroscience · 2017Article
- Expression of Tyrosine Hydroxylase is Negatively Regulated Via Prion Protein.Neurochemical research · 2016Article
- Advanced tests for early and accurate diagnosis of Creutzfeldt-Jakob disease.Nature reviews. Neurology · 2016Review
- Spectroscopic and Theoretical Study of Cu(I) Binding to His111 in the Human Prion Protein Fragment 106-115.Inorganic chemistry · 2016Article
- Article
- Neuroprotective Effects Against POCD by Photobiomodulation: Evidence from Assembly/Disassembly of the Cytoskeleton.Journal of experimental neuroscience · 2016Review
- Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria.Microbial cell factories · 2015Article
- Prion Protein Modulates Monoaminergic Systems and Depressive-like Behavior in Mice.The Journal of biological chemistry · 2015Article
- Targeting prion protein interactions in cancer.Prion · 2015Review
- Prion protein facilitates synaptic vesicle release by enhancing release probability.Human molecular genetics · 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
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transmissible spongiform encephalopathies (TSEs) are neurodegenerative diseases associated with progressive oligo- and multimerization of the prion protein (PrP(C)), its conformational conversion, aggregation and precipitation. We recently proposed that PrP(C) serves as a cell surface scaffold protein for a variety of signaling modules, the effects of which translate into wide-range functional consequences. Here we review evidence for allosteric functions of PrP(C), which constitute a common property of scaffold proteins. The available data suggest that allosteric effects among PrP(C) and its partners are involved in the assembly of multi-component signaling modules at the cell surface, impose upon both physiological and pathological conformational responses of PrP(C), and that allosteric dysfunction of PrP(C) has the potential to entail progressive signal corruption. These properties may be germane both to physiological roles of PrP(C), as well as to the pathogenesis of the TSEs and other degenerative/non-communicable diseases.
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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.