ReviewInternational journal of cell biology2013
Prion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions.
Review in International journal of cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 67 citations in OpenAlex.
- Bovine Spongiform Encephalopathy: An Integrated Review of Prion Mechanisms, Neuroanatomy, and Control.Veterinary sciences · 2026Review
- PrPEnvironmental science & technology · 2026Article
- Molecular Mechanisms and Therapeutic Potential of Degron-Mediated Proteostasis Regulation in Neurodegenerative Diseases.Cellular and molecular neurobiology · 2026Review
- Discovering, Integrating, and Reinterpreting the Molecular Logic of Life: From Classical Theories of Heredity to an Extended Functional Perspective on the Central Dogma.Life (Basel, Switzerland) · 2026Review
- Pathogens Association with Alzheimer Disease: Emerging Concepts and New Perspectives.Current gene therapy · 2026Review
- Creutzfeldt-Jakob Disease Mimicking Transient Brain Ischemia in a Patient with a Mitral Valve Prosthesis-A Case Report.Reports (MDPI) · 2025Article
- Protein aggregation and neurodegenerative disease: Structural outlook for the novel therapeutics.Proteins · 2025Review
- 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025Review
- Bovine spongiform encephalopathy: A review of current knowledge and challenges.Open veterinary journal · 2025Review
- Adaptation of the protein misfolding cyclic amplification (PMCA) technique for the screening of anti-prion compounds.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024Article
- Review
- Article
- A microfluidic biosensor for the diagnosis of chronic wasting disease.Microsystems & nanoengineering · 2023Article
- Transmission of Cerebral β-Amyloidosis Among Individuals.Neurochemical research · 2022Article
- Identification of recurrent genetic patterns from targeted sequencing panels with advanced data science: a case-study on sporadic and genetic neurodegenerative diseases.BMC medical genomics · 2022Article
- Circulation of Nor98 Atypical Scrapie in Portuguese Sheep Confirmed by Transmission of Isolates into Transgenic Ovine ARQ-PrP Mice.International journal of molecular sciences · 2021Article
- The polyphenolic phytoalexin polydatin inhibits amyloid aggregation of recombinant human prion protein.RSC advances · 2021Article
- Cellular prion protein activates Caspase 3 for apoptotic defense mechanism in astrocytes.Molecular and cellular biochemistry · 2021Article
- Sensing of Proteins by ICD Response of Iron(II) Clathrochelates Functionalized by Carboxyalkylsulfide Groups.Biomolecules · 2020Article
- Variable Protease-Sensitive Prionopathy Transmission to Bank Voles.Emerging infectious diseases · 2019Article
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
No grant is acknowledged in the PubMed record.
Abstract
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative disorders affecting humans and other mammalian species. The central event in TSE pathogenesis is the conformational conversion of the cellular prion protein, PrP(C), into the aggregate, β -sheet rich, amyloidogenic form, PrP(Sc). Increasing evidence indicates that distinct PrP(Sc) conformers, forming distinct ordered aggregates, can encipher the phenotypic TSE variants related to prion strains. Prion strains are TSE isolates that, after inoculation into syngenic hosts, cause disease with distinct characteristics, such as incubation period, pattern of PrP(Sc) distribution, and regional severity of histopathological changes in the brain. In analogy with other amyloid forming proteins, PrP(Sc) toxicity is thought to derive from the existence of various intermediate structures prior to the amyloid fiber formation and/or their specific interaction with membranes. The latter appears particularly relevant for the pathogenesis of TSEs associated with GPI-anchored PrP(Sc), which involves major cellular membrane distortions in neurons. In this review, we update the current knowledge on the molecular mechanisms underlying three fundamental aspects of the basic biology of prions such as the putative mechanism of prion protein conversion to the pathogenic form PrP(Sc) and its propagation, the molecular basis of prion strains, and the mechanism of induced neurotoxicity by PrP(Sc) aggregates.
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.