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Human Prion Disease 

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  1. Open Access 01-12-2022 | Creutzfeldt-Jakob Disease | OriginalPaper

    Sporadic Creutzfeldt-Jakob disease VM1: phenotypic and molecular characterization of a novel subtype of human prion disease

    The methionine (M)—valine (V) polymorphic codon 129 of the prion protein gene (PRNP) plays a central role in both susceptibility and phenotypic expression of sporadic Creutzfeldt-Jakob diseases (sCJD). Experimental transmissions of sCJD in …

  2. Open Access 01-10-2020 | Doxycycline | OriginalPaper

    Administration of FK506 from Late Stage of Disease Prolongs Survival of Human Prion-Inoculated Mice

    Human prion diseases are etiologically categorized into three forms: sporadic, genetic, and infectious. Sporadic Creutzfeldt-Jakob disease (sCJD) is the most common type of human prion disease that manifests as subacute progressive dementia. No …

  3. Open Access 01-12-2019 | Creutzfeldt-Jakob Disease | OriginalPaper

    Sporadic Creutzfeldt-Jakob disease prion infection of human cerebral organoids

    For the transmissible, neurogenerative family of prion diseases, few human models of infection exist and none represent structured neuronal tissue. Human cerebral organoids are self-organizing, three-dimensional brain tissues that can be grown …

  4. 26-08-2022 | OriginalPaper

    Multiple system atrophy prions transmit neurological disease to mice expressing wild-type human α-synuclein

    In multiple system atrophy (MSA), the protein α-synuclein misfolds into a prion conformation that self-templates and causes progressive neurodegeneration. While many point mutations in the α-synuclein gene, SNCA, have been identified as the cause …

  5. Open Access 01-12-2018 | OriginalPaper

    Familial human prion diseases associated with prion protein mutations Y226X and G131V are transmissible to transgenic mice expressing human prion protein

    Human familial prion diseases are associated with mutations at 34 different prion protein (PrP) amino acid residues. However, it is unclear whether infectious prions are found in all cases. Mutant PrP itself may be neurotoxic, or alternatively …

  6. 01-05-2017 | ReviewPaper

    Neuroradiology of human prion diseases, diagnosis and differential diagnosis

    Human transmissible spongiform encephalopathies (TSEs), or prion diseases, are invariably fatal conditions associated with a range of clinical presentations. TSEs are classified as sporadic [e.g. sporadic Creutzfeldt–Jakob disease (sCJD), which is …

  7. Open Access 01-12-2016 | OriginalPaper

    Emergence of two prion subtypes in ovine PrP transgenic mice infected with human MM2-cortical Creutzfeldt-Jakob disease prions

    Mammalian prions are proteinaceous pathogens responsible for a broad range of fatal neurodegenerative diseases in humans and animals [ 20 ]. Prions are primarily formed of macromolecular assemblies of PrP Sc , a misfolded, ß-sheet enriched form of …

  8. 01-08-1998 | OriginalPaper

    Prospects for the Pharmacological Treatment of Human Prion Diseases

    There is currently no effective therapy available for Creutzfeldt-Jakob disease and related prion disorders. However, a limited number of drugs have been found to affect the course of experimental prion diseases and to modify the kinetics of …

  9. Open Access 01-04-2017 | OriginalPaper

    UK Iatrogenic Creutzfeldt–Jakob disease: investigating human prion transmission across genotypic barriers using human tissue-based and molecular approaches

    Creutzfeldt–Jakob disease (CJD) is the prototypic human prion disease that occurs most commonly in sporadic and genetic forms, but it is also transmissible and can be acquired through medical procedures, resulting in iatrogenic CJD (iCJD). The …

  10. 01-05-2001 | OriginalPaper

    Marked increase of neuronal prion protein immunoreactivity in Alzheimer's disease and human prion diseases

    In neurodegenerative disorders including Alzheimer's disease (AD), free radical damage to lipids, carbohydrates, proteins and DNA has been demonstrated to play a key pathogenetic role. In vitro studies have suggested a function of the cellular …

  11. 01-01-2011 | ReviewPaper

    Molecular biology and pathology of prion strains in sporadic human prion diseases

    Prion diseases are believed to propagate by the mechanism involving self-perpetuating conformational conversion of the normal form of the prion protein, PrPC, to the misfolded, pathogenic state, PrPSc. One of the most intriguing aspects of these …

  12. 01-09-2002 | OriginalPaper

    Distribution of intraneuronal immunoreactivity for the prion protein in human prion diseases

    Intraneuronal prion protein (PrP) immunoreactivity (INIR), which might represent the non-pathological, cellular form of PrP, needs to be distinguished from disease-associated deposits specific for prion disease (PrD). In adjacent sections of PrD …

  13. Open Access 01-12-2016 | OriginalPaper

    A Fluorescent Oligothiophene-Bis-Triazine ligand interacts with PrP fibrils and detects SDS-resistant oligomers in human prion diseases

    Prions are unconventional infectious agents responsible for fatal neurodegenerative disorders in animals and humans [ 1 ]. In humans, prion diseases are mostly represented by Creutzfeldt-Jakob disease (CJD) which is classified into three groups: …

  14. Open Access 01-01-2011 | ReviewPaper

    Molecular pathology of human prion disease

    Human prion diseases are associated with a range of clinical presentations and are classified by both clinicopathological syndrome and aetiology with sub-classification according to molecular criteria. Considerable experimental evidence suggests …

  15. Open Access 01-12-2011 | ReviewPaper

    An overview of human prion diseases

    Prion diseases are transmissible, progressive and invariably fatal neurodegenerative conditions associated with misfolding and aggregation of a host-encoded cellular prion protein, PrPC. They have occurred in a wide range of mammalian species …

  16. 01-08-2015 | ReviewPaper

    The influence of PRNP polymorphisms on human prion disease susceptibility: an update

    Two normally occurring polymorphisms of the human PRNP gene, methionine (M)/valine (V) at codon 129 and glutamic acid (E)/lysine (K) at codon 219, can affect the susceptibility to prion diseases. It has long been recognized that 129M/M homozygotes …

  17. 01-11-2009 | OriginalPaper

    Management and prevention of human prion diseases

    Prion diseases are a group of fatal neurologic disorders that affect humans and animals and for which there is no available therapy. The basic pathogenic mechanism is linked to posttranslational changes of the host cellular prion protein (PrPc) …

  18. 01-09-2005 | OriginalPaper

    Redox metals and oxidative abnormalities in human prion diseases

    Prion diseases are characterized by the accumulation of diffuse and aggregated plaques of protease-resistant prion protein (PrP) in the brains of affected individuals and animals. Whereas prion diseases in animals appear to be almost exclusively …

  19. 01-06-2004 | OriginalPaper

    Cytopathological Changes in Human and Animals Brains in Prion Diseases

    Studies of histological preparations of the brains of humans and animals with prion diseases showed that neuron vacuolization often starts and develops intensely in the distal segments of dendrites. Two types of neuron body death were noted – …

  20. 01-05-2002 | OriginalPaper

    Alpha-synuclein-immunoreactive deposits in human and animal prion diseases

    Prion related disorders are associated with the accumulation of a misfolded isoform (PrPsc) of the host-encoded prion protein, PrP. There is strong evidence for the involvement of unidentified co-factors in the PrP to PrPsc conversion process. In …

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