ReviewCurrent molecular medicine2009
Prion protein misfolding.
Review in Current molecular medicine, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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
31 citing papers in PubMed.
- M232R Familial Creutzfeldt-Jacob Disease Challenging to Diagnose Due to the Absence of Characteristic Laboratory Findings.Internal medicine (Tokyo, Japan) · 2026Article
- First report of novel single-nucleotide polymorphisms and genetic characteristics in the open reading frame of the prion protein gene (Frontiers in veterinary science · 2026Article
- Novel polymorphisms and functional characterization of the prion protein gene in sparrows (Frontiers in veterinary science · 2026Article
- Advancing Prion Diagnostics: RT-QuIC Applications in Peripheral Tissues.Sub-cellular biochemistry · 2025Review
- Detecting the Undetectable: Exploring the Diagnostic Potential of Protein Misfolding Cyclic Amplification in Human Prion Diseases.Sub-cellular biochemistry · 2025Review
- Characterization of variably protease-sensitive prionopathy by capillary electrophoresis.Scientific reports · 2024Article
- Unfolding Mechanism and Fibril Formation Propensity of Human Prion Protein in the Presence of Molecular Crowding Agents.International journal of molecular sciences · 2024Article
- Perspectives on CRISPR Genome Editing to Prevent Prion Diseases in High-Risk Individuals.Biomedicines · 2024Article
- Life should be redefined: Any molecule with the ability to self-replicate should be considered life.F1000Research · 2024Article
- Repression Effects of Hydrolysates from Hen-Egg Proteins on Amyloid Fibril Formation.The journal of poultry science · 2022Article
- Article
- Novel Single Nucleotide Polymorphisms (SNPs) and Genetic Features of the Prion Protein Gene (Frontiers in veterinary science · 2022Article
- Article
- Structure of prion β-oligomers as determined by short-distance crosslinking constraint-guided discrete molecular dynamics simulations.Proteomics · 2021Article
- The Role of Vitamins in Neurodegenerative Disease: An Update.Biomedicines · 2021Review
- Insights Into the Micelle-Induced β-Hairpin-to-α-Helix Transition of a LytA-Derived Peptide by Photo-CIDNP Spectroscopy.International journal of molecular sciences · 2021Article
- Sensing of Proteins by ICD Response of Iron(II) Clathrochelates Functionalized by Carboxyalkylsulfide Groups.Biomolecules · 2020Article
- Peptide Interference with APP and Tau Association: Relevance to Alzheimer's Disease Amelioration.International journal of molecular sciences · 2020Article
- Proteasome Activation to Combat Proteotoxicity.Molecules (Basel, Switzerland) · 2019Review
- Neurogenesis in Neurodegenerative Diseases: Role of MFG-E8.Frontiers in neuroscience · 2019Review
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The crucial event in the development of transmissible spongiform encephalopathies (TSEs) is the conformational change of a host-encoded membrane protein - the cellular PrP(C) - into a disease associated, fibril-forming isoform PrP(Sc). This conformational transition from the alpha-helix-rich cellular form into the mainly beta-sheet containing counterpart initiates an 'autocatalytic' reaction which leads to the accumulation of amyloid fibrils in the central nervous system (CNS) and to neurodegeneration, a hallmark of TSEs. The exact molecular mechanisms which lead to the conformational change are still unknown. It also remains to be brought to light how a polypeptide chain can adopt at least two stable conformations. This review focuses on structural aspects of the prion protein with regard to protein-protein interactions and the initiation of prion protein misfolding. It therefore highlights parts of the protein which might play a notable role in the conformational transition from PrP(C) to PrP(Sc) and consequently in inducing a fatal chain reaction of protein misfolding. Furthermore, features of different proteins, which are able to adopt insoluble fibrillar states under certain circumstances, are compared to PrP in an attempt to understand the unique characteristics of prion 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.