ReviewFrontiers in cell and developmental biology2014
Regulation of PrP(C) signaling and processing by dimerization.
Review in Frontiers in cell and developmental biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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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.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Bovine Spongiform Encephalopathy: An Integrated Review of Prion Mechanisms, Neuroanatomy, and Control.Veterinary sciences · 2026Review
- Physiology of Cellular Prion Proteins in Reproduction.Development & reproduction · 2024Article
- Roles of prion proteins in mammalian development.Animal cells and systems · 2024Review
- Crystal structure and cellular functions of uPAR dimer.Nature communications · 2022Article
- The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling Modules.Frontiers in molecular neuroscience · 2017Article
- Actin dynamics and cofilin-actin rods in alzheimer disease.Cytoskeleton (Hoboken, N.J.) · 2016Review
- Secretory pathway retention of mutant prion protein induces p38-MAPK activation and lethal disease in mice.Scientific reports · 2016Article
- Disparate Modes of Evolution Shaped Modern Prion (PRNP) and Prion-Related Doppel (PRND) Variation in Domestic Cattle.PloS one · 2016Article
- Promiscuous functions of the prion protein family.Frontiers in cell and developmental biology · 2015Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cellular prion protein (PrP(C)) is a glycosylphosphatidylinositol (GPI)-anchored protein present at the cell surface. PrP(C) N-terminal moiety is intrinsically disordered and is able to interact with a variety of ligands. Physiological ligands have neurotrophic activity, whilst others, including protein toxic oligomers, have neurotoxic functions. These two opposite activities involve different interacting partners and result from different PrP(C)-activated signaling pathways. Remarkably, PrP(C) may be inactivated either by physiological endoproteolysis and release of the N-terminal domain, or by ectodomain shedding. Ligand-induced PrP(C) dimerization or enforced dimerization of PrP(C) indicate that PrP(C) dimerization represents an important molecular switch for both intracellular signaling and inactivation by the release of PrP(C) N-terminal domain or shedding. In this review, we summarize evidence that cell surface receptor activity of PrP(C) is finely regulated by dimerization.
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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.